|
Name |
Accession |
Description |
Interval |
E-value |
| esterase_EstP |
NF041609 |
esterase EstP; |
2-646 |
0e+00 |
|
esterase EstP;
Pssm-ID: 469493 [Multi-domain] Cd Length: 640 Bit Score: 1264.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 2 IRMALKPLVAACLLASLSTAPQAAPSPYSTLVVFGDSLSDAGQFPDPAGPAGSTSRFTNRVGPTYQNGSGEIFGPTAPML 81
Cdd:NF041609 1 MKRTLLPPAAACLLALACSSALAAPSPYSTMIVFGDSLSDAGQFPDADGPAGATLRFTNRTGPTYQDGSGEIYGPVSPML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 82 LGNQLGIAPGDLAASTSPVNAQQGIADGNNWAVGGYRTDQIYDSITAANGSLIErDNTLLRSRDGYLVDRARQglgADPN 161
Cdd:NF041609 81 LGGKLGIAPGDLGASTSPVNAAQGLPDGNNWAVGGYRTDQILDSITGQSGVVIP-DGTVLRTRPGYLVGNGFR---ADPN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 162 ALYYITGGGNDFLQGRILNDVQAQQAAGRLVDSVQALQQAGARYIVVWLLPDLGLTPATFGGPLQPFASQLSGTFNAELT 241
Cdd:NF041609 157 ALYYLTGGGNDFLQGRVTSPAQAQAAAGRLADSAQALQQAGARYIMVWLLPDLGLTPALSGTPLQATTSALSAVFNQELV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 242 AQLSQAGANVIPLNIPLLLKEGMANPASFGLAADQNLIGTCFSGNGCTMNPTYGINGSTPDPSKLLFNDSVHPTITGQRL 321
Cdd:NF041609 237 SQLAQIDAEIIPLNVPLLLSEVLADPARFGLATDQNLVGTCFSGNGCTENPVYGINGATPDPTKLLFNDSVHPTIAGQRL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 322 IADYTYSLLSAPWELTLLPEMAHGTLRAYQDELRSQWQADWENWQNVGQWRGFVGGGGQRLDFDSQDSAASGDGNGYNLT 401
Cdd:NF041609 317 IADYAYSLLAAPWELTLLPEMAHGTLRAHQDELRNQWQADWENWQAVGQWRAFVAGGGQRLDFDDQDSSASADGRGYNLT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 402 LGGSYRIDEAWRAGVAAGFYRQKLEAGAKDSDYRMNSYMASAFVQYQENRWWADAALTGGYLDYDDLKRKFALGGGERSE 481
Cdd:NF041609 397 VGGSYRLDEAWRVGLAAGFYRQKLEAGAADSDYKLNSYLATAFAQYQQNRWWADAALTGGHLDYDDLKRKFALGVSERSE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 482 KGDTNGHLWAFSARLGYDIAqQADSPWHLSPFVSADYARVEVDGYSEKGASATALDYDDQKRSSKRLGAGLQGKYAFGSD 561
Cdd:NF041609 477 KGDTDGELWALSGRLGYDIA-QPGSPWHLSPFISADYARVEVDGYSEKGARSTALTFDDQTRKSRRLGAGLQGKYQLTPQ 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 562 TQLFAEYAHEREYEDDTQDLTMSLNSLPGNRFTLEGYTPQDHLNRVSLGFSQKLAPELSLRGGYNWRKGEDDTQQSVSLA 641
Cdd:NF041609 556 TQLFGEVAHEREFEDDTQDVTMALNSLPGNDFTLEGYTPQSNLNRASLGVSQKLTPDLALRGGYNWRKSDDDTQQGVNLA 635
|
....*
gi 15600305 642 LSLDF 646
Cdd:NF041609 636 LSLDF 640
|
|
| YhjY |
COG5571 |
Uncharacterized conserved protein YhjY, contains autotransporter beta-barrel domain [General ... |
11-646 |
3.99e-91 |
|
Uncharacterized conserved protein YhjY, contains autotransporter beta-barrel domain [General function prediction only];
Pssm-ID: 444313 [Multi-domain] Cd Length: 648 Bit Score: 295.64 E-value: 3.99e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 11 AACLLASLSTAPQAAPSPYSTLVVFGDSLSDAGQFPDPAGPAGSTSRFTNRVGPTYQNGSGEIFGPTAPMLLGNQLGIAP 90
Cdd:COG5571 20 AATAPGLAAATASAAGAAGLGAASTASSLSGASLALLAAQALGAGLSGTNGFSGGAGSSSGTGPTANGGLAGAGGVDLAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 91 GDLAASTSPVNAQQGIADGNNWAVGGYRTDQIYDSITAANGSLIERDNTLLRSRDGYLVdraRQGLGADPNALYYITGGG 170
Cdd:COG5571 100 AGGGGGASGLAGGAGGAGGTAAAGGAAAAGGGAAGNAATAAAAAAAGTALQLSGLTTAG---AVGGVAGTAALNGATANT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 171 NDFLQGRILNDVQAQQAAGRLVDSVQALQQAGARYIVVWLLPDLGLTPATFGGPLQPFASQLSGTFNAELTAQLSQAGAN 250
Cdd:COG5571 177 GLGAAAALAAAAAAAAAAAAAAAAAAAAATAAAAAAAAAAAAAVLASPAPAAGGAAAAAAGAAAAAASAAANAATQANLL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 251 VIPLNIPLLLKEGMANPASFGLAADQNLIGTCFSGNGCTMNPTYGINGSTPDPSK-------LLFNDSVHPTITGQRLIA 323
Cdd:COG5571 257 LLALALGSNGNAVGLNAVGLANEAAAPGAVGGDAGSTGATPSTLSSASCVASSLTaanantlYAAADTAGPAGATAALAA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 324 DYTYSLLSAPweltllpEMAHGTLRAYQDELRSQWQADWENWQNVGQWRGFVGGGGQRLDFDSQDSAASGDGNGYNLTLG 403
Cdd:COG5571 337 AAAAVLASAA-------AVAQAALALAAAGGQARSLAVAAGQGRGARGGQTRGGGGAGGTTGGGVGAGGGDGDGPNLTLG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 404 GSYRIDEAWRAGVAAGFYRQKLEAGAkDSDYRMNSYMASAFVQYQENRWWADAALTGGYLDYDdLKRKFALGGGERSEKG 483
Cdd:COG5571 410 VDYRLSDNLLLGAALSYGRQDLDFGD-GGSYDARSTSLSLYAGYRAGGLWVDADLSYGDLDYD-IRRHIRLGPATRTETG 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 484 DTNGHLWAFSARLGYDIAQQAdspWHLSPFVSADYARVEVDGYSEKGASATALDYDDQKRSSKRLGAGLQGKYAFGSDTQ 563
Cdd:COG5571 488 DTDGSQWGARLTAGYDFTAGR---LRTGPFAGLDYQKVKVDGYTETGAGSTALSFGDQDRDSLVGSLGWRADYQLLGRFN 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 564 LFAEYAHEREYEDDTQDLTMSLNSLPGNRFTLEGYTPQDHLNRVSLGFSQKLAPELSLRGGYNWRKGEDD-TQQSVSLAL 642
Cdd:COG5571 565 PYAEVAYEHEFGDDDRDVTAGLASLPAGSFSLPAAAPDKNWGRATLGASAALTNGVSLFAGYSGTFGRDDgRQTSVNLGL 644
|
....
