|
Name |
Accession |
Description |
Interval |
E-value |
| PQQ_ADH_I |
cd10277 |
Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); ... |
36-573 |
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: 796.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 36 ARLENPEPGNWMLYRRTYDGQGFSPLDQINTSNVKDLKPVWTFSTGVL-EGHEAPPIVNNGVMFVATPMGQVIALNAKTG 114
Cdd:cd10277 1 LLNDAKETGNWLTYGRGYNGQRYSPLKQINTDNVKNLVPAWSFSFGGKqRGQESQPIVNDGVMYVTTSYNRVFAIDAKTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 115 EEYWRYKRQLPDDLF-QLHPTSRGVGLWEDKLYLATTDDHVVALDAKTGKVLWDTKVQDYKKGQYMTLMPLVVDGKVIVG 193
Cdd:cd10277 81 KELWKYKHRLPEDIRpCCDVVNRGVALYGDKVYFGTLDAHLVALDAKTGKVVWKKKVADYKAGYSMTLAPLVVKGKVIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 194 GSGGEFGVRGYVVAFDAGSGKELWRTFTIPGEGEPGHE-TWSGDDWKSGGGAAWMTGTYDKDTKTVYWGIGNASPWPGSM 272
Cdd:cd10277 161 VSGGEFGVRGFIAALDAETGKEVWRTYTVPGPGEPGSTdTWPGDAWKTGGGATWLTGTYDPETNLLYWGVGNPAPWNGDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 273 HPGDNLYTSSVLALDPDSGKIKTHFQYHQNDSWDWDEVDAPMLIDLQREGRSFKSLIHPGRDAIFWVLERKPdkINYVAG 352
Cdd:cd10277 241 RPGDNLYTSSVLALDPDTGKIKWHYQYTPNDTWDYDGVNEPVLFDYTKNGKPVKALVHADRNGFFYVLDRTN--GKLIWA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 353 WPFVKTNVWKGIEAETGRPILDPDH-KPVLGKRVEFCPSLWGGKDWPSAAYSPNTKLVYVPANEnFCGGFTGEKQPLVPG 431
Cdd:cd10277 319 TPFVKKITWASIDLKTGRPIYDEDKvPPKKGKTVDFCPSFLGGKNWPPMAYSPDTGLFYVPANH-WCMDLTGEPVSYKKG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 432 QLWLGTKPEDIGLFPapnaDHFGELQAWDPATGKKVWQHDYKtSQLFGSVTATAGDLVLAGGTnDRAFRIFNAKTGELLW 511
Cdd:cd10277 398 AAYLGAGFTIKPPFE----DHIGELQAIDPTTGKKVWEHKTP-LPLWGGVLTTAGGLVFTGTP-DGYFRAFDAKTGKELW 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1304137069 512 EQKTNSGIMAMPMSYEVDGTQYIAVQSGWGVDAQRIQdalaGKVAGFENNVPQGGVIWVFAL 573
Cdd:cd10277 472 EFQTGSGIIGPPVTWEVDGKQYVAVLSGWGGAAPLWG----GDMAKLLKNVPQGGSLWVFAL 529
|
|
| PQQ_enz_alc_DH |
TIGR03075 |
PQQ-dependent dehydrogenase, methanol/ethanol family; This protein family has a phylogenetic ... |
28-541 |
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: 703.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 28 DNYSPVTSARLEN--PEPGNWMLYRRTYDGQGFSPLDQINTSNVKDLKPVWTFSTGVLEGHEAPPIVNNGVMFVATPMGQ 105
Cdd:TIGR03075 1 AAAAAVTNEDLLNdaKDPSDWLTYGGGYAGQRYSPLDQINTDNVKKLQPAWTFSLGKQRGQESQPLVVDGVMYVTTSYSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 106 VIALNAKTGEEYWRYKRQLPDDLFQLHPT---SRGVGLWEDKLYLATTDDHVVALDAKTGKVLWDTKVQDYKKGQYMTLM 182
