|
Name |
Accession |
Description |
Interval |
E-value |
| PQQ_ADH_I |
cd10277 |
Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); ... |
26-521 |
0e+00 |
|
Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); This bacterial family of homodimeric ethanol dehydrogenases utilize pyrroloquinoline quinone (PQQ) as a cofactor. It represents proteins whose expression may be induced by ethanol, and which are similar to quinoprotein methanol dehydrogenases, but have higher specificities for ethanol and other primary and secondary alcohols. Dehydrogenases with PQQ cofactors, such as ethanol, methanol, and membrane-bound glucose dehydrogenases, form an 8-bladed beta-propeller.
Pssm-ID: 199835 [Multi-domain] Cd Length: 529 Bit Score: 580.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 26 IANADAEPGNWLTYSGNYAATRYSALNQVNTSNVKRLAPVWIYQLKSAGAPFECTPLVADKIMYISEPPSTVTALDIATG 105
Cdd:cd10277 1 LLNDAKETGNWLTYGRGYNGQRYSPLKQINTDNVKNLVPAWSFSFGGKQRGQESQPIVNDGVMYVTTSYNRVFAIDAKTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 106 RKIWTYTPEMPKDVKFMgFGPVNRGVALLDNNVYIGTLNAHLVCLDAKSGAIKWNVTVADNKLGYAITCAPVAIDGKIII 185
Cdd:cd10277 81 KELWKYKHRLPEDIRPC-CDVVNRGVALYGDKVYFGTLDAHLVALDAKTGKVVWKKKVADYKAGYSMTLAPLVVKGKVIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 186 GISGGEAGIRGFLDAYNAKTGKLEWRLYTIPGKGEPGNE-TWQGDSWKTGGAPTWVPGSYDKELNLLYWGIGNPGPdWNG 264
Cdd:cd10277 160 GVSGGEFGVRGFIAALDAETGKEVWRTYTVPGPGEPGSTdTWPGDAWKTGGGATWLTGTYDPETNLLYWGVGNPAP-WNG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 265 DNRKGDNLYSCSVLAINPTTGKMAWYFQFTPHDTHDWDANQIPVLLDIKIKGIPRKVLATANRNGFYYVLDRKTGEFLAG 344
Cdd:cd10277 239 DLRPGDNLYTSSVLALDPDTGKIKWHYQYTPNDTWDYDGVNEPVLFDYTKNGKPVKALVHADRNGFFYVLDRTNGKLIWA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 345 AAYAKQTWARGLDAK-GRPIVIPGKEPTEKGNLV--YPSLQGATNWFSPSYSKSAGLFYVSVREMGSLYFKKEVEYKPGE 421
Cdd:cd10277 319 TPFVKKITWASIDLKtGRPIYDEDKVPPKKGKTVdfCPSFLGGKNWPPMAYSPDTGLFYVPANHWCMDLTGEPVSYKKGA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 422 YFMGGG-EQLLPGDNASGAVKALDAATGETKWTFRLQSPPWSGVLSTAGGLVFGGSVEGNFFALDAVTGKSKWQFQTGGQ 500
Cdd:cd10277 399 AYLGAGfTIKPPFEDHIGELQAIDPTTGKKVWEHKTPLPLWGGVLTTAGGLVFTGTPDGYFRAFDAKTGKELWEFQTGSG 478
|
490 500
....*....|....*....|.
gi 2198886489 501 IISNPMSFSVNGQQRVAITAG 521
Cdd:cd10277 479 IIGPPVTWEVDGKQYVAVLSG 499
|
|
| Gcd |
COG4993 |
Glucose dehydrogenase, PQQ-dependent [Carbohydrate transport and metabolism]; |
32-529 |
0e+00 |
|
Glucose dehydrogenase, PQQ-dependent [Carbohydrate transport and metabolism];
Pssm-ID: 444017 [Multi-domain] Cd Length: 515 Bit Score: 566.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 32 EPGNWLTYSGNYAATRYSALNQVNTSNVKRLAPVWIYQLK-SAGAPFECTPLVADKIMYISEPPSTVTALDIATGRKIWT 110
Cdd:COG4993 1 DPGDWLAYGGDYAGQRYSPLDQINPDNVKKLKVAWTFSTGdLPERGHEATPLVVDGVLYVCTPHNRVFALDAATGKELWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 111 YTPEMPKDVkfMGFGPVNRGVALLDNNVYIGTLNAHLVCLDAKSGAIKWNVTVADNKLGYAITCAPVAIDGKIIIGISGG 190
Cdd:COG4993 81 YDPKLPDDA--ACCDVVNRGVAYYDGRIFLGTLDGRLVALDAKTGKVCWDVKVGDPKKGYTITSAPLVVKDKVIVGGSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 191 EAGIRGFLDAYNAKTGKLEWRLYTIPGKGEPGNETWQ-GDSWKTGGAPTWVPGSYDKELNLLYWGIGNPGPDWNGDNRKG 269
Cdd:COG4993 159 EFGPRGVVRAYDARTGKLVWRFDTIPDPGEPGAETWPpGDTWKRGGGNVWGTMSYDPELGLVYLPTGNPAPDWNGGQRPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 270 DNLYSCSVLAINPTTGKMAWYFQFTPHDTHDWDANQIPVLLDIKIKGIPRKVLATANRNGFYYVLDRKTGEFLAGAAYAK 349
Cdd:COG4993 239 DNLYSSSIVALDADTGELKWHYQTVPHDLWDYDGPNEPILVDLPVDGKTRKALVQATKNGFIYVLDRETGEPLVTQPFVK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 350 -QTWARGLDAKGR-PIVIPgkePTEKGN--LVYPSLQGATNWFSPSYSKSAGLFYVSVREMGSLYFKKEVEYKPGEYFMG 425
Cdd:COG4993 319 pPNWATEIDMWGAtPIQTP---PSLDGKttLICPGALGGKNWGPAAYDPETGLLYVPANELCMDYELVPREYQAGAPYLG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 426 GGEQLLPGDN-ASGAVKALDAATGETKWTFRLQSPPWSGVLSTAGGLVFGGSVEGNFFALDAVTGKSKWQFQTGGQIISN 504
Cdd:COG4993 396 ATLTMYPCPApPWGTLTAIDLNTGKIVWQVPLGFPNWGGPLATAGGLVFIGTLDGYLRAFDAKTGKELWKFRLPSGGQAT 475
|
490 500 510
....*....|....*....|....*....|....*....