gi 15600305 643 SLDF 646
Cdd:COG5571 645 SARF 648
|
|
| Triacylglycerol_lipase_like |
cd01847 |
Triacylglycerol lipase-like subfamily of the SGNH hydrolases, a diverse family of lipases and ... |
29-330 |
9.90e-58 |
|
Triacylglycerol lipase-like subfamily of the SGNH hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases. Members of this subfamily might hydrolyze triacylglycerol into diacylglycerol and fatty acid anions.
Pssm-ID: 238883 Cd Length: 281 Bit Score: 196.11 E-value: 9.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 29 YSTLVVFGDSLSDAGQFPDPAGPAGSTSRFTNRVGPTYQNGSGEIFGPTapmllgnqlgiapgdlaastsPVNAQQGIAD 108
Cdd:cd01847 1 FSRVVVFGDSLSDVGTYNRAGVGAAGGGRFTVNDGSIWSLGVAEGYGLT---------------------TGTATPTTPG 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 109 GNNWAVGGYRTDQIYDSITAANgslierdntLLRSRDGYLVDRARQGLGADPNALYYITGGGNDFL--------QGRILN 180
Cdd:cd01847 60 GTNYAQGGARVGDTNNGNGAGA---------VLPSVTTQIANYLAAGGGFDPNALYTVWIGGNDLIaalaalttATTTQA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 181 DVQAQ--QAAGRLVDSVQALQQAGARYIVVWLLPDLGLTPATFGGPL--QPFASQLSGTFNAELTAQLSQAGAN-VIPLN 255
Cdd:cd01847 131 AAVAAaaTAAADLASQVKNLLDAGARYILVPNLPDVSYTPEAAGTPAaaAALASALSQTYNQTLQSGLNQLGANnIIYVD 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600305 256 IPLLLKEGMANPASFGLAADQNLIGTCFSGNGCtmnpTYGINGSTPDPSKLLFNDSVHPTITGQRLIADYTYSLL 330
Cdd:cd01847 211 TATLLKEVVANPAAYGFTNTTTPACTSTSAAGS----GAATLVTAAAQSTYLFADDVHPTPAGHKLIAQYALSRL 281
|
|
| Autotransporter |
pfam03797 |
Autotransporter beta-domain; Secretion of protein products occurs by a number of different ... |
374-626 |
2.48e-44 |
|
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: 159.09 E-value: 2.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 374 FVGGGGQRLDFDSQDSAASGDGNGYNLTLGGSYRIDEAWRAGVAAGFYRQKLEAGAKDSDYRMNSYMASAFVQYQ-ENRW 452
Cdd:pfam03797 2 WARGFGGRGKQDGDGGAAGYDADTGGLQVGADYRLGDNLRLGVAFGYSRSDADVDGRGGSGDSDSYSLGLYGTYYgDGGW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 453 WADAALTGGYLDYdDLKRKFALGGGERSEKGDTNGHLWAFSARLGYDIaqQADSPWHLSPFVSADYARVEVDGYSEKGaS 532
Cdd:pfam03797 82 YLDGGLGYGWHDN-DTRRSVDLGGFSETAKGDYDGNGFGASLEAGYRF--ALGGGWTLEPFAGLAYVRLRLDGFTESG-G 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 533 ATALDYDDQKRSSKRLGAGLQGKYAF---GSDTQLFAEYAHEREYEDDTQDLTMSLNSLPGN-RFTLEGYTPQDHLNRVS 608
Cdd:pfam03797 158 AAALSVDSQSYDSLTGRLGLRLSYTFdlgGGTLTPYARLGWRHEFGDDDPVTTAAFAGLSGAgSFTVAGADLARDSLELG 237
|
250
....*....|....*...
gi 15600305 609 LGFSQKLAPELSLRGGYN 626
Cdd:pfam03797 238 AGLSAQLSDNLSLYANYD 255
|
|
| Autotransporter |
smart00869 |
Autotransporter beta-domain; Secretion of protein products occurs by a number of different ... |
373-636 |
1.35e-37 |
|
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: 140.78 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 373 GFVGGGGQRLDFDSQDSAASGDGNGYNLTLGGSYRIDE--AWRAGVAAGFYRQKLEAGAKD--SDYRMNSYMASAFVQYQ 448
Cdd:smart00869 1 GRGLGGFLRQDSSGSGGSAGFDYDSYGLQLGADYRLSDngNLSLGFAAGYGNSKVDFSGNKgsGKGDVDSYGLGLYAGYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 449 -ENRWWADAALTGGYLDYDdLKRKFALGGGERSeKGDTNGHLWAFSARLGYDIaqQADSPWHLSPFVSADYARVEVDGYS 527
Cdd:smart00869 81 lGNGLYLDAQLGYGRSDND-TKRKVTLGGAGRA-KGSYDGTGYGASLEAGYRF--YLGGGLTLTPFAGLAYSRVRQDGFT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 528 EKGASATALDYDDQKRSSKRLGAGLQGKYAF----GSDTQLFAEYAHEREYEDDTQDLTMSLNSlPGNRFTLEGYTPQDH 603
Cdd:smart00869 157 ESGGGAFGLSVDSQSLDSLSLPLGLRLEYRLalgdGATLTPYLRLAYVHDFYDDNPVVTASLLG-SGASFTTSGTDLDRN 235
|
250 260 270
....*....|....*....|....*....|...
