|
Name |
Accession |
Description |
Interval |
E-value |
| autotrans_barl |
TIGR01414 |
outer membrane autotransporter barrel domain; A number of Gram-negative bacterial proteins, ... |
553-1030 |
2.81e-70 |
|
outer membrane autotransporter barrel domain; A number of Gram-negative bacterial proteins, mostly found in pathogens and associated with virulence, contain a conserved C-terminal domain that integrates into the outer membrane and enables the N-terminal region to be delivered across the membrane. This C-terminal autotransporter domain is about 400 amino acids in length and includes the aromatic amino acid-rich OMP signal, typically ending with a Phe or Trp residue, at the extreme C-terminus. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 273608 [Multi-domain] Cd Length: 431 Bit Score: 240.75 E-value: 2.81e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 553 PGNSIGTLNVAGNVSFEPGSRYAVEVGP-NGQSDRIQSSGAATIGGGEVAVTLENSANLLtqsevrsllGQQYTILSAQQ 631
Cdd:TIGR01414 1 PGGAFNTLTVNGLYTGNGGFVMNTDLGGdNSQTDRLVVNGNASGTTGVVVNNIGGEGAQT---------GDGITLVTVNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 632 GVSGQFDAVAPnylflgtglSYQPTGVTLSVGRNGTsfasvaQTSNERAvaaaadalaagnpvyeslLTSGTAGEARQaF 711
Cdd:TIGR01414 72 GSDAAFTLANG---------KVDAGAYTYTLYKNGT------EDNNNWY------------------LTSSLPDLTPP-G 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 712 RQLSGQIHADIASALVNDSRYLREALNGRLRQAEGLASSSAIKADeDGAWAQLLGAWDHASGDANATGYQASTYGVLVGL 791
Cdd:TIGR01414 118 QQLSPTYRAEAGSYAANANAALFLAELDTLRQRMGDLRSAARDAG-NGVWARIFGGDNHLDGDAGAAGYDQNTTGVQLGG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 792 DSAVAGDG----RLGVATGYTRTSLHGG---YGSKADSDNYHLAAYGDKQFGALALRGGAGYTWHRIDTKRSVNYGMQsD 864
Cdd:TIGR01414 197 DILLAGNAdgdlHVGLMAGYAKADIKTRsykYGGKGKVDGYGLGLYGTWLQDSGAYVDGVLQYSRFRNDVSSTGSNGK-V 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 865 RDTAKYSARTEQLFAEAGYGVQGEWLNLEPFVNLAYVNFENNGIAESGGAAAlrgDKQHTDATVSTLGLRADTAWQVTPG 944
Cdd:TIGR01414 276 SGKYNSNGFTASLEAGYRYNLGGNGWYVEPQAQLSYFGVSGDDYKESNGTRV---LGGGGDSLQGRLGLRVGYQFDLGTG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 945 TTVALRSELGWQHQYGGldrGTGLRFNGgnapfVVDSVPVSRDGMVLKAGAEVAVNENATLSLGYGGLLSQNH-QDNSVN 1023
Cdd:TIGR01414 353 RAVKPYLKANVLHEFKG---GTGVRVNG-----VTIRNDFSGTRAEYGVGVNAKIKDNLSLYADVDYQKGGKKyTDNQGN 424
|
....*..
gi 2304590498 1024 AGFTWRF 1030
Cdd:TIGR01414 425 LGVRYSF 431
|
|
| Peptidases_S8_Autotransporter_serine_protease_like |
cd04848 |
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ... |
71-395 |
6.90e-67 |
|
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine proteases belong to Peptidase S8 or Subtilase family. Subtilases, or subtilisin-like serine proteases, have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Autotransporters are a superfamily of outer membrane/secreted proteins of gram-negative bacteria. The presence of these subtilisin-like domains in these autotransporters are may enable them to be auto-catalytic and may also serve to allow them to act as a maturation protease cleaving other outer membrane proteins at the cell surface.
Pssm-ID: 173794 [Multi-domain] Cd Length: 267 Bit Score: 225.67 E-value: 6.90e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 71 TGKGQKVGIFDTPVN-RHPEFAGdgKLINVVTegyraYTDPHRPGINAGDRfyfdgtfhfysgsqgmLSNHGVHVAGISA 149
Cdd:cd04848 1 TGAGVKVGVIDSGIDlSHPEFAG--RVSEASY-----YVAVNDAGYASNGD----------------GDSHGTHVAGVIA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 150 ANRDGIGMHGVAFDSQVISVDNDNDGPAYGeflglDGAVTNAGWQAMINSGARVINNSWGVSIPDFLSdggrdpnalhfE 229
Cdd:cd04848 58 AARDGGGMHGVAPDATLYSARASASAGSTF-----SDADIAAAYDFLAASGVRIINNSWGGNPAIDTV-----------S 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 230 LKDAQEQFDQVKPLLGSLAgagyqgaiDAARKNILVLFAAGNDGNYNQPDVISGLAYFVPDIAPNWLSVASVAQDAASTn 309
Cdd:cd04848 122 TTYKGSAATQGNTLLAALA--------RAANAGGLFVFAAGNDGQANPSLAAAALPYLEPELEGGWIAVVAVDPNGTIA- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 310 svpytISSFSSRCGYTASFCVSSPGSKIYSTVANGSdpanlvSDYGNKNGTSMATPHVTGAVAVLLQRFPYMSSAQIADV 389
Cdd:cd04848 193 -----SYSYSNRCGVAANWCLAAPGENIYSTDPDGG------NGYGRVSGTSFAAPHVSGAAALLAQKFPWLTADQVRQT 261
|
....*.
gi 2304590498 390 LKTTAT 395
Cdd:cd04848 262 LLTTAT 267
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
131-1030 |
5.70e-66 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 239.68 E-value: 5.70e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 131 SGSQGMLSNHGVHVAGISAANRDGIGMHGVAFDSQVISVDNDNDGPAYGEFLGLDGAVTNAGWQAMINSGARVINNSWGV 210
Cdd:COG4625 14 GGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGTGGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 211 SIPDFLSDGGRDPNALHFELKDAQEQFDQVKPLLGSLAGAGYQGAIDAARKNILVLFAAGNDGNYNQPDVISGLAYFVPD 290
Cdd:COG4625 94 GGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGGGGGGGGGGGG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 291 IAPNWLSVASVAQDAASTNSVPYTISSFSSRCGYTASFCVSSPGSKIYSTVANGSDPANLVSDYGNKNGTSMATPHVTGA 370
Cdd:COG4625 174 GGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 371 VAVLLQRFPYMSSAQIADVLKTTATDMGAPGIDALYGWGMINLGKAINGPGMFYTVEDIPAEFRIPDPTGVAYGPTQFVA 450
Cdd:COG4625 254 GGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 451 NIPGRGAEVDAGTlharkcddvhcGWEIYSNNISGHGGLTKEGAGILVLTGNNTYAGPTLVNQGRLAINGSVTSAVSVQS 530
Cdd:COG4625 334 AGGGGGSGGAGAG-----------GGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 531 GGIVGGSGTVGSLTARRGGTVAPGNSIGTLNVAGNVSFEPGSRYAVEVGPNGQSDRIQSSGAATIGGGEVAVTLENSANL 610
Cdd:COG4625 403 GGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGNN 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 611 LTQSEVRSLLGQQYTilsAQQGVSGQFDAVAPNYLFLGTGLSYQPTGVTLSVGRNGTSFASVAQTSNERAVAAAADALAA 690
Cdd:COG4625 483 TYTGTTTVNGGGNYT---QSAGSTLAVEVDAANSDRLVVTGTATLNGGTVVVLAGGYAPGTTYTILAVAAALDALAGNGD 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 691 GNPVYESLLTSgTAGEARQAFRQLSGQIHADIASALVNDSRYLREALNGRLRQAEGLASSSAIKADEDGAWAQLLGAWDH 770
Cdd:COG4625 560 LSALYNALAAL-DAAAARAALDQLSGEIHASAAAALLQASRALRDALSNRLRALRGAGAAGDAAAEGWGVWAQGFGSWGD 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 771 ASGDANATGYQASTYGVLVGLDSAVAGDGRLGVATGYTRTSLHG-GYGSKADSDNYHLAAYGDKQFGALALRGGAGYTWH 849
Cdd:COG4625 639 QDGDGGAAGYDSSTGGLLVGADYRLGDNWRLGVALGYSRSDVDVdDRGSSGDSDSYHLGLYGGYQFGALYLDGGLGYGWN 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 850 RIDTKRSVNYGMQSDRDTAKYSARTEQLFAEAGYGVQGEWLNLEPFVNLAYVNFENNGIAESGGAAALRGDKQHTDATVS 929
Cdd:COG4625 719 DYDTDRTIAFGGLSRTATADYDGDTASAFLEAGYRFDLGGLTLTPFAGLAYVRLRTDGFTETGGAAALSVDSQSTDSLRS 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 930 TLGLRADTAWQVTPGTTVALRSELGWQHQYGGLDRGTGLRFNG-GNAPFVVDSVPVSRDGMVLKAGAEVAVNENATLSLG 1008
Cdd:COG4625 799 TLGLRASRTFSLGGGVTLTPSGRLGWRHEFGDDDPSTTASFAGaPGAAFTVAGAPLARDALVLGAGLSARLSDGLSLGLG 878
|
890 900
....*....|....*....|..
gi 2304590498 1009 YGGLLSQNHQDNSVNAGFTWRF 1030
Cdd:COG4625 879 YDGEFGSGYTDHGGSAGLRYRF 900
|
|
| Autotransporter |
pfam03797 |
Autotransporter beta-domain; Secretion of protein products occurs by a number of different ... |
760-1010 |
7.25e-57 |
|
Autotransporter beta-domain; Secretion of protein products occurs by a number of different pathways in bacteria. One of these pathways known as the type V pathway was first described for the IgA1 protease. The protein component that mediates secretion through the outer membrane is contained within the secreted protein itself, hence the proteins secreted in this way are called autotransporters. This family corresponds to the presumed integral membrane beta-barrel domain that transports the protein. This domain is found at the C terminus of the proteins it occurs in. The N terminus contains the variable passenger domain that is translocated across the membrane. Once the passenger domain is exported it is cleaved auto-catalytically in some proteins, in others a different protease is used and in some cases no cleavage occurs.
Pssm-ID: 461054 [Multi-domain] Cd Length: 255 Bit Score: 196.84 E-value: 7.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 760 AWAQLLGAWDHASGDANATGYQASTYGVLVGLDSAVAGDGRLGVATGYTRTSLH-GGYGSKADSDNYHLAAYGDKQF-GA 837
Cdd:pfam03797 1 VWARGFGGRGKQDGDGGAAGYDADTGGLQVGADYRLGDNLRLGVAFGYSRSDADvDGRGGSGDSDSYSLGLYGTYYGdGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 838 LALRGGAGYTWHRIDTKRSVNYGMQSDRDTAKYSARTEQLFAEAGYGVQ-GEWLNLEPFVNLAYVNFENNGIAESGGAAA 916
Cdd:pfam03797 81 WYLDGGLGYGWHDNDTRRSVDLGGFSETAKGDYDGNGFGASLEAGYRFAlGGGWTLEPFAGLAYVRLRLDGFTESGGAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 917 LRGDKQHTDATVSTLGLRADTAWQvTPGTTVALRSELGWQHQYGGLDRGTGLRFNG--GNAPFVVDSVPVSRDGMVLKAG 994
Cdd:pfam03797 161 LSVDSQSYDSLTGRLGLRLSYTFD-LGGGTLTPYARLGWRHEFGDDDPVTTAAFAGlsGAGSFTVAGADLARDSLELGAG 239
|
250
....*....|....*.
gi 2304590498 995 AEVAVNENATLSLGYG 1010
Cdd:pfam03797 240 LSAQLSDNLSLYANYD 255
|
|
| AprE |
COG1404 |
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ... |
24-463 |
9.43e-43 |
|
Serine protease, subtilisin family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441014 [Multi-domain] Cd Length: 456 Bit Score: 162.58 E-value: 9.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 24 ALAGYAQAAPHEVNGQPGDPASWRSAEFNANWGLGAIHADEAYAAGYTGKGQKVGIFDTPVNR-HPEFAGdgklinVVTE 102
Cdd:COG1404 60 ALAAPLAPAALAAPAPLPVPAAAPAAVRAAQAALLAAAAAGSSAAGLTGAGVTVAVIDTGVDAdHPDLAG------RVVG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 103 GYRAYTDPHRPGINAGdrfyfdgtfhfysgsqgmlsnHGVHVAGISAANRD-GIGMHGVAFDSQVISVD-NDNDGPAYGE 180
Cdd:COG1404 134 GYDFVDGDGDPSDDNG---------------------HGTHVAGIIAANGNnGGGVAGVAPGAKLLPVRvLDDNGSGTTS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 181 FLGldgavtnAGWQAMINSGARVINNSWGVSipdflSDGGRDPnalhfelkdaqeqfdqvkpllgslagagYQGAIDAAR 260
Cdd:COG1404 193 DIA-------AAIDWAADNGADVINLSLGGP-----ADGYSDA----------------------------LAAAVDYAV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 261 -KNILVLFAAGNDGNYNQpdvisglAYFVPDIAPNWLSVASVAQDaastnsvpYTISSFSSrcgYTASFCVSSPGSKIYS 339
Cdd:COG1404 233 dKGVLVVAAAGNSGSDDA-------TVSYPAAYPNVIAVGAVDAN--------GQLASFSN---YGPKVDVAAPGVDILS 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 340 TVANGsdpanlvsDYGNKNGTSMATPHVTGAVAVLLQRFPYMSSAQIADVLKTTATDMGAPGIDalYGWGMI----NLGK 415
Cdd:COG1404 295 TYPGG--------GYATLSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLGAPGPY--YGYGLLadgaAGAT 364
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2304590498 416 AINGPGMFYTVEDIPAEFRIPDPTGVAYGPTQFVANIPGRGAEVDAGT 463
Cdd:COG1404 365 SAGAGLAAAAGAAGAAAAATAAAVSVASAGAATAAADAAAGATAAALA 412
|
|
| Peptidase_S8 |
pfam00082 |
Subtilase family; Subtilases are a family of serine proteases. They appear to have ... |
72-409 |
3.64e-41 |
|
Subtilase family; Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see pfam00089). Structure is an alpha/beta fold containing a 7-stranded parallel beta sheet, order 2314567.
Pssm-ID: 395035 [Multi-domain] Cd Length: 287 Bit Score: 153.00 E-value: 3.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 72 GKGQKVGIFDTPVNR-HPEFAGDGKLINVVTEGYRAYTDPHRPGINAGDRFYfdgtfhfysgsqgmlSNHGVHVAGISAA 150
Cdd:pfam00082 1 GKGVVVAVLDTGIDPnHPDLSGNLDNDPSDDPEASVDFNNEWDDPRDDIDDK---------------NGHGTHVAGIIAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 151 N-RDGIGMHGVAFDSQVISVDNDNDGPAYGeflgldgAVTNAGWQAMINSGARVINNSWGvsiPDFLSDGGRDPNALHFE 229
Cdd:pfam00082 66 GgNNSIGVSGVAPGAKILGVRVFGDGGGTD-------AITAQAISWAIPQGADVINMSWG---SDKTDGGPGSWSAAVDQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 230 LKDAQEqfdqvkpllgslagagyqgaidaarKNILVLFAAGNDGnynqPDVISGLAYFVPDIAPNWLSVASVAQDAAStn 309
Cdd:pfam00082 136 LGGAEA-------------------------AGSLFVWAAGNGS----PGGNNGSSVGYPAQYKNVIAVGAVDEASEG-- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 310 svpyTISSFSSRCGYTASF---CVSSPGSKIYSTVAN------GSDPANlvSDYGNKNGTSMATPHVTGAVAVLLQRFPY 380
Cdd:pfam00082 185 ----NLASFSSYGPTLDGRlkpDIVAPGGNITGGNISstllttTSDPPN--QGYDSMSGTSMATPHVAGAAALLKQAYPN 258
|
330 340
....*....|....*....|....*....
gi 2304590498 381 MSSAQIADVLKTTATDMGAPGIDALYGWG 409
Cdd:pfam00082 259 LTPETLKALLVNTATDLGDAGLDRLFGYG 287
|
|
| Autotransporter |
smart00869 |
Autotransporter beta-domain; Secretion of protein products occurs by a number of different ... |
762-1014 |
7.72e-40 |
|
Autotransporter beta-domain; Secretion of protein products occurs by a number of different pathways in bacteria. One of these pathways known as the type IV pathway was first described for the IgA1 protease. The protein component that mediates secretion through the outer membrane is contained within the secreted protein itself, hence the proteins secreted in this way are called autotransporters. This family corresponds to the presumed integral membrane beta-barrel domain that transports the protein. This domain is found at the C-terminus of the proteins it occurs in. The N-terminus contains the variable passenger domain that is translocated across the membrane. Once the passenger domain is exported it is cleaved auto-catalytically in some proteins, in others a different peptidase is used and in some cases no cleavage occurs.