gi 2198886489 505 PMSFSVNGQQRVAITAG--------------NSLIVFGL 529
Cdd:COG4993 476 PMTYEVDGKQYVAVAAGgggwlglglytpqgDYLIAFAL 514
|
|
| PQQ_enz_alc_DH |
TIGR03075 |
PQQ-dependent dehydrogenase, methanol/ethanol family; This protein family has a phylogenetic ... |
18-521 |
0e+00 |
|
PQQ-dependent dehydrogenase, methanol/ethanol family; This protein family has a phylogenetic distribution very similar to that coenzyme PQQ biosynthesis enzymes, as shown by partial phylogenetic profiling. Genes in this family often are found adjacent to the PQQ biosynthesis genes themselves. An unusual, strained disulfide bond between adjacent Cys residues contributes to PQQ-binding, as does a Trp residue that is part of a PQQ enzyme repeat (see pfam01011). Characterized members include the dehydrogenase subunit of a membrane-anchored, three subunit alcohol (ethanol) dehydrogenase of Gluconobacter suboxydans, a homodimeric ethanol dehydrogenase in Pseudomonas aeruginosa, and the large subunit of an alpha2/beta2 heterotetrameric methanol dehydrogenase in Methylobacterium extorquens.
Pssm-ID: 274419 [Multi-domain] Cd Length: 527 Bit Score: 541.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 18 AAQVSYQRIANADAEPGNWLTYSGNYAATRYSALNQVNTSNVKRLAPVWIYQLKSAGApFECTPLVADKIMYISEPPSTV 97
Cdd:TIGR03075 3 AAAVTNEDLLNDAKDPSDWLTYGGGYAGQRYSPLDQINTDNVKKLQPAWTFSLGKQRG-QESQPLVVDGVMYVTTSYSRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 98 TALDIATGRKIWTYTPEMPKDV-KFMGFGPVNRGVALLDNNVYIGTLNAHLVCLDAKSGAIKWNVTVADNKLGYAITCAP 176
Cdd:TIGR03075 82 YALDAKTGKILWKYDPKLPDDIiPVMCCDVVNRGAALYDGKVFFGTLDARLVALDAKTGKVVWSKKNGDYKKGYTITAAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 177 VAIDGKIIIGISGGEAGIRGFLDAYNAKTGKLEWRLYTIPG------------KGEPGNETWQGDSWKTGGAPTWVPGSY 244
Cdd:TIGR03075 162 LVVKGKVITGISGGEFGVRGYVTAYDAKTGKLVWRRYTVPGdmgylkktgkpvGGDPGAKTWPGDAWKTGGGATWGTGSY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 245 DKELNLLYWGIGNPGPdWNGDNRKGDNLYSCSVLAINPTTGKMAWYFQFTPHDTHDWDANQIPVLLDIKIKGIPRKVLAT 324
Cdd:TIGR03075 242 DPETNLIYFGTGNPAP-WNSHLRPGDNLYTSSIVARDPDTGKIKWHYQTTPHDEWDYDGVNEMILFDLKKDGKPRKLLAH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 325 ANRNGFYYVLDRKTGEFLAGAAYAK-QTWARGLDAK-GRPIVIPGKEPT--EKGN--LVYPSLQGATNWFSPSYSKSAGL 398
Cdd:TIGR03075 321 ADRNGFFYVLDRTNGKLLSAEPFVDkVNWATGVDLKtGRPIEVPEARSTdgKKGKpvEVCPGFLGGKNWQPMAYSPKTGL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 399 FYVSVREMGSLYFKKEVEYKPGEYFMGGGEQLLP-GDNASGAVKALDAATGETKWTFRLQSPPWSGVLSTAGGLVFGGSV 477
Cdd:TIGR03075 401 FYVPANHVCMDYWPEKVSYKKGAAYLGAGFTIKPpPDDHIGSLIAWDPITGKIVWEHKEDFPLWGGVLATAGDLVFTGTL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2198886489 478 EGNFFALDAVTGKSKWQFQTGGQIISNPMSFSVNGQQRVAITAG 521
Cdd:TIGR03075 481 EGYFKAFDAKTGEELWKFKTGSGIVGPPVTYEQDGKQYVAVLSG 524
|
|
| acido_non_PQQ |
TIGR04528 |
acido-empty-quinoprotein group A; Members of this family closely resemble quinoproteins and ... |
36-529 |
0e+00 |
|
acido-empty-quinoprotein group A; Members of this family closely resemble quinoproteins and quinohemoproteins such as PQQ-dependent methanol, glucose, and shikimate dehydrogenases, but restricted to species of Acidobacteria unable to synthesize PQQ. Seven members occur in candidatus Solibacter usitatus Ellin6076, eleven in Acidobacteriaceae bacterium KBS 96, etc. Members have N-terminal signal sequences. They lack the pair of adjacent Cys residues, involved in electron transfer, typical for family TIGR03075, and they lack CxxCH motifs for cytochrome c-like heme-binding. What cofactor these paralogous families of enzymes might use is unclear.
Pssm-ID: 275321 Cd Length: 491 Bit Score: 527.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 36 WLTYSGNYAATRYSALNQVNTSNVKRLAPVWIYQLKSAGAP-FECTPLVADKIMYISEPpSTVTALDIATGRKIWTYTPE 114
Cdd:TIGR04528 6 WPTYNGDYSGRRFSPLTQINRANVKSLSLAWAFQTTGGGGGtIKSTPLLVNGILYFTVP-DNVWAVDARTGRQLWHYTWP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 115 mPKDVKFMGfgpvNRGVALLDNNVYIGTLNAHLVCLDAKSGAIKWNVTVADNKLGYAITCAPVAIDGKIIIGISGGEAGI 194
Cdd:TIGR04528 85 -PNGGTHIG----NRGVGMYKDWLYFETPDCHLVSLDAKDGKERWDVEIADLKLGYFSTMAPLVVKNHVIVGVSGDDLDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 195 RGFLDAYNAKTGKLEWRLYTIPGKGEPGNETW-QGDSWKTGGAPTWVPGSYDKELNLLYWGIGNPGPDWNGDNRKGDNLY 273
Cdd:TIGR04528 160 PGFLESRDPETGKLQWRWYTTPKPGEPGSETWpNLDAMAHGGGMTWMTGTYDPELNLYYWGTGNPTPVLAGKGRPGDNLY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 274 SCSVLAINPTTGKMAWYFQFTPHDTHDWDANQIPVLLDIKIKGIPRKVLATANRNGFYYVLDRKTGEFLAGAAYAKQTWA 353
Cdd:TIGR04528 240 TCSIVALNPDTGKLAWYFQPSPHDTHDWDAVETPVLFDGTFDGKPRKLLAQASRNGYFFVLDRTTGKNLLTSPFVDTNWA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 354 RGLDAKGRPIVIPGKEPTEKGNLVYPSLQGATNWFSPSYSKSAGLFYVSVREMGSLYFKKEVEYKPgeYFMGGGEQllpG 433
Cdd:TIGR04528 320 KGIDAKGQPIPNPAKEPAPDGALVSPDSGGATNWPPPSFDPQTGLFYVNAHRSYSIYYLTDPDDKP--EGWGGADY---G 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 434 DNASGAVKALDAATGETKWTFRLQSP-PWSGVLSTAGGLVFGGSVEGNFFALDAVTGKSKWQFQTGGQIISNPMSFSVNG 512
Cdd:TIGR04528 395 LWSKSFLEAIDYKTGKIRWTHEWGEGgGGAGVLTTAGGLLFTGDASGNLLALDAATGKTLWHARLGGSVSNGPITYELDG 474
|
490
....*....|....*..