gi 15600305 604 LNRVSLGFSQKLAPELSLRGGYNWRKGEDDTQQ 636
Cdd:smart00869 236 AAELGLGLSAKLSNGLSLSLNYDGEFGGSSRSH 268
|
|
| PLN03156 |
PLN03156 |
GDSL esterase/lipase; Provisional |
9-325 |
3.72e-07 |
|
GDSL esterase/lipase; Provisional
Pssm-ID: 178701 Cd Length: 351 Bit Score: 52.44 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 9 LVAACLLASLSTAPQAAPSpystLVVFGDSLSDAG---QFP-------DPAG---PAGS-TSRFTN-RVGPTYQNgsgEI 73
Cdd:PLN03156 11 LLLAQLLVLVAETCAKVPA----IIVFGDSSVDAGnnnQIStvaksnfEPYGrdfPGGRpTGRFCNgRIAPDFIS---EA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 74 FG--PTAPMLLGNQLGIApgDLAASTSPVNAQQGiadgnnwavggyrtdqiYDSITAANGSLIERDNTLLRSRD------ 145
Cdd:PLN03156 84 FGlkPAIPAYLDPSYNIS--DFATGVCFASAGTG-----------------YDNATSDVLSVIPLWKELEYYKEyqtklr 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 146 GYL-VDRARQGLGadpNALYYITGGGNDFLQ------GRiLNDVQAQQAAGRLV----DSVQALQQAGARYIVVWLLPDL 214
Cdd:PLN03156 145 AYLgEEKANEIIS---EALYLISIGTNDFLEnyytfpGR-RSQYTVSQYQDFLIgiaeNFVKKLYRLGARKISLGGLPPM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 215 GLTP----ATFGGP---LQPF---ASQLSGTFNaELTAQLSQ--AGANVIPLNIPLLLKEGMANPASFGLaadQNLIGTC 282
Cdd:PLN03156 221 GCLPlertTNLMGGsecVEEYndvALEFNGKLE-KLVTKLNKelPGIKLVFSNPYDIFMQIIRNPSAYGF---EVTSVAC 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15600305 283 FS------GNGCT-MNPTygingSTPDPSKLLFNDSVHPTITGQRLIADY 325
Cdd:PLN03156 297 CAtgmfemGYLCNrNNPF-----TCSDADKYVFWDSFHPTEKTNQIIANH 341
|
|
| autotrans_barl |
TIGR01414 |
outer membrane autotransporter barrel domain; A number of Gram-negative bacterial proteins, ... |
369-570 |
4.75e-05 |
|
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: 46.22 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 369 GQWR-GFVGG-GGQRLDFDSQDSAASGDGNGYNLTLGGSYRIDE-AWRAGVA-AGFYRQKLEA----GAKDSDYRMNSYM 440
Cdd:TIGR01414 206 GDLHvGLMAGyAKADIKTRSYKYGGKGKVDGYGLGLYGTWLQDSgAYVDGVLqYSRFRNDVSStgsnGKVSGKYNSNGFT 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 441 ASAFVQYQ----ENRWWAD--AALTGGYLDYDDlkrkFALGGGERSEKGDTNghlwAFSARLGYDIAQQAD--SPWHLSP 512
Cdd:TIGR01414 286 ASLEAGYRynlgGNGWYVEpqAQLSYFGVSGDD----YKESNGTRVLGGGGD----SLQGRLGLRVGYQFDlgTGRAVKP 357
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600305 513 FVSADYAR-------VEVDGYSEKgasataldyDDQKRSSKRLGAGLQGKyaFGSDTQLFAEYAH 570
Cdd:TIGR01414 358 YLKANVLHefkggtgVRVNGVTIR---------NDFSGTRAEYGVGVNAK--IKDNLSLYADVDY 411
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| esterase_EstP |
NF041609 |
esterase EstP; |
2-646 |
0e+00 |
|
esterase EstP;
Pssm-ID: 469493 [Multi-domain] Cd Length: 640 Bit Score: 1264.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 2 IRMALKPLVAACLLASLSTAPQAAPSPYSTLVVFGDSLSDAGQFPDPAGPAGSTSRFTNRVGPTYQNGSGEIFGPTAPML 81
Cdd:NF041609 1 MKRTLLPPAAACLLALACSSALAAPSPYSTMIVFGDSLSDAGQFPDADGPAGATLRFTNRTGPTYQDGSGEIYGPVSPML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 82 LGNQLGIAPGDLAASTSPVNAQQGIADGNNWAVGGYRTDQIYDSITAANGSLIErDNTLLRSRDGYLVDRARQglgADPN 161
Cdd:NF041609 81 LGGKLGIAPGDLGASTSPVNAAQGLPDGNNWAVGGYRTDQILDSITGQSGVVIP-DGTVLRTRPGYLVGNGFR---ADPN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 162 ALYYITGGGNDFLQGRILNDVQAQQAAGRLVDSVQALQQAGARYIVVWLLPDLGLTPATFGGPLQPFASQLSGTFNAELT 241
Cdd:NF041609 157 ALYYLTGGGNDFLQGRVTSPAQAQAAAGRLADSAQALQQAGARYIMVWLLPDLGLTPALSGTPLQATTSALSAVFNQELV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 242 AQLSQAGANVIPLNIPLLLKEGMANPASFGLAADQNLIGTCFSGNGCTMNPTYGINGSTPDPSKLLFNDSVHPTITGQRL 321
Cdd:NF041609 237 SQLAQIDAEIIPLNVPLLLSEVLADPARFGLATDQNLVGTCFSGNGCTENPVYGINGATPDPTKLLFNDSVHPTIAGQRL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 322 IADYTYSLLSAPWELTLLPEMAHGTLRAYQDELRSQWQADWENWQNVGQWRGFVGGGGQRLDFDSQDSAASGDGNGYNLT 401
Cdd:NF041609 317 IADYAYSLLAAPWELTLLPEMAHGTLRAHQDELRNQWQADWENWQAVGQWRAFVAGGGQRLDFDDQDSSASADGRGYNLT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 402 LGGSYRIDEAWRAGVAAGFYRQKLEAGAKDSDYRMNSYMASAFVQYQENRWWADAALTGGYLDYDDLKRKFALGGGERSE 481
Cdd:NF041609 397 VGGSYRLDEAWRVGLAAGFYRQKLEAGAADSDYKLNSYLATAFAQYQQNRWWADAALTGGHLDYDDLKRKFALGVSERSE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 482 KGDTNGHLWAFSARLGYDIAqQADSPWHLSPFVSADYARVEVDGYSEKGASATALDYDDQKRSSKRLGAGLQGKYAFGSD 561