Pssm-ID: 214872 [Multi-domain] Cd Length: 268 Bit Score: 148.87 E-value: 7.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 762 AQLLGAWDH--ASGDANATGYQASTYGVLVGLDSAVAGDG--RLGVATGYTRTSLH---GGYGSKADSDNYHLAAYGDKQ 834
Cdd:smart00869 1 GRGLGGFLRqdSSGSGGSAGFDYDSYGLQLGADYRLSDNGnlSLGFAAGYGNSKVDfsgNKGSGKGDVDSYGLGLYAGYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 835 FGA-LALRGGAGYTWHRIDTKRSVNYGmQSDRDTAKYSARTEQLFAEAGYGVQ-GEWLNLEPFVNLAYVNFENNGIAESG 912
Cdd:smart00869 81 LGNgLYLDAQLGYGRSDNDTKRKVTLG-GAGRAKGSYDGTGYGASLEAGYRFYlGGGLTLTPFAGLAYSRVRQDGFTESG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 913 G-AAALRGDKQHTDATVSTLGLRADTAWQVTPGTTVALRSELGWQHQYGGLDRGTGLRFNGGNAPFVVDSVPVSRDGMVL 991
Cdd:smart00869 160 GgAFGLSVDSQSLDSLSLPLGLRLEYRLALGDGATLTPYLRLAYVHDFYDDNPVVTASLLGSGASFTTSGTDLDRNAAEL 239
|
250 260
....*....|....*....|...
gi 2304590498 992 KAGAEVAVNENATLSLGYGGLLS 1014
Cdd:smart00869 240 GLGLSAKLSNGLSLSLNYDGEFG 262
|
|
| T7SS_mycosin |
TIGR03921 |
type VII secretion-associated serine protease mycosin; Members of this family are ... |
71-462 |
1.11e-24 |
|
type VII secretion-associated serine protease mycosin; Members of this family are subtilisin-related serine proteases, found strictly in the Actinobacteria and associated with type VII secretion operons. The designation mycosin is used for members from Mycobacterium. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair]
Pssm-ID: 274856 [Multi-domain] Cd Length: 350 Bit Score: 106.64 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 71 TGKGQKVGIFDTPVNRHPEFAGdgkliNVVTEGyraytDPHRPGINAGDRfyfDGtfhfysgsqgmlsnHGVHVAGISAA 150
Cdd:TIGR03921 11 TGAGVTVAVIDTGVDDHPRLPG-----LVLPGG-----DFVGSGDGTDDC---DG--------------HGTLVAGIIAG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 151 NRD-GIGMHGVAFDSQVISV-------DNDNDGPAYGEFLGLDGAVTNAgwqamINSGARVINNSWGVSIPdflSDGGRD 222
Cdd:TIGR03921 64 RPGeGDGFSGVAPDARILPIrqtsaafEPDEGTSGVGDLGTLAKAIRRA-----ADLGADVINISLVACLP---AGSGAD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 223 PNALhfelkdaqeqfdqvkpllgslaGAGYQGAIDaarKNILVLFAAGNDGNYNQPDVISGLAYFvpdiaPNWLSVASVA 302
Cdd:TIGR03921 136 DPEL----------------------GAAVRYALD---KGVVVVAAAGNTGGDGQKTTVVYPAWY-----PGVLAVGSID 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 303 QDAastnsvpyTISSFSSRCGYTAsfcVSSPGSKIYSTVANGSDPANLVsdygnknGTSMATPHVTGAVAVLLQRFPYMS 382
Cdd:TIGR03921 186 RDG--------TPSSFSLPGPWVD---LAAPGENIVSLSPGGDGLATTS-------GTSFAAPFVSGTAALVRSRFPDLT 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 383 SAQIADVLKTTATDMGAPGIDALYGWGMINLGKAINGpgmfytveDIPAEFRIPDPTGVAYGPTQFVANIPGRGAEVDAG 462
Cdd:TIGR03921 248 AAQVRRRIEATADHPARGGRDDYVGYGVVDPVAALTG--------ELPPEDGRPLRPAPAPARPVAAPAPPPPPDDTPRG 319
|
|
| PTZ00262 |
PTZ00262 |
subtilisin-like protease; Provisional |
129-418 |
9.34e-11 |
|
subtilisin-like protease; Provisional
Pssm-ID: 240338 [Multi-domain] Cd Length: 639 Bit Score: 65.76 E-value: 9.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 129 FYSGSQGMLSN--HGVHVAGISAAN-RDGIGMHGVAFDSQVI---SVDNDNDGPAYGEFLGLDgavtnagwqAMINSGAR 202
Cdd:PTZ00262 367 FVNNDGGPMDDnyHGTHVSGIISAIgNNNIGIVGVDKRSKLIickALDSHKLGRLGDMFKCFD---------YCISREAH 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 203 VINNSWGVsipdflsdggrDPNALHFelkdaqeqFDQVKPLlgslagagyqgaidaARKNILVLFAAGN--DGNYNQPDV 280
Cdd:PTZ00262 438 MINGSFSF-----------DEYSGIF--------NESVKYL---------------EEKGILFVVSASNcsHTKESKPDI 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 281 ----ISGLAYFVPDIAP---NWLSVASVAQDaaSTNSVPYTISSFssrcgYTASFC-VSSPGSKIYSTVangsdPANlvs 352
Cdd:PTZ00262 484 pkcdLDVNKVYPPILSKklrNVITVSNLIKD--KNNQYSLSPNSF-----YSAKYCqLAAPGTNIYSTF-----PKN--- 548
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2304590498 353 DYGNKNGTSMATPHVTGAVAVLLQRFPYMSSAQIADVLKTTATDMgaPGIDALYGW-GMINLGKAIN 418
Cdd:PTZ00262 549 SYRKLNGTSMAAPHVAAIASLILSINPSLSYEEVIRILKESIVQL--PSLKNKVKWgGYLDIHHAVN 613
|
|
| autotrns_rpt |
TIGR02601 |
autotransporter-associated beta strand repeat; This model represent a core 32-residue region ... |
488-519 |
5.10e-08 |
|
autotransporter-associated beta strand repeat; This model represent a core 32-residue region of a class of bacterial protein repeat found in one to 30 copies per protein. Most proteins with a copy of this repeat have domains associated with membrane autotransporters (pfam03797, TIGR01414). The repeats occur with a periodicity of 60 to 100 residues. A pattern of sequence conservation is that every second residue is well-conserved across most of the domain. pfam05594 is based on a longer, much more poorly conserved multiple sequence alignment and hits some of the same proteins as this model with some overlap between the hit regions of the two models. It describes these repeats as likely to have a beta-helical structure. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274223 [Multi-domain] Cd Length: 32 Bit Score: 49.72 E-value: 5.10e-08
10 20 30
....*....|....*....|....*....|..
gi 2304590498 488 GLTKEGAGILVLTGNNTYAGPTLVNQGRLAIN 519
Cdd:TIGR02601 1 GLTKTGAGTLTLSGANTYTGGTTVNAGTLQVG 32
|
|
| PATR |
pfam12951 |
Passenger-associated-transport-repeat; This Autotransporter-associated beta strand repeat ... |
489-516 |
6.24e-08 |
|
Passenger-associated-transport-repeat; This Autotransporter-associated beta strand repeat model represents a core 32-residue region of a class of bacterial protein repeat found in one to 30 copies per protein. Most proteins with a copy of this repeat have domains associated with membrane autotransporters (pfam03797). The repeats occur with a periodicity of 60 to 100 residues. A pattern of sequence conservation is that every second residue is well-conserved across most of the domain. These repeats as likely to have a beta-helical structure. This repeat plays a role in the efficient transport of autotransporter virulence factors to the bacterial surface during growth and infection. The repeat is always associated with the passenger domain of the autotransporter. For these reasons it has been coined the Passenger-associated Transport Repeat (PATR). The mechanism by which the PATR motif promotes transport is uncertain but it is likely that the conserved glycines (see HMM Logo) are required for flexibility of folding and that this folding drives secretion. Autotransporters that contain PATR(s) associate with distinct virulence traits such as subtilisin (S8) type protease domains and polymorphic outer-membrane protein repeats, whilst SPATE (S6) type protease and lipase-like autotransporters do not tend to contain PATR motifs.
Pssm-ID: 463760 [Multi-domain] Cd Length: 28 Bit Score: 49.27 E-value: 6.24e-08
10 20
....*....|....*....|....*...
gi 2304590498 489 LTKEGAGILVLTGNNTYAGPTLVNQGRL 516
Cdd:pfam12951 1 LTKTGAGTLTLTGANTYTGGTTVNAGTL 28
|
|
| PRK15319 |
PRK15319 |
fibronectin-binding autotransporter adhesin ShdA; |
456-611 |
4.21e-05 |
|
fibronectin-binding autotransporter adhesin ShdA;
Pssm-ID: 185219 [Multi-domain] Cd Length: 2039 Bit Score: 47.77 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 456 GAEVDAGTLHARKCDDV-----------HCGWEIYSNNISGHGGLTKEGAGILVLTGNNTYAGPTLVNQGRLAIN--GSV 522
Cdd:PRK15319 709 GTTISGGTLTADHADSLgsgdvdnsgvlKVGEGELENILSGSGSLVKTGTGELTLSGDNTYSGGTTITGGTLTADhaDSL 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 523 TSAVSVQSGGIVGGSGTVGSLTARRGGTVAPGNSIGTL----NVAGNVSFEPGSRYAVEVGPNGQSDrIQSSGAATIGGG 598
Cdd:PRK15319 789 GSGDIDNSGVLKVGEGDLENTLSGSGSLVKTGTGELTLsggnDYSGGTTIIGGTLTADHADSLGSGD-IDNSGVLQVGEG 867
|
170
....*....|...
gi 2304590498 599 EVAVTLENSANLL 611
Cdd:PRK15319 868 ELKNTLFGSGSLV 880
|
|
| germ_prot_CspBA |
NF040809 |
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ... |
308-413 |
1.45e-03 |
|
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in Clostridium difficile, is translated as a fusion protein, but cleaved into separate homologous CspB and CspA proteins during spore formation. CspB is a protease, required to active SleC by cleaving it in order to trigger germination. CspA, like the bile salt germinant receptor CspC (encoded by the adjacent gene), has lost the catalytic residues necessary for subtilisin-like serine protease activity.
Pssm-ID: 468750 [Multi-domain] Cd Length: 1099 Bit Score: 42.84 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 308 TNSVPYTISSFSSRCGYTASFC-------------VSSPGSKIYSTVANGSDpanlvsdyGNKNGTSMATPHVTGAVAVL 374
Cdd:NF040809 401 TASRVITVGSFNSRTDVVSVFSgegdiengiykpdLLAPGENIVSYLPGGTT--------GALTGTSMATPHVTGVCSLL 472
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2304590498 375 LQ------RFPYMSSAQIADVLKTTA---TDMGAPgiDALYGWGMINL 413
Cdd:NF040809 473 MQwgivegNDLFLYSQKLKALLLQNArrsPNRTYP--NNSSGYGFLNL 518
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| autotrans_barl |
TIGR01414 |
outer membrane autotransporter barrel domain; A number of Gram-negative bacterial proteins, ... |
553-1030 |
2.81e-70 |
|
outer membrane autotransporter barrel domain; A number of Gram-negative bacterial proteins, mostly found in pathogens and associated with virulence, contain a conserved C-terminal domain that integrates into the outer membrane and enables the N-terminal region to be delivered across the membrane. This C-terminal autotransporter domain is about 400 amino acids in length and includes the aromatic amino acid-rich OMP signal, typically ending with a Phe or Trp residue, at the extreme C-terminus. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 273608 [Multi-domain] Cd Length: 431 Bit Score: 240.75 E-value: 2.81e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 553 PGNSIGTLNVAGNVSFEPGSRYAVEVGP-NGQSDRIQSSGAATIGGGEVAVTLENSANLLtqsevrsllGQQYTILSAQQ 631
Cdd:TIGR01414 1 PGGAFNTLTVNGLYTGNGGFVMNTDLGGdNSQTDRLVVNGNASGTTGVVVNNIGGEGAQT---------GDGITLVTVNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 632 GVSGQFDAVAPnylflgtglSYQPTGVTLSVGRNGTsfasvaQTSNERAvaaaadalaagnpvyeslLTSGTAGEARQaF 711
Cdd:TIGR01414 72 GSDAAFTLANG---------KVDAGAYTYTLYKNGT------EDNNNWY------------------LTSSLPDLTPP-G 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 712 RQLSGQIHADIASALVNDSRYLREALNGRLRQAEGLASSSAIKADeDGAWAQLLGAWDHASGDANATGYQASTYGVLVGL 791
Cdd:TIGR01414 118 QQLSPTYRAEAGSYAANANAALFLAELDTLRQRMGDLRSAARDAG-NGVWARIFGGDNHLDGDAGAAGYDQNTTGVQLGG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 792 DSAVAGDG----RLGVATGYTRTSLHGG---YGSKADSDNYHLAAYGDKQFGALALRGGAGYTWHRIDTKRSVNYGMQsD 864
Cdd:TIGR01414 197 DILLAGNAdgdlHVGLMAGYAKADIKTRsykYGGKGKVDGYGLGLYGTWLQDSGAYVDGVLQYSRFRNDVSSTGSNGK-V 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 865 RDTAKYSARTEQLFAEAGYGVQGEWLNLEPFVNLAYVNFENNGIAESGGAAAlrgDKQHTDATVSTLGLRADTAWQVTPG 944
Cdd:TIGR01414 276 SGKYNSNGFTASLEAGYRYNLGGNGWYVEPQAQLSYFGVSGDDYKESNGTRV---LGGGGDSLQGRLGLRVGYQFDLGTG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 945 TTVALRSELGWQHQYGGldrGTGLRFNGgnapfVVDSVPVSRDGMVLKAGAEVAVNENATLSLGYGGLLSQNH-QDNSVN 1023
Cdd:TIGR01414 353 RAVKPYLKANVLHEFKG---GTGVRVNG-----VTIRNDFSGTRAEYGVGVNAKIKDNLSLYADVDYQKGGKKyTDNQGN 424
|
....*..
gi 2304590498 1024 AGFTWRF 1030
Cdd:TIGR01414 425 LGVRYSF 431
|
|
| Peptidases_S8_Autotransporter_serine_protease_like |
cd04848 |
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ... |
71-395 |
6.90e-67 |
|
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine proteases belong to Peptidase S8 or Subtilase family. Subtilases, or subtilisin-like serine proteases, have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Autotransporters are a superfamily of outer membrane/secreted proteins of gram-negative bacteria. The presence of these subtilisin-like domains in these autotransporters are may enable them to be auto-catalytic and may also serve to allow them to act as a maturation protease cleaving other outer membrane proteins at the cell surface.