gi 2198886489 513 QQRVAITAGNSLIVFGL 529
Cdd:TIGR04528 475 KQYVLVAAGDTLYAFAL 491
|
|
| PQQ_ADH_II |
cd10279 |
PQQ_like domain of the quinohemoprotein alcohol dehydrogenase (type II); This family of ... |
34-522 |
1.57e-155 |
|
PQQ_like domain of the quinohemoprotein alcohol dehydrogenase (type II); This family of monomeric and soluble type II alcohol dehydrogenases utilizes pyrroloquinoline quinone (PQQ) as a cofactor and is related to ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller.
Pssm-ID: 199837 [Multi-domain] Cd Length: 549 Bit Score: 455.18 E-value: 1.57e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 34 GNWLTYSGNYAATRYSALNQVNTSNVKRLAPVWIYQLKSAGAPfECTPLVADKIMYISEPPSTVTALDIATGRKIWTYTP 113
Cdd:cd10279 1 GNWLSYGRDYDEQRFSPLTQINRSNVGQLGLAWYFDLDTNRGQ-EATPLVVDGVMYVSGPWSVVYALDARTGKLLWQYDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 114 EMPKDVKFMG-FGPVNRGVALLDNNVYIGTLNAHLVCLDAKSGAIKWNVTVADNKLGYAITCAPVAIDGKIIIGISGGEA 192
Cdd:cd10279 80 EVDRESGRKAcCDVVNRGVAVWDGKVFVGTLDGRLIALDAKTGKEVWSVDTIDPRKPYTITGAPRVAKGKVVIGNGGAEF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 193 GIRGFLDAYNAKTGKLEWRLYTIPGKGEPGNE----------TWQGDSWKTGGAPT-WVPGSYDKELNLLYWGIGNPGPd 261
Cdd:cd10279 160 GVRGYVSAYDAETGKLVWRFYTVPGNPAKPFEhasleaaaatWWTGEWWRTGGGGTvWDSITYDPELDLLYIGTGNGSP- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 262 WNGDNR---KGDNLYSCSVLAINPTTGKMAWYFQFTPHDTHDWDANQIPVLLDIKIKGIPRKVLATANRNGFYYVLDRKT 338
Cdd:cd10279 239 WNRKVRspgGGDNLFLSSIVALDADTGRYKWHYQTTPGDTWDYTATQPIILADLEIDGKPRKVLMHAPKNGFFYVLDRAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 339 GEFLAGAAYAKQTWARGLDAK-GRPIVIPGKEPTEKGNLVYPSLQGATNWFSPSYSKSAGLFYVSVREMGSLYFKKEVEY 417
Cdd:cd10279 319 GKLLSAEPFVPVNWATGIDLKtGRPIENPEARYTKGPKLVFPGPLGAHNWHPMSYNPDTGLVYIPAQEIPAVYEDDPGDF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 418 K-----------PGEYFMGGGEQLLPGDNASGAVKALDAATGETKWTfRLQSPPWS-GVLSTAGGLVFGGSVEGNFFALD 485
Cdd:cd10279 399 GynplgwntgitPDATPPPAAAKRALRKATRGRLVAWDPVTQKAAWR-VEHPGPWNgGVLATAGNLVFQGTADGELAAYD 477
|
490 500 510
....*....|....*....|....*....|....*..
gi 2198886489 486 AVTGKSKWQFQTGGQIISNPMSFSVNGQQRVAITAGN 522
Cdd:cd10279 478 ARTGEKLWSFDTGSGIVAAPMTYSVDGEQYVAVLAGW 514
|
|
| PQQ_MDH |
cd10278 |
Large subunit of methanol dehydrogenase (moxF); Methanol dehydrogenase is a key enzyme in the ... |
36-521 |
1.35e-134 |
|
Large subunit of methanol dehydrogenase (moxF); Methanol dehydrogenase is a key enzyme in the utilization of C1 compounds as a source of energy and carbon by bacteria. It catalyzes the oxidation of methanol to formaldehyde, transfering two electrons per methanol to cytochrome c(L) as the acceptor. Methanol dehydrogenase belongs to a family of dehydrogenases with pyrroloquinoline quinone (PQQ) as cofactor, which also includes dehydrogenases specific to other alcohols and membrane-bound glucose dehydrogenases. This alignment model for the large subunit contains an 8-bladed beta-propeller; the functional enzyme forms a heterotetramer composed of two large and two small subunits.