Cdd:TIGR03075 81 VYALDAKTGKILWKYDPKLPDDIIPVMCCdvvNRGAALYDGKVFFGTLDARLVALDAKTGKVVWSKKNGDYKKGYTITAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 183 PLVVDGKVIVGGSGGEFGVRGYVVAFDAGSGKELWRTFTIPGE------------GEPGHETWSGDDWKSGGGAAWMTGT 250
Cdd:TIGR03075 161 PLVVKGKVITGISGGEFGVRGYVTAYDAKTGKLVWRRYTVPGDmgylkktgkpvgGDPGAKTWPGDAWKTGGGATWGTGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 251 YDKDTKTVYWGIGNASPWPGSMHPGDNLYTSSVLALDPDSGKIKTHFQYHQNDSWDWDEVDAPMLIDLQREGRSFKSLIH 330
Cdd:TIGR03075 241 YDPETNLIYFGTGNPAPWNSHLRPGDNLYTSSIVARDPDTGKIKWHYQTTPHDEWDYDGVNEMILFDLKKDGKPRKLLAH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 331 PGRDAIFWVLERKPDKinYVAGWPFVKTNVW-KGIEAETGRPILDPDHKPVL---GKRVEFCPSLWGGKDWPSAAYSPNT 406
Cdd:TIGR03075 321 ADRNGFFYVLDRTNGK--LLSAEPFVDKVNWaTGVDLKTGRPIEVPEARSTDgkkGKPVEVCPGFLGGKNWQPMAYSPKT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 407 KLVYVPANEnFCGGFTGEKQPLVPGQLWLGtkpedIGL-FPAPNADHFGELQAWDPATGKKVWQHDYKTSqLFGSVTATA 485
Cdd:TIGR03075 399 GLFYVPANH-VCMDYWPEKVSYKKGAAYLG-----AGFtIKPPPDDHIGSLIAWDPITGKIVWEHKEDFP-LWGGVLATA 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1304137069 486 GDLVLAgGTNDRAFRIFNAKTGELLWEQKTNSGIMAMPMSYEVDGTQYIAVQSGWG 541
Cdd:TIGR03075 472 GDLVFT-GTLEGYFKAFDAKTGEELWKFKTGSGIVGPPVTYEQDGKQYVAVLSGWG 526
|
|
| Gcd |
COG4993 |
Glucose dehydrogenase, PQQ-dependent [Carbohydrate transport and metabolism]; |
42-573 |
0e+00 |
|
Glucose dehydrogenase, PQQ-dependent [Carbohydrate transport and metabolism];
Pssm-ID: 444017 [Multi-domain] Cd Length: 515 Bit Score: 640.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 42 EPGNWMLYRRTYDGQGFSPLDQINTSNVKDLKPVWTFSTGVLE--GHEAPPIVNNGVMFVATPMGQVIALNAKTGEEYWR 119
Cdd:COG4993 1 DPGDWLAYGGDYAGQRYSPLDQINPDNVKKLKVAWTFSTGDLPerGHEATPLVVDGVLYVCTPHNRVFALDAATGKELWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 120 YKRQLPDDLFQLHPTSRGVGLWEDKLYLATTDDHVVALDAKTGKVLWDTKVQDYKKGQYMTLMPLVVDGKVIVGGSGGEF 199
Cdd:COG4993 81 YDPKLPDDAACCDVVNRGVAYYDGRIFLGTLDGRLVALDAKTGKVCWDVKVGDPKKGYTITSAPLVVKDKVIVGGSGGEF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 200 GVRGYVVAFDAGSGKELWRTFTIPGEGEPGHETWS-GDDWKSGGGAAWMTGTYDKDTKTVYWGIGNASP-WPGSMHPGDN 277
Cdd:COG4993 161 GPRGVVRAYDARTGKLVWRFDTIPDPGEPGAETWPpGDTWKRGGGNVWGTMSYDPELGLVYLPTGNPAPdWNGGQRPGDN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 278 LYTSSVLALDPDSGKIKTHFQYHQNDSWDWDEVDAPMLIDLQREGRSFKSLIHPGRDAIFWVLER---KPdkinyVAGWP 354
Cdd:COG4993 241 LYSSSIVALDADTGELKWHYQTVPHDLWDYDGPNEPILVDLPVDGKTRKALVQATKNGFIYVLDRetgEP-----LVTQP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 355 FVKT-NVWKGIEAETGRPILDPDHKpvLGKRVEFCPSLWGGKDWPSAAYSPNTKLVYVPANENfCGGFTGEKQPLVPGQL 433
