|
Name |
Accession |
Description |
Interval |
E-value |
| XynB_like |
cd01833 |
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ... |
33-229 |
8.14e-51 |
|
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted hydrolase with xylanase activity. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
Pssm-ID: 238871 Cd Length: 157 Bit Score: 174.35 E-value: 8.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 33 RIMALGDSITGSpgcwrallwkhlqetghtdidfvgtlpaqgcgftyDGENEGHGGFLATGIARDNQlpGWLSATHPDIV 112
Cdd:cd01833 2 RIMPLGDSITWG-----------------------------------DKDHEGHSGYLIDQIAAAAA--DWVLAAKPDVV 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 113 LMHLGTNDVWNNIPASTILDAFTTLLGQMRAANPATKLIVAKIIPMNPANCTacgQRVVDLNNAIPGWAQAHSTAASPIT 192
Cdd:cd01833 45 LLHLGTNDLVLNRDPDTAPDRLRALIDQMRAANPDVKIIVATLIPTTDASGN---ARIAEYNAAIPGVVADLRTAGSPVV 121
|
170 180 190
....*....|....*....|....*....|....*..
gi 502994194 193 VVDQWTGFDTAADTGDGVHPNGtTGIQKMESRWYPAL 229
Cdd:cd01833 122 LVDMSTGYTTADDLYDGLHPND-QGYKKMADAWYEAL 157
|
|
| Cellulase |
pfam00150 |
Cellulase (glycosyl hydrolase family 5); |
251-499 |
4.39e-38 |
|
Cellulase (glycosyl hydrolase family 5);
Pssm-ID: 395098 [Multi-domain] Cd Length: 272 Bit Score: 142.90 E-value: 4.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 251 LEANGSPFVMRGVNHAYVWYP---GQNRAFADIKSFGANTVRVVLGSGQ--------RWGPTSAAEVTSVIGQCKQNRLI 319
Cdd:pfam00150 1 VDANGKPVQLRGVTHGGQWGNpyvTTKAMIDLVKDWGFNVVRLPVSWGGyvpnnpdyLIDENWLNRVDEVVDYAIDNGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 320 CVLEVHDTTGYGE---QSGAATLDQAAGYWISVADALkGQENYVVINLGNEPFGNDQQ-VSATWTSATSNAIKRLRAAGL 395
Cdd:pfam00150 81 VIIDWHHDGGWPGdpnGNIDTAKAFFKKIWTQIATRY-GNNPNVIFELMNEPHGNDQAtWADDVKDYAQEAIDAIRAAGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 396 QHLLMADAPMWGQDwqnimrdNAGTVFNaDP--QHNTVFSIHMYG-------------VYDTAAEINAYFDAFRTAGLPL 460
Cdd:pfam00150 160 NNLIIVGGNSWSQN-------PDGAALN-DPndDDNLIYSVHFYApsdfsgtwfdcedPTNLAQRLRAAANWALDNGIPV 231
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 502994194 461 VVGEFGSMHTDGNPDE--DTIMAQAQARGLGYLGWSWSGNS 499
Cdd:pfam00150 232 FIGEFGGGNADGPCRDeaEKWLDYLKENGISWTGWSNGNKS 272
|
|
| BglC |
COG2730 |
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism]; |
261-510 |
3.27e-33 |
|
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];
Pssm-ID: 442036 [Multi-domain] Cd Length: 295 Bit Score: 129.78 E-value: 3.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 261 RGVN--------HAYVWYPGQNRAFADIKSFGANTVRV-----VLGSGQRWG---PTSAAEVTSVIGQCKQNRLICVLEV 324
Cdd:COG2730 8 RGVNlgnwlelwFETLWGNITEEDIDAIADWGFNTVRLpvsweRLQDPDNPYtldEAYLERVDEVVDWAKARGLYVILDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 325 HDTTGYGEQSGAATLDQAAGYWISVADALKGQENYVVINLGNEPFGNDqqvSATWTSATSNAIKRLRAAGLQHLLMADAP 404
Cdd:COG2730 88 HHAPGYQGWYDAATQERFIAFWRQLAERYKDYPNVLGFELLNEPHGAT---WADWNALAQRAIDAIRATNPDRLIIVEGN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 405 MWGQDWQNImrdnagtVFNADPQHNTVFSIHMYGVYD------------TAAEINAYFDAF----RTAGLPLVVGEFGSM 468
Cdd:COG2730 165 NWGGAHNLR-------ALDPLDDDNLVYSVHFYGPFVfthqgawfagptYPANLEARLDNWgdwaADNGVPVFVGEFGAY 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 502994194 469 HTDGNPDE----DTIMAQAQARGLGYLGWSWSGNSSDVAYLDMTNN 510
Cdd:COG2730 238 NDDPDASRlawlRDLLDYLEENGIGWTYWSFNPSGDTGGLLDRGTG 283
|
|
| TesA |
COG2755 |
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ... |
31-229 |
5.36e-29 |
|
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];
Pssm-ID: 442045 [Multi-domain] Cd Length: 191 Bit Score: 114.36 E-value: 5.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 31 PTRIMALGDSIT-----GSPGCWRALLWKHLQETghtDIDFVgtlpaqgcgftydgeNEGHGGFLATGIArdNQLPGWLS 105
Cdd:COG2755 8 PLRIVALGDSITagygaSRERGWPALLARRLAAA---DVRVV---------------NAGISGATTADLL--ARLDRDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 106 ATHPDIVLMHLGTNDVWNNI--PASTILDAFTTLLGQMRAANPATKLIVAKIIPMNPANCTAcgQRVVDLNNAIPGWAQA 183
Cdd:COG2755 68 ALKPDLVVIELGTNDLLRGLgvSPEEFRANLEALIDRLRAAGPGARVVLVTPPPRLRPNYLN--ERIEAYNAAIRELAAE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502994194 184 HStaaspITVVDQWTGFDTAAD-----TGDGVHPNgTTGIQKMESRWYPAL 229
Cdd:COG2755 146 YG-----VPLVDLYAALRDAGDlpdllTADGLHPN-AAGYRLIAEAVLPAL 190
|
|
| CBM_2 |
pfam00553 |
Cellulose binding domain; Two tryptophan residues are involved in cellulose binding. Cellulose ... |
650-752 |
7.91e-29 |
|
Cellulose binding domain; Two tryptophan residues are involved in cellulose binding. Cellulose binding domain found in bacteria.