Pssm-ID: 199836 [Multi-domain] Cd Length: 553 Bit Score: 401.71 E-value: 1.35e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 36 WLTYSGNYAATRYSALNQVNTSNVKRLAPVWIYqlkSAGA--PFECTPLVADKIMYISEP-PSTVTALDIATGRKI-WTY 111
Cdd:cd10278 1 WVMPGKDYANTRYSPLAQINKDNVKNLKVAWTF---STGVlrGHEGAPLVVGDTMYVVTPfPNNVYALDLNDPGKIlWKY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 112 TPEM-PKDVKFMGFGPVNRGVALLDNNVYIGTLNAHLVCLDAKSGAIKWNVTVADNKLGYAITCAPVAIDGKIIIGISGG 190
Cdd:cd10278 78 KPKQdPSAVAVACCDVVNRGLAYADGKIFFNQLDGHLVALDAKTGKEVWKVKNGDPKVGETLTMAPLVVKDKVIVGISGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 191 EAGIRGFLDAYNAKTGKLEWRLYTI------------------PGKGEPGNETWQGDSWKTGGAPTWVPGSYDKELNLLY 252
Cdd:cd10278 158 EFGVRGYVTAYDLKTGKLVWRAYSTgpdkdvligpdfnpfnphDGGKDLGLSTWPGDAWKIGGGTNWGWYSYDPKLNLVY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 253 WGIGNPGPdWNGDNRKGDNLYSCSVLAINPTTGKMAWYFQFTPHDTHDWDANQIPVLLDIKIKGIPRKVLATANRNGFYY 332
Cdd:cd10278 238 YGTGNPGP-WNPTQRPGDNKWSMTIFARDPDTGEAKWAYQMTPHDEWDYDGVNEMILVDQTVDGKKRKLLVHFDRNGFVY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 333 VLDRKTGEFLAGAAYAKQTWARGLDAK-GRPIVIPGKEPTEKGNL--VYPSLQGATNWFSPSYSKSAGLFYVSVREMGSL 409
Cdd:cd10278 317 TLDRTTGELLSAEKFDPVNNWKGVDLKtGRPVKDPEKSTHMDHNVtdICPSAMGGKDQQPSSYSPKTGLFYVPTNHLCMD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 410 YFKKEVEYKPGEYFMGGGEQLLPGDN-ASGAVKALDAATGETKWTFRLQSPPWSGVLSTAGGLVFGGSVEGNFFALDAVT 488
Cdd:cd10278 397 YEPFEVNYTAGQPYVGATLAMYPGPGgHMGQFKAWDPVTGKTKWEIKERFPVWSGTLATAGGLVFYGTLDGWFKAVDAKT 476
|
490 500 510
....*....|....*....|....*....|...
gi 2198886489 489 GKSKWQFQTGGQIISNPMSFSVNGQQRVAITAG 521
Cdd:cd10278 477 GKLLWKFKLPSGIIGNPITYKHDGKQYVAVLSG 509
|
|
| PQQ_DH_like |
cd00216 |
PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases ... |
58-521 |
2.65e-95 |
|
PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases with pyrroloquinoline quinone (PQQ) as a cofactor, such as ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller, and the family also includes distantly related proteins which are not enzymatically active and do not bind PQQ.
Pssm-ID: 199833 [Multi-domain] Cd Length: 434 Bit Score: 296.44 E-value: 2.65e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 58 NVKRLAPVWIYQLKSAGAPF-ECTPLVADKIMYISEPPSTVTALDIATGRKIWTYTPEMPKDVKFMGFGPVNRGVALLDN 136
Cdd:cd00216 3 NVFQLTPAWSFSTGDGGNRGsELTPIVVDGVMYATTSFSRVFALDADDGKEIWSYDPALKDGWFEACCDLVNRGVAVWGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 137 NVYIGTLNAHLVCLDAKSGAIKWNVTVADNKLGYAITCAPVAIDGKIIIGISGGEAGIRGFLDAYNAKTGKLEWRLYTIP 216
Cdd:cd00216 83 KVYIGVLDGRVYALNAETGKVAWKVKNADVLGGYTATSAPVVVDGLVIIGSSGDEFGVRGYLTAYDVATGEEKWRFYLVM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 217 G-----------KGEPGNETWQGDSWKTGGAPTWVPGSYDKELNLLYWGIGNPGP-DWNGDNRKGDNLYSCSVLAINPTT 284
Cdd:cd00216 163 PdpnllpgkdstVTDRNTPTGDEHTWTSGGGTGWSSAAYDAELNLIYVGGGNPTPwNWGGNRTPGDNLYTSSIVAVNADT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 285 GKMAWYFQFTPHDTHDWDANQIPVLLDIKIKGIPRKVLATANRNGFYYVLDRKTGEFLagaayakqtWARGLDakgrPIv 364
Cdd:cd00216 243 GEMKWQYQTTPHDAWDYDGDNTPVLADIKVKGKKVKVLFAPAKNGNFYVLDRRNGELV---------SARPLV----PD- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 365 ipgkeptekgnlvypslqgatnwfspSYSKSAGLFYVsvremgslyfkkeveykpgeyfmgggeqllpgdNASGAVKALD 444
Cdd:cd00216 309 --------------------------SYDPDRELFYV---------------------------------PANGRIMALD 329
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2198886489 445 AATGETKWTFRLQSPPWSGVLSTAGGLVFGGSVEGNFFALDAVTGKSKWQFQTGGQIISNPMSFSVNGQQRVAITAG 521
Cdd:cd00216 330 PVTGVVVWEKSELHPLLGGPLSTAGNLVFVGTSDGYLKAYNADTGEKLWQQKVPSGFQAEPVTYEVDGEQYVLIQAG 406
|
|
| PQQ_mGDH |
cd10280 |
Membrane-bound PQQ-dependent glucose dehydrogenase; This bacterial subfamily of enzymes ... |
36-529 |
2.51e-90 |
|
Membrane-bound PQQ-dependent glucose dehydrogenase; This bacterial subfamily of enzymes belongs to the dehydrogenase family with pyrroloquinoline quinone (PQQ) as cofactor, and is the only subfamily that is bound to the membrane. Glucose dehydrogenase converts D-glucose to D-glucono-1,5-lactone in a reaction that is coupled with the respiratory chain in the periplasmic oxidation of sugars and alcohols in gram-negative bacteria. Ubiquinone functions as the electron acceptor. The alignment model contains an 8-bladed beta-propeller.