Cdd:COG4993 316 FVKPpNWATEIDMWGATPIQTPPSL--DGKTTLICPGALGGKNWGPAAYDPETGLLYVPANEL-CMDYELVPREYQAGAP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 434 WLGTkpeDIGLFPAPnADHFGELQAWDPATGKKVWQHDYKTSqLFGSVTATAGDLVLAgGTNDRAFRIFNAKTGELLWEQ 513
Cdd:COG4993 393 YLGA---TLTMYPCP-APPWGTLTAIDLNTGKIVWQVPLGFP-NWGGPLATAGGLVFI-GTLDGYLRAFDAKTGKELWKF 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 514 KTNSGIMAMPMSYEVDGTQYIAVQSGWGVdaqriqdalagkVAGFENNVPQGGVIWVFAL 573
Cdd:COG4993 467 RLPSGGQATPMTYEVDGKQYVAVAAGGGG------------WLGLGLYTPQGDYLIAFAL 514
|
|
| PQQ_MDH |
cd10278 |
Large subunit of methanol dehydrogenase (moxF); Methanol dehydrogenase is a key enzyme in the ... |
46-573 |
2.81e-156 |
|
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: 458.71 E-value: 2.81e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 46 WMLYRRTYDGQGFSPLDQINTSNVKDLKPVWTFSTGVLEGHEAPPIVNNGVMFVATPM-GQVIALN-AKTGEEYWRYKRQ 123
Cdd:cd10278 1 WVMPGKDYANTRYSPLAQINKDNVKNLKVAWTFSTGVLRGHEGAPLVVGDTMYVVTPFpNNVYALDlNDPGKILWKYKPK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 124 lPDDLFQ----LHPTSRGVGLWEDKLYLATTDDHVVALDAKTGKVLWDTKVQDYKKGQYMTLMPLVVDGKVIVGGSGGEF 199
Cdd:cd10278 81 -QDPSAVavacCDVVNRGLAYADGKIFFNQLDGHLVALDAKTGKEVWKVKNGDPKVGETLTMAPLVVKDKVIVGISGGEF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 200 GVRGYVVAFDAGSGKELWRTFTI------------------PGEGEPGHETWSGDDWKSGGGAAWMTGTYDKDTKTVYWG 261
Cdd:cd10278 160 GVRGYVTAYDLKTGKLVWRAYSTgpdkdvligpdfnpfnphDGGKDLGLSTWPGDAWKIGGGTNWGWYSYDPKLNLVYYG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 262 IGNASPWPGSMHPGDNLYTSSVLALDPDSGKIKTHFQYHQNDSWDWDEVDAPMLIDLQREGRSFKSLIHPGRDAIFWVLE 341
Cdd:cd10278 240 TGNPGPWNPTQRPGDNKWSMTIFARDPDTGEAKWAYQMTPHDEWDYDGVNEMILVDQTVDGKKRKLLVHFDRNGFVYTLD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 342 RKPDkiNYVAGWPFVKTNVWKGIEAETGRPILDPDHKPVLGKRV-EFCPSLWGGKDWPSAAYSPNTKLVYVPANeNFCGG 420
Cdd:cd10278 320 RTTG--ELLSAEKFDPVNNWKGVDLKTGRPVKDPEKSTHMDHNVtDICPSAMGGKDQQPSSYSPKTGLFYVPTN-HLCMD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 421 FTGEKQPLVPGQLWLGTkpeDIGLFPAPNAdHFGELQAWDPATGKKVWQHDYKTSqLFGSVTATAGDLVLAgGTNDRAFR 500
Cdd:cd10278 397 YEPFEVNYTAGQPYVGA---TLAMYPGPGG-HMGQFKAWDPVTGKTKWEIKERFP-VWSGTLATAGGLVFY-GTLDGWFK 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 501 IFNAKTGELLWEQKTNSGIMAMPMSYEVDGTQYIAVQSGWG--------VDAQRIQDAL--AGKVAGFENNVPQGGVIWV 570
Cdd:cd10278 471 AVDAKTGKLLWKFKLPSGIIGNPITYKHDGKQYVAVLSGVGgwagvgvaAGLRDPTAGLgaVGAFKDLPNYTQMGGTLYV 550
|
...