Cdd:NF041609 477 KGDTDGELWALSGRLGYDIA-QPGSPWHLSPFISADYARVEVDGYSEKGARSTALTFDDQTRKSRRLGAGLQGKYQLTPQ 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 562 TQLFAEYAHEREYEDDTQDLTMSLNSLPGNRFTLEGYTPQDHLNRVSLGFSQKLAPELSLRGGYNWRKGEDDTQQSVSLA 641
Cdd:NF041609 556 TQLFGEVAHEREFEDDTQDVTMALNSLPGNDFTLEGYTPQSNLNRASLGVSQKLTPDLALRGGYNWRKSDDDTQQGVNLA 635
|
....*
gi 15600305 642 LSLDF 646
Cdd:NF041609 636 LSLDF 640
|
|
| YhjY |
COG5571 |
Uncharacterized conserved protein YhjY, contains autotransporter beta-barrel domain [General ... |
11-646 |
3.99e-91 |
|
Uncharacterized conserved protein YhjY, contains autotransporter beta-barrel domain [General function prediction only];
Pssm-ID: 444313 [Multi-domain] Cd Length: 648 Bit Score: 295.64 E-value: 3.99e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 11 AACLLASLSTAPQAAPSPYSTLVVFGDSLSDAGQFPDPAGPAGSTSRFTNRVGPTYQNGSGEIFGPTAPMLLGNQLGIAP 90
Cdd:COG5571 20 AATAPGLAAATASAAGAAGLGAASTASSLSGASLALLAAQALGAGLSGTNGFSGGAGSSSGTGPTANGGLAGAGGVDLAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 91 GDLAASTSPVNAQQGIADGNNWAVGGYRTDQIYDSITAANGSLIERDNTLLRSRDGYLVdraRQGLGADPNALYYITGGG 170
Cdd:COG5571 100 AGGGGGASGLAGGAGGAGGTAAAGGAAAAGGGAAGNAATAAAAAAAGTALQLSGLTTAG---AVGGVAGTAALNGATANT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 171 NDFLQGRILNDVQAQQAAGRLVDSVQALQQAGARYIVVWLLPDLGLTPATFGGPLQPFASQLSGTFNAELTAQLSQAGAN 250
Cdd:COG5571 177 GLGAAAALAAAAAAAAAAAAAAAAAAAAATAAAAAAAAAAAAAVLASPAPAAGGAAAAAAGAAAAAASAAANAATQANLL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 251 VIPLNIPLLLKEGMANPASFGLAADQNLIGTCFSGNGCTMNPTYGINGSTPDPSK-------LLFNDSVHPTITGQRLIA 323
Cdd:COG5571 257 LLALALGSNGNAVGLNAVGLANEAAAPGAVGGDAGSTGATPSTLSSASCVASSLTaanantlYAAADTAGPAGATAALAA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 324 DYTYSLLSAPweltllpEMAHGTLRAYQDELRSQWQADWENWQNVGQWRGFVGGGGQRLDFDSQDSAASGDGNGYNLTLG 403
Cdd:COG5571 337 AAAAVLASAA-------AVAQAALALAAAGGQARSLAVAAGQGRGARGGQTRGGGGAGGTTGGGVGAGGGDGDGPNLTLG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 404 GSYRIDEAWRAGVAAGFYRQKLEAGAkDSDYRMNSYMASAFVQYQENRWWADAALTGGYLDYDdLKRKFALGGGERSEKG 483
Cdd:COG5571 410 VDYRLSDNLLLGAALSYGRQDLDFGD-GGSYDARSTSLSLYAGYRAGGLWVDADLSYGDLDYD-IRRHIRLGPATRTETG 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 484 DTNGHLWAFSARLGYDIAQQAdspWHLSPFVSADYARVEVDGYSEKGASATALDYDDQKRSSKRLGAGLQGKYAFGSDTQ 563
Cdd:COG5571 488 DTDGSQWGARLTAGYDFTAGR---LRTGPFAGLDYQKVKVDGYTETGAGSTALSFGDQDRDSLVGSLGWRADYQLLGRFN 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 564 LFAEYAHEREYEDDTQDLTMSLNSLPGNRFTLEGYTPQDHLNRVSLGFSQKLAPELSLRGGYNWRKGEDD-TQQSVSLAL 642
Cdd:COG5571 565 PYAEVAYEHEFGDDDRDVTAGLASLPAGSFSLPAAAPDKNWGRATLGASAALTNGVSLFAGYSGTFGRDDgRQTSVNLGL 644
|
....
gi 15600305 643 SLDF 646
Cdd:COG5571 645 SARF 648
|
|
| COG3240 |
COG3240 |
Phospholipase/lecithinase/hemolysin [Lipid transport and metabolism, General function ... |
2-336 |
4.39e-75 |
|
Phospholipase/lecithinase/hemolysin [Lipid transport and metabolism, General function prediction only];
Pssm-ID: 442472 [Multi-domain] Cd Length: 305 Bit Score: 243.02 E-value: 4.39e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 2 IRMALKPLVAACLLASLSTAPQAAPSPYSTLVVFGDSLSDAGQFPD-----PAGPAGSTSRFTNrvgptyqngsgeifGP 76
Cdd:COG3240 1 MKKRLAAALALLALLLAACGGAASAAAFSRIVVFGDSLSDTGNLFNltgglPPSPPYFGGRFSN--------------GP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 77 TAPMLLGNQLGIapgDLAASTspvnaqqgiADGNNWAVGGYRTDQIYDSITAAngsliERDNTLLRSRDGYLvdrARQGL 156
Cdd:COG3240 67 VWVEYLAAALGL---PLTPSS---------AGGTNYAVGGARTGDGNGVLGGA-----ALLPGLAQQVDAYL---AAAGG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 157 GADPNALYYITGGGNDFLQGRILNDVQ-------AQQAAGRLVDSVQALQQAGARYIVVWLLPDLGLTPAT--FGGPLQP 227
Cdd:COG3240 127 TADPNALYIVWAGANDLLAALAAVGATpaqaqaaATAAAANLAAAVGALAAAGARHILVPNLPDLGLTPAAqaLGAAAAA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 228 FASQLSGTFNAELTAQLSQAGANVIPLNIPLLLKEGMANPASFGLAadqNLIGTCFSGNG----CtmnptygingsTPDP 303
Cdd:COG3240 207 LLSALTAAFNQALAAALPALGVNIILFDVNSLFNEIIANPAAYGFT---NVTDACLSGTVsallC-----------VANP 272
|
330 340 350
....*....|....*....|....*....|...