Pssm-ID: 199838 [Multi-domain] Cd Length: 616 Bit Score: 289.09 E-value: 2.51e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 36 WLTYSGNYAATRYSALNQVNTSNVKRLAPVWIYQLKSAGAP------FECTPLVADKIMYISEPPSTVTALDIATGRKIW 109
Cdd:cd10280 1 WPAYGGDPGGTRYSPLDQITPDNVGKLKVAWTYHTGDLPGPdgnegtFEATPLKVGGTLYLCTPHNRVIALDAATGKELW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 110 TYTPEMPKDVKFMGFgpVNRGVA---------LLDNNVYIGTLNAHLVCLDAKSGA------------IKWNVTVADNKL 168
Cdd:cd10280 81 RFDPKAGADAAPGHQ--TCRGVSywedgaaaaACARRIFFGTGDARLIALDARTGKpcpdfgdngvvdLREGLGRVKPGF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 169 gYAITCAPVAIDGK----IIIGISGGEAGIRGFLDAYNAKTGKLEWRLYTIPGKGEPGNETwqGDSWKT-GGAPTWVPGS 243
Cdd:cd10280 159 -YSSTSPPTVYGDLvivgSAVADNQAVDAPSGVIRAFDVRTGKLVWAFDTIPPPGEAGPDT--AGAWYTrGGPNVWAGMS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 244 YDKELNLLYWGIGNPGPDWNGDNRKGDNLYSCSVLAINPTTGKMAWYFQFTPHDTHDWDANQIPVLLDIKIKGIPRKVLA 323
Cdd:cd10280 236 ADEKLGLVYLPTGSATPDFYGGDRPGDNLFANSLVALDAATGKRRWHFQTVHHDLWDYDLPAQPTLVDVPRDGKTVPAVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 324 TANRNGFYYVLDRKTGE-------------------------F----------------LAGAAYAKQTWARGLDAKGR- 361
Cdd:cd10280 316 QPTKQGFVFVLDRRTGKplwpveerpvpqgdvpgertsptqpFptlpppfarqglteddMWGATPFDQLACRIQFRSLRy 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 362 -PIVIPgkePTEKGNLVYPSLQGATNWFSPSYSKSAGLFYVSVREMGSL---------------------YFKKEVEYKP 419
Cdd:cd10280 396 eGLFTP---PSLDGTLIFPGNDGGANWGGAAVDPERGILYVNSNRLPFViqlvprapgdpagvagggeggGGGGGPSPQA 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 420 GEYFMGGGEQLLPGDNAS------GAVKALDAATGETKW-----------------TFRLQSPPWSGVLSTAGGLVF-GG 475
Cdd:cd10280 473 GTPYGVGRGRFLSPLGLPcqappwGTLTAIDLNTGKILWqvplgtvpdlgpkgiplPIPTGTPNLGGPVVTAGGLVFiAA 552
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2198886489 476 SVEGNFFALDAVTGKSKWQFQ--TGGQiiSNPMSFSVNGQQRVAITAG----------NSLIVFGL 529
Cdd:cd10280 553 TQDNYLRAFDKATGKELWEARlpAGGQ--ATPMTYEVDGKQYVVIAAGghgslgtkrgDSVIAYAL 616
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
436-527 |
2.59e-11 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 63.58 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 436 ASGAVKALDAATGETKWTFRLQSPpWSGVLSTAGGLVFGGSVEGNFFALDAVTGKSKWQFQTGGQIISNPmsfSVNGQQR 515
Cdd:pfam13360 1 ADGVVTALDAATGAELWRVDLETG-LGGGVAVDGGRLFVATGGGQLVALDAATGKLLWRQTLSGEVLGAP---LVAGGRV 76
|
90
....*....|..
gi 2198886489 516 VAITAGNSLIVF 527
Cdd:pfam13360 77 FVVAGDGSLIAL 88
|
|
| assembly_YfgL |
TIGR03300 |
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
436-527 |
8.13e-11 |
|
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274511 [Multi-domain] Cd Length: 377 Bit Score: 63.80 E-value: 8.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 436 ASGAVKALDAATGETKWTFRLQSPPWSGVLStAGGLVFGGSVEGNFFALDAVTGKSKWQFQTGGQIISNPMsfsVNGQQR 515
Cdd:TIGR03300 73 ADGTVAALDAETGKRLWRVDLDERLSGGVGA-DGGLVFVGTEKGEVIALDAEDGKELWRAKLSSEVLSPPL---VANGLV 148
|
90
....*....|..
gi 2198886489 516 VAITAGNSLIVF 527
Cdd:TIGR03300 149 VVRTNDGRLTAL 160
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
435-527 |
1.70e-10 |
|
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441129 [Multi-domain] Cd Length: 370 Bit Score: 62.91 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 435 NASGAVKALDAATGETKWTFRLQSPPWSGVlSTAGGLVFGGSVEGNFFALDAVTGKSKWQFQTGGQIISNPmsfSVNGQQ 514
Cdd:COG1520 64 DADGRVAALDAATGKELWRVDLGEPLSGGV-GADGGLVVVGTEDGEVIALDADDGEELWRARLSSEVLAAP---AVAGGR 139
|
90
....*....|...
gi 2198886489 515 RVAITAGNSLIVF 527
Cdd:COG1520 140 VVVRTGDGRVYAL 152
|
|
| PRK11138 |
PRK11138 |
outer membrane biogenesis protein BamB; Provisional |
438-505 |
3.95e-09 |
|
outer membrane biogenesis protein BamB; Provisional
Pssm-ID: 236857 [Multi-domain] Cd Length: 394 Bit Score: 58.79 E-value: 3.95e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2198886489 438 GAVKALDAATGETKWT--------FRLQSPP--WSGVLSTAGGLVFGGSVEGNFFALDAVTGKSKWQFQTGGQIISNP 505
Cdd:PRK11138 79 GLVKALDADTGKEIWSvdlsekdgWFSKNKSalLSGGVTVAGGKVYIGSEKGQVYALNAEDGEVAWQTKVAGEALSRP 156
|
|
| BamB_YfgL |
cd10276 |
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ... |
66-168 |
1.99e-08 |
|
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization.
Pssm-ID: 199834 [Multi-domain] Cd Length: 358 Bit Score: 56.19 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 66 WIYQLKSAGAPF-ECTPLVADKIMYISEPPSTVTALDIATGRKIWTYtpEMPKDVKFMGfgpvnrGVALLDNNVYIGTLN 144
Cdd:cd10276 18 WSKSVGNGGMAGiDLTPVVAGDMVYAADANGQVSAFNATTGKIIWET--SLSGKGFLGG------TPAVGNGKIFVGTES 89
|
90 100
....*....|....*....|....