Pssm-ID: 425748 [Multi-domain] Cd Length: 101 Bit Score: 110.62 E-value: 7.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 650 CKVAYAASN-WGggNGFTANVTITNTGTSAVTGWTLAFAFAGGQQVTlPGWGATFAQSGGAVTAKNLSWNGTLAPNASTG 728
Cdd:pfam00553 1 CTATYAVTNqWG--TGFTANVTITNTGSSPINGWTVSWTYPAGQRVT-QSWNATVSQSGNPVTATNVSWNGTIAPGGSAS 77
|
90 100
....*....|....*....|....
gi 502994194 729 IGFNGTFTGTNSAPSAFTLNGSSC 752
Cdd:pfam00553 78 FGFQGSGTGSNSAPTSFTVNGAAC 101
|
|
| CBD_II |
smart00637 |
CBD_II domain; |
657-751 |
4.30e-24 |
|
CBD_II domain;
Pssm-ID: 214754 [Multi-domain] Cd Length: 92 Bit Score: 96.71 E-value: 4.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 657 SNWGGGngFTANVTITNTGTSAVTGWTLAFAFAGGQQVTlPGWGATFAQSGGAVTAKNLSWNGTLAPNASTGIGFNGTfT 736
Cdd:smart00637 2 SDWGSG--FTANVTVTNTGSSAINGWTLTFDLPGGQTVT-NSWNATVSQSGGHVTATNASWNGTIAPGGSVSFGFQGK-T 77
|
90
....*....|....*
gi 502994194 737 GTNSAPSAFTLNGSS 751
Cdd:smart00637 78 GSSAAPTGFTLNGAA 92
|
|
| CelA1 |
COG5297 |
Cellulase/cellobiase CelA1 [Carbohydrate transport and metabolism]; |
471-755 |
1.01e-23 |
|
Cellulase/cellobiase CelA1 [Carbohydrate transport and metabolism];
Pssm-ID: 444099 [Multi-domain] Cd Length: 301 Bit Score: 102.20 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 471 DGNPDEDTIMAQAQARGLGYLGWSWSGNSSDVAYLDMTNNFDPASLTAWGERFLNGINGIRQTAKEATIYGGSQADTQAP 550
Cdd:COG5297 14 AGALAGSDGTGAAGSGSGGDVASGAASASGSASGSSASGAGAGAGAAASGADTGSGGGAGAGAGVGVGAGGAAGGAGGSA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 551 SVPGTPAVSGVTSSGATLSWAASTDNVGVTGYDVLRAPGASGGTFAVVGSTATTSYTDSGLTASSTY--------RYQVR 622
Cdd:COG5297 94 GVAGAASAAGAAGAAATSSGATSSSSSGTSSGGGGGSSSSTSDTTTSSATSGSSTSTSSPTTGSTSTttgggianQPTAV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 623 ARDAAGNTSAGSGVATATTSAGGGSGACKVAYAA-SNWGGGngFTANVTITNTGTSAVTGWTLAFAFAGGQQVTlPGWGA 701
Cdd:COG5297 174 WDRIAAITATVRAHLDAALAAPLPGRDCGVTYSVySDWGSG--YTAAVTVTNPGSLPLNGWTLAWDLPGGAGVT-NAWGF 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 502994194 702 TFAQSGGAVTAKNLSWNGTLAPNASTGIGFNGTFTGTNsaPSAFTLNGsSCTAA 755
Cdd:COG5297 251 TLNQSGYTVTATNVSWNGTLAPGGSVSFGFDTSRNGWN--PSGRGLDG-ACTGG 301
|
|
| Lipase_GDSL_2 |
pfam13472 |
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ... |
36-213 |
2.20e-16 |
|
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are similar to pfam00657.
Pssm-ID: 463889 Cd Length: 176 Bit Score: 77.59 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 36 ALGDSIT------GSPGCWRALLWKHLQETGHTDIDfvgtlpaqgcgftydgENEGHGGflATGIARDNQLPGWLSATHP 109
Cdd:pfam13472 1 ALGDSITagygatGGDRSYPGWLARLLARRLGADVV----------------NNLGISG--ATTRLDLLERLDDVLRLKP 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 110 DIVLMHLGTNDVWNNIPASTILDAFTTLLGQMRAANPATKLIVAKIIPMNP---ANCTACGQRVVDLNNAIPGWAQAHSt 186
Cdd:pfam13472 63 DLVVILLGTNDLGRGVSAARAAANLEALIDALRAAGPDARVLLIGPLPVGPpppLDERRLNARIAEYNAAIREVAAERG- 141
|
170 180 190
....*....|....*....|....*....|...
gi 502994194 187 aaspITVVDQWTGFDTAAD------TGDGVHPN 213
Cdd:pfam13472 142 ----VPYVDLWDALRDDGGwlpdllADDGLHPN 170
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
550-641 |
2.43e-11 |
|
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.
Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 60.59 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 550 PSVPGTPAVSGVTSSGATLSWAASTDNVG-VTGYDV-LRAPGASGGTFAVVGSTATTSYTDSGLTASSTYRYQVRARDAA 627
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGpITGYVVeYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
|
90
....*....|....
gi 502994194 628 GnTSAGSGVATATT 641
Cdd:cd00063 81 G-ESPPSESVTVTT 93
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
550-628 |
5.57e-10 |
|
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.
Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 56.47 E-value: 5.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 550 PSVPGTPAVSGVTSSGATLSWAASTDNVG---VTGYDVLRAPGASGGTfAVVGSTATTSYTDSGLTASSTYRYQVRARDA 626
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItgyIVGYRVEYREEGSEWK-EVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79
|
..
gi 502994194 627 AG 628
Cdd:smart00060 80 AG 81
|
|
| COG4733 |
COG4733 |
Phage-related protein, tail protein J [Mobilome: prophages, transposons]; |
556-751 |
1.73e-07 |
|
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
Pssm-ID: 443767 [Multi-domain] Cd Length: 978 Bit Score: 54.95 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 556 PAVSGVTSS----GATLSWAASTDnVGVTGYDVLRAPGASGGTFAVVGS-TATTSYTDSGLTASSTYRYQVRARDAAGNT 630
Cdd:COG4733 631 PAPTGLTATgglgGITLSWSFPVD-ADTLRTEIRYSTTGDWASATVAQAlYPGNTYTLAGLKAGQTYYYRARAVDRSGNV 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 631 SAGSGVATATTSAGGGSGACKVAYAASNWGGGNGFTANVTITNTGTSAVTGWTLAFAFAGGQQVTLPGW--GATFAQSGG 708
Cdd:COG4733 710 SAWWVSGQASADAAGILDAITGQILETELGQELDAIIQNATVAEVVAATVTDVTAQIDTAVLFAGVATAaaIGAEARVAA 789
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502994194 709 AVTAKNLSWNGTLAPNASTGIGFNGTFTGTNSAPSAFTLNGSS 751
Cdd:COG4733 790 TVAESATAAAATGTAADAAGDASGGVTAGTSGTTGAGDTAAST 832
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
551-629 |
1.80e-07 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 49.34 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 551 SVPGTPAVSGVTSSGATLSWAASTDNVG-VTGYDV-LRAPGASGGTFAVVGSTATTSYTDSGLTASSTYRYQVRARDAAG 628
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGpITGYEVeYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80
|
.
gi 502994194 629 N 629
Cdd:pfam00041 81 E 81
|
|
| PRK12688 |
PRK12688 |
flagellin; Reviewed |
600-734 |
9.06e-03 |
|
flagellin; Reviewed
Pssm-ID: 171664 [Multi-domain] Cd Length: 751 Bit Score: 39.48 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 600 STATTSYTDSGLTASSTYRYQVRARDAAGNTSAGSGVATATTSAGGGSGACKVAYAASNWGGGNGFTANVTITNTGTSAV 679
Cdd:PRK12688 112 STTISGATADDLRGTTSYASATASSNVLYDGAAGGATAATGATTLGGTAGSLAGTGATAGDGTTALTGTITLIATNGTTA 191
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 502994194 680 TGWTLAFAFAGGQQVTLPGWGATFAqSGGAVTAKNLSWNGTLAPNASTGIGFNGT 734
Cdd:PRK12688 192 TGLLGNAQPADGDTLTVNGKTITFR-SGAAPASTAVPSGSGVSGNLVTDGNGNST 245
|
|
| PRK10528 |
PRK10528 |
multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1; Provisional |
91-213 |
9.56e-03 |
|
multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1; Provisional
Pssm-ID: 182521 Cd Length: 191 Bit Score: 38.21 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 91 ATGIARdnqLPGWLSATHPDIVLMHLGTNDVWNNIPASTILDAFTTLLGQMRAANPATKLIVAKIipmnPANctaCGQRV 170
Cdd:PRK10528 57 QQGLAR---LPALLKQHQPRWVLVELGGNDGLRGFPPQQTEQTLRQIIQDVKAANAQPLLMQIRL----PAN---YGRRY 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 502994194 171 VDLNNAI-PGWAQAHSTAASP-----ITVVDQWTgfdtaadTGDGVHPN 213
Cdd:PRK10528 127 NEAFSAIyPKLAKEFDIPLLPffmeeVYLKPQWM-------QDDGIHPN 168
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| XynB_like |
cd01833 |
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ... |
33-229 |
8.14e-51 |
|
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted hydrolase with xylanase activity. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
Pssm-ID: 238871 Cd Length: 157 Bit Score: 174.35 E-value: 8.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 33 RIMALGDSITGSpgcwrallwkhlqetghtdidfvgtlpaqgcgftyDGENEGHGGFLATGIARDNQlpGWLSATHPDIV 112
Cdd:cd01833 2 RIMPLGDSITWG-----------------------------------DKDHEGHSGYLIDQIAAAAA--DWVLAAKPDVV 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 113 LMHLGTNDVWNNIPASTILDAFTTLLGQMRAANPATKLIVAKIIPMNPANCTacgQRVVDLNNAIPGWAQAHSTAASPIT 192
Cdd:cd01833 45 LLHLGTNDLVLNRDPDTAPDRLRALIDQMRAANPDVKIIVATLIPTTDASGN---ARIAEYNAAIPGVVADLRTAGSPVV 121
|
170 180 190
....*....|....*....|....*....|....*..
