|
Name |
Accession |
Description |
Interval |
E-value |
| YhjY |
COG5571 |
Uncharacterized conserved protein YhjY, contains autotransporter beta-barrel domain [General ... |
18-594 |
2.10e-103 |
|
Uncharacterized conserved protein YhjY, contains autotransporter beta-barrel domain [General function prediction only];
Pssm-ID: 444313 [Multi-domain] Cd Length: 648 Bit Score: 326.45 E-value: 2.10e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 18 FDQTVFFGDSLTDSGYYNPLLPAASRAVTGKFTTNPGWVWAEYVGDHFGTNAAPNGNGQTGDNYAAGGARIQASSVSALG 97
Cdd:COG5571 70 GFSGGAGSSSGTGPTANGGLAGAGGVDLAGAGGGGGASGLAGGAGGAGGTAAAGGAAAAGGGAAGNAATAAAAAAAGTAL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 98 AAPSVTSQINTYLTANGGRANPNALYTVWGGANDLLAASLAPAQAQAIIGSAVTAQVGAVATLQNAGARYVMVPTIPDVG 177
Cdd:COG5571 150 QLSGLTTAGAVGGVAGTAALNGATANTGLGAAAALAAAAAAAAAAAAAAAAAAAAATAAAAAAAAAAAAAVLASPAPAAG 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 178 LTPRFRAGGAVGMAQGTAAATAYNTALFNGLQSAGLRVIPVDTFHMLQEIVANPGTYGFSNVTSTACNPAVPLPACNPTS 257
Cdd:COG5571 230 GAAAAAAGAAAAAASAAANAATQANLLLLALALGSNGNAVGLNAVGLANEAAAPGAVGGDAGSTGATPSTLSSASCVASS 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 258 LVAANAQNTYVFADGIHPTTAVHQILGEYAISLLEAPRLQQVLTHSAQAGGRARADQVAWHLDGKPDADGMRWWGSVRGD 337
Cdd:COG5571 310 LTAANANTLYAAADTAGPAGATAALAAAAAAVLASAAAVAQAALALAAAGGQARSLAVAAGQGRGARGGQTRGGGGAGGT 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 338 MQRYDHADLYDGMAPAGLFGVDWTAGD-LVFGGFAGFGRMDADFGNrNGSFKQDDTTLGGFFGWYTGPVWVNAQVSYSWL 416
Cdd:COG5571 390 TGGGVGAGGGDGDGPNLTLGVDYRLSDnLLLGAALSYGRQDLDFGD-GGSYDARSTSLSLYAGYRAGGLWVDADLSYGDL 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 417 SYDVDREVQLGPATRVHSGSPDGSNLTAALNAGYSLGEGNLKYGPVAGLTWQKIKLDGYTESNDSATALGYANQDIDSLV 496
Cdd:COG5571 469 DYDIRRHIRLGPATRTETGDTDGSQWGARLTAGYDFTAGRLRTGPFAGLDYQKVKVDGYTETGAGSTALSFGDQDRDSLV 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 497 GRVGFQVRLDGAM-VKPYLQATYDHEFKDGGE-ASAWLQSMPEvGMYTVPGQNFDRNYATVVLGARTGL-WGLQSNIGLS 573
Cdd:COG5571 549 GSLGWRADYQLLGrFNPYAEVAYEHEFGDDDRdVTAGLASLPA-GSFSLPAAAPDKNWGRATLGASAALtNGVSLFAGYS 627
|
570 580
....*....|....*....|.