gi 2198886489 145 AHLVCLDAKSGAIKWNVTVADNKL 168
Cdd:cd10276 90 GYLYALDAKDGSELWRTEVSDSQL 113
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
80-164 |
2.71e-08 |
|
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441129 [Multi-domain] Cd Length: 370 Bit Score: 55.98 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 80 TPLVADKIMYISEPPSTVTALDIATGRKIWTYTPEMPkdvkfmgfgpVNRGVALLDNNVYIGTLNAHLVCLDAKSGAIKW 159
Cdd:COG1520 52 APAVAGDRVYAADADGRVAALDAATGKELWRVDLGEP----------LSGGVGADGGLVVVGTEDGEVIALDADDGEELW 121
|
....*
gi 2198886489 160 NVTVA 164
Cdd:COG1520 122 RARLS 126
|
|
| PRK11138 |
PRK11138 |
outer membrane biogenesis protein BamB; Provisional |
80-212 |
3.44e-08 |
|
outer membrane biogenesis protein BamB; Provisional
Pssm-ID: 236857 [Multi-domain] Cd Length: 394 Bit Score: 55.71 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 80 TPLVADKIMYISEPPSTVTALDIATGRKIWTytpempKDV-KFMGFGPVNR------GVALLDNNVYIGTLNAHLVCLDA 152
Cdd:PRK11138 64 HPAVAYNKVYAADRAGLVKALDADTGKEIWS------VDLsEKDGWFSKNKsallsgGVTVAGGKVYIGSEKGQVYALNA 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 153 KSGAIKWNVTVAdnklGYAITcAPVAidgkiiIGISGGEAGIRGFLDAYNAKTGKLEWRL 212
Cdd:PRK11138 138 EDGEVAWQTKVA----GEALS-RPVV------SDGLVLVHTSNGMLQALNESDGAVKWTV 186
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
71-172 |
4.26e-08 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 53.95 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 71 KSAGAPFECTPLVADKIMYISEPPSTVTALDIATGRKIWTYtpEMPKDVKFMGfgpVNRGVALLDNNVYIGTLNAHLVCL 150
Cdd:pfam13360 59 QTLSGEVLGAPLVAGGRVFVVAGDGSLIALDAADGRRLWSY--QRSGEPLALR---SSGSPAVVGDTVVAGFSSGKLVAL 133
|
90 100
....*....|....*....|..
gi 2198886489 151 DAKSGAIKWNVTVADNKLGYAI 172
Cdd:pfam13360 134 DPATGKVRWEAPLAAPRGTNEL 155
|
|
| assembly_YfgL |
TIGR03300 |
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
80-210 |
7.67e-08 |
|
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274511 [Multi-domain] Cd Length: 377 Bit Score: 54.55 E-value: 7.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 80 TPLVADKIMYISEPPSTVTALDIATGRKIWTytpempKDVKfmgfGPVNRGVALLDNNVYIGTLNAHLVCLDAKSGAIKW 159
Cdd:TIGR03300 60 QPAVAGGKVYAADADGTVAALDAETGKRLWR------VDLD----ERLSGGVGADGGLVFVGTEKGEVIALDAEDGKELW 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2198886489 160 NvtvadNKLGYAITCAPVAidgkiiIGISGGEAGIRGFLDAYNAKTGKLEW 210
Cdd:TIGR03300 130 R-----AKLSSEVLSPPLV------ANGLVVVRTNDGRLTALDAATGERLW 169
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
436-527 |
3.21e-07 |
|
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441129 [Multi-domain] Cd Length: 370 Bit Score: 52.51 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 436 ASGAVKALDAATGETKWTFRLQSPpwsgVLST---AGGLVFGGSVEGNFFALDAVTGKSKWQFQTggqiiSNPmSFSVNG 512
Cdd:COG1520 105 EDGEVIALDADDGEELWRARLSSE----VLAApavAGGRVVVRTGDGRVYALDAATGERLWSYQR-----PVP-ALTLRG 174
|
90
....*....|....*
gi 2198886489 513 QQRVAITAGNSLIVF 527
Cdd:COG1520 175 TSSPVIVGGAVLVGF 189
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
95-163 |
4.90e-07 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 50.86 E-value: 4.90e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2198886489 95 STVTALDIATGRKIWTYTPEMPKDVkfmgfgpvnrGVALLDNNVYIGTLNAHLVCLDAKSGAIKWNVTV 163
Cdd:pfam13360 3 GVVTALDAATGAELWRVDLETGLGG----------GVAVDGGRLFVATGGGQLVALDAATGKLLWRQTL 61
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
435-499 |
1.54e-06 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 49.32 E-value: 1.54e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2198886489 435 NASGAVKALDAATGETKWTFRLQSPpWSGVLSTAGGLVFGGSVEGNFFALDAVTGKSKWQFQTGG 499
Cdd:pfam13360 40 TGGGQLVALDAATGKLLWRQTLSGE-VLGAPLVAGGRVFVVAGDGSLIALDAADGRRLWSYQRSG 103
|
|
| assembly_YfgL |
TIGR03300 |
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
435-497 |
1.87e-06 |
|
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274511 [Multi-domain] Cd Length: 377 Bit Score: 50.32 E-value: 1.87e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2198886489 435 NASGAVKALDAATGETKWTFRLQSPpwsgVLS---TAGGLVFGGSVEGNFFALDAVTGKSKWQFQT 497
Cdd:TIGR03300 112 TEKGEVIALDAEDGKELWRAKLSSE----VLSpplVANGLVVVRTNDGRLTALDAATGERLWTYSR 173
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
81-164 |
2.51e-06 |
|
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441129 [Multi-domain] Cd Length: 370 Bit Score: 49.81 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 81 PLVADKIMYISEPPSTVTALDIATGRKIWTYTPEMPkdvkfmgfgPVN-RG---VALLDNNVYIGTLNAHLVCLDAKSGA 156
Cdd:COG1520 133 PAVAGGRVVVRTGDGRVYALDAATGERLWSYQRPVP---------ALTlRGtssPVIVGGAVLVGFANGKLVALDLANGQ 203
|
....*...
gi 2198886489 157 IKWNVTVA 164
Cdd:COG1520 204 PLWEQRVA 211
|
|
| assembly_YfgL |
TIGR03300 |
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
436-494 |
4.24e-06 |
|
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274511 [Multi-domain] Cd Length: 377 Bit Score: 49.16 E-value: 4.24e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2198886489 436 ASGAVKALDAATGETKWTFRLQSPPW----SGVLSTAGGLVFGGSVEGNFFALDAVTGKSKWQ 494
Cdd:TIGR03300 153 NDGRLTALDAATGERLWTYSRVTPPLtlrgSASPVIADGGVLVGFAGGKLVALDLQTGQPLWE 215
|
|
| assembly_YfgL |
TIGR03300 |
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
81-164 |
6.47e-06 |
|
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274511 [Multi-domain] Cd Length: 377 Bit Score: 48.39 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 81 PLVADKIMYISEPPSTVTALDIATGRKIWTYTPEMPkdvkfmgfgPVN-RGVA---LLDNNVYIGTLNAHLVCLDAKSGA 156
Cdd:TIGR03300 141 PLVANGLVVVRTNDGRLTALDAATGERLWTYSRVTP---------PLTlRGSAspvIADGGVLVGFAGGKLVALDLQTGQ 211
|
....*...