gi 502994194 193 VVDQWTGFDTAADTGDGVHPNGtTGIQKMESRWYPAL 229
Cdd:cd01833 122 LVDMSTGYTTADDLYDGLHPND-QGYKKMADAWYEAL 157
|
|
| Cellulase |
pfam00150 |
Cellulase (glycosyl hydrolase family 5); |
251-499 |
4.39e-38 |
|
Cellulase (glycosyl hydrolase family 5);
Pssm-ID: 395098 [Multi-domain] Cd Length: 272 Bit Score: 142.90 E-value: 4.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 251 LEANGSPFVMRGVNHAYVWYP---GQNRAFADIKSFGANTVRVVLGSGQ--------RWGPTSAAEVTSVIGQCKQNRLI 319
Cdd:pfam00150 1 VDANGKPVQLRGVTHGGQWGNpyvTTKAMIDLVKDWGFNVVRLPVSWGGyvpnnpdyLIDENWLNRVDEVVDYAIDNGMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 320 CVLEVHDTTGYGE---QSGAATLDQAAGYWISVADALkGQENYVVINLGNEPFGNDQQ-VSATWTSATSNAIKRLRAAGL 395
Cdd:pfam00150 81 VIIDWHHDGGWPGdpnGNIDTAKAFFKKIWTQIATRY-GNNPNVIFELMNEPHGNDQAtWADDVKDYAQEAIDAIRAAGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 396 QHLLMADAPMWGQDwqnimrdNAGTVFNaDP--QHNTVFSIHMYG-------------VYDTAAEINAYFDAFRTAGLPL 460
Cdd:pfam00150 160 NNLIIVGGNSWSQN-------PDGAALN-DPndDDNLIYSVHFYApsdfsgtwfdcedPTNLAQRLRAAANWALDNGIPV 231
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 502994194 461 VVGEFGSMHTDGNPDE--DTIMAQAQARGLGYLGWSWSGNS 499
Cdd:pfam00150 232 FIGEFGGGNADGPCRDeaEKWLDYLKENGISWTGWSNGNKS 272
|
|
| BglC |
COG2730 |
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism]; |
261-510 |
3.27e-33 |
|
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];
Pssm-ID: 442036 [Multi-domain] Cd Length: 295 Bit Score: 129.78 E-value: 3.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 261 RGVN--------HAYVWYPGQNRAFADIKSFGANTVRV-----VLGSGQRWG---PTSAAEVTSVIGQCKQNRLICVLEV 324
Cdd:COG2730 8 RGVNlgnwlelwFETLWGNITEEDIDAIADWGFNTVRLpvsweRLQDPDNPYtldEAYLERVDEVVDWAKARGLYVILDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 325 HDTTGYGEQSGAATLDQAAGYWISVADALKGQENYVVINLGNEPFGNDqqvSATWTSATSNAIKRLRAAGLQHLLMADAP 404
Cdd:COG2730 88 HHAPGYQGWYDAATQERFIAFWRQLAERYKDYPNVLGFELLNEPHGAT---WADWNALAQRAIDAIRATNPDRLIIVEGN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 405 MWGQDWQNImrdnagtVFNADPQHNTVFSIHMYGVYD------------TAAEINAYFDAF----RTAGLPLVVGEFGSM 468
Cdd:COG2730 165 NWGGAHNLR-------ALDPLDDDNLVYSVHFYGPFVfthqgawfagptYPANLEARLDNWgdwaADNGVPVFVGEFGAY 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 502994194 469 HTDGNPDE----DTIMAQAQARGLGYLGWSWSGNSSDVAYLDMTNN 510
Cdd:COG2730 238 NDDPDASRlawlRDLLDYLEENGIGWTYWSFNPSGDTGGLLDRGTG 283
|
|
| TesA |
COG2755 |
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ... |
31-229 |
5.36e-29 |
|
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];
Pssm-ID: 442045 [Multi-domain] Cd Length: 191 Bit Score: 114.36 E-value: 5.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 31 PTRIMALGDSIT-----GSPGCWRALLWKHLQETghtDIDFVgtlpaqgcgftydgeNEGHGGFLATGIArdNQLPGWLS 105
Cdd:COG2755 8 PLRIVALGDSITagygaSRERGWPALLARRLAAA---DVRVV---------------NAGISGATTADLL--ARLDRDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 106 ATHPDIVLMHLGTNDVWNNI--PASTILDAFTTLLGQMRAANPATKLIVAKIIPMNPANCTAcgQRVVDLNNAIPGWAQA 183
Cdd:COG2755 68 ALKPDLVVIELGTNDLLRGLgvSPEEFRANLEALIDRLRAAGPGARVVLVTPPPRLRPNYLN--ERIEAYNAAIRELAAE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502994194 184 HStaaspITVVDQWTGFDTAAD-----TGDGVHPNgTTGIQKMESRWYPAL 229
Cdd:COG2755 146 YG-----VPLVDLYAALRDAGDlpdllTADGLHPN-AAGYRLIAEAVLPAL 190
|
|
| CBM_2 |
pfam00553 |
Cellulose binding domain; Two tryptophan residues are involved in cellulose binding. Cellulose ... |
650-752 |
7.91e-29 |
|
Cellulose binding domain; Two tryptophan residues are involved in cellulose binding. Cellulose binding domain found in bacteria.