gi 503856910 574 TTTAQRSARDATLFVNFSGNF 594
Cdd:COG5571 628 GTFGRDDGRQTSVNLGLSARF 648
|
|
| Triacylglycerol_lipase_like |
cd01847 |
Triacylglycerol lipase-like subfamily of the SGNH hydrolases, a diverse family of lipases and ... |
18-291 |
2.38e-70 |
|
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: 228.47 E-value: 2.38e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 18 FDQTVFFGDSLTDSGYYNPLLPAAsrAVTGKFTTNPGWVWAEYVGDHFG-TNAAPNGNGQTGDNYAAGGARIQASSVSAL 96
Cdd:cd01847 1 FSRVVVFGDSLSDVGTYNRAGVGA--AGGGRFTVNDGSIWSLGVAEGYGlTTGTATPTTPGGTNYAQGGARVGDTNNGNG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 97 GAA--PSVTSQINTYLTANGGRAnPNALYTVWGGANDLLAA-------SLAPAQAQAIIGSAVTAQVGAVATLQNAGARY 167
Cdd:cd01847 79 AGAvlPSVTTQIANYLAAGGGFD-PNALYTVWIGGNDLIAAlaalttaTTTQAAAVAAAATAAADLASQVKNLLDAGARY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 168 VMVPTIPDVGLTPRFRAGGAVGMAQGTAAATAYNTALFNGL-QSAGLRVIPVDTFHMLQEIVANPGTYGFSNVTSTACNP 246
Cdd:cd01847 158 ILVPNLPDVSYTPEAAGTPAAAAALASALSQTYNQTLQSGLnQLGANNIIYVDTATLLKEVVANPAAYGFTNTTTPACTS 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 503856910 247 AVPLPACNPTsLVAANAQNTYVFADGIHPTTAVHQILGEYAISLL 291
Cdd:cd01847 238 TSAAGSGAAT-LVTAAAQSTYLFADDVHPTPAGHKLIAQYALSRL 281
|
|
| Autotransporter |
pfam03797 |
Autotransporter beta-domain; Secretion of protein products occurs by a number of different ... |
330-563 |
1.76e-35 |
|
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: 134.05 E-value: 1.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 330 WWGSVRGDMQRYDHADLYDGM---APAGLFGVDWTAGD-LVFGGFAGFGRMDADFGNRNGSFKQDDTTLGGFFGWY-TGP 404
Cdd:pfam03797 1 VWARGFGGRGKQDGDGGAAGYdadTGGLQVGADYRLGDnLRLGVAFGYSRSDADVDGRGGSGDSDSYSLGLYGTYYgDGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 405 VWVNAQVSYSWLSYDVDREVQLGPATRVHSGSPDGSNLTAALNAGYSLG-EGNLKYGPVAGLTWQKIKLDGYTESNDSAt 483
Cdd:pfam03797 81 WYLDGGLGYGWHDNDTRRSVDLGGFSETAKGDYDGNGFGASLEAGYRFAlGGGWTLEPFAGLAYVRLRLDGFTESGGAA- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 484 ALGYANQDIDSLVGRVGFQVR----LDGAMVKPYLQATYDHEFKDGGEAS-AWLQSMPEVGMYTVPGQNFDRNYATVVLG 558
Cdd:pfam03797 160 ALSVDSQSYDSLTGRLGLRLSytfdLGGGTLTPYARLGWRHEFGDDDPVTtAAFAGLSGAGSFTVAGADLARDSLELGAG 239
|
....*
gi 503856910 559 ARTGL 563
Cdd:pfam03797 240 LSAQL 244
|
|
| Autotransporter |
smart00869 |
Autotransporter beta-domain; Secretion of protein products occurs by a number of different ... |
332-563 |
9.92e-27 |
|
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: 109.58 E-value: 9.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 332 GSVRGDMQRYDHADLYDGMAPAGLFGVDWTAGD---LVFGGFAGFGRMDADFGNRNGSFKQDDTT--LGGFFGWYTGP-V 405
Cdd:smart00869 6 GFLRQDSSGSGGSAGFDYDSYGLQLGADYRLSDngnLSLGFAAGYGNSKVDFSGNKGSGKGDVDSygLGLYAGYSLGNgL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 406 WVNAQVSYSWLSYDVDREVQLGPATRVhSGSPDGSNLTAALNAGYSL-GEGNLKYGPVAGLTWQKIKLDGYTESNDSATA 484
Cdd:smart00869 86 YLDAQLGYGRSDNDTKRKVTLGGAGRA-KGSYDGTGYGASLEAGYRFyLGGGLTLTPFAGLAYSRVRQDGFTESGGGAFG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 485 LGYANQDIDSLVGRVGFQVRL-----DGAMVKPYLQATYDHEFKDGGEASAwLQSMPEVGMYTVPGQNFDRNYATVVLGA 559
Cdd:smart00869 165 LSVDSQSLDSLSLPLGLRLEYrlalgDGATLTPYLRLAYVHDFYDDNPVVT-ASLLGSGASFTTSGTDLDRNAAELGLGL 243
|
....