gi 2198886489 157 IKWNVTVA 164
Cdd:TIGR03300 212 PLWEQRVA 219
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
436-494 |
1.03e-05 |
|
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441129 [Multi-domain] Cd Length: 370 Bit Score: 47.89 E-value: 1.03e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2198886489 436 ASGAVKALDAATGETKWTFRLQSPPWS----GVLSTAGGLVFGGSVEGNFFALDAVTGKSKWQ 494
Cdd:COG1520 145 GDGRVYALDAATGERLWSYQRPVPALTlrgtSSPVIVGGAVLVGFANGKLVALDLANGQPLWE 207
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
276-525 |
1.30e-05 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 46.63 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 276 SVLAINPTTGKMAWyfQFTPHDTHDWDAnqipvlldikikGIPRKVLATANRNGFYYVLDRKTGeflagaayaKQTWARG 355
Cdd:pfam13360 4 VVTALDAATGAELW--RVDLETGLGGGV------------AVDGGRLFVATGGGQLVALDAATG---------KLLWRQT 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 356 LDAK--GRPIVIPGKE--PTEKGNL-VYPSLQGATNWfspSYSKSAGLFYVSVremgslyfkkeveykPGEYFMGGGEQL 430
Cdd:pfam13360 61 LSGEvlGAPLVAGGRVfvVAGDGSLiALDAADGRRLW---SYQRSGEPLALRS---------------SGSPAVVGDTVV 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 431 LPgdNASGAVKALDAATGETKWTFRLQSPPWSGVLST----------AGGLVFGGSVEGNFFALDAVTGKSKWQfqtggQ 500
Cdd:pfam13360 123 AG--FSSGKLVALDPATGKVRWEAPLAAPRGTNELERlvditgtpvvAGGRVFASAYQGRLVAFDAATGRRLWT-----R 195
|
250 260
....*....|....*....|....*
gi 2198886489 501 IISNPMSFSVNGQQRVAITAGNSLI 525
Cdd:pfam13360 196 EISGPNGPILDGDLLYVVSDDGELY 220
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
80-164 |
1.37e-05 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 46.63 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 80 TPLVADKIMYISEPPSTVTALDIATGRKIWTYTPEMPK---DVKFMGfgPVNRGVALLDNNVYIGTLNAHLVCLDAKSGA 156
Cdd:pfam13360 113 SPAVVGDTVVAGFSSGKLVALDPATGKVRWEAPLAAPRgtnELERLV--DITGTPVVAGGRVFASAYQGRLVAFDAATGR 190
|
....*...
gi 2198886489 157 IKWNVTVA 164
Cdd:pfam13360 191 RLWTREIS 198
|
|
| Luminal_IRE1_like |
cd09213 |
The Luminal domain, a dimerization domain, of Inositol-requiring protein 1-like proteins; The ... |
54-165 |
3.37e-05 |
|
The Luminal domain, a dimerization domain, of Inositol-requiring protein 1-like proteins; The Luminal domain is a dimerization domain present in Inositol-requiring protein 1 (IRE1), eukaryotic translation Initiation Factor 2-Alpha Kinase 3 (EIF2AK3), and similar proteins. IRE1 and EIF2AK3 are serine/threonine protein kinases (STKs) and are type I transmembrane proteins that are localized in the endoplasmic reticulum (ER). They are kinase receptors that are activated through the release of BiP, a chaperone bound to their luminal domains under unstressed conditions. This results in dimerization through their luminal domains, allowing trans-autophosphorylation of their kinase domains and activation. They play roles in the signaling of the unfolded protein response (UPR), which is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), contains an endoribonuclease domain in its cytoplasmic side and acts as an ER stress sensor. It is the oldest and most conserved component of the UPR in eukaryotes. Its activation results in the cleavage of its mRNA substrate, HAC1 in yeast and Xbp1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. EIF2AK3, also called PKR-like Endoplasmic Reticulum Kinase (PERK), phosphorylates the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. It functions as the central regulator of translational control during the UPR pathway. In addition to the eIF-2 alpha subunit, EIF2AK3 also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR.
Pssm-ID: 188873 [Multi-domain] Cd Length: 312 Bit Score: 45.95 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 54 VNTSNVKRLaPVWIYQLKSAgAPFECTPLVADKImYISEPPSTVTALDIATGRKIWTYTPE------MPKDVKFMGFGPV 127
Cdd:cd09213 65 KGHGSLQRL-PLTIEDLVEA-SPLVSDTNEDDVV-VVGSKRTSVFALDAKTGKIIKTYRADglpstgGSDSDGNSTPGPD 141
|
90 100 110
....*....|....*....|....*....|....*...
gi 2198886489 128 NrgVALLDNNVYIGTLNAHLVCLDAKSGAIKWNVTVAD 165
Cdd:cd09213 142 E--LQEEEELLYIGRTDYVLQAIDPRSGKELWNVTYGE 177
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
80-159 |
3.75e-05 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 45.09 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 80 TPLVADKIMYISEPPSTVTALDIATGRKIWTYTPEMPkdvkfmgfgpvnRGVALLDNNVYIGTLNAHLVCLDAKSGAIKW 159
Cdd:pfam13360 164 TPVVAGGRVFASAYQGRLVAFDAATGRRLWTREISGP------------NGPILDGDLLYVVSDDGELYALDRATGAVVW 231
|
|
| PQQ |
pfam01011 |
PQQ enzyme repeat; The family represent a single repeat of a beta propeller. This propeller ... |
470-505 |
5.24e-05 |
|
PQQ enzyme repeat; The family represent a single repeat of a beta propeller. This propeller has been found in several enzymes which utilize pyrrolo-quinoline quinone as a prosthetic group.
Pssm-ID: 395799 [Multi-domain] Cd Length: 36 Bit Score: 40.25 E-value: 5.24e-05
10 20 30
....*....|....*....|....*....|....*.
gi 2198886489 470 GLVFGGSVEGNFFALDAVTGKSKWQFQTGGQIISNP 505
Cdd:pfam01011 1 GTVYLGSDDGYLYALDAETGKVLWSFKTGGAVLSSP 36
|
|
| BamB_YfgL |
cd10276 |
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ... |
58-167 |
8.69e-05 |
|
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization.