Pssm-ID: 173794 [Multi-domain] Cd Length: 267 Bit Score: 225.67 E-value: 6.90e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 71 TGKGQKVGIFDTPVN-RHPEFAGdgKLINVVTegyraYTDPHRPGINAGDRfyfdgtfhfysgsqgmLSNHGVHVAGISA 149
Cdd:cd04848 1 TGAGVKVGVIDSGIDlSHPEFAG--RVSEASY-----YVAVNDAGYASNGD----------------GDSHGTHVAGVIA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 150 ANRDGIGMHGVAFDSQVISVDNDNDGPAYGeflglDGAVTNAGWQAMINSGARVINNSWGVSIPDFLSdggrdpnalhfE 229
Cdd:cd04848 58 AARDGGGMHGVAPDATLYSARASASAGSTF-----SDADIAAAYDFLAASGVRIINNSWGGNPAIDTV-----------S 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 230 LKDAQEQFDQVKPLLGSLAgagyqgaiDAARKNILVLFAAGNDGNYNQPDVISGLAYFVPDIAPNWLSVASVAQDAASTn 309
Cdd:cd04848 122 TTYKGSAATQGNTLLAALA--------RAANAGGLFVFAAGNDGQANPSLAAAALPYLEPELEGGWIAVVAVDPNGTIA- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 310 svpytISSFSSRCGYTASFCVSSPGSKIYSTVANGSdpanlvSDYGNKNGTSMATPHVTGAVAVLLQRFPYMSSAQIADV 389
Cdd:cd04848 193 -----SYSYSNRCGVAANWCLAAPGENIYSTDPDGG------NGYGRVSGTSFAAPHVSGAAALLAQKFPWLTADQVRQT 261
|
....*.
gi 2304590498 390 LKTTAT 395
Cdd:cd04848 262 LLTTAT 267
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
131-1030 |
5.70e-66 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 239.68 E-value: 5.70e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 131 SGSQGMLSNHGVHVAGISAANRDGIGMHGVAFDSQVISVDNDNDGPAYGEFLGLDGAVTNAGWQAMINSGARVINNSWGV 210
Cdd:COG4625 14 GGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGTGGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 211 SIPDFLSDGGRDPNALHFELKDAQEQFDQVKPLLGSLAGAGYQGAIDAARKNILVLFAAGNDGNYNQPDVISGLAYFVPD 290
Cdd:COG4625 94 GGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGGGGGGGGGGGG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 291 IAPNWLSVASVAQDAASTNSVPYTISSFSSRCGYTASFCVSSPGSKIYSTVANGSDPANLVSDYGNKNGTSMATPHVTGA 370
Cdd:COG4625 174 GGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 371 VAVLLQRFPYMSSAQIADVLKTTATDMGAPGIDALYGWGMINLGKAINGPGMFYTVEDIPAEFRIPDPTGVAYGPTQFVA 450
Cdd:COG4625 254 GGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 451 NIPGRGAEVDAGTlharkcddvhcGWEIYSNNISGHGGLTKEGAGILVLTGNNTYAGPTLVNQGRLAINGSVTSAVSVQS 530
Cdd:COG4625 334 AGGGGGSGGAGAG-----------GGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 531 GGIVGGSGTVGSLTARRGGTVAPGNSIGTLNVAGNVSFEPGSRYAVEVGPNGQSDRIQSSGAATIGGGEVAVTLENSANL 610
Cdd:COG4625 403 GGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGNN 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 611 LTQSEVRSLLGQQYTilsAQQGVSGQFDAVAPNYLFLGTGLSYQPTGVTLSVGRNGTSFASVAQTSNERAVAAAADALAA 690
Cdd:COG4625 483 TYTGTTTVNGGGNYT---QSAGSTLAVEVDAANSDRLVVTGTATLNGGTVVVLAGGYAPGTTYTILAVAAALDALAGNGD 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 691 GNPVYESLLTSgTAGEARQAFRQLSGQIHADIASALVNDSRYLREALNGRLRQAEGLASSSAIKADEDGAWAQLLGAWDH 770
Cdd:COG4625 560 LSALYNALAAL-DAAAARAALDQLSGEIHASAAAALLQASRALRDALSNRLRALRGAGAAGDAAAEGWGVWAQGFGSWGD 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 771 ASGDANATGYQASTYGVLVGLDSAVAGDGRLGVATGYTRTSLHG-GYGSKADSDNYHLAAYGDKQFGALALRGGAGYTWH 849
Cdd:COG4625 639 QDGDGGAAGYDSSTGGLLVGADYRLGDNWRLGVALGYSRSDVDVdDRGSSGDSDSYHLGLYGGYQFGALYLDGGLGYGWN 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 850 RIDTKRSVNYGMQSDRDTAKYSARTEQLFAEAGYGVQGEWLNLEPFVNLAYVNFENNGIAESGGAAALRGDKQHTDATVS 929
Cdd:COG4625 719 DYDTDRTIAFGGLSRTATADYDGDTASAFLEAGYRFDLGGLTLTPFAGLAYVRLRTDGFTETGGAAALSVDSQSTDSLRS 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 930 TLGLRADTAWQVTPGTTVALRSELGWQHQYGGLDRGTGLRFNG-GNAPFVVDSVPVSRDGMVLKAGAEVAVNENATLSLG 1008
Cdd:COG4625 799 TLGLRASRTFSLGGGVTLTPSGRLGWRHEFGDDDPSTTASFAGaPGAAFTVAGAPLARDALVLGAGLSARLSDGLSLGLG 878
|
890 900
....*....|....*....|..
gi 2304590498 1009 YGGLLSQNHQDNSVNAGFTWRF 1030
Cdd:COG4625 879 YDGEFGSGYTDHGGSAGLRYRF 900
|
|
| Autotransporter |
pfam03797 |
Autotransporter beta-domain; Secretion of protein products occurs by a number of different ... |
760-1010 |
7.25e-57 |
|
Autotransporter beta-domain; Secretion of protein products occurs by a number of different pathways in bacteria. One of these pathways known as the type V pathway was first described for the IgA1 protease. The protein component that mediates secretion through the outer membrane is contained within the secreted protein itself, hence the proteins secreted in this way are called autotransporters. This family corresponds to the presumed integral membrane beta-barrel domain that transports the protein. This domain is found at the C terminus of the proteins it occurs in. The N terminus contains the variable passenger domain that is translocated across the membrane. Once the passenger domain is exported it is cleaved auto-catalytically in some proteins, in others a different protease is used and in some cases no cleavage occurs.
Pssm-ID: 461054 [Multi-domain] Cd Length: 255 Bit Score: 196.84 E-value: 7.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 760 AWAQLLGAWDHASGDANATGYQASTYGVLVGLDSAVAGDGRLGVATGYTRTSLH-GGYGSKADSDNYHLAAYGDKQF-GA 837
Cdd:pfam03797 1 VWARGFGGRGKQDGDGGAAGYDADTGGLQVGADYRLGDNLRLGVAFGYSRSDADvDGRGGSGDSDSYSLGLYGTYYGdGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 838 LALRGGAGYTWHRIDTKRSVNYGMQSDRDTAKYSARTEQLFAEAGYGVQ-GEWLNLEPFVNLAYVNFENNGIAESGGAAA 916
Cdd:pfam03797 81 WYLDGGLGYGWHDNDTRRSVDLGGFSETAKGDYDGNGFGASLEAGYRFAlGGGWTLEPFAGLAYVRLRLDGFTESGGAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 917 LRGDKQHTDATVSTLGLRADTAWQvTPGTTVALRSELGWQHQYGGLDRGTGLRFNG--GNAPFVVDSVPVSRDGMVLKAG 994
Cdd:pfam03797 161 LSVDSQSYDSLTGRLGLRLSYTFD-LGGGTLTPYARLGWRHEFGDDDPVTTAAFAGlsGAGSFTVAGADLARDSLELGAG 239
|
250
....*....|....*.
gi 2304590498 995 AEVAVNENATLSLGYG 1010
Cdd:pfam03797 240 LSAQLSDNLSLYANYD 255
|
|
| AprE |
COG1404 |
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ... |
24-463 |
9.43e-43 |
|
Serine protease, subtilisin family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441014 [Multi-domain] Cd Length: 456 Bit Score: 162.58 E-value: 9.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 24 ALAGYAQAAPHEVNGQPGDPASWRSAEFNANWGLGAIHADEAYAAGYTGKGQKVGIFDTPVNR-HPEFAGdgklinVVTE 102
Cdd:COG1404 60 ALAAPLAPAALAAPAPLPVPAAAPAAVRAAQAALLAAAAAGSSAAGLTGAGVTVAVIDTGVDAdHPDLAG------RVVG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 103 GYRAYTDPHRPGINAGdrfyfdgtfhfysgsqgmlsnHGVHVAGISAANRD-GIGMHGVAFDSQVISVD-NDNDGPAYGE 180
Cdd:COG1404 134 GYDFVDGDGDPSDDNG---------------------HGTHVAGIIAANGNnGGGVAGVAPGAKLLPVRvLDDNGSGTTS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 181 FLGldgavtnAGWQAMINSGARVINNSWGVSipdflSDGGRDPnalhfelkdaqeqfdqvkpllgslagagYQGAIDAAR 260
Cdd:COG1404 193 DIA-------AAIDWAADNGADVINLSLGGP-----ADGYSDA----------------------------LAAAVDYAV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 261 -KNILVLFAAGNDGNYNQpdvisglAYFVPDIAPNWLSVASVAQDaastnsvpYTISSFSSrcgYTASFCVSSPGSKIYS 339
Cdd:COG1404 233 dKGVLVVAAAGNSGSDDA-------TVSYPAAYPNVIAVGAVDAN--------GQLASFSN---YGPKVDVAAPGVDILS 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 340 TVANGsdpanlvsDYGNKNGTSMATPHVTGAVAVLLQRFPYMSSAQIADVLKTTATDMGAPGIDalYGWGMI----NLGK 415
Cdd:COG1404 295 TYPGG--------GYATLSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLGAPGPY--YGYGLLadgaAGAT 364
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2304590498 416 AINGPGMFYTVEDIPAEFRIPDPTGVAYGPTQFVANIPGRGAEVDAGT 463
Cdd:COG1404 365 SAGAGLAAAAGAAGAAAAATAAAVSVASAGAATAAADAAAGATAAALA 412
|
|
| Peptidase_S8 |
pfam00082 |
Subtilase family; Subtilases are a family of serine proteases. They appear to have ... |
72-409 |
3.64e-41 |
|
Subtilase family; Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see pfam00089). Structure is an alpha/beta fold containing a 7-stranded parallel beta sheet, order 2314567.
Pssm-ID: 395035 [Multi-domain] Cd Length: 287 Bit Score: 153.00 E-value: 3.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 72 GKGQKVGIFDTPVNR-HPEFAGDGKLINVVTEGYRAYTDPHRPGINAGDRFYfdgtfhfysgsqgmlSNHGVHVAGISAA 150
Cdd:pfam00082 1 GKGVVVAVLDTGIDPnHPDLSGNLDNDPSDDPEASVDFNNEWDDPRDDIDDK---------------NGHGTHVAGIIAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 151 N-RDGIGMHGVAFDSQVISVDNDNDGPAYGeflgldgAVTNAGWQAMINSGARVINNSWGvsiPDFLSDGGRDPNALHFE 229
Cdd:pfam00082 66 GgNNSIGVSGVAPGAKILGVRVFGDGGGTD-------AITAQAISWAIPQGADVINMSWG---SDKTDGGPGSWSAAVDQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 230 LKDAQEqfdqvkpllgslagagyqgaidaarKNILVLFAAGNDGnynqPDVISGLAYFVPDIAPNWLSVASVAQDAAStn 309
Cdd:pfam00082 136 LGGAEA-------------------------AGSLFVWAAGNGS----PGGNNGSSVGYPAQYKNVIAVGAVDEASEG-- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 310 svpyTISSFSSRCGYTASF---CVSSPGSKIYSTVAN------GSDPANlvSDYGNKNGTSMATPHVTGAVAVLLQRFPY 380
Cdd:pfam00082 185 ----NLASFSSYGPTLDGRlkpDIVAPGGNITGGNISstllttTSDPPN--QGYDSMSGTSMATPHVAGAAALLKQAYPN 258
|
330 340
....*....|....*....|....*....
gi 2304590498 381 MSSAQIADVLKTTATDMGAPGIDALYGWG 409
Cdd:pfam00082 259 LTPETLKALLVNTATDLGDAGLDRLFGYG 287
|
|
| Autotransporter |
smart00869 |
Autotransporter beta-domain; Secretion of protein products occurs by a number of different ... |
762-1014 |
7.72e-40 |
|
Autotransporter beta-domain; Secretion of protein products occurs by a number of different pathways in bacteria. One of these pathways known as the type IV pathway was first described for the IgA1 protease. The protein component that mediates secretion through the outer membrane is contained within the secreted protein itself, hence the proteins secreted in this way are called autotransporters. This family corresponds to the presumed integral membrane beta-barrel domain that transports the protein. This domain is found at the C-terminus of the proteins it occurs in. The N-terminus contains the variable passenger domain that is translocated across the membrane. Once the passenger domain is exported it is cleaved auto-catalytically in some proteins, in others a different peptidase is used and in some cases no cleavage occurs.
Pssm-ID: 214872 [Multi-domain] Cd Length: 268 Bit Score: 148.87 E-value: 7.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 762 AQLLGAWDH--ASGDANATGYQASTYGVLVGLDSAVAGDG--RLGVATGYTRTSLH---GGYGSKADSDNYHLAAYGDKQ 834
Cdd:smart00869 1 GRGLGGFLRqdSSGSGGSAGFDYDSYGLQLGADYRLSDNGnlSLGFAAGYGNSKVDfsgNKGSGKGDVDSYGLGLYAGYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 835 FGA-LALRGGAGYTWHRIDTKRSVNYGmQSDRDTAKYSARTEQLFAEAGYGVQ-GEWLNLEPFVNLAYVNFENNGIAESG 912
Cdd:smart00869 81 LGNgLYLDAQLGYGRSDNDTKRKVTLG-GAGRAKGSYDGTGYGASLEAGYRFYlGGGLTLTPFAGLAYSRVRQDGFTESG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 913 G-AAALRGDKQHTDATVSTLGLRADTAWQVTPGTTVALRSELGWQHQYGGLDRGTGLRFNGGNAPFVVDSVPVSRDGMVL 991
Cdd:smart00869 160 GgAFGLSVDSQSLDSLSLPLGLRLEYRLALGDGATLTPYLRLAYVHDFYDDNPVVTASLLGSGASFTTSGTDLDRNAAEL 239
|
250 260
....*....|....*....|...