gi 503856910 560 RTGL 563
Cdd:smart00869 244 SAKL 247
|
|
| autotrans_barl |
TIGR01414 |
outer membrane autotransporter barrel domain; A number of Gram-negative bacterial proteins, ... |
286-525 |
1.00e-13 |
|
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: 73.57 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 286 YAISLLEAPRLQQVLTHSaqaggraradqvawHLDGKPDADGMrwWGSVRGDMQRYD--------HADLYDGMAPAGLFG 357
Cdd:TIGR01414 137 AALFLAELDTLRQRMGDL--------------RSAARDAGNGV--WARIFGGDNHLDgdagaagyDQNTTGVQLGGDILL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 358 VDWTAGDLVFGGFAGFGRMDADFGN--RNGSFKQDDTTLGGFFGWYTGP-VWVNAQVSYSWLSYDVDREVqlgpATRVHS 434
Cdd:TIGR01414 201 AGNADGDLHVGLMAGYAKADIKTRSykYGGKGKVDGYGLGLYGTWLQDSgAYVDGVLQYSRFRNDVSSTG----SNGKVS 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 435 GSPDGSNLTAALNAGY--SLGEGNLKYGPVAGLTWQKIKLDGYTESNDSAtALGyanQDIDSLVGRVGFQVRLD-----G 507
Cdd:TIGR01414 277 GKYNSNGFTASLEAGYryNLGGNGWYVEPQAQLSYFGVSGDDYKESNGTR-VLG---GGGDSLQGRLGLRVGYQfdlgtG 352
|
250
....*....|....*...
gi 503856910 508 AMVKPYLQATYDHEFKDG 525
Cdd:TIGR01414 353 RAVKPYLKANVLHEFKGG 370
|
|
| PLN03156 |
PLN03156 |
GDSL esterase/lipase; Provisional |
212-288 |
8.68e-06 |
|
GDSL esterase/lipase; Provisional
Pssm-ID: 178701 Cd Length: 351 Bit Score: 48.20 E-value: 8.68e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503856910 212 GLRVIPVDTFHMLQEIVANPGTYGFSNVTSTACNPAV--PLPACNPTSLVAANAQNTYVFADGIHPTTAVHQILGEYAI 288
Cdd:PLN03156 265 GIKLVFSNPYDIFMQIIRNPSAYGFEVTSVACCATGMfeMGYLCNRNNPFTCSDADKYVFWDSFHPTEKTNQIIANHVV 343
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YhjY |
COG5571 |
Uncharacterized conserved protein YhjY, contains autotransporter beta-barrel domain [General ... |
18-594 |
2.10e-103 |
|
Uncharacterized conserved protein YhjY, contains autotransporter beta-barrel domain [General function prediction only];
Pssm-ID: 444313 [Multi-domain] Cd Length: 648 Bit Score: 326.45 E-value: 2.10e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 18 FDQTVFFGDSLTDSGYYNPLLPAASRAVTGKFTTNPGWVWAEYVGDHFGTNAAPNGNGQTGDNYAAGGARIQASSVSALG 97
Cdd:COG5571 70 GFSGGAGSSSGTGPTANGGLAGAGGVDLAGAGGGGGASGLAGGAGGAGGTAAAGGAAAAGGGAAGNAATAAAAAAAGTAL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 98 AAPSVTSQINTYLTANGGRANPNALYTVWGGANDLLAASLAPAQAQAIIGSAVTAQVGAVATLQNAGARYVMVPTIPDVG 177
Cdd:COG5571 150 QLSGLTTAGAVGGVAGTAALNGATANTGLGAAAALAAAAAAAAAAAAAAAAAAAAATAAAAAAAAAAAAAVLASPAPAAG 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 178 LTPRFRAGGAVGMAQGTAAATAYNTALFNGLQSAGLRVIPVDTFHMLQEIVANPGTYGFSNVTSTACNPAVPLPACNPTS 257