gi 1304137069 571 FAL 573
Cdd:cd10278 551 FSL 553
|
|
| PQQ_ADH_II |
cd10279 |
PQQ_like domain of the quinohemoprotein alcohol dehydrogenase (type II); This family of ... |
44-541 |
1.08e-149 |
|
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: 441.70 E-value: 1.08e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 44 GNWMLYRRTYDGQGFSPLDQINTSNVKDLKPVWTFSTGVLEGHEAPPIVNNGVMFVATPMGQVIALNAKTGEEYWRYKRQ 123
Cdd:cd10279 1 GNWLSYGRDYDEQRFSPLTQINRSNVGQLGLAWYFDLDTNRGQEATPLVVDGVMYVSGPWSVVYALDARTGKLLWQYDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 124 LP---DDLFQLHPTSRGVGLWEDKLYLATTDDHVVALDAKTGKVLWDTKVQDYKKGQYMTLMPLVVDGKVIVGGSGGEFG 200
Cdd:cd10279 81 VDresGRKACCDVVNRGVAVWDGKVFVGTLDGRLIALDAKTGKEVWSVDTIDPRKPYTITGAPRVAKGKVVIGNGGAEFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 201 VRGYVVAFDAGSGKELWRTFTIPGEGEPGHE----------TWSGDDWKSG-GGAAWMTGTYDKDTKTVYWGIGNASPWP 269
Cdd:cd10279 161 VRGYVSAYDAETGKLVWRFYTVPGNPAKPFEhasleaaaatWWTGEWWRTGgGGTVWDSITYDPELDLLYIGTGNGSPWN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 270 ---GSMHPGDNLYTSSVLALDPDSGKIKTHFQYHQNDSWDWDEVDAPMLIDLQREGRSFKSLIHPGRDAIFWVLERKPDK 346
Cdd:cd10279 241 rkvRSPGGGDNLFLSSIVALDADTGRYKWHYQTTPGDTWDYTATQPIILADLEIDGKPRKVLMHAPKNGFFYVLDRATGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 347 inYVAGWPFVKTNVWKGIEAETGRPILDPDHKPVLGKRVEFcPSLWGGKDWPSAAYSPNTKLVYVPANENfcgGFTGEKQ 426
Cdd:cd10279 321 --LLSAEPFVPVNWATGIDLKTGRPIENPEARYTKGPKLVF-PGPLGAHNWHPMSYNPDTGLVYIPAQEI---PAVYEDD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 427 PLVPGQL---W-----LGTKPEDIGLFPAPNADHFGELQAWDPATGKKVWQHDYKtSQLFGSVTATAGDLVLAgGTNDRA 498
Cdd:cd10279 395 PGDFGYNplgWntgitPDATPPPAAAKRALRKATRGRLVAWDPVTQKAAWRVEHP-GPWNGGVLATAGNLVFQ-GTADGE 472
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1304137069 499 FRIFNAKTGELLWEQKTNSGIMAMPMSYEVDGTQYIAVQSGWG 541
Cdd:cd10279 473 LAAYDARTGEKLWSFDTGSGIVAAPMTYSVDGEQYVAVLAGWG 515
|
|
| PQQ_DH_like |
cd00216 |
PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases ... |
68-572 |
6.32e-108 |
|
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: 330.72 E-value: 6.32e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 68 NVKDLKPVWTFSTGV--LEGHEAPPIVNNGVMFVATPMGQVIALNAKTGEEYWRYKRQLPDDLFQ--LHPTSRGVGLWED 143
Cdd:cd00216 3 NVFQLTPAWSFSTGDggNRGSELTPIVVDGVMYATTSFSRVFALDADDGKEIWSYDPALKDGWFEacCDLVNRGVAVWGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 144 KLYLATTDDHVVALDAKTGKVLWDTKVQDYKKGQYMTLMPLVVDGKVIVGGSGGEFGVRGYVVAFDAGSGKELWRTFTIP 223