gi 2304590498 992 KAGAEVAVNENATLSLGYGGLLS 1014
Cdd:smart00869 240 GLGLSAKLSNGLSLSLNYDGEFG 262
|
|
| Peptidases_S8_C5a_Peptidase |
cd07475 |
Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), ... |
69-418 |
1.32e-31 |
|
Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), is a highly specific protease and adhesin/invasin. The subtilisin-like protease domain is located at the N-terminus and contains a protease-associated domain inserted into a loop. There are three fibronectin type III (Fn) domains at the C-terminus. SCP binds to integrins with the help of Arg-Gly-Asp motifs which are thought to stabilize conformational changes required for substrate binding. Peptidases S8 or Subtilases are a serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173801 [Multi-domain] Cd Length: 346 Bit Score: 127.00 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 69 GYTGKGQKVGIFDTPVN-RHPEFAGDGKLINVVTEGYRAytDPHRPGINAG----DRFYF---------DGTFHFYSGSQ 134
Cdd:cd07475 7 GYKGEGMVVAVIDSGVDpTHDAFRLDDDSKAKYSEEFEA--KKKKAGIGYGkyynEKVPFaynyadnndDILDEDDGSSH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 135 GMlsnhgvHVAGISAAN----RDGIGMHGVAFDSQVISV---DNDNDGPAYGE--FLGLDGAVtnagwqamiNSGARVIN 205
Cdd:cd07475 85 GM------HVAGIVAGNgdeeDNGEGIKGVAPEAQLLAMkvfSNPEGGSTYDDayAKAIEDAV---------KLGADVIN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 206 NSWGvsipdflSDGGrdpnalhfelkdaqeqfdqvkpllGSLAGAGYQGAIDAARKN-ILVLFAAGNDGNYNQPDViSGL 284
Cdd:cd07475 150 MSLG-------STAG------------------------FVDLDDPEQQAIKRAREAgVVVVVAAGNDGNSGSGTS-KPL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 285 AYFVPD--------IAPNWLSVASVaqDAASTNSVPYTISSFSSrCGYTASFC----VSSPGSKIYSTVANGSdpanlvs 352
Cdd:cd07475 198 ATNNPDtgtvgspaTADDVLTVASA--NKKVPNPNGGQMSGFSS-WGPTPDLDlkpdITAPGGNIYSTVNDNT------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 353 dYGNKNGTSMATPHVTGAVAVLLQR----FPYMSSAQIADVLKT----TATDMGAPGIDALY------GWGMINLGKAIN 418
Cdd:cd07475 268 -YGYMSGTSMASPHVAGASALVKQRlkekYPKLSGEELVDLVKNllmnTATPPLDSEDTKTYysprrqGAGLIDVAKAIA 346
|
|
| Peptidases_S8_Subtilisin_like |
cd07473 |
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ... |
140-395 |
3.36e-27 |
|
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173799 [Multi-domain] Cd Length: 259 Bit Score: 111.90 E-value: 3.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 140 HGVHVAGISAANRD-GIGMHGVAFDSQVISV---DNDNDGPAYGEFLGLDGAVTNagwqaminsGARVINNSWGvsipdf 215
Cdd:cd07473 65 HGTHVAGIIGAVGNnGIGIAGVAWNVKIMPLkflGADGSGTTSDAIKAIDYAVDM---------GAKIINNSWG------ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 216 lsdgGRDPNALHFElkdaqeqfdqvkpllgslagagyqgAI-DAARKNILVLFAAGNDGNYNQPDVISGLAYFVPDIapn 294
Cdd:cd07473 130 ----GGGPSQALRD-------------------------AIaRAIDAGILFVAAAGNDGTNNDKTPTYPASYDLDNI--- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 295 wLSVASVAQDAastnsvpyTISSFSSrcGYTASFCVSSPGSKIYSTVANGsdpanlvsDYGNKNGTSMATPHVTGAVAVL 374
Cdd:cd07473 178 -ISVAATDSND--------ALASFSN--YGKKTVDLAAPGVDILSTSPGG--------GYGYMSGTSMATPHVAGAAALL 238
|
250 260
....*....|....*....|.
gi 2304590498 375 LQRFPYMSSAQIADVLKTTAT 395
Cdd:cd07473 239 LSLNPNLTAAQIKDAILSSAD 259
|
|
| Peptidases_S8_Kp43_protease |
cd04842 |
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 ... |
69-378 |
1.40e-26 |
|
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 or Subtilase clan of proteases. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Kp43 is topologically similar to kexin and furin both of which are proprotein convertases, but differ in amino acids sequence and the position of its C-terminal barrel. Kp43 has 3 Ca2+ binding sites that differ from the corresponding sites in the other known subtilisin-like proteases. KP-43 protease is known to be an oxidation-resistant protease when compared with the other subtilisin-like proteases
Pssm-ID: 173791 [Multi-domain] Cd Length: 293 Bit Score: 110.88 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 69 GYTGKGQKVGIFDTPVNR-HPEFAgdgklinvvtegyraytDPHRPGINAGDR--FYFDgtfhFYSGSQGMLSNHGVHVA 145
Cdd:cd04842 3 GLTGKGQIVGVADTGLDTnHCFFY-----------------DPNFNKTNLFHRkiVRYD----SLSDTKDDVDGHGTHVA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 146 GISAANR----DGIGMHGVAFDSQVISVDNDNDGPAYGEFLGLDGAVTNAGwqamiNSGARVINNSWGVSIPDFLSDggr 221
Cdd:cd04842 62 GIIAGKGndssSISLYKGVAPKAKLYFQDIGDTSGNLSSPPDLNKLFSPMY-----DAGARISSNSWGSPVNNGYTL--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 222 dpnalhfelkDAQEqFDQVkpllgslagagyqgAIDAarKNILVLFAAGNDGNYNQPDVISglayfvPDIAPNWLSVASV 301
Cdd:cd04842 134 ----------LARA-YDQF--------------AYNN--PDILFVFSAGNDGNDGSNTIGS------PATAKNVLTVGAS 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 302 AQ-------DAASTNSVPYTISSFSSRcGYTASFC----VSSPGSKIYSTVANGSDPANLVSD-YGNKNGTSMATPHVTG 369
Cdd:cd04842 181 NNpsvsngeGGLGQSDNSDTVASFSSR-GPTYDGRikpdLVAPGTGILSARSGGGGIGDTSDSaYTSKSGTSMATPLVAG 259
|
....*....
gi 2304590498 370 AVAVLLQRF 378
Cdd:cd04842 260 AAALLRQYF 268
|
|
| Peptidases_S8_Subtilisin_subset |
cd07477 |
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ... |
74-393 |
3.05e-25 |
|
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different subtilisins: Pro-TK-subtilisin, subtilisin Carlsberg, serine protease Pb92 subtilisin, and BPN subtilisins just to name a few. Pro-TK-subtilisin is a serine protease from the hyperthermophilic archaeon Thermococcus kodakaraensis and consists of a signal peptide, a propeptide, and a mature domain. TK-subtilisin is matured from pro-TK-subtilisin upon autoprocessing and degradation of the propeptide. Unlike other subtilisins though, the folding of the unprocessed form of pro-TK-subtilisin is induced by Ca2+ binding which is almost completed prior to autoprocessing. Ca2+ is required for activity unlike the bacterial subtilisins. The propeptide is not required for folding of the mature domain unlike the bacterial subtilases because of the stability produced from Ca2+ binding. Subtilisin Carlsberg is extremely similar in structure to subtilisin BPN'/Novo thought it has a 30% difference in amino acid sequence. The substrate binding regions are also similar and 2 possible Ca2+ binding sites have been identified recently. Subtilisin Carlsberg possesses the highest commercial importance as a proteolytic additive for detergents. Serine protease Pb92, the serine protease from the alkalophilic Bacillus strain PB92, also contains two calcium ions and the overall folding of the polypeptide chain closely resembles that of the subtilisins. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173803 [Multi-domain] Cd Length: 229 Bit Score: 105.31 E-value: 3.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 74 GQKVGIFDTPV-NRHPEFAGdgkliNVVTegyraytdphrpGINagdrfYFDGTFHFYSGSQGmlsnHGVHVAGISAANR 152
Cdd:cd07477 1 GVKVAVIDTGIdSSHPDLKL-----NIVG------------GAN-----FTGDDNNDYQDGNG----HGTHVAGIIAALD 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 153 DGIGMHGVAFDSQVISVDN-DNDGPAYGEFL--GLDGAvtnagwqamINSGARVINnswgvsipdfLSDGGRDPNAlhfE 229
Cdd:cd07477 55 NGVGVVGVAPEADLYAVKVlNDDGSGTYSDIiaGIEWA---------IENGMDIIN----------MSLGGPSDSP---A 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 230 LKDAQEQFDQvkpllgslagagyqgaidaarKNILVLFAAGNDGNynqpdviSGLAYFVPDIAPNWLSVASVAQDaastn 309
Cdd:cd07477 113 LREAIKKAYA---------------------AGILVVAAAGNSGN-------GDSSYDYPAKYPSVIAVGAVDSN----- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 310 svpYTISSFSSrcgYTASFCVSSPGSKIYSTVANGsdpanlvsDYGNKNGTSMATPHVTGAVAVLLQRFPYMSSAQIADV 389
Cdd:cd07477 160 ---NNRASFSS---TGPEVELAAPGVDILSTYPNN--------DYAYLSGTSMATPHVAGVAALVWSKRPELTNAQVRQA 225
|
....
gi 2304590498 390 LKTT 393
Cdd:cd07477 226 LNKT 229
|
|
| YhjY |
COG5571 |
Uncharacterized conserved protein YhjY, contains autotransporter beta-barrel domain [General ... |
493-1030 |
4.65e-25 |
|
Uncharacterized conserved protein YhjY, contains autotransporter beta-barrel domain [General function prediction only];
Pssm-ID: 444313 [Multi-domain] Cd Length: 648 Bit Score: 111.51 E-value: 4.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 493 GAGILVLTGNNTYAGPTLVNQGRLAINGSVTSAVSVQSGGIVGGSGTVGSLTARRGGTVAPGNSIGTLNVAGNVSFE-PG 571
Cdd:COG5571 103 GGGASGLAGGAGGAGGTAAAGGAAAAGGGAAGNAATAAAAAAAGTALQLSGLTTAGAVGGVAGTAALNGATANTGLGaAA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 572 SRYAVEVGPNGQSDRIQSSGAATIGGGEVAVTLENSANLLTQSEVRSLLGQQYTILSAQQGVSGQFDAVAPNYLFLGTGL 651
Cdd:COG5571 183 ALAAAAAAAAAAAAAAAAAAAAATAAAAAAAAAAAAAVLASPAPAAGGAAAAAAGAAAAAASAAANAATQANLLLLALAL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 652 SYQPTGVTLSVGRNGTSFASVAQTSNERAVAAAADALAAGNPVYESLLTSGTAG---------EARQAFRQLSGQIHADI 722
Cdd:COG5571 263 GSNGNAVGLNAVGLANEAAAPGAVGGDAGSTGATPSTLSSASCVASSLTAANANtlyaaadtaGPAGATAALAAAAAAVL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 723 ASALVNDSRYLREALNGRLRQAEGLASSSAIKADEDGAWAQLlGAWDHASGDANATGYQASTYGVLVGLDSAVAGDGRLG 802
Cdd:COG5571 343 ASAAAVAQAALALAAAGGQARSLAVAAGQGRGARGGQTRGGG-GAGGTTGGGVGAGGGDGDGPNLTLGVDYRLSDNLLLG 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 803 VATGYTRTSLHGGYGSKADSDNYHLAAYGDKQFGALALRGGAGYTWHRIDTKRSVNYGMQSDRDTAKYSARTEQLFAEAG 882
Cdd:COG5571 422 AALSYGRQDLDFGDGGSYDARSTSLSLYAGYRAGGLWVDADLSYGDLDYDIRRHIRLGPATRTETGDTDGSQWGARLTAG 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 883 YGVQGEWLNLEPFVNLAYVNFENNGIAESGGAA-ALRGDKQHTDATVSTLGLRADTAWqvtpGTTVALRSELGWQHQYGG 961
Cdd:COG5571 502 YDFTAGRLRTGPFAGLDYQKVKVDGYTETGAGStALSFGDQDRDSLVGSLGWRADYQL----LGRFNPYAEVAYEHEFGD 577
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2304590498 962 LDRGTGLRFNGGNAP-FVVDSVPVSRDGMVLKAGAEVAVNENATLSLGYGGLLSQNHQ-DNSVNAGFTWRF 1030
Cdd:COG5571 578 DDRDVTAGLASLPAGsFSLPAAAPDKNWGRATLGASAALTNGVSLFAGYSGTFGRDDGrQTSVNLGLSARF 648
|
|
| T7SS_mycosin |
TIGR03921 |
type VII secretion-associated serine protease mycosin; Members of this family are ... |
71-462 |
1.11e-24 |
|
type VII secretion-associated serine protease mycosin; Members of this family are subtilisin-related serine proteases, found strictly in the Actinobacteria and associated with type VII secretion operons. The designation mycosin is used for members from Mycobacterium. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair]
Pssm-ID: 274856 [Multi-domain] Cd Length: 350 Bit Score: 106.64 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 71 TGKGQKVGIFDTPVNRHPEFAGdgkliNVVTEGyraytDPHRPGINAGDRfyfDGtfhfysgsqgmlsnHGVHVAGISAA 150
Cdd:TIGR03921 11 TGAGVTVAVIDTGVDDHPRLPG-----LVLPGG-----DFVGSGDGTDDC---DG--------------HGTLVAGIIAG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 151 NRD-GIGMHGVAFDSQVISV-------DNDNDGPAYGEFLGLDGAVTNAgwqamINSGARVINNSWGVSIPdflSDGGRD 222
Cdd:TIGR03921 64 RPGeGDGFSGVAPDARILPIrqtsaafEPDEGTSGVGDLGTLAKAIRRA-----ADLGADVINISLVACLP---AGSGAD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 223 PNALhfelkdaqeqfdqvkpllgslaGAGYQGAIDaarKNILVLFAAGNDGNYNQPDVISGLAYFvpdiaPNWLSVASVA 302
Cdd:TIGR03921 136 DPEL----------------------GAAVRYALD---KGVVVVAAAGNTGGDGQKTTVVYPAWY-----PGVLAVGSID 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 303 QDAastnsvpyTISSFSSRCGYTAsfcVSSPGSKIYSTVANGSDPANLVsdygnknGTSMATPHVTGAVAVLLQRFPYMS 382
Cdd:TIGR03921 186 RDG--------TPSSFSLPGPWVD---LAAPGENIVSLSPGGDGLATTS-------GTSFAAPFVSGTAALVRSRFPDLT 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 383 SAQIADVLKTTATDMGAPGIDALYGWGMINLGKAINGpgmfytveDIPAEFRIPDPTGVAYGPTQFVANIPGRGAEVDAG 462
Cdd:TIGR03921 248 AAQVRRRIEATADHPARGGRDDYVGYGVVDPVAALTG--------ELPPEDGRPLRPAPAPARPVAAPAPPPPPDDTPRG 319
|
|
| Peptidases_S8_Thermitase_like |
cd07484 |
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ... |
51-398 |
1.24e-24 |
|
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, trypsin-related serine protease with a very high specific activity. It contains a subtilisin like domain. The tertiary structure of thermitase is similar to that of subtilisin BPN'. It contains a Asp/His/Ser catalytic triad. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53 the it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.
Pssm-ID: 173810 [Multi-domain] Cd Length: 260 Bit Score: 104.27 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 51 FNANWGLGAIHADEAYAAGyTGKGQKVGIFDTPVNR-HPEFAGDgklinVVTEGYRAYTDphrpginagdrfyfDGTFHF 129
Cdd:cd07484 7 YSYQWNLDQIGAPKAWDIT-GGSGVTVAVVDTGVDPtHPDLLKV-----KFVLGYDFVDN--------------DSDAMD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 130 YSGsqgmlsnHGVHVAGISAANRD-GIGMHGVAFDSQVISVDNDNdgpAYGEflGLDGAVTNA-GWQAmiNSGARVINNS 207
Cdd:cd07484 67 DNG-------HGTHVAGIIAAATNnGTGVAGVAPKAKIMPVKVLD---ANGS--GSLADIANGiRYAA--DKGAKVINLS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 208 WGvsipdflsdGGRDPNALhfelkdaqeqfdqvkpllgslagagyQGAID-AARKNILVLFAAGNDGNynqpdviSGLAY 286
Cdd:cd07484 133 LG---------GGLGSTAL--------------------------QEAINyAWNKGVVVVAAAGNEGV-------SSVSY 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 287 fvPDIAPNWLSVASVAQDaastnsvpYTISSFSSrcgYTASFCVSSPGSKIYSTVANGsdpanlvsDYGNKNGTSMATPH 366
Cdd:cd07484 171 --PAAYPGAIAVAATDQD--------DKRASFSN---YGKWVDVSAPGGGILSTTPDG--------DYAYMSGTSMATPH 229
|
330 340 350
....*....|....*....|....*....|..
gi 2304590498 367 VTGaVAVLLQRFPYMSSAQIADVLKTTATDMG 398
Cdd:cd07484 230 VAG-VAALLYSQGPLSASEVRDALKKTADDIG 260
|
|
| Peptidases_S8_1 |
cd07487 |
Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the ... |
72-395 |
1.07e-22 |
|
Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173812 [Multi-domain] Cd Length: 264 Bit Score: 98.81 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 72 GKGQKVGIFDTPV-NRHPEFAGDGKLInvvtegyraytdphrpginAGDRFYFDGTFHFYSGSqgmlsNHGVHVAGISAA 150
Cdd:cd07487 1 GKGITVAVLDTGIdAPHPDFDGRIIRF-------------------ADFVNTVNGRTTPYDDN-----GHGTHVAGIIAG 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 151 N-RDGIG-MHGVAFDSQVISV---DNDNDGPAYGEFLGLDGAVTNAGwqamiNSGARVINNSWGVSipdFLSDGGRDPna 225
Cdd:cd07487 57 SgRASNGkYKGVAPGANLVGVkvlDDSGSGSESDIIAGIDWVVENNE-----KYNIRVVNLSLGAP---PDPSYGEDP-- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 226 lhfelkdaqeqFDQvkpllgslagagyqgAIDAARKN-ILVLFAAGNDGnynqPDVISglaYFVPDIAPNWLSVASVaqD 304
Cdd:cd07487 127 -----------LCQ---------------AVERLWDAgIVVVVAAGNSG----PGPGT---ITSPGNSPKVITVGAV--D 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 305 AASTNSvpYTISSFSSRcGYTAS-FC---VSSPGSKIYSTVANGSDP-ANLVSDYGNKNGTSMATPHVTGAVAVLLQRFP 379
Cdd:cd07487 172 DNGPHD--DGISYFSSR-GPTGDgRIkpdVVAPGENIVSCRSPGGNPgAGVGSGYFEMSGTSMATPHVSGAIALLLQANP 248
|
330
....*....|....*.
gi 2304590498 380 YMSSAQIADVLKTTAT 395
Cdd:cd07487 249 ILTPDEVKCILRDTAT 264
|
|
| Peptidases_S8_S53 |
cd00306 |
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ... |
75-393 |
2.51e-22 |
|
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) family include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.