Cdd:COG5571 230 GAAAAAAGAAAAAASAAANAATQANLLLLALALGSNGNAVGLNAVGLANEAAAPGAVGGDAGSTGATPSTLSSASCVASS 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 258 LVAANAQNTYVFADGIHPTTAVHQILGEYAISLLEAPRLQQVLTHSAQAGGRARADQVAWHLDGKPDADGMRWWGSVRGD 337
Cdd:COG5571 310 LTAANANTLYAAADTAGPAGATAALAAAAAAVLASAAAVAQAALALAAAGGQARSLAVAAGQGRGARGGQTRGGGGAGGT 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 338 MQRYDHADLYDGMAPAGLFGVDWTAGD-LVFGGFAGFGRMDADFGNrNGSFKQDDTTLGGFFGWYTGPVWVNAQVSYSWL 416
Cdd:COG5571 390 TGGGVGAGGGDGDGPNLTLGVDYRLSDnLLLGAALSYGRQDLDFGD-GGSYDARSTSLSLYAGYRAGGLWVDADLSYGDL 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 417 SYDVDREVQLGPATRVHSGSPDGSNLTAALNAGYSLGEGNLKYGPVAGLTWQKIKLDGYTESNDSATALGYANQDIDSLV 496
Cdd:COG5571 469 DYDIRRHIRLGPATRTETGDTDGSQWGARLTAGYDFTAGRLRTGPFAGLDYQKVKVDGYTETGAGSTALSFGDQDRDSLV 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 497 GRVGFQVRLDGAM-VKPYLQATYDHEFKDGGE-ASAWLQSMPEvGMYTVPGQNFDRNYATVVLGARTGL-WGLQSNIGLS 573
Cdd:COG5571 549 GSLGWRADYQLLGrFNPYAEVAYEHEFGDDDRdVTAGLASLPA-GSFSLPAAAPDKNWGRATLGASAALtNGVSLFAGYS 627
|
570 580
....*....|....*....|.
gi 503856910 574 TTTAQRSARDATLFVNFSGNF 594
Cdd:COG5571 628 GTFGRDDGRQTSVNLGLSARF 648
|
|
| COG3240 |
COG3240 |
Phospholipase/lecithinase/hemolysin [Lipid transport and metabolism, General function ... |
18-297 |
5.33e-85 |
|
Phospholipase/lecithinase/hemolysin [Lipid transport and metabolism, General function prediction only];
Pssm-ID: 442472 [Multi-domain] Cd Length: 305 Bit Score: 267.29 E-value: 5.33e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 18 FDQTVFFGDSLTDSGYYNPL---LPAASRAVTGKFTtNpGWVWAEYVGDHFGTNAAPNGNGqtGDNYAAGGARI--QASS 92
Cdd:COG3240 28 FSRIVVFGDSLSDTGNLFNLtggLPPSPPYFGGRFS-N-GPVWVEYLAAALGLPLTPSSAG--GTNYAVGGARTgdGNGV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 93 VSALGAAPSVTSQINTYLTANGGRANPNALYTVWGGANDLLAA----SLAPAQAQAIIGSAVTAQVGAVATLQNAGARYV 168
Cdd:COG3240 104 LGGAALLPGLAQQVDAYLAAAGGTADPNALYIVWAGANDLLAAlaavGATPAQAQAAATAAAANLAAAVGALAAAGARHI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 169 MVPTIPDVGLTPRFRAGGAVGMAQGTAAATAYNTALFNGLQSAGLRVIPVDTFHMLQEIVANPGTYGFSNVTsTACNPAv 248
Cdd:COG3240 184 LVPNLPDLGLTPAAQALGAAAAALLSALTAAFNQALAAALPALGVNIILFDVNSLFNEIIANPAAYGFTNVT-DACLSG- 261
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 503856910 249 plpacNPTSLVAANAQNTYVFADGIHPTTAVHQILGEYAISLLEAPRLQ 297
Cdd:COG3240 262 -----TVSALLCVANPDTYLFWDGVHPTTAAHRLIADYAYSALAAPGQL 305
|
|
| Triacylglycerol_lipase_like |
cd01847 |
Triacylglycerol lipase-like subfamily of the SGNH hydrolases, a diverse family of lipases and ... |
18-291 |
2.38e-70 |
|
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: 228.47 E-value: 2.38e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 18 FDQTVFFGDSLTDSGYYNPLLPAAsrAVTGKFTTNPGWVWAEYVGDHFG-TNAAPNGNGQTGDNYAAGGARIQASSVSAL 96