Pssm-ID: 199834 [Multi-domain] Cd Length: 358 Bit Score: 45.02 E-value: 8.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 58 NVKRLAPVWIYQLKSAGapFECTPLVADKIMYISEPPSTVTALDIATGRKIWTYTPEMPKdvkfmGFGPVNRGVALLDNN 137
Cdd:cd10276 96 DAKDGSELWRTEVSDSQ--LLSPPTYADGKIYVGTGDGRLYYCNAETGKVVWNRTSTAPE-----LSLRGGAAPVGAYDV 168
|
90 100 110
....*....|....*....|....*....|
gi 2198886489 138 VYIGTLNAHLVCLDAKSGAIKWNVTVADNK 167
Cdd:cd10276 169 VFVGDGNGTVVALNTGTGVDIWEFSVSEPR 198
|
|
| BamB_YfgL |
cd10276 |
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ... |
435-505 |
1.61e-04 |
|
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization.
Pssm-ID: 199834 [Multi-domain] Cd Length: 358 Bit Score: 43.86 E-value: 1.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2198886489 435 NASGAVKALDAATGETKWTFRLQSPPWSGVLSTAG-GLVFGGSVEGNFFALDAVTGKSKWQFQTG-GQIISNP 505
Cdd:cd10276 45 DANGQVSAFNATTGKIIWETSLSGKGFLGGTPAVGnGKIFVGTESGYLYALDAKDGSELWRTEVSdSQLLSPP 117
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
438-526 |
2.26e-04 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 42.78 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 438 GAVKALDAATGETKWTFRLQSPPW----SGVLSTAGGLVFGGSVEGNFFALDAVTGKSKWQFQTGGQIISNPMSFSVNGQ 513
Cdd:pfam13360 83 GSLIALDAADGRRLWSYQRSGEPLalrsSGSPAVVGDTVVAGFSSGKLVALDPATGKVRWEAPLAAPRGTNELERLVDIT 162
|
90
....*....|...
gi 2198886489 514 QRVAITAGNSLIV 526
Cdd:pfam13360 163 GTPVVAGGRVFAS 175
|
|
| BamB_YfgL |
cd10276 |
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ... |
437-529 |
2.32e-04 |
|
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization.
Pssm-ID: 199834 [Multi-domain] Cd Length: 358 Bit Score: 43.47 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 437 SGAVKALDAATGETKWTFRLQSppwSGVLS---TAGGLVFGGSVEGNFFALDAVTGKSKWQFQTGGQIISNPMSFSVNGQ 513
Cdd:cd10276 89 SGYLYALDAKDGSELWRTEVSD---SQLLSpptYADGKIYVGTGDGRLYYCNAETGKVVWNRTSTAPELSLRGGAAPVGA 165
|
90
....*....|....*.
gi 2198886489 514 QRVAITAGNSLIVFGL 529
Cdd:cd10276 166 YDVVFVGDGNGTVVAL 181
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
80-159 |
5.23e-04 |
|
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441129 [Multi-domain] Cd Length: 370 Bit Score: 42.49 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 80 TPLVADKIMYISEPPSTVTALDIATGRKIWTytpempKDVKfmgfgpVNRGVALLDNNVYIGTLNAHLVCLDAKSGAIKW 159
Cdd:COG1520 228 TPVVDGGVVYAVAYQGRLAALDLRSGRVLWS------RDLS------SYTGLAVDGNNLYVTDDDGRVWALDRRNGAELW 295
|
|
| assembly_YfgL |
TIGR03300 |
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
80-159 |
1.11e-03 |
|
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274511 [Multi-domain] Cd Length: 377 Bit Score: 41.46 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 80 TPLVADKIMYISEPPSTVTALDIATGRKIWTytpempKDVKfmgfgpVNRGVALLDNNVYIGTLNAHLVCLDAKSGAIKW 159
Cdd:TIGR03300 236 DPVVDGGQVYAVSYQGRVAALDLRSGRVLWK------RDAS------SYQGPAVDDNRLYVTDADGVVVALDRRSGSELW 303
|
|
| PQQ |
pfam01011 |
PQQ enzyme repeat; The family represent a single repeat of a beta propeller. This propeller ... |
436-462 |
1.40e-03 |
|
PQQ enzyme repeat; The family represent a single repeat of a beta propeller. This propeller has been found in several enzymes which utilize pyrrolo-quinoline quinone as a prosthetic group.
Pssm-ID: 395799 [Multi-domain] Cd Length: 36 Bit Score: 36.40 E-value: 1.40e-03
10 20
....*....|....*....|....*..
gi 2198886489 436 ASGAVKALDAATGETKWTFRLQSPPWS 462
Cdd:pfam01011 8 DDGYLYALDAETGKVLWSFKTGGAVLS 34
|
|
| PRK11138 |
PRK11138 |
outer membrane biogenesis protein BamB; Provisional |
436-505 |
2.26e-03 |
|
outer membrane biogenesis protein BamB; Provisional
Pssm-ID: 236857 [Multi-domain] Cd Length: 394 Bit Score: 40.30 E-value: 2.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2198886489 436 ASGAVKALDAATGETKWTFRLQSPPWS----GVLSTAGGLVFGGSVEGNFFALDAVTGKSKWQfqtggQIISNP 505
Cdd:PRK11138 168 SNGMLQALNESDGAVKWTVNLDVPSLTlrgeSAPATAFGGAIVGGDNGRVSAVLMEQGQLIWQ-----QRISQP 236
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
63-210 |
2.74e-03 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 39.69 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198886489 63 APVWIyqlKSAGAPFECTPLVADKIMYISEPPSTVTALDIATGRKIWTYTPEmpkdvkfmgfGPVNRGVALLDNNVYIGT 142
Cdd:pfam13360 14 AELWR---VDLETGLGGGVAVDGGRLFVATGGGQLVALDAATGKLLWRQTLS----------GEVLGAPLVAGGRVFVVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2198886489 143 LNAHLVCLDAKSGAIKWNVTVADNKLGYAITCAPVAidgkiiIGISGGEAGIRGFLDAYNAKTGKLEW 210
Cdd:pfam13360 81 GDGSLIALDAADGRRLWSYQRSGEPLALRSSGSPAV------VGDTVVAGFSSGKLVALDPATGKVRW 142
|
|
| PQQ_3 |
pfam13570 |
PQQ-like domain; |
448-484 |
3.27e-03 |
|
PQQ-like domain;
Pssm-ID: 463925 [Multi-domain] Cd Length: 36 Bit Score: 35.26 E-value: 3.27e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2198886489 448 GETKWTFRLQSPPWSGVLsTAGGLVFGGSVEGNFFAL 484
Cdd:pfam13570 1 GEVLWRFETGGPIVSSPA-VAGGLVYVGTGDGTLYAL 36
|
|
|