Pssm-ID: 173787 [Multi-domain] Cd Length: 241 Bit Score: 97.27 E-value: 2.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 75 QKVGIFDTPVNR-HPEFAGDGklinvvtegyraytDPHRPGINAGDRFYFDGTFHFYSGsqgmlsnHGVHVAGISAANRD 153
Cdd:cd00306 1 VTVAVIDTGVDPdHPDLDGLF--------------GGGDGGNDDDDNENGPTDPDDGNG-------HGTHVAGIIAASAN 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 154 GIGMHGVAFDSQVISVDNDNDgpaygEFLGLDGAVTNAGWQAMINSGARVINNSWGvsipdflSDGGRDPNALHFELKDA 233
Cdd:cd00306 60 NGGGVGVAPGAKLIPVKVLDG-----DGSGSSSDIAAAIDYAAADQGADVINLSLG-------GPGSPPSSALSEAIDYA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 234 qeqfdqvkpllgslagagyqgaidAARKNILVLFAAGNDGNYNQPDVISGLAYfvpdiaPNWLSVASVAQDaastnsvpY 313
Cdd:cd00306 128 ------------------------LAKLGVLVVAAAGNDGPDGGTNIGYPAAS------PNVIAVGAVDRD--------G 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 314 TISSFSSRCGYTASFCVssPGSKIYSTVANGSDPanlvsdYGNKNGTSMATPHVTGAVAVLLQRFPYMSSAQIADVLKTT 393
Cdd:cd00306 170 TPASPSSNGGAGVDIAA--PGGDILSSPTTGGGG------YATLSGTSMAAPIVAGVAALLLSANPDLTPAQVKAALLST 241
|
|
| Peptidases_S8_Fervidolysin_like |
cd07485 |
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ... |
64-393 |
3.14e-20 |
|
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans is an extracellular subtilisin-like keratinase. It is contains a signal peptide, a propeptide, and a catalytic region. The tertiary structure of fervidolysin is similar to that of subtilisin. It contains a Asp/His/Ser catalytic triad and is a member of the peptidase S8 (subtilisin and kexin) family. The catalytic triad is similar to that found in trypsin-like proteases, but it does not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.
Pssm-ID: 173811 [Multi-domain] Cd Length: 273 Bit Score: 91.78 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 64 EAYAAGYTGKGQKVGIFDTPVN-RHPEFAGdgkliNVVTEGYRAYTDPHRPGINAGDrfyfDGTFHFYSGSqgmlsnHGV 142
Cdd:cd07485 1 AAWEFGTGGPGIIVAVVDTGVDgTHPDLQG-----NGDGDGYDPAVNGYNFVPNVGD----IDNDVSVGGG------HGT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 143 HVAG-ISAANRDGIGMHGVAFDSQV-----ISVDNDNDGPAYGeflGLDGAVTNAGWQAmiNSGARVINNSWGvsipdfl 216
Cdd:cd07485 66 HVAGtIAAVNNNGGGVGGIAGAGGVapgvkIMSIQIFAGRYYV---GDDAVAAAIVYAA--DNGAVILQNSWG------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 217 sdgGRDPNALHFELKDAqeqFDQvkpllgslagagyqgAIDAAR----KNILVLFAAGNDGnynqpdviSGLAYFvPDIA 292
Cdd:cd07485 134 ---GTGGGIYSPLLKDA---FDY---------------FIENAGgsplDGGIVVFSAGNSY--------TDEHRF-PAAY 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 293 PNWLSVASVAQDaastnsvpYTISSFSSRCGYTAsfcVSSPG-SKIYSTVANGSDPANlvSDYGNKNGTSMATPHVTGAV 371
Cdd:cd07485 184 PGVIAVAALDTN--------DNKASFSNYGRWVD---IAAPGvGTILSTVPKLDGDGG--GNYEYLSGTSMAAPHVSGVA 250
|
330 340
....*....|....*....|...
gi 2304590498 372 AVLLQRFPYMSSA-QIADVLKTT 393
Cdd:cd07485 251 ALVLSKFPDVFTPeQIRKLLEES 273
|
|
| Peptidases_S8_subtilisin_Vpr-like |
cd07474 |
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ... |
72-395 |
4.59e-20 |
|
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic (lantibiotic) subtilin in Bacillus subtilis ATCC 6633 includes posttranslational modifications of the propeptide and proteolytic cleavage of the leader peptide. Vpr was identified as one of the proteases, along with WprA, that are capable of processing subtilin. Asp, Ser, His triadPeptidases S8 or Subtilases are a serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173800 [Multi-domain] Cd Length: 295 Bit Score: 92.01 E-value: 4.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 72 GKGQKVGIFDTPVN-RHPEFAGDGKLINVVTEGYRAYTDPHRPG-INAGDRFYFDGTFHFYSGsqgmlsnHGVHVAGISA 149
Cdd:cd07474 1 GKGVKVAVIDTGIDyTHPDLGGPGFPNDKVKGGYDFVDDDYDPMdTRPYPSPLGDASAGDATG-------HGTHVAGIIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 150 ANRDGIG-MHGVAFDSQVISVdndndgpaygEFLGLDGAVTN----AGWQAMINSGARVINNSWGVSIPdflsdGGRDPN 224
Cdd:cd07474 74 GNGVNVGtIKGVAPKADLYAY----------KVLGPGGSGTTdviiAAIEQAVDDGMDVINLSLGSSVN-----GPDDPD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 225 ALhfelkdaqeqfdqvkpllgslagagyqgAID-AARKNILVLFAAGNDG--NYNQPDvisglayfvPDIAPNWLSV-AS 300
Cdd:cd07474 139 AI----------------------------AINnAVKAGVVVVAAAGNSGpaPYTIGS---------PATAPSAITVgAS 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 301 VAQDAASTNsvpyTISSFSSRCGYTASFC----VSSPGSKIYSTVANGSDpanlvsDYGNKNGTSMATPHVTGAVAVLLQ 376
Cdd:cd07474 182 TVADVAEAD----TVGPSSSRGPPTSDSAikpdIVAPGVDIMSTAPGSGT------GYARMSGTSMAAPHVAGAAALLKQ 251
|
330
....*....|....*....
gi 2304590498 377 RFPYMSSAQIADVLKTTAT 395
Cdd:cd07474 252 AHPDWSPAQIKAALMNTAK 270
|
|
| Peptidases_S8_Subtilisin_Novo-like |
cd07483 |
Peptidase S8 family domain in Subtilisin_Novo-like proteins; Subtilisins are a group of ... |
140-395 |
2.18e-17 |
|
Peptidase S8 family domain in Subtilisin_Novo-like proteins; Subtilisins are a group of alkaline proteinases originating from different strains of Bacillus subtilis. Novo is one of the strains that produced enzymes belonging to this group. The enzymes obtained from the Novo and BPN' strains are identical. The Carlsburg and Novo subtilisins are thought to have arisen from a common ancestral protein. They have similar peptidase and esterase activities, pH profiles, catalyze transesterification reactions, and are both inhibited by diispropyl fluorophosphate, though they differ in 85 positions in the amino acid sequence. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin.. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173809 [Multi-domain] Cd Length: 291 Bit Score: 83.95 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 140 HGVHVAGISAANRD-GIGMHGVAFDSQVISVDNDNDGPAYgeflglDGAVTNAGWQAmINSGARVINNSWGVSIpdflsd 218
Cdd:cd07483 87 HGTHVAGIIAAVRDnGIGIDGVADNVKIMPLRIVPNGDER------DKDIANAIRYA-VDNGAKVINMSFGKSF------ 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 219 ggrdpnALHFELKDAQEQFdqvkpllgslagagyqgaidAARKNILVLFAAGNDGNY--NQPDVISGLAYFVPDIAPNWL 296
Cdd:cd07483 154 ------SPNKEWVDDAIKY--------------------AESKGVLIVHAAGNDGLDldITPNFPNDYDKNGGEPANNFI 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 297 SVASVAQDAASTnsvpyTISSFSSRCGYTASfcVSSPGSKIYSTVANgsdpanlvSDYGNKNGTSMATPHVTGAVAVLLQ 376
Cdd:cd07483 208 TVGASSKKYENN-----LVANFSNYGKKNVD--VFAPGERIYSTTPD--------NEYETDSGTSMAAPVVSGVAALIWS 272
|
250
....*....|....*....
gi 2304590498 377 RFPYMSSAQIADVLKTTAT 395
Cdd:cd07483 273 YYPNLTAKEVKQIILESGV 291
|
|
| Peptidases_S8_5 |
cd07489 |
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ... |
62-418 |
2.08e-16 |
|
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173814 [Multi-domain] Cd Length: 312 Bit Score: 81.50 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 62 ADEAYAAGYTGKGQKVGIFDTPVN-RHPEFAG---DGKLI----NVVTEGYRAyTDPHRPGINAGDrfyfdgtfhfysgS 133
Cdd:cd07489 2 VDKLHAEGITGKGVKVAVVDTGIDyTHPALGGcfgPGCKVaggyDFVGDDYDG-TNPPVPDDDPMD-------------C 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 134 QGmlsnHGVHVAGISAANRDGIGMHGVAFDSQVIsvdndndgpAYGEFlGLDGAVTN----AGWQAMINSGARVINNSWG 209
Cdd:cd07489 68 QG----HGTHVAGIIAANPNAYGFTGVAPEATLG---------AYRVF-GCSGSTTEdtiiAAFLRAYEDGADVITASLG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 210 VsipdflsDGGRDPNALhfelkdaqeqfdqvkpllgslagagyqgAIDAAR---KNILVLFAAGNDGNYnqpdvisGLAY 286
Cdd:cd07489 134 G-------PSGWSEDPW----------------------------AVVASRivdAGVVVTIAAGNDGER-------GPFY 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 287 -FVPDIAPNWLSVASVAqdaastnsvpytiSSFSSRcGYTASFC----VSSPGSKIYSTVANGSDPANLVSdygnknGTS 361
Cdd:cd07489 172 aSSPASGRGVIAVASVD-------------SYFSSW-GPTNELYlkpdVAAPGGNILSTYPLAGGGYAVLS------GTS 231
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2304590498 362 MATPHVTGAVAVLLQ-RFPYMSSAQIADVLKTTATDM-GAPGIDALYGW--------GMINLGKAIN 418
Cdd:cd07489 232 MATPYVAGAAALLIQaRHGKLSPAELRDLLASTAKPLpWSDGTSALPDLapvaqqgaGLVNAYKALY 298
|
|
| Peptidases_S8_3 |
cd04852 |
Peptidase S8 family domain, uncharacterized subfamily 3; This family is a member of the ... |
55-395 |
7.33e-15 |
|
Peptidase S8 family domain, uncharacterized subfamily 3; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173795 [Multi-domain] Cd Length: 307 Bit Score: 76.48 E-value: 7.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 55 WGLGAIHADEAyaagytGKGQKVGIFDTPVN-RHPEFAGDGklinvvtegyrAYTDPHR-PGINA--------------- 117
Cdd:cd04852 18 WGGSLLGAANA------GEGIIIGVLDTGIWpEHPSFADVG-----------GGPYPHTwPGDCVtgedfnpfscnnkli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 118 GDRFYFDGTFHFYSGSQGMLSN-------HGVHVAGISAANR-DGIGMHGVAFdsqvisvdndndGPAYG---------- 179
Cdd:cd04852 81 GARYFSDGYDAYGGFNSDGEYRsprdydgHGTHTASTAAGNVvVNASVGGFAF------------GTASGvaprariavy 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 180 ----EFLGLDGAVTNAGWQAMINSGARVINNSWGVSIPDFLSDggrdpnalhfelkdaqeqfdqvkpllgSLAgagyQGA 255
Cdd:cd04852 149 kvcwPDGGCFGSDILAAIDQAIADGVDVISYSIGGGSPDPYED---------------------------PIA----IAF 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 256 IDAARKNILVLFAAGNDGnynqPDvisglAYFVPDIAPnWlsVASVAqdaASTnSVPYtissfssrcgytasfcVSSPGS 335
Cdd:cd04852 198 LHAVEAGIFVAASAGNSG----PG-----ASTVPNVAP-W--VTTVA---AST-LKPD----------------IAAPGV 245
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2304590498 336 KIYS--TVANGSDPANLVSDYGNKNGTSMATPHVTGAVAVLLQRFPYMSSAQIADVLKTTAT 395
Cdd:cd04852 246 DILAawTPEGADPGDARGEDFAFISGTSMASPHVAGVAALLKSAHPDWSPAAIKSALMTTAY 307
|
|
| Peptidases_S8_Protein_convertases_Kexins_Furin-lik |
cd04059 |
Peptidase S8 family domain in Protein convertases; Protein convertases, whose members include ... |
60-376 |
2.30e-14 |
|
Peptidase S8 family domain in Protein convertases; Protein convertases, whose members include furins and kexins, are members of the peptidase S8 or Subtilase clan of proteases. They have an Asp/His/Ser catalytic triad that is not homologous to trypsin. Kexins are involved in the activation of peptide hormones, growth factors, and viral proteins. Furin cleaves cell surface vasoactive peptides and proteins involved in cardiovascular tissue remodeling in the TGN, at cell surface, or in endosomes but rarely in the ER. Furin also plays a key role in blood pressure regulation though the activation of transforming growth factor (TGF)-beta. High specificity is seen for cleavage after dibasic (Lys-Arg or Arg-Arg) or multiple basic residues in protein convertases. There is also strong sequence conservation.