Cdd:cd01847 1 FSRVVVFGDSLSDVGTYNRAGVGA--AGGGRFTVNDGSIWSLGVAEGYGlTTGTATPTTPGGTNYAQGGARVGDTNNGNG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 97 GAA--PSVTSQINTYLTANGGRAnPNALYTVWGGANDLLAA-------SLAPAQAQAIIGSAVTAQVGAVATLQNAGARY 167
Cdd:cd01847 79 AGAvlPSVTTQIANYLAAGGGFD-PNALYTVWIGGNDLIAAlaalttaTTTQAAAVAAAATAAADLASQVKNLLDAGARY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 168 VMVPTIPDVGLTPRFRAGGAVGMAQGTAAATAYNTALFNGL-QSAGLRVIPVDTFHMLQEIVANPGTYGFSNVTSTACNP 246
Cdd:cd01847 158 ILVPNLPDVSYTPEAAGTPAAAAALASALSQTYNQTLQSGLnQLGANNIIYVDTATLLKEVVANPAAYGFTNTTTPACTS 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 503856910 247 AVPLPACNPTsLVAANAQNTYVFADGIHPTTAVHQILGEYAISLL 291
Cdd:cd01847 238 TSAAGSGAAT-LVTAAAQSTYLFADDVHPTPAGHKLIAQYALSRL 281
|
|
| fatty_acyltransferase_like |
cd01846 |
Fatty acyltransferase-like subfamily of the SGNH hydrolases, a diverse family of lipases and ... |
22-287 |
1.60e-49 |
|
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: 172.95 E-value: 1.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 22 VFFGDSLTDSG----YYNPLLPAASRAVTGKFTTNpGWVWAEYVGDHFGTNAapngnGQTGDNYAAGGARIQASSVSA-L 96
Cdd:cd01846 3 VVFGDSLSDTGnifkLTGGSNPPPSPPYFGGRFSN-GPVWVEYLAATLGLSG-----LKQGYNYAVGGATAGAYNVPPyP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 97 GAAPSVTSQINTYLTANGGRANPNALYTVWGGANDLLAASLAPAQAQAIIGSAVTAQVGAVATLQNAGARYVMVPTIPDV 176
Cdd:cd01846 77 PTLPGLSDQVAAFLAAHKLRLPPDTLVAIWIGANDLLNALDLPQNPDTLVTRAVDNLFQALQRLYAAGARNFLVLNLPDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 177 GLTPRFRAGGAVGMAQGTAAATAYNTALFNGLQS-----AGLRVIPVDTFHMLQEIVANPGTYGFSNVTstacnPAVPLP 251
Cdd:cd01846 157 GLTPAFQAQGDAVAARATALTAAYNAKLAEKLAElkaqhPGVNILLFDTNALFNDILDNPAAYGFTNVT-----DPCLDY 231
|
250 260 270
....*....|....*....|....*....|....*.
gi 503856910 252 ACNPTSLVAANAQNTYVFADGIHPTTAVHQILGEYA 287
Cdd:cd01846 232 VYSYSPREACANPDKYLFWDEVHPTTAVHQLIAEEV 267
|
|
| Autotransporter |
pfam03797 |
Autotransporter beta-domain; Secretion of protein products occurs by a number of different ... |
330-563 |
1.76e-35 |
|
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: 134.05 E-value: 1.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 330 WWGSVRGDMQRYDHADLYDGM---APAGLFGVDWTAGD-LVFGGFAGFGRMDADFGNRNGSFKQDDTTLGGFFGWY-TGP 404
Cdd:pfam03797 1 VWARGFGGRGKQDGDGGAAGYdadTGGLQVGADYRLGDnLRLGVAFGYSRSDADVDGRGGSGDSDSYSLGLYGTYYgDGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 405 VWVNAQVSYSWLSYDVDREVQLGPATRVHSGSPDGSNLTAALNAGYSLG-EGNLKYGPVAGLTWQKIKLDGYTESNDSAt 483
