BLAST at NCBI
Find the amino acid sequence for the protein involved with your disease phenotype.
Perform a Blast search on the protein.
Is your protein found only in primates? All mammals? How about amphibians and
reptiles? Are there homologs in bacteria? (You can search these types of organisms
individually in blast).
Protein is found in mammals of all kinds, fish, toads, and bacteria.
Find out as much as you can about your protein and the conserved domains in your
protein of interest:
Examine and compile all relevant information. Save all information which you think may
be useful for your presentation.
Submit:
1. The FASTA file for your protein. >gi|189181666|ref|NP_000511.2|
hexosaminidase A preproprotein [Homo sapiens]
MTSSRLWFSLLLAAAFAGRATALWPWPQNFQTSDQRYVLYPNNFQFQYDVSSAAQPGCSVLDEAFQRYRD
LLFGSGSWPRPYLTGKRHTLEKNVLVVSVVTPGCNQLPTLESVENYTLTINDDQCLLLSETVWGALRGLE
TFSQLVWKSAEGTFFINKTEIEDFPRFPHRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDDPS
FPYESFTFPELMRKGSYNPVTHIYTAQDVKEVIEYARLRGIRVLAEFDTPGHTLSWGPGIPGLLTPCYSG
SEPSGTFGPVNPSLNNTYEFMSTFFLEVSSVFPDFYLHLGGDEVDFTCWKSNPEIQDFMRKKGFGEDFKQ
LESFYIQTLLDIVSSYGKGYVVWQEVFDNKVKIQPDTIIQVWREDIPVNYMKELELVTKAGFRALLSAPW
YLNRISYGPDWKDFYIVEPLAFEGTPEQKALVIGGEACMWGEYVDNTNLVPRLWPRAGAVAERLWSNKLT
SDLTFAYERLSHFRCELLRRGVQAQPLNVGFCEQEFEQT
2. Report how far back evolutionarily you can find homologs for your
protein.
Could not find this.
2. List each of your conserved domains and give a brief explanation of the
structure and function of these domains. Where are they located in the
protein sequence molecule? (estimate the aa region using linear map of the
conserved domains). If there are no conserved domains state that as well.
GH-20 HexA hexb like- Catalyze removal of beta-1, results in lipid storage disorders
and mutations cause deficiency in Hex A enzyme resulting in Tay-sachs.
GH-20-hexosaminidase, GH-20-chitobiase-like-1, GH-20-sphex-like, GH-20-DspBLnbB-like, GH-20-Sm-chitobiase-like, GH-20- GcnA-like, Glyco-hydro-20, GH20hexosaminidase superfamily.
cd06562, GH20_HexA_HexB-like, Beta-N-acetylhexosaminidases catalyze the removal of
beta-1,4-linked N-acetyl-D-...
119332
no
8e-156
Beta-N-acetylhexosaminidases catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine residues from the
non-reducing ends of N-acetyl-beta-D-hexosaminides including N-acetylglucosides and N-acetylgalactosides. The
hexA and hexB genes encode the alpha- and beta-subunits of the two major beta-N-acetylhexosaminidase
isoenzymes, N-acetyl-beta-D-hexosaminidase A (HexA) and beta-N-acetylhexosaminidase B (HexB). Both the alpha
and the beta catalytic subunits have a TIM-barrel fold and belong to the glycosyl hydrolase family 20 (GH20). The
HexA enzyme is a heterodimer containing one alpha and one beta subunit while the HexB enzyme is a homodimer
containing two beta-subunits. Hexosaminidase mutations cause an inability to properly hydrolyze certain
sphingolipids which accumulate in lysosomes within the brain, resulting in the lipid storage disorders Tay-Sachs
and Sandhoff. Mutations in the alpha subunit cause in a deficiency in the HexA enzyme and result in Tay-Sachs,
mutations in the beta-subunit cause in a deficiency in both HexA and HexB enzymes and result in Sandhoff
disease. In both disorders GM(2) gangliosides accumulate in lysosomes. The GH20 hexosaminidases are thought to
act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by
the substrate itself.