gi 15600305 304 SKLLFNDSVHPTITGQRLIADYTYSLLSAPWEL 336
Cdd:COG3240 273 DTYLFWDGVHPTTAAHRLIADYAYSALAAPGQL 305
|
|
| Triacylglycerol_lipase_like |
cd01847 |
Triacylglycerol lipase-like subfamily of the SGNH hydrolases, a diverse family of lipases and ... |
29-330 |
9.90e-58 |
|
Triacylglycerol lipase-like subfamily of the SGNH hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases. Members of this subfamily might hydrolyze triacylglycerol into diacylglycerol and fatty acid anions.
Pssm-ID: 238883 Cd Length: 281 Bit Score: 196.11 E-value: 9.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 29 YSTLVVFGDSLSDAGQFPDPAGPAGSTSRFTNRVGPTYQNGSGEIFGPTapmllgnqlgiapgdlaastsPVNAQQGIAD 108
Cdd:cd01847 1 FSRVVVFGDSLSDVGTYNRAGVGAAGGGRFTVNDGSIWSLGVAEGYGLT---------------------TGTATPTTPG 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 109 GNNWAVGGYRTDQIYDSITAANgslierdntLLRSRDGYLVDRARQGLGADPNALYYITGGGNDFL--------QGRILN 180
Cdd:cd01847 60 GTNYAQGGARVGDTNNGNGAGA---------VLPSVTTQIANYLAAGGGFDPNALYTVWIGGNDLIaalaalttATTTQA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 181 DVQAQ--QAAGRLVDSVQALQQAGARYIVVWLLPDLGLTPATFGGPL--QPFASQLSGTFNAELTAQLSQAGAN-VIPLN 255
Cdd:cd01847 131 AAVAAaaTAAADLASQVKNLLDAGARYILVPNLPDVSYTPEAAGTPAaaAALASALSQTYNQTLQSGLNQLGANnIIYVD 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600305 256 IPLLLKEGMANPASFGLAADQNLIGTCFSGNGCtmnpTYGINGSTPDPSKLLFNDSVHPTITGQRLIADYTYSLL 330
Cdd:cd01847 211 TATLLKEVVANPAAYGFTNTTTPACTSTSAAGS----GAATLVTAAAQSTYLFADDVHPTPAGHKLIAQYALSRL 281
|
|
| Autotransporter |
pfam03797 |
Autotransporter beta-domain; Secretion of protein products occurs by a number of different ... |
374-626 |
2.48e-44 |
|
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: 159.09 E-value: 2.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 374 FVGGGGQRLDFDSQDSAASGDGNGYNLTLGGSYRIDEAWRAGVAAGFYRQKLEAGAKDSDYRMNSYMASAFVQYQ-ENRW 452
Cdd:pfam03797 2 WARGFGGRGKQDGDGGAAGYDADTGGLQVGADYRLGDNLRLGVAFGYSRSDADVDGRGGSGDSDSYSLGLYGTYYgDGGW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 453 WADAALTGGYLDYdDLKRKFALGGGERSEKGDTNGHLWAFSARLGYDIaqQADSPWHLSPFVSADYARVEVDGYSEKGaS 532
Cdd:pfam03797 82 YLDGGLGYGWHDN-DTRRSVDLGGFSETAKGDYDGNGFGASLEAGYRF--ALGGGWTLEPFAGLAYVRLRLDGFTESG-G 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 533 ATALDYDDQKRSSKRLGAGLQGKYAF---GSDTQLFAEYAHEREYEDDTQDLTMSLNSLPGN-RFTLEGYTPQDHLNRVS 608
Cdd:pfam03797 158 AAALSVDSQSYDSLTGRLGLRLSYTFdlgGGTLTPYARLGWRHEFGDDDPVTTAAFAGLSGAgSFTVAGADLARDSLELG 237
|
250
....*....|....*...
gi 15600305 609 LGFSQKLAPELSLRGGYN 626
Cdd:pfam03797 238 AGLSAQLSDNLSLYANYD 255
|
|
| Autotransporter |
smart00869 |
Autotransporter beta-domain; Secretion of protein products occurs by a number of different ... |
373-636 |
1.35e-37 |
|
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: 140.78 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 373 GFVGGGGQRLDFDSQDSAASGDGNGYNLTLGGSYRIDE--AWRAGVAAGFYRQKLEAGAKD--SDYRMNSYMASAFVQYQ 448
Cdd:smart00869 1 GRGLGGFLRQDSSGSGGSAGFDYDSYGLQLGADYRLSDngNLSLGFAAGYGNSKVDFSGNKgsGKGDVDSYGLGLYAGYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 449 -ENRWWADAALTGGYLDYDdLKRKFALGGGERSeKGDTNGHLWAFSARLGYDIaqQADSPWHLSPFVSADYARVEVDGYS 527
Cdd:smart00869 81 lGNGLYLDAQLGYGRSDND-TKRKVTLGGAGRA-KGSYDGTGYGASLEAGYRF--YLGGGLTLTPFAGLAYSRVRQDGFT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 528 EKGASATALDYDDQKRSSKRLGAGLQGKYAF----GSDTQLFAEYAHEREYEDDTQDLTMSLNSlPGNRFTLEGYTPQDH 603
Cdd:smart00869 157 ESGGGAFGLSVDSQSLDSLSLPLGLRLEYRLalgdGATLTPYLRLAYVHDFYDDNPVVTASLLG-SGASFTTSGTDLDRN 235
|
250 260 270
....*....|....*....|....*....|...