Cdd:cd00216 83 KVYIGVLDGRVYALNAETGKVAWKVKNADVLGGYTATSAPVVVDGLVIIGSSGDEFGVRGYLTAYDVATGEEKWRFYLVM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 224 G-----------EGEPGHETWSGDDWKSGGGAAWMTGTYDKDTKTVYWGIGNASPW--PGSMHPGDNLYTSSVLALDPDS 290
Cdd:cd00216 163 PdpnllpgkdstVTDRNTPTGDEHTWTSGGGTGWSSAAYDAELNLIYVGGGNPTPWnwGGNRTPGDNLYTSSIVAVNADT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 291 GKIKTHFQYHQNDSWDWDEVDAPMLIDLQREGRSFKSLIHPGRDAIFWVLERKPDKInyvagwpfvktnVWKgieaetgR 370
Cdd:cd00216 243 GEMKWQYQTTPHDAWDYDGDNTPVLADIKVKGKKVKVLFAPAKNGNFYVLDRRNGEL------------VSA-------R 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 371 PiLDPDhkpvlgkrvefcpslwggkdwpsaAYSPNTKLVYVPANenfcggftgekqplvpgqlwlgtkpediglfpapna 450
Cdd:cd00216 304 P-LVPD------------------------SYDPDRELFYVPAN------------------------------------ 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 451 dhfGELQAWDPATGKKVWQHDYKTSqLFGSVTATAGDLVLAgGTNDRAFRIFNAKTGELLWEQKTNSGIMAMPMSYEVDG 530
Cdd:cd00216 323 ---GRIMALDPVTGVVVWEKSELHP-LLGGPLSTAGNLVFV-GTSDGYLKAYNADTGEKLWQQKVPSGFQAEPVTYEVDG 397
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1304137069 531 TQYIAVQSGWGVDAqriqdALAGKVAGFENNVPQGGVIWVFA 572
Cdd:cd00216 398 EQYVLIQAGGGGAF-----PLWGGMADLTRGTQMGGTVVVYK 434
|
|
| PQQ_mGDH |
cd10280 |
Membrane-bound PQQ-dependent glucose dehydrogenase; This bacterial subfamily of enzymes ... |
46-539 |
5.71e-98 |
|
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: 310.66 E-value: 5.71e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 46 WMLYRRTYDGQGFSPLDQINTSNVKDLKPVWTFSTGVLEGH-------EAPPIVNNGVMFVATPMGQVIALNAKTGEEYW 118
Cdd:cd10280 1 WPAYGGDPGGTRYSPLDQITPDNVGKLKVAWTYHTGDLPGPdgnegtfEATPLKVGGTLYLCTPHNRVIALDAATGKELW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 119 RYKRQLPDDLFQLHPTSRGVGLWEDK---------LYLATTDDHVVALDAKTGKVLWD----------TKVQDYKKGQY- 178
Cdd:cd10280 81 RFDPKAGADAAPGHQTCRGVSYWEDGaaaaacarrIFFGTGDARLIALDARTGKPCPDfgdngvvdlrEGLGRVKPGFYs 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 179 MTLMPLVVDGKVIVGGSGGEF----GVRGYVVAFDAGSGKELWrTF-TIPGEGEPGHETwsGDDWKSGGGA-AWMTGTYD 252
Cdd:cd10280 161 STSPPTVYGDLVIVGSAVADNqavdAPSGVIRAFDVRTGKLVW-AFdTIPPPGEAGPDT--AGAWYTRGGPnVWAGMSAD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 253 KDTKTVYWGIGNASP--WpGSMHPGDNLYTSSVLALDPDSGKIKTHFQYHQNDSWDWDEVDAPMLIDLQREGRSFKSLIH 330