Cd Length: 348 Bit Score: 545.66 E-value: 8e-156
10
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....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 167
FPHRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKGSYNPvTHIYTAQDVKEVI
EYA 246
Cdd|cd06562
1
FPHRGLLLDTSRHFLSVDSIKRTIDAMAYNKLNVLHWHITDSQSFPLESPSYPELSKKGAYSPSEVYTPEDVKEIVEYA 79
90
100
110
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160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 247 RLRGIRVLAEFDTPGHTLSWGPGIPGLLTPCYSGSE--PSGTFGPVNPSLNNTYEFMSTFFLEVSSVFPDFYLHLGGDE 323
Cdd|cd06562
80
RLRGIRVIPEIDTPGHTGSWGQGYPELLTGCYAVWRkycPEPPCGQLNPTNPKTYDFLKTLFKEVSELFPDKYFHLG
GDE 159
170
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....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 324 VDFTCWKSNPEIQDFMRKKGfGEDFKQLESFYIQTLLDIVSSYGKGYVVWQEVFDNKVKIQPDTIIQVWREDIpvnymk 402
Cdd|cd06562 160 VNFNCWNSNPEIQKFMKKNNGTDYSDLESYFIQRALDIVRSLGKTPIVWEEVFDNGVyLLPKDTIVQVWGGSD------ 232
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....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 403 ELELVTKAGFRALLSA--PWYLNRISYG----PDWKDFYIVEPLAFEGTPEQKALVIGGEACMWGEYVDNTNLVPRLWP 475
Cdd|cd06562 233
ELKNVLAAGYKVILSSydFWYLDCGFGGwvgpgNDWCDPYKNWPRIYSGTPEQKKLVLGGEACMWGEQVDDTNLDQR
LWP 312
330
340
350
....*....|....*....|....*....|....*.
gi 189181666 476 RAGAVAERLWSNKLTSDLTFAYERLSHFRCELLRRG 511
Cdd|cd06562 313 RASALAERLWSGPSDTNLTDAEPRLVEFRCRLVRRG 348
119331
cd02742, GH20_hexosaminidase, Beta-N-acetylhexosaminidases of glycosyl hydrolase
no 4e-110
family 20 (GH20) catalyze the...
Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) catalyze the removal of beta-1,4-linked Nacetyl-D-hexosamine residues from the non-reducing ends of N-acetyl-beta-D-hexosaminides including Nacetylglucosides and N-acetylgalactosides. These enzymes are broadly distributed in microorganisms, plants and
animals, and play roles in various key physiological and pathological processes. These processes include cell
structural integrity, energy storage, cellular signaling, fertilization, pathogen defense, viral penetration, the
development of carcinomas, inflammatory events and lysosomal storage disorders. The GH20 enzymes include the
eukaryotic beta-N-acetylhexosaminidases A and B, the bacterial chitobiases, dispersin B, and lacto-N-biosidase.
The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not
provided by the solvent or the enzyme, but by the substrate itself.
Cd Length: 303 Bit Score: 393.72 E-value: 4e-110
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....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 169 HRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKG--SYNPVTHIYTAQDVKEVIEY 245
Cdd|cd02742
1
IRGIMLDVSRHFLSVESIKRTIDVLARYKINTFHWHLTDDQAWRIESKKFPELAEKGgqiNPRSPGGFYTYAQLKDI
IEY 80
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120
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160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 246
ARLRGIRVLAEFDTPGHTLSWGPGIPGLLTPCYSGSEPSGTFGPVNPSLNNTYEFMSTFFLEVSSVFPDFYLHLGGD
EVD 325
Cdd|cd02742
81
AAARGIEVIPEIDMPGHSTAFVKSFPKLLTECYAGLKLRDVFDPLDPTLPKGYDFLDDLFGEIAELFPDRYLHIGGD
EAH 160
170
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230
240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 326
FTcwksnpeiqdfmrkkgfgEDFKQLESFYIQTLLDIVSSYGKGYVVWQEVFDNKVKIQPDTIIQVWREDIPvNYMK
ELE 405
Cdd|cd02742 161 FK-----------------QDRKHLMSQFIQRVLDIVKKKGKKVIVWQDGFDKKMKLKEDVIVQYWDYDGD-KYNVELP 221
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....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 406 LVTKAGFRALLSAPWYLNRISYGPDWKDFYIVEPLAFEgTPEQKALVIGGEACMWGEYVDNT-NLVPRLWPRAGAVAER 483
Cdd|cd02742 222 EAAAKGFPVILSNGYYLDIfIDGALDARKVYKNDPLAVPTPQQKDLVLGVIACLWGETVKDTkTLQYRFWPRALAVAER 300
...