Pssm-ID: 173789 [Multi-domain] Cd Length: 297 Bit Score: 74.90 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 60 IHADEAYAAGYTGKGQKVGIFDTPVN-RHPEFAGdgkliNVVTEGYRAYTDPhrpginagdrfyFDGTFHFYSGSQgmls 138
Cdd:cd04059 26 LNVTPAWEQGITGKGVTVAVVDDGLEiTHPDLKD-----NYDPEASYDFNDN------------DPDPTPRYDDDN---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 139 NHGVHVAGISAANRD-GIGMHGVAFDSQVISVdndndgpaygEFLglDGAVTNAGW-QAMINSG--ARVINNSWGVSiPD 214
Cdd:cd04059 85 SHGTRCAGEIAAVGNnGICGVGVAPGAKLGGI----------RML--DGDVTDVVEaESLGLNPdyIDIYSNSWGPD-DD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 215 FLSDGGRDPNAlhfelkdaQEQFDQvkpllGSLAGAGYQGAIdaarknilVLFAAGNDGNYNQPDVISGLA--YFVpdia 292
Cdd:cd04059 152 GKTVDGPGPLA--------QRALEN-----GVTNGRNGKGSI--------FVWAAGNGGNLGDNCNCDGYNnsIYT---- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 293 pnwLSVASVAQDAastnsvpyTISSFSSRCgytASFCVSSPGSkiystvANGSDPANLVSD--YGNK------NGTSMAT 364
Cdd:cd04059 207 ---ISVSAVTANG--------VRASYSEVG---SSVLASAPSG------GSGNPEASIVTTdlGGNCnctsshNGTSAAA 266
|
330
....*....|..
gi 2304590498 365 PHVTGAVAVLLQ 376
Cdd:cd04059 267 PLAAGVIALMLE 278
|
|
| Peptidases_S8_13 |
cd07496 |
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ... |
140-393 |
2.51e-14 |
|
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173820 [Multi-domain] Cd Length: 285 Bit Score: 74.64 E-value: 2.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 140 HGVHVAGISAANRD-GIGMHGVAFDSQVISV---------DND-NDGPAYGEFLGLDGAVTNAgwqaminSGARVINNSW 208
Cdd:cd07496 73 HGTHVAGTIAAVTNnGVGVAGVAWGARILPVrvlgkcggtLSDiVDGMRWAAGLPVPGVPVNP-------NPAKVINLSL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 209 GvsipdflSDGGRDPNalhfelkdaqeqfdqvkpllgslagagYQGAIDAAR-KNILVLFAAGNDGNYNQPDvisglayf 287
Cdd:cd07496 146 G-------GDGACSAT---------------------------MQNAINDVRaRGVLVVVAAGNEGSSASVD-------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 288 VPDIAPNWLSVASVAQDAastnsvpyTISSFSSrcgYTASFCVSSPGSKIYSTVANGSDPANLVSD-------YGNKNGT 360
Cdd:cd07496 184 APANCRGVIAVGATDLRG--------QRASYSN---YGPAVDVSAPGGDCASDVNGDGYPDSNTGTtspggstYGFLQGT 252
|
250 260 270
....*....|....*....|....*....|...
gi 2304590498 361 SMATPHVTGAVAVLLQRFPYMSSAQIADVLKTT 393
Cdd:cd07496 253 SMAAPHVAGVAALMKSVNPSLTPAQIESLLQST 285
|
|
| Peptidases_S8_BacillopeptidaseF-like |
cd07481 |
Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and ... |
138-395 |
3.39e-14 |
|
Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and secretes proteases and other types of exoenzymes at the end of the exponential phase of growth. The ones that make up this group is known as bacillopeptidase F, encoded by bpr, a serine protease with high esterolytic activity which is inhibited by PMSF. Like other members of the peptidases S8 family these have a Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity.
Pssm-ID: 173807 [Multi-domain] Cd Length: 264 Bit Score: 73.95 E-value: 3.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 138 SNHGVHVAGISAANRDGIGMHGVAFDSQVISVDNdndgpaYGEFLGLDGAVTNAGwQAMINS------------GARVIN 205
Cdd:cd07481 52 NGHGTHTMGTMVGNDGDGQQIGVAPGARWIACRA------LDRNGGNDADYLRCA-QWMLAPtdsagnpadpdlAPDVIN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 206 NSWGvsipdflSDGGRDPnalhfelkdaqeqfdqvkpllgslagaGYQGAIDAARK-NILVLFAAGNDGnynqPDVISGL 284
Cdd:cd07481 125 NSWG-------GPSGDNE---------------------------WLQPAVAAWRAaGIFPVFAAGNDG----PRCSTLN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 285 AYfvPDIAPNWLSVASVAQDAAstnsvpytISSFSSRCGYTASFC---VSSPGSKIYSTVANGSdpanlvsdYGNKNGTS 361
Cdd:cd07481 167 AP--PANYPESFAVGATDRNDV--------LADFSSRGPSTYGRIkpdISAPGVNIRSAVPGGG--------YGSSSGTS 228
|
250 260 270
....*....|....*....|....*....|....*.
gi 2304590498 362 MATPHVTGAVAVLLQRFPYMSSA--QIADVLKTTAT 395
Cdd:cd07481 229 MAAPHVAGVAALLWSANPSLIGDvdATEAILTETAR 264
|
|
| Peptidases_S53_like |
cd05562 |
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ... |
258-417 |
1.32e-13 |
|
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include endopeptidases and exopeptidases. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of Asn in subtilisin. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. Characterized sedolisins include Kumamolisin, an extracellular calcium-dependent thermostable endopeptidase from Bacillus. The enzyme is synthesized with a 188 amino acid N-terminal preprotein region which is cleaved after the extraction into the extracellular space with low pH. One kumamolysin paralog, kumamolisin-As, is believed to be a collagenase. TPP1 is a serine protease that functions as a tripeptidyl exopeptidase as well as an endopeptidase. Less is known about PSCP from Pseudomonas which is thought to be an aspartic proteinase.
Pssm-ID: 173798 [Multi-domain] Cd Length: 275 Bit Score: 72.33 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 258 AARKNILVLFAAGNDGNynqpdviSGLAYFVPDiAPNWLSVASVA-QDAASTNSVPYTISSFSSRCGYTASFCVSSPGSK 336
Cdd:cd05562 119 VASPGVLYFSSAGNDGQ-------SGSIFGHAA-APGAIAVGAVDyGNTPAFGSDPAPGGTPSSFDPVGIRLPTPEVRQK 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 337 IYSTVANGSDPANLVSDYGNKN--GTSMATPHVTGAVAVLLQRFPYMSSAQIADVLKTTATDMGAPGIDALYGWGMINLG 414
Cdd:cd05562 191 PDVTAPDGVNGTVDGDGDGPPNffGTSAAAPHAAGVAALVLSANPGLTPADIRDALRSTALDMGEPGYDNASGSGLVDAD 270
|
...
gi 2304590498 415 KAI 417
Cdd:cd05562 271 RAV 273
|
|
| Peptidases_S8_15 |
cd07498 |
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ... |
76-393 |
2.69e-13 |
|
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173822 [Multi-domain] Cd Length: 242 Bit Score: 70.83 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 76 KVGIFDTPVN-RHPEFAGDGKLINVVtegyraytDPHRPGINAGDRFyfdgtfhfysgsqgmlsNHGVHVAGISAANRD- 153
Cdd:cd07498 2 VVAIIDTGVDlNHPDLSGKPKLVPGW--------NFVSNNDPTSDID-----------------GHGTACAGVAAAVGNn 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 154 GIGMHGVAFDSQVISVdNDNDGPAYGEFLGLDGAVTNAGWQaminsGARVINNSWGVSIPDFLSDggrdpnalhfelkda 233
Cdd:cd07498 57 GLGVAGVAPGAKLMPV-RIADSLGYAYWSDIAQAITWAADN-----GADVISNSWGGSDSTESIS--------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 234 qeqfdqvkpllgslagAGYQGAIDAAR--KNILVLFAAGNDGNynqpDVISGLAYFvpdiaPNWLSVAsvaqdAASTNSv 311
Cdd:cd07498 116 ----------------SAIDNAATYGRngKGGVVLFAAGNSGR----SVSSGYAAN-----PSVIAVA-----ATDSND- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 312 pyTISSFSSrcgYTASFCVSSPGSKIYSTVA-NGSDPANLVSDYGNKNGTSMATPHVTGAVAVLLQRFPYMSSAQIADVL 390
Cdd:cd07498 165 --ARASYSN---YGNYVDLVAPGVGIWTTGTgRGSAGDYPGGGYGSFSGTSFASPVAAGVAALILSANPNLTPAEVEDIL 239
|
...
gi 2304590498 391 KTT 393
Cdd:cd07498 240 TST 242
|
|
| Peptidases_S8_PCSK9_ProteinaseK_like |
cd04077 |
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ... |
55-395 |
7.94e-13 |
|
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of proteases have a Asp/His/Ser catalytic triad that is not homologous to trypsin. This CD contains several members of this clan including: PCSK9 (Proprotein convertase subtilisin/kexin type 9), Proteinase_K, Proteinase_T, and other subtilisin-like serine proteases. PCSK9 posttranslationally regulates hepatic low-density lipoprotein receptors (LDLRs) by binding to LDLRs on the cell surface, leading to their degradation. The binding site of PCSK9 has been localized to the epidermal growth factor-like repeat A (EGF-A) domain of the LDLR. Characterized Proteinases K are secreted endopeptidases with a high degree of sequence conservation. Proteinases K are not substrate-specific and function in a wide variety of species in different pathways. It can hydrolyze keratin and other proteins with subtilisin-like specificity. The number of calcium-binding motifs found in these differ. Proteinase T is a novel proteinase from the fungus Tritirachium album Limber. The amino acid sequence of proteinase T as deduced from the nucleotide sequence is about 56% identical to that of proteinase K.
Pssm-ID: 173790 [Multi-domain] Cd Length: 255 Bit Score: 69.47 E-value: 7.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 55 WGLGAI-HAD-----EAYAAGYTGKGQKVGIFDTPVN-RHPEFAGdgklinvvtegyRAytdphRPGINAGDrfyfDGTF 127
Cdd:cd04077 1 WGLDRIsQRDlpldgTYYYDSSTGSGVDVYVLDTGIRtTHVEFGG------------RA-----IWGADFVG----GDPD 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 128 hfySGSQGmlsnHGVHVAGISAANRdgigmHGVAFDSQVISV---DNDNDGPAYGEFLGLDGAVTNAgwqamINSGAR-V 203
Cdd:cd04077 60 ---SDCNG----HGTHVAGTVGGKT-----YGVAKKANLVAVkvlDCNGSGTLSGIIAGLEWVANDA-----TKRGKPaV 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 204 INNSWGvsipdflsdGGRDPnALhfelkDAqeqfdqvkpllgslagagyqgAIDAA-RKNILVLFAAGNDG----NYNqp 278
Cdd:cd04077 123 ANMSLG---------GGAST-AL-----DA---------------------AVAAAvNAGVVVVVAAGNSNqdacNYS-- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 279 dvisglayfvPDIAPNWLSVASVAQDAastnsvpyTISSFSsrcGYTAsfCVS--SPGSKIYSTvANGSDpanlvSDYGN 356
Cdd:cd04077 165 ----------PASAPEAITVGATDSDD--------ARASFS---NYGS--CVDifAPGVDILSA-WIGSD-----TATAT 215
|
330 340 350
....*....|....*....|....*....|....*....
gi 2304590498 357 KNGTSMATPHVTGAVAVLLQRFPYMSSAQIADVLKTTAT 395
Cdd:cd04077 216 LSGTSMAAPHVAGLAAYLLSLGPDLSPAEVKARLLNLAT 254
|
|
| Peptidases_S8_CspA-like |
cd07478 |
Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts ... |
272-409 |
8.73e-13 |
|
Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts the spore peptidoglycan hydrolase (SleC) precursor to an active enzyme during germination of Clostridium perfringens S40 spores. Analysis of an enzyme fraction of GSP showed that it was composed of a gene cluster containing the processed forms of products of cspA, cspB, and cspC which are positioned in a tandem array just upstream of the 5' end of sleC. The amino acid sequences deduced from the nucleotide sequences of the csp genes showed significant similarity and showed a high degree of homology with those of the catalytic domain and the oxyanion binding region of subtilisin-like serine proteases. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173804 [Multi-domain] Cd Length: 455 Bit Score: 71.88 E-value: 8.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 272 DGNYN----QPDVISGLAYFVPDIAPNWLSVASVAQDA---ASTNSVPYTISSFSSRcGYTASFCV----SSPGSKIYST 340
Cdd:cd07478 309 DGRFDawlpSRGLLSENTRFLEPDPYTTLTIPGTARSVitvGAYNQNNNSIAIFSGR-GPTRDGRIkpdiAAPGVNILTA 387
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2304590498 341 VANGSdpanlvsdYGNKNGTSMATPHVTGAVAVLLQ------RFPYMSSAQIADVLKTTAT-DMGAPGIDALYGWG 409
Cdd:cd07478 388 SPGGG--------YTTRSGTSVAAAIVAGACALLLQwgivrgNDPYLYGEKIKTYLIRGARrRPGDEYPNPEWGYG 455
|
|
| Peptidases_S8_12 |
cd07480 |
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ... |
70-379 |
5.59e-11 |
|
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173806 [Multi-domain] Cd Length: 297 Bit Score: 64.70 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 70 YTGKGQKVGIFDTPVNR-HPEFAGdgklINVVTEGYRaytdphrPGINAGDRfyfDGtfhfysgsqgmlsnHGVHVAGIs 148
Cdd:cd07480 5 FTGAGVRVAVLDTGIDLtHPAFAG----RDITTKSFV-------GGEDVQDG---HG--------------HGTHCAGT- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 149 AANRDGIGM-HGVAFDSQ--VISVDNDNDGPAYGEFLgldgavtnAGWQAMINSGARVINNSWGVSIPDFLSDGgrDPNA 225
Cdd:cd07480 56 IFGRDVPGPrYGVARGAEiaLIGKVLGDGGGGDGGIL--------AGIQWAVANGADVISMSLGADFPGLVDQG--WPPG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 226 LHFelKDAQEQFDQVKPLLGSLAGAgyQGAIDAARKNILVLFAAGNDGNYNQ--PDVISglayfvPDIAPNWLSVASVAQ 303
Cdd:cd07480 126 LAF--SRALEAYRQRARLFDALMTL--VAAQAALARGTLIVAAAGNESQRPAgiPPVGN------PAACPSAMGVAAVGA 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2304590498 304 DAASTNSvpYTISSFSSrcgytASFCVSSPGSKIYStvangsdpANLVSDYGNKNGTSMATPHVTGAVAVLLQRFP 379
Cdd:cd07480 196 LGRTGNF--SAVANFSN-----GEVDIAAPGVDIVS--------AAPGGGYRSMSGTSMATPHVAGVAALWAEALP 256
|
|
| PTZ00262 |
PTZ00262 |
subtilisin-like protease; Provisional |
129-418 |
9.34e-11 |
|
subtilisin-like protease; Provisional
Pssm-ID: 240338 [Multi-domain] Cd Length: 639 Bit Score: 65.76 E-value: 9.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 129 FYSGSQGMLSN--HGVHVAGISAAN-RDGIGMHGVAFDSQVI---SVDNDNDGPAYGEFLGLDgavtnagwqAMINSGAR 202
Cdd:PTZ00262 367 FVNNDGGPMDDnyHGTHVSGIISAIgNNNIGIVGVDKRSKLIickALDSHKLGRLGDMFKCFD---------YCISREAH 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 203 VINNSWGVsipdflsdggrDPNALHFelkdaqeqFDQVKPLlgslagagyqgaidaARKNILVLFAAGN--DGNYNQPDV 280
Cdd:PTZ00262 438 MINGSFSF-----------DEYSGIF--------NESVKYL---------------EEKGILFVVSASNcsHTKESKPDI 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 281 ----ISGLAYFVPDIAP---NWLSVASVAQDaaSTNSVPYTISSFssrcgYTASFC-VSSPGSKIYSTVangsdPANlvs 352
Cdd:PTZ00262 484 pkcdLDVNKVYPPILSKklrNVITVSNLIKD--KNNQYSLSPNSF-----YSAKYCqLAAPGTNIYSTF-----PKN--- 548
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2304590498 353 DYGNKNGTSMATPHVTGAVAVLLQRFPYMSSAQIADVLKTTATDMgaPGIDALYGW-GMINLGKAIN 418
Cdd:PTZ00262 549 SYRKLNGTSMAAPHVAAIASLILSINPSLSYEEVIRILKESIVQL--PSLKNKVKWgGYLDIHHAVN 613
|
|
| Peptidases_S8_6 |
cd07490 |
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ... |
74-394 |
7.53e-10 |
|
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173815 [Multi-domain] Cd Length: 254 Bit Score: 60.64 E-value: 7.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 74 GQKVGIFDTPVN-RHPEFAGDgklinvvTEGYRAYTDPHRPGinagDRFYFDGtfhfysgsqgmlSNHGVHVAGISAANR 152
Cdd:cd07490 1 GVTVAVLDTGVDaDHPDLAGR-------VAQWADFDENRRIS----ATEVFDA------------GGHGTHVSGTIGGGG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 153 DGIGMHGVAFDSQVIS--VDNDNDGPAYGEFLGLDGAVTNagwqaminsGARVINNSWGVSipdflsDGGRDPNALHFEL 230
Cdd:cd07490 58 AKGVYIGVAPEADLLHgkVLDDGGGSLSQIIAGMEWAVEK---------DADVVSMSLGGT------YYSEDPLEEAVEA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 231 KDAQEqfdqvkpllgslagagyqgaidaarkNILVLFAAGNDGnynqPDVISglayfVPDIAPNWLSVASVAQD------ 304
Cdd:cd07490 123 LSNQT--------------------------GALFVVSAGNEG----HGTSG-----SPGSAYAALSVGAVDRDdedawf 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 305 AASTNSVPYTISSFSSRCGYTASFCVSSPGSKIYStvanGSDPANLVSDYGNKNGTSMATPHVTGAVAVLLQRFPYMSSA 384
Cdd:cd07490 168 SSFGSSGASLVSAPDSPPDEYTKPDVAAPGVDVYS----ARQGANGDGQYTRLSGTSMAAPHVAGVAALLAAAHPDLSPE 243
|
330
....*....|
gi 2304590498 385 QIADVLKTTA 394
Cdd:cd07490 244 QIKDALTETA 253
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
736-1030 |
9.01e-10 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 63.04 E-value: 9.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 736 ALNGRLRQAEG-LASSSAIKADEDGAWAQLLGAWDHASGDANATGYQASTYGVLVGLDSAVAGDG----RLGVATGYTRT 810
Cdd:COG3468 554 FELGTLHDRLGeRRYTDTGESDNSGAWLRVEGGHNRSRDSSGQLDYDSNRYGLQLGGDLLQWEDGggrlHVGVMAGYGNG 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 811 SLH----GGYGSKADSDNYHLAAYGDKQFGA-LALRGGAGYTWHRIDTKrsvnyGMQSDRDTAKYSARTEQLFAEAGYGV 885
Cdd:COG3468 634 DSDvrsrATGTGKGDVDGYSLGLYGTWYGNNgFYVDGVLQYSWFDNDVS-----SDDLGGVTGSYDGNGYSASLEAGYPF 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 886 Q-GEWLNLEPFVNLAYVNFENNGIAESGGAAAlrgDKQHTDATVSTLGLRADTAWQVTPGTTVALRSELGWQHQYGGldr 964
Cdd:COG3468 709 KlGEGWSLEPQAQLIYQGVDFDDFTDSNGTRV---SGDDGDSLQGRLGLRLGYEFHWDDGRALQPYLEANWLHEFLG--- 782
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2304590498 965 GTGLRFNGgnapfVVDSVPVSRDGMVLKAGAEVAVNENATLSLGYGGLLSQNH---QDNSVNAGFTWRF 1030
Cdd:COG3468 783 DNSVTVNG-----VSFSQDGSGTWGELGLGVTGQLNKNLSLYGDVGYQTGLDGydsSDTSGNLGVRYSF 846
|
|
| Peptidases_S8_9 |
cd07493 |
Peptidase S8 family domain, uncharacterized subfamily 9; This family is a member of the ... |
253-394 |
1.13e-09 |
|
Peptidase S8 family domain, uncharacterized subfamily 9; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173818 [Multi-domain] Cd Length: 261 Bit Score: 60.40 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 253 QGAIDAARKNILVLFAAGNDGNYNQPDVISglayfvPDIAPNWLSVASVAQDAastnsvpyTISSFSSRcGYTASFC--- 329
Cdd:cd07493 138 RAANIAASKGMLVVNSAGNEGSTQWKGIGA------PADAENVLSVGAVDANG--------NKASFSSI-GPTADGRlkp 202
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2304590498 330 -VSSPGSKIYSTVANGSdpanlvsdYGNKNGTSMATPHVTGAVAVLLQRFPYMSSAQIADVLKTTA 394
Cdd:cd07493 203 dVMALGTGIYVINGDGN--------ITYANGTSFSCPLIAGLIACLWQAHPNWTNLQIKEAILKSA 260
|
|
| Peptidases_S8_4 |
cd05561 |
Peptidase S8 family domain, uncharacterized subfamily 4; This family is a member of the ... |
246-409 |
2.32e-09 |
|
Peptidase S8 family domain, uncharacterized subfamily 4; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173797 [Multi-domain] Cd Length: 239 Bit Score: 58.84 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 246 SLAG---AGYQGAIDAA-RKNILVLFAAGNDGNYNQPdvisglAYfvPDIAPNWLSVASVAQDAAstnsvpytISSFSSR 321
Cdd:cd05561 100 SLAGppnALLAAAVAAAaARGMVLVAAAGNDGPAAPP------LY--PAAYPGVIAVTAVDARGR--------LYREANR 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 322 CGYTAsfcVSSPGSKIYSTVANGSdpanlvsdYGNKNGTSMATPHVTGAVAVLLQRFPyMSSAQIADVLKTTATDMGAPG 401
Cdd:cd05561 164 GAHVD---FAAPGVDVWVAAPGGG--------YRYVSGTSFAAPFVTAALALLLQASP-LAPDDARARLAATAKDLGPPG 231
|
....*...