Pssm-ID: 425748 [Multi-domain] Cd Length: 101 Bit Score: 110.62 E-value: 7.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 650 CKVAYAASN-WGggNGFTANVTITNTGTSAVTGWTLAFAFAGGQQVTlPGWGATFAQSGGAVTAKNLSWNGTLAPNASTG 728
Cdd:pfam00553 1 CTATYAVTNqWG--TGFTANVTITNTGSSPINGWTVSWTYPAGQRVT-QSWNATVSQSGNPVTATNVSWNGTIAPGGSAS 77
|
90 100
....*....|....*....|....
gi 502994194 729 IGFNGTFTGTNSAPSAFTLNGSSC 752
Cdd:pfam00553 78 FGFQGSGTGSNSAPTSFTVNGAAC 101
|
|
| CBD_II |
smart00637 |
CBD_II domain; |
657-751 |
4.30e-24 |
|
CBD_II domain;
Pssm-ID: 214754 [Multi-domain] Cd Length: 92 Bit Score: 96.71 E-value: 4.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 657 SNWGGGngFTANVTITNTGTSAVTGWTLAFAFAGGQQVTlPGWGATFAQSGGAVTAKNLSWNGTLAPNASTGIGFNGTfT 736
Cdd:smart00637 2 SDWGSG--FTANVTVTNTGSSAINGWTLTFDLPGGQTVT-NSWNATVSQSGGHVTATNASWNGTIAPGGSVSFGFQGK-T 77
|
90
....*....|....*
gi 502994194 737 GTNSAPSAFTLNGSS 751
Cdd:smart00637 78 GSSAAPTGFTLNGAA 92
|
|
| CelA1 |
COG5297 |
Cellulase/cellobiase CelA1 [Carbohydrate transport and metabolism]; |
471-755 |
1.01e-23 |
|
Cellulase/cellobiase CelA1 [Carbohydrate transport and metabolism];
Pssm-ID: 444099 [Multi-domain] Cd Length: 301 Bit Score: 102.20 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 471 DGNPDEDTIMAQAQARGLGYLGWSWSGNSSDVAYLDMTNNFDPASLTAWGERFLNGINGIRQTAKEATIYGGSQADTQAP 550
Cdd:COG5297 14 AGALAGSDGTGAAGSGSGGDVASGAASASGSASGSSASGAGAGAGAAASGADTGSGGGAGAGAGVGVGAGGAAGGAGGSA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 551 SVPGTPAVSGVTSSGATLSWAASTDNVGVTGYDVLRAPGASGGTFAVVGSTATTSYTDSGLTASSTY--------RYQVR 622
Cdd:COG5297 94 GVAGAASAAGAAGAAATSSGATSSSSSGTSSGGGGGSSSSTSDTTTSSATSGSSTSTSSPTTGSTSTttgggianQPTAV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 623 ARDAAGNTSAGSGVATATTSAGGGSGACKVAYAA-SNWGGGngFTANVTITNTGTSAVTGWTLAFAFAGGQQVTlPGWGA 701
Cdd:COG5297 174 WDRIAAITATVRAHLDAALAAPLPGRDCGVTYSVySDWGSG--YTAAVTVTNPGSLPLNGWTLAWDLPGGAGVT-NAWGF 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 502994194 702 TFAQSGGAVTAKNLSWNGTLAPNASTGIGFNGTFTGTNsaPSAFTLNGsSCTAA 755
Cdd:COG5297 251 TLNQSGYTVTATNVSWNGTLAPGGSVSFGFDTSRNGWN--PSGRGLDG-ACTGG 301
|
|
| Lipase_GDSL_2 |
pfam13472 |
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ... |
36-213 |
2.20e-16 |
|
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are similar to pfam00657.
Pssm-ID: 463889 Cd Length: 176 Bit Score: 77.59 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 36 ALGDSIT------GSPGCWRALLWKHLQETGHTDIDfvgtlpaqgcgftydgENEGHGGflATGIARDNQLPGWLSATHP 109
Cdd:pfam13472 1 ALGDSITagygatGGDRSYPGWLARLLARRLGADVV----------------NNLGISG--ATTRLDLLERLDDVLRLKP 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 110 DIVLMHLGTNDVWNNIPASTILDAFTTLLGQMRAANPATKLIVAKIIPMNP---ANCTACGQRVVDLNNAIPGWAQAHSt 186
Cdd:pfam13472 63 DLVVILLGTNDLGRGVSAARAAANLEALIDALRAAGPDARVLLIGPLPVGPpppLDERRLNARIAEYNAAIREVAAERG- 141
|
170 180 190
....*....|....*....|....*....|...
gi 502994194 187 aaspITVVDQWTGFDTAAD------TGDGVHPN 213
Cdd:pfam13472 142 ----VPYVDLWDALRDDGGwlpdllADDGLHPN 170
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
547-642 |
1.41e-15 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 80.43 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 547 TQAPSVPGTPAVSGVTSSGATLSWAASTDNvGVTGYDVLRAPgASGGTFAVVGSTATTSYTDSGLTASSTYRYQVRARDA 626
Cdd:COG3401 230 TTPPSAPTGLTATADTPGSVTLSWDPVTES-DATGYRVYRSN-SGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDA 307
|
90
....*....|....*.
gi 502994194 627 AGNTSAGSGVATATTS 642
Cdd:COG3401 308 AGNESAPSNVVSVTTD 323
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
544-750 |
4.46e-15 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 78.89 E-value: 4.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 544 QADTQAPSVPGTPAVSGVTSSGATLSWAASTDNvGVTGYDVLRApGASGGTFAVVGSTAT-TSYTDSGLTASSTYRYQVR 622
Cdd:COG3401 321 TTDLTPPAAPSGLTATAVGSSSITLSWTASSDA-DVTGYNVYRS-TSGGGTYTKIAETVTtTSYTDTGLTPGTTYYYKVT 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 623 ARDAAGNTSAGSGVATATTSAGGGSGACKVAYAA-SNWGGGNGFTANVTITNTGTSAVTGWTLAFAFAGGQQVTLPGWGA 701
Cdd:COG3401 399 AVDAAGNESAPSEEVSATTASAASGESLTASVDAvPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVT 478
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502994194 702 TFAQSGGAVTAKNLSWNGTLAPNASTGIGFNGTFTGTNSAPSAFTLNGS 750
Cdd:COG3401 479 ATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGT 527
|
|
| SGNH_hydrolase |
cd00229 |
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ... |
34-213 |
9.61e-15 |
|
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.