gi 189181666 484 LWS 486
Cdd|cd02742 301 SWS 303
cd06570, GH20_chitobiase-like_1, A functionally uncharacterized subgroup of the Glycosyl 119338
no 2e-74
hydrolase family 20 (GH20)...
A functionally uncharacterized subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in
proteins similar to the chitobiase of Serratia marcescens, a beta-N-1,4-acetylhexosaminidase that hydrolyzes the
beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a
chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and
chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This subgroup lacks the C-terminal
PKD (polycystic kidney disease I)-like domain found in the chitobiases. The GH20 hexosaminidases are thought to
act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by
the substrate itself.
Cd Length: 311 Bit Score: 274.67 E-value: 2e-74
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....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 167
FPHRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKGSYNpvtHIYTAQDVKEVI
EYA 246
Cdd|cd06570
1
FPWRGLLIDVSRHFIPVAVIKRQLDAMASVKLNVFHWHLTDDQGFRIESKKYPKLQQKASDG--LYYTQEQIREVVAYA 77
90
100
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....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 247 RLRGIRVLAEFDTPGHTLSWGPGIPGLLT-PCYSGSEPS-GTFGPVNPSLNNTYEFMSTFFLEVSSVFPDFYLHLGGDE 323
Cdd|cd06570
78
RDRGIRVVPEIDVPGHASAIAVAYPELASgPGPYVIERGwGVFEPLlDPTNEETYTFLDNLFGEMAELFPDEYFHIG
GDE 157
170
180
190
200
210
220
230
240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 324
VDFTCWKSNPEIQDFMRKKGFgEDFKQLESFYIQTLLDIVSSYGKGYVVWQEVFdnkvkiQPD---TIIQVWREDipvn 399
Cdd|cd06570 158 VDPKQWNENPRIQAFMKEHGL-KDAAALQAYFNQRVEKILSKHGKKMIGWDEVL-----HPDlpknVVIQSWRGH---- 226
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....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 400 ymKELELVTKAGFRALLSAPWYLNRisygPDW-
KDFYIVEPlafegtpeqkaLVIGGEACMWGEYVDNTNLVPRLWPRAG 478
Cdd|cd06570 227 --DSLGEAAKAGYQGILSTGYYIDQ----PQPaAYHYRVDP----------MILGGEATMWAELVSEETIDSRLWPRTA 289
330
340
....*....|....*....|..
gi 189181666 479 AVAERLWSNKLTSDLTFAYERL 500
Cdd|cd06570 290 AIAERLWSAQDVRDEDDMYRRL 311
119333
cd06563, GH20_chitobiase-like, The chitobiase of Serratia marcescens is a beta-N-1,4no 1e-65
acetylhexosaminidase with a...