gi 15600305 604 LNRVSLGFSQKLAPELSLRGGYNWRKGEDDTQQ 636
Cdd:smart00869 236 AAELGLGLSAKLSNGLSLSLNYDGEFGGSSRSH 268
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
337-646 |
8.30e-36 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 144.54 E-value: 8.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 337 TLLPEMAHGTLRAYQDELRSQWQADWENWQNVGQWRGFVGGGGQRLDFDSQDSAASGDGNGYNLTLGGSYRIDEAWRAGV 416
Cdd:COG4625 592 AALLQASRALRDALSNRLRALRGAGAAGDAAAEGWGVWAQGFGSWGDQDGDGGAAGYDSSTGGLLVGADYRLGDNWRLGV 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 417 AAGFYRQKLEAGAKDSDYRMNSYMASAFVQYQENRWWADAALTGGYLDYdDLKRKFALGGGERSEKGDTNGHLWAFSARL 496
Cdd:COG4625 672 ALGYSRSDVDVDDRGSSGDSDSYHLGLYGGYQFGALYLDGGLGYGWNDY-DTDRTIAFGGLSRTATADYDGDTASAFLEA 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 497 GYDIAQqadSPWHLSPFVSADYARVEVDGYSEKGASAtALDYDDQKRSSKRLGAGLQGKYAF----GSDTQLFAEYAHER 572
Cdd:COG4625 751 GYRFDL---GGLTLTPFAGLAYVRLRTDGFTETGGAA-ALSVDSQSTDSLRSTLGLRASRTFslggGVTLTPSGRLGWRH 826
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600305 573 EYEDDTQDLTMSLNSLPGNRFTLEGYTPQDHLNRVSLGFSQKLAPELSLRGGYNWRKGEDDTQQSVSLALSLDF 646
Cdd:COG4625 827 EFGDDDPSTTASFAGAPGAAFTVAGAPLARDALVLGAGLSARLSDGLSLGLGYDGEFGSGYTDHGGSAGLRYRF 900
|
|
| fatty_acyltransferase_like |
cd01846 |
Fatty acyltransferase-like subfamily of the SGNH hydrolases, a diverse family of lipases and ... |
31-325 |
4.42e-35 |
|
Fatty acyltransferase-like subfamily of the SGNH hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases. Might catalyze fatty acid transfer between phosphatidylcholine and sterols.
Pssm-ID: 238882 [Multi-domain] Cd Length: 270 Bit Score: 133.66 E-value: 4.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 31 TLVVFGDSLSDAG-------QFPDPAGPAGSTSRFTNrvgptyqngsgeifGPTAPMLLGNQLGIAPGDLaastspvnaq 103
Cdd:cd01846 1 RLVVFGDSLSDTGnifkltgGSNPPPSPPYFGGRFSN--------------GPVWVEYLAATLGLSGLKQ---------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 104 qgiadGNNWAVGGYRTD-QIYDSITAANGSLIERDNTLLrsrdgylvdrARQGLGADPNALYYITGGGNDFLQGRILNDV 182
Cdd:cd01846 57 -----GYNYAVGGATAGaYNVPPYPPTLPGLSDQVAAFL----------AAHKLRLPPDTLVAIWIGANDLLNALDLPQN 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 183 Q---AQQAAGRLVDSVQALQQAGARYIVVWLLPDLGLTPA--TFGGPLQPFASQLSGTFNAELTAQLSQAGANVIPLNIP 257
Cdd:cd01846 122 PdtlVTRAVDNLFQALQRLYAAGARNFLVLNLPDLGLTPAfqAQGDAVAARATALTAAYNAKLAEKLAELKAQHPGVNIL 201
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600305 258 L-----LLKEGMANPASFGLAadqNLIGTCFSGNGCTMNPTygingSTPDPSKLLFNDSVHPTITGQRLIADY 325
Cdd:cd01846 202 LfdtnaLFNDILDNPAAYGFT---NVTDPCLDYVYSYSPRE-----ACANPDKYLFWDEVHPTTAVHQLIAEE 266
|
|
| SGNH_plant_lipase_like |
cd01837 |
SGNH_plant_lipase_like, a plant specific subfamily of the SGNH-family of hydrolases, a diverse ... |
34-328 |
5.42e-16 |
|
SGNH_plant_lipase_like, a plant specific subfamily of the SGNH-family of hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
Pssm-ID: 238875 [Multi-domain] Cd Length: 315 Bit Score: 79.20 E-value: 5.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 34 VFGDSLSDAGQFPD----------PAG---PAGSTSRFTNrvgptyqngsgeifGPTAPMLLGNQLGIaPGDLAAStSPV 100
Cdd:cd01837 5 VFGDSLVDTGNNNYlptlakanfpPYGidfPGRPTGRFSN--------------GRLIIDFIAEALGL-PLLPPPY-LSP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 101 NAQQGIADGNNWAVGG----YRTDQIYDSITAanGSLIERDNTLLRSRDGYLVDRARQGLGAdpNALYYITGGGNDFLQ- 175
Cdd:cd01837 69 NGSSDFLTGVNFASGGagilDSTGFLGSVISL--SVQLEYFKEYKERLRALVGEEAAADILS--KSLFLISIGSNDYLNn 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 176 ----GRILNDVQAQQA--AGRLVDSVQALQQAGARYIVVWLLPDLGLTPA---TFGGPLQ---PFASQLSGTFNAELTAQ 243
Cdd:cd01837 145 yfanPTRQYEVEAYVPflVSNISSAIKRLYDLGARKFVVPGLGPLGCLPSqrtLFGGDGGgclEELNELARLFNAKLKKL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 244 LSQ-----AGANVIPLNIPLLLKEGMANPASFGLaaDQNLIGTCfsGNGcTMNPTYGINGST----PDPSKLLFNDSVHP 314
Cdd:cd01837 225 LAElrrelPGAKFVYADIYNALLDLIQNPAKYGF--ENTLKACC--GTG-GPEGGLLCNPCGstvcPDPSKYVFWDGVHP 299
|
330
....*....|....