gi 2304590498 402 IDALYGWG 409
Cdd:cd05561 232 RDPVFGYG 239
|
|
| autotrns_rpt |
TIGR02601 |
autotransporter-associated beta strand repeat; This model represent a core 32-residue region ... |
488-519 |
5.10e-08 |
|
autotransporter-associated beta strand repeat; This model represent a core 32-residue region of a class of bacterial protein repeat found in one to 30 copies per protein. Most proteins with a copy of this repeat have domains associated with membrane autotransporters (pfam03797, TIGR01414). The repeats occur with a periodicity of 60 to 100 residues. A pattern of sequence conservation is that every second residue is well-conserved across most of the domain. pfam05594 is based on a longer, much more poorly conserved multiple sequence alignment and hits some of the same proteins as this model with some overlap between the hit regions of the two models. It describes these repeats as likely to have a beta-helical structure. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274223 [Multi-domain] Cd Length: 32 Bit Score: 49.72 E-value: 5.10e-08
10 20 30
....*....|....*....|....*....|..
gi 2304590498 488 GLTKEGAGILVLTGNNTYAGPTLVNQGRLAIN 519
Cdd:TIGR02601 1 GLTKTGAGTLTLSGANTYTGGTTVNAGTLQVG 32
|
|
| PATR |
pfam12951 |
Passenger-associated-transport-repeat; This Autotransporter-associated beta strand repeat ... |
489-516 |
6.24e-08 |
|
Passenger-associated-transport-repeat; This Autotransporter-associated beta strand repeat model represents a core 32-residue region of a class of bacterial protein repeat found in one to 30 copies per protein. Most proteins with a copy of this repeat have domains associated with membrane autotransporters (pfam03797). The repeats occur with a periodicity of 60 to 100 residues. A pattern of sequence conservation is that every second residue is well-conserved across most of the domain. These repeats as likely to have a beta-helical structure. This repeat plays a role in the efficient transport of autotransporter virulence factors to the bacterial surface during growth and infection. The repeat is always associated with the passenger domain of the autotransporter. For these reasons it has been coined the Passenger-associated Transport Repeat (PATR). The mechanism by which the PATR motif promotes transport is uncertain but it is likely that the conserved glycines (see HMM Logo) are required for flexibility of folding and that this folding drives secretion. Autotransporters that contain PATR(s) associate with distinct virulence traits such as subtilisin (S8) type protease domains and polymorphic outer-membrane protein repeats, whilst SPATE (S6) type protease and lipase-like autotransporters do not tend to contain PATR motifs.
Pssm-ID: 463760 [Multi-domain] Cd Length: 28 Bit Score: 49.27 E-value: 6.24e-08
10 20
....*....|....*....|....*...
gi 2304590498 489 LTKEGAGILVLTGNNTYAGPTLVNQGRL 516
Cdd:pfam12951 1 LTKTGAGTLTLTGANTYTGGTTVNAGTL 28
|
|
| Peptidases_S8_10 |
cd07494 |
Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the ... |
60-396 |
7.84e-08 |
|
Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173819 [Multi-domain] Cd Length: 298 Bit Score: 55.18 E-value: 7.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 60 IHADEAYAAGYTGKGQKVGIFDTPVNRHPEFAGDGKLINVVTEGyrAYTDPHRPGINagdrfyfdgtfhfysgsqgmlsn 139
Cdd:cd07494 8 LNATRVHQRGITGRGVRVAMVDTGFYAHPFFESRGYQVRVVLAP--GATDPACDENG----------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 140 hgvHVAGISAAnrdgigMHGVAFDSQVISVDNDNDgpaygeflglDGAVTNAGWQAMINSGARVINNSWGVSipdfLSDG 219
Cdd:cd07494 63 ---HGTGESAN------LFAIAPGAQFIGVKLGGP----------DLVNSVGAFKKAISLSPDIISNSWGYD----LRSP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 220 GRDPnalhfelkdaqeqfdqVKPLLGSLAGAGYQGAiDAARKNILVLFAAGNDGnynqpdvisglaYFVPDIAPNWLSVA 299
Cdd:cd07494 120 GTSW----------------SRSLPNALKALAATLQ-DAVARGIVVVFSAGNGG------------WSFPAQHPEVIAAG 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 300 SVAQDA-----ASTNSVPYTISSFSSR-----CGYTASFCVS-------SPGSKIYSTVANGSDPANLVSDYGNKNGTSM 362
Cdd:cd07494 171 GVFVDEdgarrASSYASGFRSKIYPGRqvpdvCGLVGMLPHAaylmlpvPPGSQLDRSCAAFPDGTPPNDGWGVFSGTSA 250
|
330 340 350
....*....|....*....|....*....|....
gi 2304590498 363 ATPHVTGAVAVLLQRFPYMSSAQIADVLKTTATD 396
Cdd:cd07494 251 AAPQVAGVCALMLQANPGLSPERARSLLNKTARD 284
|
|
| Peptidases_S8_8 |
cd07492 |
Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the ... |
74-395 |
1.80e-07 |
|
Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173817 [Multi-domain] Cd Length: 222 Bit Score: 53.11 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 74 GQKVGIFDTPVNR-HPEFaGDGKLINVVTEgyraytdPHRPGINAGDRFYFDGtfhfysgsqgmlsnHGVHVAGIsaanr 152
Cdd:cd07492 1 GVRVAVIDSGVDTdHPDL-GNLALDGEVTI-------DLEIIVVSAEGGDKDG--------------HGTACAGI----- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 153 dgigMHGVAFDSQVISVdndndgPAYGEFLGLDGAVTNAGWQAMINSGARVINNSWGVSIPDFLsdggrdpnalhfelkd 232
Cdd:cd07492 54 ----IKKYAPEAEIGSI------KILGEDGRCNSFVLEKALRACVENDIRIVNLSLGGPGDRDF---------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 233 aqeqfdqvkPLLGSLAGAGYqgaidAARKNILVlfAAGNDGNYNQPdvisglayfvPDIAPNWLSVASVAQDAASTNSVP 312
Cdd:cd07492 108 ---------PLLKELLEYAY-----KAGGIIVA--AAPNNNDIGTP----------PASFPNVIGVKSDTADDPKSFWYI 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 313 YTissfssrcgytasfCVSSPGSKIYSTVANGsdpanlvsDYGNKNGTSMATPHVTGAVAVLLQRFPYMSSAQIADVLKT 392
Cdd:cd07492 162 YV--------------EFSADGVDIIAPAPHG--------RYLTVSGNSFAAPHVTGMVALLLSEKPDIDANDLKRLLQR 219
|
...
gi 2304590498 393 TAT 395
Cdd:cd07492 220 LAV 222
|
|
| Peptidases_S8_Lantibiotic_specific_protease |
cd07482 |
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ... |
76-393 |
1.07e-05 |
|
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific proteases; Lantiobiotic (lanthionine-containing antibiotics) specific proteases are very similar in structure to serine proteases. Lantibiotics are ribosomally synthesised antimicrobial agents derived from ribosomally synthesised peptides with antimicrobial activities against Gram-positive bacteria. The proteases that cleave the N-terminal leader peptides from lantiobiotics include: epiP, nsuP, mutP, and nisP. EpiP, from Staphylococcus, is thought to cleave matured epidermin. NsuP, a dehydratase from Streptococcus and NisP, a membrane-anchored subtilisin-like serine protease from Lactococcus cleave nisin. MutP is highly similar to epiP and nisP and is thought to process the prepeptide mutacin III of S. mutans. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53 the it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.
Pssm-ID: 173808 [Multi-domain] Cd Length: 294 Bit Score: 48.52 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 76 KVGIFDTPVNRH-----PEFAGDGKliNVVTEGYRAYTDPHRPGINagdRFYFDgtfhfysgsqgmLSNHGVHVAGISAA 150
Cdd:cd07482 3 TVAVIDSGIDPDhpdlkNSISSYSK--NLVPKGGYDGKEAGETGDI---NDIVD------------KLGHGTAVAGQIAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 151 NRDGIGmhgVAFDSQVISV---DNDNDGPaygeflglDGAVTNAGWQAmINSGARVINnswgvsipdfLSDGGrdpnalh 227
Cdd:cd07482 66 NGNIKG---VAPGIGIVSYrvfGSCGSAE--------SSWIIKAIIDA-ADDGVDVIN----------LSLGG------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 228 FELKDAQEQFDQVKPLLgslagagYQGAID-AARKNILVLFAAGNDG-------------NYNQPDVISGLAYFVPDIAP 293
Cdd:cd07482 117 YLIIGGEYEDDDVEYNA-------YKKAINyAKSKGSIVVAAAGNDGldvsnkqelldflSSGDDFSVNGEVYDVPASLP 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 294 NWLSVASvaqdaasTNSVPYtISSFSSRcgYTASFCVSSPG---------------SKIYSTVANGSDPANLvSDYGNKN 358
Cdd:cd07482 190 NVITVSA-------TDNNGN-LSSFSNY--GNSRIDLAAPGgdfllldqygkekwvNNGLMTKEQILTTAPE-GGYAYMY 258
|
330 340 350
....*....|....*....|....*....|....*.
gi 2304590498 359 GTSMATPHVTGAVAVLLQRFPYMS-SAQIADVLKTT 393
Cdd:cd07482 259 GTSLAAPKVSGALALIIDKNPLKKpPDEAIRILYNT 294
|
|
| PRK15319 |
PRK15319 |
fibronectin-binding autotransporter adhesin ShdA; |
456-611 |
4.21e-05 |
|
fibronectin-binding autotransporter adhesin ShdA;
Pssm-ID: 185219 [Multi-domain] Cd Length: 2039 Bit Score: 47.77 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 456 GAEVDAGTLHARKCDDV-----------HCGWEIYSNNISGHGGLTKEGAGILVLTGNNTYAGPTLVNQGRLAIN--GSV 522
Cdd:PRK15319 709 GTTISGGTLTADHADSLgsgdvdnsgvlKVGEGELENILSGSGSLVKTGTGELTLSGDNTYSGGTTITGGTLTADhaDSL 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 523 TSAVSVQSGGIVGGSGTVGSLTARRGGTVAPGNSIGTL----NVAGNVSFEPGSRYAVEVGPNGQSDrIQSSGAATIGGG 598
Cdd:PRK15319 789 GSGDIDNSGVLKVGEGDLENTLSGSGSLVKTGTGELTLsggnDYSGGTTIIGGTLTADHADSLGSGD-IDNSGVLQVGEG 867
|
170
....*....|...