The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20
(GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded
by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetylD-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This GH20
domain family includes an N-acetylglucosamidase (GlcNAcase A) from Pseudoalteromonas piscicida and an Nacetylhexosaminidase (SpHex) from Streptomyces plicatus. SpHex lacks the C-terminal PKD (polycystic kidney
disease I)-like domain found in the chitobiases. The GH20 hexosaminidases are thought to act via a catalytic
mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
Cd Length: 357 Bit Score: 245.95 E-value: 1e-65
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..|
gi 189181666 167
FPHRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKGSYNPVTHI------------ 233
Cdd|cd06563
1
FSWRGLMLDVSRHFFPVDEVKRFIDLMALYKLNVFHWHLTDDQGWRIEIKKYPKLTEVGAWRGPTEIglpqgggdgt
pyg 80
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....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 234 --YTAQDVKEVIEYARLRGIRVLAEFDTPGHTLSWGPGIPGLLTPCYSGSEPSGTFG--PVNPSLNNTYEFMSTFFLEV 308
Cdd|cd06563
81
gfYTQEEIREIVAYAAERGITVIPEIDMPGHALAALAAYPELGCTGGPGSVVSVQGVvsnVLCPGKPETYTFLEDVL
DEV 160
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....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 309
SSVFPDFYLHLGGDEVDFTCWKSNPEIQDFMRKKGFgEDFKQLESFYIQTLLDIVSSYGKGYVVWQEVfdNKVKIQP
DTI 388
Cdd|cd06563 161 AELFPSPYIHIGGDEVPKGQWEKSPACQARMKEEGLKDEHELQSYFIKRVEKILASKGKKMIGWDEI--LEGGLPPNAT 237
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....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 389 IQVWREDipvnymKELELVTKAGFRALLS--APWYLNR-ISYGPDW---------KDFYIVEPLAFEGTPEQKALVIGG 455
Cdd|cd06563 238 VMSWRGE-----DGGIKAAKQGYDVIMSpgQYLYLDYaQSKGPDEpaswagfntlEKVYSFEPVPGGLTPEQAKRILGV 311
330
340
350
360
....*....|....*....|....*....|....*....|....*.
gi 189181666 456 EACMWGEYVDNTNLVPR-LWPRAGAVAERLWSNKLTSDLTFAYERL 500
Cdd|cd06563 312 QANLWTEYIPTPERVEYmAFPRLLALAEVAWTPPEKKDWEDFRKRL 357
119336
cd06568, GH20_SpHex_like, A subgroup of the Glycosyl hydrolase family 20 (GH20)
no 2e-37
catalytic domain found in...
A subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the Nacetylhexosaminidase from Streptomyces plicatus (SpHex). SpHex catalyzes the hydrolysis of N-acetyl-betahexosaminides. An Asp residue within the active site plays a critical role in substrate-assisted catalysis by orienting
the 2-acetamido group and stabilizing the transition state. The GH20 hexosaminidases are thought to act via a
catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the
substrate itself. Proteins belonging to this subgroup lack the C-terminal PKD (polycystic kidney disease I)-like
domain found in the chitobiases.
Cd Length: 329 Bit Score: 152.10 E-value: 2e-37
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..|
gi 189181666 167
FPHRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKGSYNPV---THIYTAQDVKEV 242
Cdd|cd06568
1
FAYRGLMLDVARHFFTVAEVKRYIDLLALYKLNVLHLHLTDDQGWRIEIKSWPKLTEIGGSTEVgggpGGYYTQEDY
KDI 80
90
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120
130
140
150
160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 243 IEYARLRGIRVLAEFDTPGHTLSWGPGIPGL----LTPCYSGSEPSgtFGPVNPSLNNTYEFMSTFFLEVSSVFPDFYL 317
Cdd|cd06568
81 VAYAAERHITVVPEIDMPGHTNAALAAYPELncdgkAKPLYTGIEVG-FSSLDVDKPTTYEFVDDVFRELAALTPGPYI 158
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....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 318
HLGGDEVDFTcwksnPEiqdfmrkkgfgEDFKqlesFYIQTLLDIVSSYGKGYVVWQEVfdNKVKIQPDTIIQVWRE
DIP 397
Cdd|cd06568 159 HIGGDEAHST-----PH-----------DDYA----YFVNRVRAIVAKYGKTPVGWQEI-ARADLPAGTVAQYWSDRAP 216
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....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 398 vnyMKELELVTKAGFRALLS--APWYLNR----------ISYGP-DWKDFYIVEPLAFE-
GTPEQkaLVIGGEACMWGEY 463
Cdd|cd06568 217 --DADAAAALDKGAKVILSpaDKAYLDMkydadsplglTWAGPvEVREAYDWDPAAYGpGVPDE--AILGVEAPLWTET
291
330
340
350
....*....|....*....|....*....|
gi 189181666 464 VDNT-NLVPRLWPRAGAVAERLWSNKLTSD 492
Cdd|cd06568 292 IRNLdDLEYMAFPRLAGVAEIGWSPQEARD 321
cd06564, GH20_DspB_LnbB-like, Glycosyl hydrolase family 20 (GH20) catalytic domain of 119334
yes 2e-22
dispersin B (DspB), lacto-N-...
Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and related
proteins. Dispersin B is a soluble beta-N-acetylglucosamidase found in bacteria that hydrolyzes the beta-1,6linkages of PGA (poly-beta-(1,6)-N-acetylglucosamine), a major component of the extracellular polysaccharide
matrix. Lacto-N-biosidase hydrolyzes lacto-N-biose (LNB) type I oligosaccharides at the nonreducing terminus to
produce lacto-N-biose as part of the GNB/LNB (galacto-N-biose/lacto-N-biose I) degradation pathway. The lacto-Nbiosidase from Bifidobacterium bifidum has this GH20 domain, a carbohydrate binding module 32, and a bacterial
immunoglobulin-like domain 2, as well as a YSIRK signal peptide and a G5 membrane anchor at the N and C
termini, respectively. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the
catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
Cd Length: 326 Bit Score: 102.75 E-value: 2e-22
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..|
gi 189181666 168 PHRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHL------VDDPSFPYESFTFPELMRKGSYNPVTHI-----YT 235
Cdd|cd06564
1
EVRGFMLDVGRKYYSMDFLKDIIKTMSWYKMNDLQLHLndnlifnLDDMSTTVNNATYASDDVKSGNNYYNLTandg
yYT 80
90
100
110
120
130
140
150
160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 236
AQDVKEVIEYARLRGIRVLAEFDTPGHTLSWGPGIPGLLTPCYSGSEPSGTFGPVNPSlnnTYEFMSTFFLEVSSVF
PDF 315
Cdd|cd06564
81 KEEFKELIAYAKDRGVNIIPEIDSPGHSLAFTKAMPELGLKNPFSKYDKDTLDISNPE--AVKFVKALFDEYLDGFNPK 157
170
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....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 316 -YLHLGGDEvdftcwksnpeiqdFMRKKGFGEDFKQlesfYIQTLLDIVSSYGKGYVVWQ--EVFDNKVKIQPDTIIQ 390
Cdd|cd06564 158 sdTVHIGADE--------------YAGDAGYAEAFRA---YVNDLAKYVKDKGKTPRVWGdgiYYKGDTTVLSKDVIIN 219
250
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....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 391 VWREDipvnYMKELELVTKaGFRaLLSAP--WY---LNRISYGPDWKDFYI--VEPLAFEGT----PEQKALVIGGEAC 458
Cdd|cd06564 220 YWSYG----WADPKELLNK-GYKIINTNdgYLyivPGAGYYGDYLNTEDIynnWTPNKFGGTnatlPEGDPQILGGMFA 293
330
340
350
....*....|....*....|....*....|.
gi 189181666 459 MWGEYVDNT----NLVPRLWPRAGAVAERLW 485
Cdd|cd06564 294 IWNDDSDAGisevDIYDRIFPALPAFAEKTW 324
cd06569, GH20_Sm-chitobiase-like, The chitobiase of Serratia marcescens is a beta-N-1,4- 119337
no 1e-21
acetylhexosaminidase with a...