gi 15600305 315 TITGQRLIADYTYS 328
Cdd:cd01837 300 TEAANRIIADALLS 313
|
|
| PLN03156 |
PLN03156 |
GDSL esterase/lipase; Provisional |
9-325 |
3.72e-07 |
|
GDSL esterase/lipase; Provisional
Pssm-ID: 178701 Cd Length: 351 Bit Score: 52.44 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 9 LVAACLLASLSTAPQAAPSpystLVVFGDSLSDAG---QFP-------DPAG---PAGS-TSRFTN-RVGPTYQNgsgEI 73
Cdd:PLN03156 11 LLLAQLLVLVAETCAKVPA----IIVFGDSSVDAGnnnQIStvaksnfEPYGrdfPGGRpTGRFCNgRIAPDFIS---EA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 74 FG--PTAPMLLGNQLGIApgDLAASTSPVNAQQGiadgnnwavggyrtdqiYDSITAANGSLIERDNTLLRSRD------ 145
Cdd:PLN03156 84 FGlkPAIPAYLDPSYNIS--DFATGVCFASAGTG-----------------YDNATSDVLSVIPLWKELEYYKEyqtklr 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 146 GYL-VDRARQGLGadpNALYYITGGGNDFLQ------GRiLNDVQAQQAAGRLV----DSVQALQQAGARYIVVWLLPDL 214
Cdd:PLN03156 145 AYLgEEKANEIIS---EALYLISIGTNDFLEnyytfpGR-RSQYTVSQYQDFLIgiaeNFVKKLYRLGARKISLGGLPPM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 215 GLTP----ATFGGP---LQPF---ASQLSGTFNaELTAQLSQ--AGANVIPLNIPLLLKEGMANPASFGLaadQNLIGTC 282
Cdd:PLN03156 221 GCLPlertTNLMGGsecVEEYndvALEFNGKLE-KLVTKLNKelPGIKLVFSNPYDIFMQIIRNPSAYGF---EVTSVAC 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15600305 283 FS------GNGCT-MNPTygingSTPDPSKLLFNDSVHPTITGQRLIADY 325
Cdd:PLN03156 297 CAtgmfemGYLCNrNNPF-----TCSDADKYVFWDSFHPTEKTNQIIANH 341
|
|
| Lipase_GDSL |
pfam00657 |
GDSL-like Lipase/Acylhydrolase; |
32-325 |
5.15e-07 |
|
GDSL-like Lipase/Acylhydrolase;
Pssm-ID: 459892 [Multi-domain] Cd Length: 210 Bit Score: 50.65 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 32 LVVFGDSLSDAGQfpdpagpAGSTSRFTNrvgptyqngsgeifGPTAPMLLGNQLGIApgdlaastspvnaQQGIADGNN 111
Cdd:pfam00657 1 IVAFGDSLTDGGG-------DGPGGRFSW--------------GDLLADFLARKLGVP-------------GSGYNHGAN 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 112 WAVGGYRTDQIYDSItaangslierdntllrsrdGYLVDRARQGLGADPNALYYITGGGNDFLQGRILNDVQAQ---QAA 188
Cdd:pfam00657 47 FAIGGATIEDLPIQL-------------------EQLLRLISDVKDQAKPDLVTIFIGANDLCNFLSSPARSKKrvpDLL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 189 GRLVDSVQALqQAGARYIVVWLLPDLGLTPatfGGPLQPFASQLSGTFNAELTAQLSQAGANVIPLNIPLLLKEGManpa 268
Cdd:pfam00657 108 DELRANLPQL-GLGARKFWVHGLGPLGCTP---PKGCYELYNALAEEYNERLNELVNSLAAAAEDANVVYVDIYGF---- 179
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600305 269 sfglaadqnligtcfsgngctMNPTYGINGSTPDPskllfnDSVHPTITGQRLIADY 325
Cdd:pfam00657 180 ---------------------EDPTDPCCGIGLEP------DGLHPSEKGYKAVAEA 209
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
379-637 |
1.17e-05 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 48.79 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 379 GQRLDFDSQDSAASGDGNGYNLTLGGSYRIDEA----WRAGVAAGFYRQKLEAGAK---DSDYRMNSYMASAFV-QYQEN 450
Cdd:COG3468 585 GGHNRSRDSSGQLDYDSNRYGLQLGGDLLQWEDgggrLHVGVMAGYGNGDSDVRSRatgTGKGDVDGYSLGLYGtWYGNN 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 451 RWWADAALTGGYLDYDdlkrkfALGGGERSEKGDTNGHLWAFSARLGYDIAqqADSPWHLSPFVSADYARVEVDGYSEkg 530
Cdd:COG3468 665 GFYVDGVLQYSWFDND------VSSDDLGGVTGSYDGNGYSASLEAGYPFK--LGEGWSLEPQAQLIYQGVDFDDFTD-- 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 531 ASATALDYDDQKRSSKRLGAGLQGKYAFGSD--TQLFAE--YAHEReyeDDTQDLTMSlnslpGNRFTLEGytpQDHLNR 606
Cdd:COG3468 735 SNGTRVSGDDGDSLQGRLGLRLGYEFHWDDGraLQPYLEanWLHEF---LGDNSVTVN-----GVSFSQDG---SGTWGE 803
|
250 260 270
....*....|....*....|....*....|.