Pssm-ID: 238141 [Multi-domain] Cd Length: 187 Bit Score: 73.22 E-value: 9.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 34 IMALGDSIT-----GSPGCWRALLWKHLQETGHTDIDFVgtlpaqgcgftydgeNEGHGGFLATGIARDNQLPGWLSATH 108
Cdd:cd00229 1 ILVIGDSITagygaSSGSTFYSLLLYLLLLAGGPGVEVI---------------NLGVSGATTADALRRLGLRLALLKDK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 109 PDIVLMHLGTNDVWNNIPAS--TILDAFTTLLGQMRAANPATKLIVAKIIPMNPANcTACGQRVVDLNNAIPGWAQAHSt 186
Cdd:cd00229 66 PDLVIIELGTNDLGRGGDTSidEFKANLEELLDALRERAPGAKVILITPPPPPPRE-GLLGRALPRYNEAIKAVAAENP- 143
|
170 180 190
....*....|....*....|....*....|
gi 502994194 187 AASPITVVDQWTGF---DTAADTGDGVHPN 213
Cdd:cd00229 144 APSGVDLVDLAALLgdeDKSLYSPDGIHPN 173
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
550-641 |
2.43e-11 |
|
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.
Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 60.59 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 550 PSVPGTPAVSGVTSSGATLSWAASTDNVG-VTGYDV-LRAPGASGGTFAVVGSTATTSYTDSGLTASSTYRYQVRARDAA 627
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGpITGYVVeYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80
|
90
....*....|....
gi 502994194 628 GnTSAGSGVATATT 641
Cdd:cd00063 81 G-ESPPSESVTVTT 93
|
|
| COG3979 |
COG3979 |
Chitodextrinase [Carbohydrate transport and metabolism]; |
548-751 |
8.45e-11 |
|
Chitodextrinase [Carbohydrate transport and metabolism];
Pssm-ID: 443178 [Multi-domain] Cd Length: 369 Bit Score: 64.41 E-value: 8.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 548 QAPSVPGTPAVSGVTSSGATLSWAASTDNVGVTGYDVLRapgasgGTFAVVGSTATTSYTDSGLTASSTYRYQVRARDAA 627
Cdd:COG3979 1 QAPTAPTGLTASNVTSSSVSLSWDASTDNVGVTGYDVYR------GGDQVATVTGLTAWTVTGLTPGTEYTFTVGACDAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 628 GNTSAGSGVATATTSAGGGSGACKVAYAASNWGGGNGFTANVTITNTGTSAVTGWTLAFAFAGGQQVTLPGWGATFAQSG 707
Cdd:COG3979 75 GNVSAASGTSTAMFGGSSTTLGSAEGVADTSGNLAASGAFFGVTTPPTPSSTLVVDGTTTVNAAATANGGTGGSGGTTTI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502994194 708 GAVTAKNLSWNGTLAPNASTGIGFNGTFTGTNSAPSAFTLNGSS 751
Cdd:COG3979 155 ITTGVEGGGGSKTAQSLNAITAAGTAALNGGVVGGADEVLTCSA 198
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
550-628 |
5.57e-10 |
|
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.
Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 56.47 E-value: 5.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 550 PSVPGTPAVSGVTSSGATLSWAASTDNVG---VTGYDVLRAPGASGGTfAVVGSTATTSYTDSGLTASSTYRYQVRARDA 626
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItgyIVGYRVEYREEGSEWK-EVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79
|
..
gi 502994194 627 AG 628
Cdd:smart00060 80 AG 81
|
|
| Endoglucanase_E_like |
cd01831 |
Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the ... |
33-229 |
2.45e-08 |
|
Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Pssm-ID: 238869 Cd Length: 169 Bit Score: 54.27 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 33 RIMALGDSITGspGCwrallwkhlqetghtdidfvGTLPAQGCGFTYDGENEGHGgfLATGIAR----DNQLPGWlSATH 108
Cdd:cd01831 1 KIEFIGDSITC--GY--------------------GVTGKSRCDFSAATEDPSLS--YAALLARalnaEYSIIAY-SGIG 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 109 PDIVLMHLGTNDVW--NNIPASTILDAFTTLLGQMRAANP-ATKLIVAKIIPMNPANCTACGQRVVDlnnaipgwaQAHS 185
Cdd:cd01831 56 PDLVVINLGTNDFStgNNPPGEDFTNAYVEFIEELRKRYPdAPIVLMLGPMLFGPYGTEEEIKRVAE---------AFKD 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502994194 186 TAASPITVVDqWTGFDTAADTGDGVHPNgTTGIQKMESRWYPAL 229
Cdd:cd01831 127 QKSKKVHYFD-TPGILQHNDIGCDWHPT-VAGHQKIAKHLLPAI 168
|
|
| sialate_O-acetylesterase_like2 |
cd01828 |
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ... |
82-215 |
4.16e-08 |
|
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
Pssm-ID: 238866 Cd Length: 169 Bit Score: 53.44 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 82 ENEGHGGFLATGIARDNQLpgwLSATHPDIVLMHLGTNDVWNNIPASTILDAFTTLLGQMRAANPATKLIVAKIIPMNPA 161
Cdd:cd01828 25 ANRGISGDTTRGLLARLDE---DVALQPKAIFIMIGINDLAQGTSDEDIVANYRTILEKLRKHFPNIKIVVQSILPVGEL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502994194 162 NcTACGQRVVDLNNAIPGWAQAHStaaspITVVDQWTGFdTAAD-------TGDGVHPNGT 215
Cdd:cd01828 102 K-SIPNEQIEELNRQLAQLAQQEG-----VTFLDLWAVF-TNADgdlknefTTDGLHLNAK 155
|
|
| COG4733 |
COG4733 |