gi 2304590498 599 EVAVTLENSANLL 611
Cdd:PRK15319 868 ELKNTLFGSGSLV 880
|
|
| Peptidases_S8_2 |
cd07488 |
Peptidase S8 family domain, uncharacterized subfamily 2; This family is a member of the ... |
114-381 |
6.39e-05 |
|
Peptidase S8 family domain, uncharacterized subfamily 2; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173813 Cd Length: 247 Bit Score: 45.54 E-value: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 114 GINAGDRFYFDGTFHFYSGSQG-------MLSNHGVHVAGIsAANRDGIGmhgvafdsqvisvdndndgPAYGEFLGLDG 186
Cdd:cd07488 6 LWDKNDSKNAPNTLAAVFIRNNprfgrnnTFDDHATLVASI-MGGRDGGL-------------------PAVNLYSSAFG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 187 AVTNAG------WQAMINSGARVINNSWGVSIpdflsdgGRDPNALHFELKDAQEQFDQVkpllgslagagyqgaidAAR 260
Cdd:cd07488 66 IKSNNGqwqeclEAQQNGNNVKIINHSYGEGL-------KRDPRAVLYGYALLSLYLDWL-----------------SRN 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 261 KNILVLFAAGNDGNYNQPDvisglayfvPDIAPNWLSVASVAQDAASTNSVPYTISSFSSRCGYTASFCVSSPgskiyST 340
Cdd:cd07488 122 YEVINVFSAGNQGKEKEKF---------GGISIPTLAYNSIVVGSTDRNGDRFFASDVSNAGSEINSYGRRKV-----LI 187
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2304590498 341 VANGSDPANLVSDYGNKNGTSMATPHVTGAVAVLLQRFPYM 381
Cdd:cd07488 188 VAPGSNYNLPDGKDDFVSGTSFSAPLVTGIIALLLEFYDRQ 228
|
|
| PRK15319 |
PRK15319 |
fibronectin-binding autotransporter adhesin ShdA; |
439-611 |
6.47e-05 |
|
fibronectin-binding autotransporter adhesin ShdA;
Pssm-ID: 185219 [Multi-domain] Cd Length: 2039 Bit Score: 47.39 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 439 TGVAYGPTQFVANI--PGRGAEVDAGTLHARKCDDVHCGWEIYSNNISGHGGLTKEGAGILVLTGNNTYAGPTLVNQGRL 516
Cdd:PRK15319 638 TGNDYGDTEIDGGIlaAKDAAALGTGDVTIAESATLALSQGTLDNNVTGEGQIVKSGSDELIVTGDNNYSGGTTISGGTL 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 517 AIN--GSVTSAVSVQSGGIVGGSGTVGSLTARRGGTVAPGNSIGTL----NVAGNVSFEPGSRYAVEVGPNGQSDrIQSS 590
Cdd:PRK15319 718 TADhaDSLGSGDVDNSGVLKVGEGELENILSGSGSLVKTGTGELTLsgdnTYSGGTTITGGTLTADHADSLGSGD-IDNS 796
|
170 180
....*....|....*....|.
gi 2304590498 591 GAATIGGGEVAVTLENSANLL 611
Cdd:PRK15319 797 GVLKVGEGDLENTLSGSGSLV 817
|
|
| Peptidases_S8_Tripeptidyl_Aminopeptidase_II |
cd04857 |
Peptidase S8 family domain in Tripeptidyl aminopeptidases_II; Tripeptidyl aminopeptidases II ... |
138-397 |
1.52e-04 |
|
Peptidase S8 family domain in Tripeptidyl aminopeptidases_II; Tripeptidyl aminopeptidases II are member of the peptidase S8 or Subtilase family. Subtilases, or subtilisin-like serine proteases, have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Tripeptidyl aminopeptidase II removes tripeptides from the free N terminus of oligopeptides as well as having endoproteolytic activity. Some tripeptidyl aminopeptidases have been shown to cleave tripeptides and small peptides, e.g. angiotensin II and glucagon, while others are believed to be involved in MHC I processing.
Pssm-ID: 173796 [Multi-domain] Cd Length: 412 Bit Score: 45.35 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 138 SNHGVHVAGISAAN-RDGIGMHGVAFDSQVISVdNDNDGPaygeflgLDGAVTNAG----WQAMINSGARVINNSWG--V 210
Cdd:cd04857 185 GAHGTHVAGIAAAHfPEEPERNGVAPGAQIVSI-KIGDTR-------LGSMETGTAlvraMIAAIETKCDLINMSYGeaT 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 211 SIPDflsdGGRDPNALHfelkdaqeqfdqvkpllgslagagyqgaiDAARK-NILVLFAAGNDG----NYNQPD-----V 280
Cdd:cd04857 257 HWPN----SGRIIELMN-----------------------------EAVNKhGVIFVSSAGNNGpalsTVGAPGgttssV 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 281 ISGLAYFVPDIAPNWLSVASvaqdaaSTNSVPYTissFSSRcGYTAS----FCVSSPGSKIYStVANGSDPANLVsdygn 356
Cdd:cd04857 304 IGVGAYVSPEMMAAEYSLRE------KLPGNQYT---WSSR-GPTADgalgVSISAPGGAIAS-VPNWTLQGSQL----- 367
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2304590498 357 KNGTSMATPHVTGAVAVLL-----QRFPYmSSAQIADVLKTTATDM 397
Cdd:cd04857 368 MNGTSMSSPNACGGIALLLsglkaEGIPY-TPYSVRRALENTAKKL 412
|
|
| Peptidases_S8_Subtilisin_like_2 |
cd04847 |
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ... |
76-382 |
1.96e-04 |
|
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173793 [Multi-domain] Cd Length: 291 Bit Score: 44.60 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 76 KVGIFDTPVNR-HPefagdgkLINVVTEGYRAYTDPhrPGINAGDRFyfdgtfhfysgsqgmlsnHGVHVAGIsAANRDG 154
Cdd:cd04847 2 IVCVLDSGINRgHP-------LLAPALAEDDLDSDE--PGWTADDLG------------------HGTAVAGL-ALYGDL 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 155 IGMHG-------VAFDSQVISVDNDNDGPAYGEFLglDGAVTnagwQAMINSG--ARVINNSWGvsipdflSDGGRDPNA 225
Cdd:cd04847 54 TLPGNglprpgcRLESVRVLPPNGENDPELYGDIT--LRAIR----RAVIQNPdiVRVFNLSLG-------SPLPIDDGR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 226 LHfelkdaqeqfdqvkpllgSLAGAgyqgaID--AARKNILVLFAAGNDGNYN-QPDVISGLAYFVPDIAPNW--LSVAS 300
Cdd:cd04847 121 PS------------------SWAAA-----LDqlAAEYDVLFVVSAGNLGDDDaADGPPRIQDDEIEDPADSVnaLTVGA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 301 VAQDAASTNSVPYTISSFSSRCGYTAS-----FCV------------------SSPGSKIYSTVANGSDPANLVSDygnk 357
Cdd:cd04847 178 ITSDDDITDRARYSAVGPAPAGATTSSgpgspGPIkpdvvafggnlaydpsgnAADGDLSLLTTLSSPSGGGFVTV---- 253
|
330 340
....*....|....*....|....*
gi 2304590498 358 NGTSMATPHVTGAVAVLLQRFPYMS 382
Cdd:cd04847 254 GGTSFAAPLAARLAAGLFAELPELS 278
|
|
| PRK15319 |
PRK15319 |
fibronectin-binding autotransporter adhesin ShdA; |
481-638 |
2.61e-04 |
|
fibronectin-binding autotransporter adhesin ShdA;
Pssm-ID: 185219 [Multi-domain] Cd Length: 2039 Bit Score: 45.46 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 481 NNISGHGGLTKEGAGILVLTGNNTYAGPTLVNQGRL-AINGSVTSAVSVQSGGIV----GGSGTVGSLTARRGGTVAPgn 555
Cdd:PRK15319 997 NTLSGSGSLVKTGTGELTLGGDNSYSGDTTIADGTLiAANVNALGSGNIDNSGTLmldaNGAFELANITTHSGATTAL-- 1074
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 556 SIGTLNVAGNVSFEPGSRYAVEVGPnGQSDRIQSSGAATIGGgevavTLeNSANLLTQSEVRSLLGQQYTILSAQQGVSG 635
Cdd:PRK15319 1075 AAGSTLDAGQLTQEDGSTLSIDLGA-ATDDAVITADSVTLGG-----TL-NVTGIGSVTDSWTPEAYTYTLIDSDSAITS 1147
|
...
gi 2304590498 636 QFD 638
Cdd:PRK15319 1148 DFD 1150
|
|
| PRK15319 |
PRK15319 |
fibronectin-binding autotransporter adhesin ShdA; |
489-643 |
2.61e-04 |
|
fibronectin-binding autotransporter adhesin ShdA;
Pssm-ID: 185219 [Multi-domain] Cd Length: 2039 Bit Score: 45.46 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 489 LTKEGAGILVLTGNNTYAGPTLVNQGRLaingsVTSAVSVQSGGIVGGSGT-----------VGSLTARRGGT--VAPGN 555
Cdd:PRK15319 1235 LTKEGAGTLILSGDNDYSGGTTINEGTL-----VAASTTALGTGLVDNNATlvldadgevsaVGGITTHSGATtqLALGT 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 556 SIGTLNVAgnVSFEPGSRYAVEVgpngQSDRIQ---SSGAATIGGGEVAvtleNSANLltQSEVRSLLGQQYTILSAQQG 632
Cdd:PRK15319 1310 SLDLGDSA--LIQQDGSTLNVEL----NSDSVQpliTGGSATLGGDLVV----SDASL--QARASDAEFQSFKLMDMDSD 1377
|
170
....*....|.
gi 2304590498 633 VSGQFDAVAPN 643
Cdd:PRK15319 1378 ISGDFTSLTMN 1388
|
|
| PRK15319 |
PRK15319 |
fibronectin-binding autotransporter adhesin ShdA; |
481-611 |
3.09e-04 |
|
fibronectin-binding autotransporter adhesin ShdA;
Pssm-ID: 185219 [Multi-domain] Cd Length: 2039 Bit Score: 45.07 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 481 NNISGHGGLTKEGAGILVLTGNNTYAGPTLVNQGRL-AINGSVTSAVSVQSGGIVG-GSGTVGSLTARRGGTVAPGNSIG 558
Cdd:PRK15319 871 NTLFGSGSLVKTGTGELTLNGDNDYSGGTTIDDGVLiADHADSLGTGAVANSGVLQvGEGELKNTLSGSGSLVKTGTGEL 950
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2304590498 559 TLN----VAGNVSFEPGSRYAVEVGPNGQSDrIQSSGAATIGGGEVAVTLENSANLL 611
Cdd:PRK15319 951 TLSgdnsYSGGTTIIGGTLIADHADSLGTGA-VANSGVLQVGEGELENTLSGSGSLV 1006
|
|
| Peptidases_S8_11 |
cd04843 |
Peptidase S8 family domain, uncharacterized subfamily 11; This family is a member of the ... |
138-395 |
1.35e-03 |
|
Peptidase S8 family domain, uncharacterized subfamily 11; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173792 Cd Length: 277 Bit Score: 41.92 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 138 SNHGVHVAGISAANRDGIGMHGVAFDSQVISVDNdndGPAYGEFLGLDGAVTNAGWQAMINSGARVINNswgvsipdfls 217
Cdd:cd04843 51 SDHGTAVLGIIVAKDNGIGVTGIAHGAQAAVVSS---TRVSNTADAILDAADYLSPGDVILLEMQTGGP----------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 218 DGGRDPNALHFElkdaQEQFDQVKpllgslagagyqgaiDAARKNILVLFAAGNdGNYNqpdvisgLAYFVPDIAP-NWL 296
Cdd:cd04843 117 NNGYPPLPVEYE----QANFDAIR---------------TATDLGIIVVEAAGN-GGQD-------LDAPVYNRGPiLNR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 297 SVASVAQD-----AASTNSVPYTISSFSSrcgYTASFCVSSPGSKIYSTVANGS-DPANLVSDY-GNKNGTSMATPHVTG 369
Cdd:cd04843 170 FSPDFRDSgaimvGAGSSTTGHTRLAFSN---YGSRVDVYGWGENVTTTGYGDLqDLGGENQDYtDSFSGTSSASPIVAG 246
|
250 260 270
....*....|....*....|....*....|.
gi 2304590498 370 AVAVL-----LQRFPYMSSAQIADVLKTTAT 395
Cdd:cd04843 247 AAASIqgiakQKGGTPLTPIEMRELLTATGT 277
|
|
| germ_prot_CspBA |
NF040809 |
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ... |
308-413 |
1.45e-03 |
|
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in Clostridium difficile, is translated as a fusion protein, but cleaved into separate homologous CspB and CspA proteins during spore formation. CspB is a protease, required to active SleC by cleaving it in order to trigger germination. CspA, like the bile salt germinant receptor CspC (encoded by the adjacent gene), has lost the catalytic residues necessary for subtilisin-like serine protease activity.
Pssm-ID: 468750 [Multi-domain] Cd Length: 1099 Bit Score: 42.84 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 308 TNSVPYTISSFSSRCGYTASFC-------------VSSPGSKIYSTVANGSDpanlvsdyGNKNGTSMATPHVTGAVAVL 374
Cdd:NF040809 401 TASRVITVGSFNSRTDVVSVFSgegdiengiykpdLLAPGENIVSYLPGGTT--------GALTGTSMATPHVTGVCSLL 472
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2304590498 375 LQ------RFPYMSSAQIADVLKTTA---TDMGAPgiDALYGWGMINL 413
Cdd:NF040809 473 MQwgivegNDLFLYSQKLKALLLQNArrsPNRTYP--NNSSGYGFLNL 518
|
|
| Peptidases_S8_thiazoline_oxidase_subtilisin-like_p |
cd07476 |
Peptidase S8 family domain in Thiazoline oxidase/subtilisin-like proteases; Thiazoline oxidase ... |
76-401 |
2.57e-03 |
|
Peptidase S8 family domain in Thiazoline oxidase/subtilisin-like proteases; Thiazoline oxidase/subtilisin-like protease is produced by the symbiotic bacteria Prochloron spp. that inhabit didemnid family ascidians. The cyclic peptides of the patellamide class found in didemnid extracts are now known to be synthesized by the Prochloron spp. The prepatellamide is heterocyclized to form thiazole and oxazoline rings and the peptide is cleaved to form the two cyclic patellamides A and C. Subtilases, or subtilisin-like serine proteases, have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution).
Pssm-ID: 173802 [Multi-domain] Cd Length: 267 Bit Score: 40.78 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 76 KVGIFDTPVNR-HPEFAGdgklINVVtegyraYTDPHRPGInagdrfyfdgtfhfysGSQGMLSNHGVHVAGISAAnRDG 154
Cdd:cd07476 13 TIAILDGPVDRtHPCFRG----ANLT------PLFTYAAAA----------------CQDGGASAHGTHVASLIFG-QPC 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 155 IGMHGVAFDSQVISVDNDNDGPAYGEFLGLDGAVTNAgwqamINSGARVINNSWGVSIPDFLSDggrdpnalhFELKDAQ 234
Cdd:cd07476 66 SSVEGIAPLCRGLNIPIFAEDRRGCSQLDLARAINLA-----LEQGAHIINISGGRLTQTGEAD---------PILANAV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 235 EQfdqvkpllgslagagyqgaidAARKNILVLFAAGNDGnynqpdvisGLAYFVPDIAPNWLSVAsvaqdAASTNSVPyt 314
Cdd:cd07476 132 AM---------------------CQQNNVLIVAAAGNEG---------CACLHVPAALPSVLAVG-----AMDDDGLP-- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 315 iSSFSSRCGYTASFCVSSPGSKIYstvanGSDPANLVsdyGNKNGTSMATPHVTGAVAVLL----QRFPYMSSAQIADVL 390
Cdd:cd07476 175 -LKFSNWGADYRKKGILAPGENIL-----GAALGGEV---VRRSGTSFAAAIVAGIAALLLslqlRRGAPPDPLAVRRAL 245
|
330
....*....|.
gi 2304590498 391 KTTATDMGAPG 401
Cdd:cd07476 246 LETATPCDPEA 256
|
|
| PRK15319 |
PRK15319 |
fibronectin-binding autotransporter adhesin ShdA; |
489-577 |
3.54e-03 |
|
fibronectin-binding autotransporter adhesin ShdA;
Pssm-ID: 185219 [Multi-domain] Cd Length: 2039 Bit Score: 41.61 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304590498 489 LTKEGAGILVLTGNNTYAGPTLVNQGRLAINGSVT-------SAVSVQSGGIVGGS-GTVGSLTARRGGTVAPGNS---- 556
Cdd:PRK15319 1460 LTKLGAGKLTLSGANTYTGDTNVQEGTLWLSGDGSigemgsqQAVNVASGATFGGSnGTTVNGKVTNEGTLVFGDSeetg 1539
|
90 100 110
....*....|....*....|....*....|.
gi 2304590498 557 -IGTLN---------VAGNVSFEPGSRYAVE 577
Cdd:PRK15319 1540 aIFTLNgdlinmgtmTSGSSSSTPGNTLYVD 1570
|
|
| |