gi 15600305 607 VSLGFSQKLAPELSLRGGYNWRKGEDDTQQS 637
Cdd:COG3468 804 LGLGVTGQLNKNLSLYGDVGYQTGLDGYDSS 834
|
|
| autotrans_barl |
TIGR01414 |
outer membrane autotransporter barrel domain; A number of Gram-negative bacterial proteins, ... |
369-570 |
4.75e-05 |
|
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: 46.22 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 369 GQWR-GFVGG-GGQRLDFDSQDSAASGDGNGYNLTLGGSYRIDE-AWRAGVA-AGFYRQKLEA----GAKDSDYRMNSYM 440
Cdd:TIGR01414 206 GDLHvGLMAGyAKADIKTRSYKYGGKGKVDGYGLGLYGTWLQDSgAYVDGVLqYSRFRNDVSStgsnGKVSGKYNSNGFT 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 441 ASAFVQYQ----ENRWWAD--AALTGGYLDYDDlkrkFALGGGERSEKGDTNghlwAFSARLGYDIAQQAD--SPWHLSP 512
Cdd:TIGR01414 286 ASLEAGYRynlgGNGWYVEpqAQLSYFGVSGDD----YKESNGTRVLGGGGD----SLQGRLGLRVGYQFDlgTGRAVKP 357
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600305 513 FVSADYAR-------VEVDGYSEKgasataldyDDQKRSSKRLGAGLQGKyaFGSDTQLFAEYAH 570
Cdd:TIGR01414 358 YLKANVLHefkggtgVRVNGVTIR---------NDFSGTRAEYGVGVNAK--IKDNLSLYADVDY 411
|
|
| FepA |
COG4771 |
Outer membrane receptor for ferrienterochelin and colicins [Inorganic ion transport and ... |
344-626 |
8.08e-05 |
|
Outer membrane receptor for ferrienterochelin and colicins [Inorganic ion transport and metabolism];
Pssm-ID: 443803 [Multi-domain] Cd Length: 612 Bit Score: 45.62 E-value: 8.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 344 HGTLRA-YQDELRSQWQADWENWQNVGQWRGFVGGGGQR----LDFDSQDSAASGDGNGYNLTLGGSYRIDEAWRAGVAA 418
Cdd:COG4771 161 EGSVSLgYGSNGNGTYSGSLSLGGPGDKLSFLLSGSYRDrdgyLDYRNGGFVGNSGYERYNLNAKLGYRLSDNHRLSLSG 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 419 GFYRQKLEAGAKDSDYRMNSYMASAFVQYQENRWWADAALTGGYLD-------YDDLKRKFALGGGERSEKGDTNGHLWA 491
Cdd:COG4771 241 GYSRQDRDGGPPTLGDTEISSDNAGDRDTTTDRGNYSLRYNGDLGDnldlslyYSRTDRDSTNGSLGGSTGSFSDSDDTT 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 492 FSARLGYDIaqQADSPWHLSpfVSADYARVEVDGYSEkgasataldYDDQKRSSKRLGAGLQGKYAFGSDTQLfaeyahe 571
Cdd:COG4771 321 YGLELDLTY--PLGGNHTLT--LGAEYRYDDLDSSSF---------LGGADASRDTYGLFAQDEWKLTDKLTL------- 380
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600305 572 reyeddtqdltmslnsLPGNRFTLEGYTPQDHLNRVS--LGFSQKLAPELSLRGGYN 626
Cdd:COG4771 381 ----------------TAGLRYDYYSTFGASNYTAFSprLGLRYDLSDNLTLRASYG 421
|
|
| TesA |
COG2755 |
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ... |
111-330 |
2.07e-04 |
|
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];
Pssm-ID: 442045 [Multi-domain] Cd Length: 191 Bit Score: 42.71 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 111 NWAVGGYRTDQIYDSItaangslierDNTLLRSRDGYLVdrarqglgadpnalyyITGGGNDFLQGRILNDVQAQQAAGR 190
Cdd:COG2755 47 NAGISGATTADLLARL----------DRDLLALKPDLVV----------------IELGTNDLLRGLGVSPEEFRANLEA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 191 LVDSVQAlQQAGARYIVVwllpdlGLTPATFGGPLQPFASQlsgtFNAELTAQLSQAGANVIPLNIPLLLKEgmanpasf 270
Cdd:COG2755 101 LIDRLRA-AGPGARVVLV------TPPPRLRPNYLNERIEA----YNAAIRELAAEYGVPLVDLYAALRDAG-------- 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 271 glaadqnligtcfsgngctmnptygingstpDPSKLLFNDSVHPTITGQRLIADYTYSLL 330
Cdd:COG2755 162 -------------------------------DLPDLLTADGLHPNAAGYRLIAEAVLPAL 190
|
|
| ligand_gated_channel |
cd01347 |
TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) ... |
351-627 |
5.14e-04 |
|
TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.
Pssm-ID: 238657 [Multi-domain] Cd Length: 635 Bit Score: 43.21 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 351 QDELRSQWQADWENWQNVGQWR---GFVGGGGQRLDFDSQDSAASGDGNG---------------YNLTLGGSYRIDEAW 412
Cdd:cd01347 110 TDEFGGSVTAGYGSDNSGSSGGggfDVSGALADDGAFGARLYGAYRDGDGtidgdgqaddsdeerYNVAGKLDWRPDDDT 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 413 RAGVAAGFYRQkleagakDSDYRMNSYMASAFVQYQENRWWADAALTGGYlDYDDLKRKFALGGGERsekgDTNGHLWAF 492
Cdd:cd01347 190 RLTLDAGYQDQ-------DADGPGGTLPANGTGSSLGGGPSSNTNGDRDW-DYRDRYRKRASLGLEH----DLNDTGWTL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 493 SARLGYDIAQQADSPWHLSPFVSADYARVEVDGYSEKgasataldyddQKRSSKRLGAGLQGKYAFGSDTQLF---AEYA 569
Cdd:cd01347 258 RANLSYSYTDNDGDPLILNGGNNAAGGDLGRSGYSSE-----------RDTTQLGFDAGLNAPFGTGPVAHTLtlgVEYR 326
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600305 570 HEREYED-------DTQDLTMSLNSLPGNRFTLEGYTPQDHLNRV------------SLGFSQKLAPELSLRGGYNW 627
Cdd:cd01347 327 REELDEKqtalyaqDTIELTDDLTLTLGLRYDHYDQDSKDTIAGGttakksyshwspSLGLVYKLTDGLSLYASYSQ 403
|
|
| LomR |
COG3637 |
Opacity protein LomR and related surface antigens [Cell wall/membrane/envelope biogenesis]; |
436-570 |
5.02e-03 |
|
Opacity protein LomR and related surface antigens [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442854 [Multi-domain] Cd Length: 154 Bit Score: 38.03 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600305 436 MNSYMASAFV-------QYQENRWWADAALTGGYLDYDDlkrkfalGGGERSEKGDTNGhlWAFSARLGYDIaqqadsPW 508
Cdd:COG3637 1 MKKLLLAALAagvqagyNFQFDNFVLGVEGDYSYSDIDG-------DSSGTTGSGDLDY--LSLRARAGYDF------ND 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600305 509 HLSPFVSA--DYARVEVDGYSEKGASATaldyDDQKRSSKRLGAGLQgkYAFGSDTQLFAEYAH 570
Cdd:COG3637 66 RFLPYATAgvAYARVKVTGNTGSGTSGS----DSDTRFGWTVGAGVE--YALTDNWSLRLEYRY 123
|
|
| |