The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20
(GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded
by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetylD-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. The GH20
hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by
solvent or the enzyme, but by the substrate itself.
Cd Length: 445 Bit Score: 99.67 E-value: 1e-21
10
70
80
20
30
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50
60
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 163
DFPRFPHRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKGSY-------------- 227
Cdd|cd06569
1
DAPRFEYRGMHLDVARNFHSKETVLKLLDQMAAYKLNKLHLHLTDDEGWRLEIPGLPELTEVGAKrchdlsettcll
pql 80
90
100
110
120
....*....|....*....|....*....|....*....|..
gi 189181666 228 -------NPVTHIYTAQDVKEVIEYARLRGIRVLAEFDTPGH 262
Cdd|cd06569
81 gsgpdtnNSGSGYYSRADYIEILKYAKARHIEVIPEIDMPGH 122
119335
cd06565, GH20_GcnA-like, Glycosyl hydrolase family 20 (GH20) catalytic domain of Nno 7e-11
acetyl-beta-D-glucosaminidase...
Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, also known as
BhsA) and related proteins. GcnA is an exoglucosidase which cleaves N-acetyl-beta-D-galactosamine (NAG) and Nacetyl-beta-D-galactosamine residues from 4-methylumbelliferylated (4MU) substrates, as well as cleaving NAG
from chito-oligosaccharides (i.e. NAG polymers). In contrast, sulfated forms of the substrate are unable to be
cleaved and act instead as mild competitive inhibitors. Additionally, the enzyme is known to be poisoned by
several first-row transition metals as well as by mercury. GcnA forms a homodimer with subunits comprised of
three domains, an N-terminal zincin-like domain, this central catalytic GH20 domain, and a C-terminal alpha helical
domain. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile
is not provided by solvent or the enzyme, but by the substrate itself.
Cd Length: 301 Bit Score: 64.15 E-value: 7e-11
10
70
80
20
30
40
50
60
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 169 HRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDdpSFPYESFtfPELMRkgSYNPvthiYTAQDVKEVIEYAR 247
Cdd|cd06565
1 FRGVHLDLKRNAVPkVSYLKKLLRLLALLGANGLLLYYED--TFPYEGE--PEVGR-MRGA----YTKEEIREIDDYAA 70
90
100
110
120
130
140
150
160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 248 LRGIRVLAEFDTPGHT---LSWGPgipglltpcYSG---SEPSGTFgpvNPSLNNTYEFMSTFFLEVSSVFPDFYLHLG 320
Cdd|cd06565
71 ELGIEVIPLIQTLGHLefiLKHPE---------FRHlrevDDPPQTL--CPGEPKTYDFIEEMIRQVLELHPSKYIHIG 138
170
180
190
200
210
220
230
240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 321 GDEVdftcwksnpeiQDFMR---KKGFGEDFKQLESFYIQTLLDIVSSYGKGYVVWQEVFdNKVKIQPDTIIQVWREDI 396
Cdd|cd06565 139 MDEA----------YDLGRgrslRKHGNLGRGELYLEHLKKVLKIIKKRGPKPMMWDDML-RKLSIEPEALSGLPKLVT 206
...
gi 189181666 397 PVN 399
Cdd|cd06565 207 PVV 209
cd06569, GH20_Sm-chitobiase-like, The chitobiase of Serratia marcescens is a beta-N-1,4- 119337
no 7e-08
acetylhexosaminidase with a...
The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20
(GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded
by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetylD-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. The GH20
hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by
solvent or the enzyme, but by the substrate itself.