Cdd:pfam03797 81 WYLDGGLGYGWHDNDTRRSVDLGGFSETAKGDYDGNGFGASLEAGYRFAlGGGWTLEPFAGLAYVRLRLDGFTESGGAA- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 484 ALGYANQDIDSLVGRVGFQVR----LDGAMVKPYLQATYDHEFKDGGEAS-AWLQSMPEVGMYTVPGQNFDRNYATVVLG 558
Cdd:pfam03797 160 ALSVDSQSYDSLTGRLGLRLSytfdLGGGTLTPYARLGWRHEFGDDDPVTtAAFAGLSGAGSFTVAGADLARDSLELGAG 239
|
....*
gi 503856910 559 ARTGL 563
Cdd:pfam03797 240 LSAQL 244
|
|
| Autotransporter |
smart00869 |
Autotransporter beta-domain; Secretion of protein products occurs by a number of different ... |
332-563 |
9.92e-27 |
|
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: 109.58 E-value: 9.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 332 GSVRGDMQRYDHADLYDGMAPAGLFGVDWTAGD---LVFGGFAGFGRMDADFGNRNGSFKQDDTT--LGGFFGWYTGP-V 405
Cdd:smart00869 6 GFLRQDSSGSGGSAGFDYDSYGLQLGADYRLSDngnLSLGFAAGYGNSKVDFSGNKGSGKGDVDSygLGLYAGYSLGNgL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 406 WVNAQVSYSWLSYDVDREVQLGPATRVhSGSPDGSNLTAALNAGYSL-GEGNLKYGPVAGLTWQKIKLDGYTESNDSATA 484
Cdd:smart00869 86 YLDAQLGYGRSDNDTKRKVTLGGAGRA-KGSYDGTGYGASLEAGYRFyLGGGLTLTPFAGLAYSRVRQDGFTESGGGAFG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 485 LGYANQDIDSLVGRVGFQVRL-----DGAMVKPYLQATYDHEFKDGGEASAwLQSMPEVGMYTVPGQNFDRNYATVVLGA 559
Cdd:smart00869 165 LSVDSQSLDSLSLPLGLRLEYrlalgDGATLTPYLRLAYVHDFYDDNPVVT-ASLLGSGASFTTSGTDLDRNAAELGLGL 243
|
....
gi 503856910 560 RTGL 563
Cdd:smart00869 244 SAKL 247
|
|
| SGNH_plant_lipase_like |
cd01837 |
SGNH_plant_lipase_like, a plant specific subfamily of the SGNH-family of hydrolases, a diverse ... |
24-289 |
4.88e-23 |
|
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: 100.00 E-value: 4.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 24 FGDSLTDSGYyNPLLPAASRAV------------TGKFTtNpGWVWAEYVGDHFGTN------AAPNGNGQ--TGDNYAA 83
Cdd:cd01837 6 FGDSLVDTGN-NNYLPTLAKANfppygidfpgrpTGRFS-N-GRLIIDFIAEALGLPllpppyLSPNGSSDflTGVNFAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 84 GGARIQASSvSALGAAPSVTSQIN------TYLTANGGRAN-----PNALYTVWGGANDLLAASLAP----AQAQAIIGS 148
Cdd:cd01837 83 GGAGILDST-GFLGSVISLSVQLEyfkeykERLRALVGEEAaadilSKSLFLISIGSNDYLNNYFANptrqYEVEAYVPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 149 AVTAQVGAVATLQNAGARYVMVPTIPDVGLTPRFRAGGAvGMAQGTAAATAYNTALFN-GLQSA---------GLRVIPV 218
Cdd:cd01837 162 LVSNISSAIKRLYDLGARKFVVPGLGPLGCLPSQRTLFG-GDGGGCLEELNELARLFNaKLKKLlaelrrelpGAKFVYA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503856910 219 DTFHMLQEIVANPGTYGFSNVTSTACN---PAVPLPACNPTSLVAANAqNTYVFADGIHPTTAVHQILGEYAIS 289
Cdd:cd01837 241 DIYNALLDLIQNPAKYGFENTLKACCGtggPEGGLLCNPCGSTVCPDP-SKYVFWDGVHPTEAANRIIADALLS 313
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
21-563 |