Phage-related protein, tail protein J [Mobilome: prophages, transposons]; |
556-751 |
1.73e-07 |
|
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
Pssm-ID: 443767 [Multi-domain] Cd Length: 978 Bit Score: 54.95 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 556 PAVSGVTSS----GATLSWAASTDnVGVTGYDVLRAPGASGGTFAVVGS-TATTSYTDSGLTASSTYRYQVRARDAAGNT 630
Cdd:COG4733 631 PAPTGLTATgglgGITLSWSFPVD-ADTLRTEIRYSTTGDWASATVAQAlYPGNTYTLAGLKAGQTYYYRARAVDRSGNV 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 631 SAGSGVATATTSAGGGSGACKVAYAASNWGGGNGFTANVTITNTGTSAVTGWTLAFAFAGGQQVTLPGW--GATFAQSGG 708
Cdd:COG4733 710 SAWWVSGQASADAAGILDAITGQILETELGQELDAIIQNATVAEVVAATVTDVTAQIDTAVLFAGVATAaaIGAEARVAA 789
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502994194 709 AVTAKNLSWNGTLAPNASTGIGFNGTFTGTNSAPSAFTLNGSS 751
Cdd:COG4733 790 TVAESATAAAATGTAADAAGDASGGVTAGTSGTTGAGDTAAST 832
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
551-629 |
1.80e-07 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 49.34 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 551 SVPGTPAVSGVTSSGATLSWAASTDNVG-VTGYDV-LRAPGASGGTFAVVGSTATTSYTDSGLTASSTYRYQVRARDAAG 628
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGpITGYEVeYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80
|
.
gi 502994194 629 N 629
Cdd:pfam00041 81 E 81
|
|
| Lipase_GDSL |
pfam00657 |
GDSL-like Lipase/Acylhydrolase; |
34-213 |
8.22e-07 |
|
GDSL-like Lipase/Acylhydrolase;
Pssm-ID: 459892 [Multi-domain] Cd Length: 210 Bit Score: 50.65 E-value: 8.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 34 IMALGDSIT-------GSPGCWRALLWKHLQETghtdIDFVGTLPAQGCGFTYDGENEGHGGFLATGIARdnQLPGWLSA 106
Cdd:pfam00657 1 IVAFGDSLTdgggdgpGGRFSWGDLLADFLARK----LGVPGSGYNHGANFAIGGATIEDLPIQLEQLLR--LISDVKDQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 107 THPDIVLMHLGTNDV-WNNIPASTILDAFTTLLGQMRAANPATKLIVAKIIPMN--PANCT---ACGQR----VVDLNNA 176
Cdd:pfam00657 75 AKPDLVTIFIGANDLcNFLSSPARSKKRVPDLLDELRANLPQLGLGARKFWVHGlgPLGCTppkGCYELynalAEEYNER 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502994194 177 IPGWAQAHSTAAS--PITVVDQWTGFDTAAD------TGDGVHPN 213
Cdd:pfam00657 155 LNELVNSLAAAAEdaNVVYVDIYGFEDPTDPccgiglEPDGLHPS 199
|
|
| SGNH_hydrolase_like_4 |
cd04501 |
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ... |
32-213 |
1.09e-05 |
|
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.
Pssm-ID: 239945 Cd Length: 183 Bit Score: 46.55 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 32 TRIMALGDSIT-----GSPGCWRALLWKHlqetghTDIDFVgtlpaqgcgftydgeNEGHGGFLATGI-ARDNQLpgwLS 105
Cdd:cd04501 1 MRVVCLGDSITygypvGPEASWVNLLAEF------LGKEVI---------------NRGINGDTTSQMlVRFYED---VI 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 106 ATHPDIVLMHLGTNDVWNNIPASTILDAFTTLLGQMRAANpaTKLIVAKIIPMNPANCTACGQRV----VDLNNAIPGWA 181
Cdd:cd04501 57 ALKPAVVIIMGGTNDIIVNTSLEMIKDNIRSMVELAEANG--IKVILASPLPVDDYPWKPQWLRPanklKSLNRWLKDYA 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 502994194 182 QAHStaaspITVVDQWTGFDTAADTG-------DGVHPN 213
Cdd:cd04501 135 RENG-----LLFLDFYSPLLDERNVGlkpglltDGLHPS 168
|
|
| Lysophospholipase_L1_like |
cd01822 |
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ... |
33-229 |
1.25e-05 |
|
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this family is TesA, an E. coli periplasmic protein with thioesterase, esterase, arylesterase, protease and lysophospholipase activity.
Pssm-ID: 238860 [Multi-domain] Cd Length: 177 Bit Score: 46.35 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 33 RIMALGDSITGSPGC-----WRALLWKHLQETGHtDIDFVgtlpaqgcgftydgeNEGHGGFL-ATGIARdnqLPGWLSA 106
Cdd:cd01822 2 TILALGDSLTAGYGLppeegWPALLQKRLDARGI-DVTVI---------------NAGVSGDTtAGGLAR---LPALLAQ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 107 THPDIVLMHLGTNDVWNNIPASTILDAFTTLLGQMRAANpATKLIVAKIIPMNpanctaCGQRVVDLNNAI-PGWAQAHS 185
Cdd:cd01822 63 HKPDLVILELGGNDGLRGIPPDQTRANLRQMIETAQARG-APVLLVGMQAPPN------YGPRYTRRFAAIyPELAEEYG 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502994194 186 TAASPitvvDQWTGFdtAADTG----DGVHPNGtTGIQKMESRWYPAL 229
Cdd:cd01822 136 VPLVP----FFLEGV--AGDPElmqsDGIHPNA-EGQPIIAENVWPAL 176
|
|
| NnaC_like |
cd01841 |
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ... |
109-213 |
2.35e-05 |
|
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases. E. coli NnaC appears to be involved in polysaccharide synthesis.