Cd Length: 445 Bit Score: 53.83 E-value: 7e-08
10
70
80
20
30
40
50
60
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 290 VNPSLNNTYEFMSTFFLEVSSVFPDFY-----LHLGGDEVDFTCWKSNPEIQDFMRKKGFGEDFKQLESFYIQTLLDIV 363
Cdd|cd06569 171
INPCMPSTYRFVDKVIDEIARMHQEAGqplttIHFGGDEVPEGAWGGSPACKAqLFAKEGSVKDVEDLKDYFFERVS
KIL 250
90
100
110
120
130
140
150
160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 364 SSYGKGYVVWQEVFDNKVKIQPDTI------IQVWRedipVNYMKELELVTK--AGFRALLSAPWYL------------ 422
Cdd|cd06569 251 KAHGITLAGWEDGLLGKDTTNVDGFatpyvwNNVWG---WGYWGGEDRAYKlanKGYDVVLSNATNLyfdfpyekhpee 326
170
180
190
200
210
220
230
240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 423 ------NRI-------SYGPD--------WKDFYIVEPLAFEG---TPEQKALVIGGEACMWGEYVDNTNLVPRL-WPR 476
Cdd|cd06569 327
rgyywaGRFvdtkkvfSFMPDnlyanaevTRDGDPIDDTALNGkvrlTLEGPKNILGLQGQLWSETIRTDEQLEYMv
FPR 406
....*....
gi 189181666 477 AGAVAERLW 485
Cdd|cd06569 407 LLALAERAW 415
pfam00728, Glyco_hydro_20, Glycosyl hydrolase family 20, catalytic domain
Glycosyl hydrolase family 20, catalytic domain
Cd Length: 335 Bit Score: 317.37 E-value: 3e-87
10
60
70
80
20
30
144359
40
no
3e-87
50
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 167
FPHRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKGSYNPVThIYTAQDVKEVI
EYA 246
Cdd|pfam00728
1
FPYRGLMLDVARHFFSVDTIKRLIDAMAFYKLNVLHWHLTDDQGWRLEIKAYPELTEVGAYRGSDFYTQEDIREIVAYA 79
90
100
110
120
130
140
150
160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 247 RLRGIRVLAEFDTPGHTLSWGPGIPGLLTPCYSGS-EPSGTFGP---VNPSLNNTYEFMSTFFLEVSSVFPDFYLHLGG 321
Cdd|pfam00728 80
AARGIEVIPEIDMPGHARAALKAYPELGCKPEDTSwYVSVQVGPpngtLNPGNPKTYDFLDKVLDEVAELFPSEYIH
IGG 159
170
180
190
200
210
220
230
240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 322
DEVDFTCWKSNPEIQDFMRKKGFGEDfkqLESFYIQTLLDIVSSYGKGYVVWQEVFDNKVKIQPDTIIQVWRedipvNY 400
Cdd|pfam00728 160 DEVNKGCWLKSPKCQAFMKQEGLKSE--LQSYFIKRVVKIVKKRGKKPIGWEEILTGGGtLLPPDTTVQSWR-----NG 231
250
260
270
280
290
300
310
320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 401 MKELELVTKAGFRALLSAP--WYL------NRISYGPDW-----KDFYIVEPLAFEGT-PEQKALVIGGEACMWGEYV- 464
Cdd|pfam00728 232
GAQARQAANQGYKVILSPGdfLYLdhgygkWPTERGYYWagfmplKKFYAWEPPYDTWGaPLEAGNVLGGEAALWGE
YIr 311
330
340
....*....|....*....|....
gi 189181666 465 DNTNLVPRLWPRAGAVAERLWSNK 488
Cdd|pfam00728 312 DPENLEYMVFPRLAALAERAWSPP 335
pfam02838, Glyco_hydro_20b, Glycosyl hydrolase family 20, domain 2
Glycosyl hydrolase family 20, domain 2
Cd Length: 131 Bit Score: 180.30 E-value: 8e-46
10
60
70
80
20
30
111707
40
no
8e-46
50
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666
35
QRYVLYPNNFQFQYDVSSAAQPGCSVLDEAFQRYRDLLFGSGSWPRPYLTGKRHTLEKNVLVVSVVTPGCNQLPTLE
SVE 114
Cdd|pfam02838
1
QLIHLAPGNFVITHSLPSPAQTSCSLLKVAFARYINLIFGFKAWQFPSVNFRAETVIKSVLVPVVVTSPCDSLQSLG
SDE 80
90
100
110
120
130
....*....|....*....|....*....|....*....|....*....|.