3.51e-20 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 95.23 E-value: 3.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 21 TVFFGDSLTDSGYYNPLLPAASRAVTGKFTTNPGWVWAEYVGDHFGTNAAPNGNGQTGDNYAAGGARIQASSVSALGAAP 100
Cdd:COG4625 330 GGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGGGAGGTG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 101 SVTSQINTYLTANGGRANPNALYTVWGGANDLLAASLAPAQAQAIIGSAVTAQVGAVATLQNAGARYVMVPTIPDVGLTp 180
Cdd:COG4625 410 GGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGNNTYTGTT- 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 181 RFRAGGAVGMAQGTAAATAYNTALFNGLQSAGLRVIPVDTFHMLQEIVANPGTYGFSNVtSTACNPAVPLPACNPTSLVA 260
Cdd:COG4625 489 TVNGGGNYTQSAGSTLAVEVDAANSDRLVVTGTATLNGGTVVVLAGGYAPGTTYTILAV-AAALDALAGNGDLSALYNAL 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 261 ANAQNTYVFAdgihpttAVHQILGEYAISLLEApRLQQVLTHSAQAGGRARADQVAwHLDGKPDADGMRWWGSVRGDMQR 340
Cdd:COG4625 568 AALDAAAARA-------ALDQLSGEIHASAAAA-LLQASRALRDALSNRLRALRGA-GAAGDAAAEGWGVWAQGFGSWGD 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 341 YDHADLYDGM---APAGLFGVDWTAGD-LVFGGFAGFGRMDADFGNRNGSFKQDDTTLGGFFGWYTGPVWVNAQVSYSWL 416
Cdd:COG4625 639 QDGDGGAAGYdssTGGLLVGADYRLGDnWRLGVALGYSRSDVDVDDRGSSGDSDSYHLGLYGGYQFGALYLDGGLGYGWN 718
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 417 SYDVDREVQLGPATRVHSGSPDGSNLTAALNAGYSLGEGNLKYGPVAGLTWQKIKLDGYTESNDSAtALGYANQDIDSLV 496
Cdd:COG4625 719 DYDTDRTIAFGGLSRTATADYDGDTASAFLEAGYRFDLGGLTLTPFAGLAYVRLRTDGFTETGGAA-ALSVDSQSTDSLR 797
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503856910 497 GRVGFQVRLD-----GAMVKPYLQATYDHEFKD-GGEASAWLQSMPEVGmYTVPGQNFDRNYATVVLGARTGL 563
Cdd:COG4625 798 STLGLRASRTfslggGVTLTPSGRLGWRHEFGDdDPSTTASFAGAPGAA-FTVAGAPLARDALVLGAGLSARL 869
|
|
| autotrans_barl |
TIGR01414 |
outer membrane autotransporter barrel domain; A number of Gram-negative bacterial proteins, ... |
286-525 |
1.00e-13 |
|
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: 73.57 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 286 YAISLLEAPRLQQVLTHSaqaggraradqvawHLDGKPDADGMrwWGSVRGDMQRYD--------HADLYDGMAPAGLFG 357
Cdd:TIGR01414 137 AALFLAELDTLRQRMGDL--------------RSAARDAGNGV--WARIFGGDNHLDgdagaagyDQNTTGVQLGGDILL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 358 VDWTAGDLVFGGFAGFGRMDADFGN--RNGSFKQDDTTLGGFFGWYTGP-VWVNAQVSYSWLSYDVDREVqlgpATRVHS 434
Cdd:TIGR01414 201 AGNADGDLHVGLMAGYAKADIKTRSykYGGKGKVDGYGLGLYGTWLQDSgAYVDGVLQYSRFRNDVSSTG----SNGKVS 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 435 GSPDGSNLTAALNAGY--SLGEGNLKYGPVAGLTWQKIKLDGYTESNDSAtALGyanQDIDSLVGRVGFQVRLD-----G 507
Cdd:TIGR01414 277 GKYNSNGFTASLEAGYryNLGGNGWYVEPQAQLSYFGVSGDDYKESNGTR-VLG---GGGDSLQGRLGLRVGYQfdlgtG 352
|
250
....*....|....*...