Pssm-ID: 238879 Cd Length: 174 Bit Score: 45.40 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 109 PDIVLMHLGTNDVWNNIPASTILDAFTTLLGQMRAANPATKLIVAKIIPMNPA--NCTACGQRVVDLNNAIPGWAQAHSt 186
Cdd:cd01841 52 PSKVFLFLGTNDIGKEVSSNQFIKWYRDIIEQIREEFPNTKIYLLSVLPVLEEdeIKTRSNTRIQRLNDAIKELAPELG- 130
|
90 100 110
....*....|....*....|....*....|...
gi 502994194 187 aaspITVVDQWTGF-----DTAAD-TGDGVHPN 213
Cdd:cd01841 131 ----VTFIDLNDVLvdefgNLKKEyTTDGLHFN 159
|
|
| SGNH_hydrolase_like_1 |
cd01832 |
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ... |
33-214 |
3.04e-04 |
|
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid. Myxobacterial members of this subfamily have been reported to be involved in adventurous gliding motility.
Pssm-ID: 238870 Cd Length: 185 Bit Score: 42.26 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 33 RIMALGDSIT------GSPGCWRAL--LWKHLQETGHTDIDFvgtlpaqgcgftydgENEGHGGfLATGIARDNQLPGWL 104
Cdd:cd01832 1 RYVALGDSITegvgdpVPDGGYRGWadRLAAALAAADPGIEY---------------ANLAVRG-RRTAQILAEQLPAAL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 105 SAThPDIVLMHLGTNDVWN-NIPASTILDAFTTLLGQMRAanPATKLIVAKIIPMNPAN--CTACGQRVVDLNNAIPGWA 181
Cdd:cd01832 65 ALR-PDLVTLLAGGNDILRpGTDPDTYRADLEEAVRRLRA--AGARVVVFTIPDPAVLEpfRRRVRARLAAYNAVIRAVA 141
|
170 180 190
....*....|....*....|....*....|....*.
gi 502994194 182 QAHStaaspITVVDQWTGFDTAAD---TGDGVHPNG 214
Cdd:cd01832 142 ARYG-----AVHVDLWEHPEFADPrlwASDRLHPSA 172
|
|
| FeeA_FeeB_like |
cd01836 |
SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of ... |
103-233 |
1.48e-03 |
|
SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of a biosynthetic gene cluster and may participate in the biosynthesis of long-chain N-acyltyrosines by providing saturated and unsaturated fatty acids, which it turn are loaded onto the acyl carrier protein FeeL. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
Pssm-ID: 238874 Cd Length: 191 Bit Score: 40.33 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 103 WLSATHPDIVLMHLGTNDVWNNIPASTILDAFTTLLGQMRAANPATKLIVAKIIPM-------NPANcTACGQRVVDLNN 175
Cdd:cd01836 62 PLPETRFDVAVISIGVNDVTHLTSIARWRKQLAELVDALRAKFPGARVVVTAVPPLgrfpalpQPLR-WLLGRRARLLNR 140
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 502994194 176 AIPGWAQahstAASPITVVDQWTGFDTAADTGDGVHPNgttgiQKMESRWYPALVAAL 233
Cdd:cd01836 141 ALERLAS----EAPRVTLLPATGPLFPALFASDGFHPS-----AAGYAVWAEALAPAI 189
|
|
| PRK12688 |
PRK12688 |
flagellin; Reviewed |
600-734 |
9.06e-03 |
|
flagellin; Reviewed
Pssm-ID: 171664 [Multi-domain] Cd Length: 751 Bit Score: 39.48 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 600 STATTSYTDSGLTASSTYRYQVRARDAAGNTSAGSGVATATTSAGGGSGACKVAYAASNWGGGNGFTANVTITNTGTSAV 679
Cdd:PRK12688 112 STTISGATADDLRGTTSYASATASSNVLYDGAAGGATAATGATTLGGTAGSLAGTGATAGDGTTALTGTITLIATNGTTA 191
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 502994194 680 TGWTLAFAFAGGQQVTLPGWGATFAqSGGAVTAKNLSWNGTLAPNASTGIGFNGT 734
Cdd:PRK12688 192 TGLLGNAQPADGDTLTVNGKTITFR-SGAAPASTAVPSGSGVSGNLVTDGNGNST 245
|
|
| PRK10528 |
PRK10528 |
multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1; Provisional |
91-213 |
9.56e-03 |
|
multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1; Provisional
Pssm-ID: 182521 Cd Length: 191 Bit Score: 38.21 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502994194 91 ATGIARdnqLPGWLSATHPDIVLMHLGTNDVWNNIPASTILDAFTTLLGQMRAANPATKLIVAKIipmnPANctaCGQRV 170
Cdd:PRK10528 57 QQGLAR---LPALLKQHQPRWVLVELGGNDGLRGFPPQQTEQTLRQIIQDVKAANAQPLLMQIRL----PAN---YGRRY 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 502994194 171 VDLNNAI-PGWAQAHSTAASP-----ITVVDQWTgfdtaadTGDGVHPN 213
Cdd:PRK10528 127 NEAFSAIyPKLAKEFDIPLLPffmeeVYLKPQWM-------QDDGIHPN 168
|
|
| |