gi 189181666 115 NYTLTINDDQCLLLSETVWGALRGLETFSQLVWKSAEGTFFINKTEIEDFP 165
Cdd|pfam02838 81 SYTLSIKSDGIVIKANTVWGALRGLETLSQLIVYDSEGTFVINQVSISDSP 131
COG3525, Chb, N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism] 33328
yes 2e-44
N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism]
Cd Length: 732 Bit Score: 175.62 E-value: 2e-44
10
70
80
20
30
40
50
60
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 91 EKNVLVVSVVTPGCNQLPTLESVENYTLTINDDQCLLLSETVWGALRGLETFSQLV-WKSAEGTFFINKTEIEDFPRFP 168
Cdd|COG3525 183
EKGLSPLQADKYYPNRKGPTLGEEAYRLAINDKAIKVTAHDLAGLFYADGTLLQLDtsADSFQGDIRFPAVTIVDAP
RFA 262
90
100
110
120
130
140
150
160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 169 HRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKGSY--------------NPVTHI 233
Cdd|COG3525 263
WRGLLVDVARQFHSTDDVKRLIDQLAAHKLNVLHLHLTDDEGWRLEIKRYPKLTTIGAWripdepdlpqlgygpERM
GGF 342
170
180
190
200
210
220
230
240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 234 YTAQDVKEVIEYARLRGIRVLAEFDTPGHTLSWGPGIPGL-LTPCYSGSEPSGTFGP--VNPSLNNTYEFMSTFFLEVS 309
Cdd|COG3525 343
YTQDDIRELVAYASARQITVIPEIDMPGHARAAVVAYPDLnLGRADPDSYDSVQAYLnpvLNPTLDPTYQFLDKVLD
EVA 422
250
260
270
280
290
300
310
320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 310 SVFPDFYLHLGGDEVDFTCWKSNPEIQDFMRKKGFgEDFKQLESFYIQTLLDIVSSYGKGYVVWQEVFD----NKVKIQ 384
Cdd|COG3525 423 DLFPSTTIHIGGDEFIDGQWKaSSPLVQALMEKLGNKDTFELQSYFITQVGKTLASKGRRLIGWDEGAHggdvNGTALT 501
330
340
350
360
370
380
390
400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
..|
gi 189181666 385 PDTIIQVWRedipvNYMKELELVtKAGFRALLS-APWYLNRISYGPDW-------------KDFYIVEPLAFEGT-PEQ 448
Cdd|COG3525 502 ANVTVMSWY-----GKDKAIELAKQGYDVVLTpAQFVYLDMLQIAAPeepgyswatttpleRNKYAYDFAGKQPInDEL 575
410
420
430
440
450
....*....|....*....|....*....|....*....|....*....|....
gi 189181666 449 KALVIGGEACMWGEYVDN-TNLVPRLWPRAGAVAERLWSNKLTSDLTFAYERLS 501
Cdd|COG3525 576 AKRILGVQAALWSEHIQTrGRFEYMVFPRLAAAAERAWTPMAFNDWLYYLDRLS 629
Biology Workbench
Use Biology Workbench to:
Import the FASTA sequence into the Biology Workbench and search for similar proteins
using BLASTP.
Pick a diverse group of hits to perform a ClustalW alignment.
Do a multiple alignment and display the results with BOXSHADE. Do the conserved
areas of the protein align with certain domains? Yes
Display the evolutionary relationships in a rooted and unrooted tree.
 Download a PostScript version of the output
 Download a PostScript version of the output
Examine and compile all relevant information. Save all information which you think may
be useful for your presentation. (HINT: Are there mutations associated with your
disease found in conserved regions?)
Submit:
The BOXSHADE, DRAWTREE and DRAWGRAM images for your protein.