gi 503856910 508 AMVKPYLQATYDHEFKDG 525
Cdd:TIGR01414 353 RAVKPYLKANVLHEFKGG 370
|
|
| Lipase_GDSL |
pfam00657 |
GDSL-like Lipase/Acylhydrolase; |
22-286 |
1.29e-11 |
|
GDSL-like Lipase/Acylhydrolase;
Pssm-ID: 459892 [Multi-domain] Cd Length: 210 Bit Score: 64.13 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 22 VFFGDSLTDSGYYNPllpaasravTGKFTtnPGWVWAEYVGDHFGtnaAPNGNGQTGDNYAAGGARIQASsvsalgaaPS 101
Cdd:pfam00657 2 VAFGDSLTDGGGDGP---------GGRFS--WGDLLADFLARKLG---VPGSGYNHGANFAIGGATIEDL--------PI 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 102 VTSQINTYLTANGGRANPnALYTVWGGANDLLAASLAPAQAQAIIGSAVTAQVGAVATLqNAGARYVMVPTIPDVGLTPR 181
Cdd:pfam00657 60 QLEQLLRLISDVKDQAKP-DLVTIFIGANDLCNFLSSPARSKKRVPDLLDELRANLPQL-GLGARKFWVHGLGPLGCTPP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 182 FRAGGAVGMAQGTAAATAYNTALFNGLQSAGLRVIPVDtfhmlqeivanpgTYGFSNVTSTACnpavplpacnptslvaa 261
Cdd:pfam00657 138 KGCYELYNALAEEYNERLNELVNSLAAAAEDANVVYVD-------------IYGFEDPTDPCC----------------- 187
|
250 260
....*....|....*....|....*
gi 503856910 262 naqNTYVFADGIHPTTAVHQILGEY 286
Cdd:pfam00657 188 ---GIGLEPDGLHPSEKGYKAVAEA 209
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
362-529 |
5.22e-07 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 52.64 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 362 AGDLVFGGFAGFGRMDAD---FGNRNGSFKQDDTTLGGFFGWY--TGpVWVNAQVSYSWLSYDVDrevqlGPATRVHSGS 436
Cdd:COG3468 619 GGRLHVGVMAGYGNGDSDvrsRATGTGKGDVDGYSLGLYGTWYgnNG-FYVDGVLQYSWFDNDVS-----SDDLGGVTGS 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 437 PDGSNLTAALNAGYS--LGEGnLKYGPVAGLTWQKIKLDGYTESNDSATALgyanQDIDSLVGRVGFQVRLDGAM----- 509
Cdd:COG3468 693 YDGNGYSASLEAGYPfkLGEG-WSLEPQAQLIYQGVDFDDFTDSNGTRVSG----DDGDSLQGRLGLRLGYEFHWddgra 767
|
170 180
....*....|....*....|
gi 503856910 510 VKPYLQATYDHEFKDGGEAS 529
Cdd:COG3468 768 LQPYLEANWLHEFLGDNSVT 787
|
|
| PLN03156 |
PLN03156 |
GDSL esterase/lipase; Provisional |
212-288 |
8.68e-06 |
|
GDSL esterase/lipase; Provisional
Pssm-ID: 178701 Cd Length: 351 Bit Score: 48.20 E-value: 8.68e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503856910 212 GLRVIPVDTFHMLQEIVANPGTYGFSNVTSTACNPAV--PLPACNPTSLVAANAQNTYVFADGIHPTTAVHQILGEYAI 288
Cdd:PLN03156 265 GIKLVFSNPYDIFMQIIRNPSAYGFEVTSVACCATGMfeMGYLCNRNNPFTCSDADKYVFWDSFHPTEKTNQIIANHVV 343
|
|
| PRK15381 |
PRK15381 |
type III secretion system effector; |
22-281 |
1.82e-05 |
|
type III secretion system effector;
Pssm-ID: 185279 Cd Length: 408 Bit Score: 47.35 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 22 VFFGDSLTDS-----GYYNPLLPAASRAVTGKFTTnpGWVWAEYVgdhfgtnAAPNGNGQTGDNYAAGGARIQA-SSVSA 95
Cdd:PRK15381 146 VFFGDSLSDSlgrmfEKTHHILPSYGQYFGGRFTN--GFTWTEFL-------SSPHFLGKEMLNFAEGGSTSASySCFNC 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 96 LGAAPSVTS-QINTYLTANggraNPNALYTVwgGANDLLAASlapaqaQAIIGSAVTAQVGAVATLQNAGARYVMVPTIP 174
Cdd:PRK15381 217 IGDFVSNTDrQVASYTPSH----QDLAIFLL--GANDYMTLH------KDNVIMVVEQQIDDIEKIISGGVNNVLVMGIP 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503856910 175 DVGLTPrfraggaVGMAQGTAAATAYNTALFNGLQSAGL----------RVIPVDTFHMLQEIVANPGTYGFSNVTSTAC 244
Cdd:PRK15381 285 DLSLTP-------YGKHSDEKRKLKDESIAHNALLKTNVeelkekypqhKICYYETADAFKVIMEAASNIGYDTENPYTH 357
|
250 260 270
....*....|....*....|....*....|....*..
gi 503856910 245 NPAVPLPACNPTSLvaaNAQNTYVFADGIHPTTAVHQ 281
Cdd:PRK15381 358 HGYVHVPGAKDPQL---DICPQYVFNDLVHPTQEVHH 391
|
|
| |