Cdd:cd10280 238 EKLGLVYLPTGSATPdfY-GGDRPGDNLFANSLVALDAATGKRRWHFQTVHHDLWDYDLPAQPTLVDVPRDGKTVPAVAQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 331 PGRDAIFWVLER---KPdkinyvaGWPFVKTNVWKG-IEAE---------TGRPILDP--------------DHK----- 378
Cdd:cd10280 317 PTKQGFVFVLDRrtgKP-------LWPVEERPVPQGdVPGErtsptqpfpTLPPPFARqglteddmwgatpfDQLacriq 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 379 ------------PVLGKRVEFcPSLWGGKDWPSAAYSPNTKLVYVPANE----------------NFCGGFTGEKQPLVP 430
Cdd:cd10280 390 frslryeglftpPSLDGTLIF-PGNDGGANWGGAAVDPERGILYVNSNRlpfviqlvprapgdpaGVAGGGEGGGGGGGP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 431 GQLWLGTKPEDIGLFPAP-----NADHFGELQAWDPATGKKVWQHDYKTSQ-----------------LFGSVTaTAGDL 488
Cdd:cd10280 469 SPQAGTPYGVGRGRFLSPlglpcQAPPWGTLTAIDLNTGKILWQVPLGTVPdlgpkgiplpiptgtpnLGGPVV-TAGGL 547
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1304137069 489 VLAGGTNDRAFRIFNAKTGELLWEQKTNSGIMAMPMSYEVDGTQYIAVQSG 539
Cdd:cd10280 548 VFIAATQDNYLRAFDKATGKELWEARLPAGGQATPMTYEVDGKQYVVIAAG 598
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
59-218 |
4.54e-20 |
|
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: 92.18 E-value: 4.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 59 SPLDQINtsNVKDLKPVWTFSTGVLEGHEA---PPIVNNGVMFVATPMGQVIALNAKTGEEYWRYKrqLPDDLfqlhptS 135
Cdd:COG1520 21 APLPEFE--PSVKVKQLWSASVGDGVGKGYsrlAPAVAGDRVYAADADGRVAALDAATGKELWRVD--LGEPL------S 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 136 RGVGLWEDKLYLATTDDHVVALDAKTGKVLWDTKVqdykKGQYMTlMPLVVDGKVIVGGSGGEfgvrgyVVAFDAGSGKE 215
Cdd:COG1520 91 GGVGADGGLVVVGTEDGEVIALDADDGEELWRARL----SSEVLA-APAVAGGRVVVRTGDGR------VYALDAATGER 159
|
...
gi 1304137069 216 LWR 218
Cdd:COG1520 160 LWS 162
|
|
| BamB_YfgL |
cd10276 |
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ... |
54-295 |
6.59e-20 |
|
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: 91.62 E-value: 6.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 54 DGQGFSPLDQINTSNVKDLkpvwtfSTGVLEGHEAPPIVNNGVMFVATPMGQVIALNAKTGEEYWRYKrqLPDDLFQlhp 133
Cdd:cd10276 4 DLPEPTPEFDPEVLWSKSV------GNGGMAGIDLTPVVAGDMVYAADANGQVSAFNATTGKIIWETS--LSGKGFL--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 134 tSRGVGLWEDKLYLATTDDHVVALDAKTGKVLWDTKVQDykkGQYMTlMPLVVDGKVIVGGSGGEfgvrgyVVAFDAGSG 213
Cdd:cd10276 73 -GGTPAVGNGKIFVGTESGYLYALDAKDGSELWRTEVSD---SQLLS-PPTYADGKIYVGTGDGR------LYYCNAETG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 214 KELW-RTFTIPGEGEPGHETWSGDDWKSGGGAAWMTGTY-DKDTKTVYWGIGNASPWPGSMHPG----------DNLYTS 281
Cdd:cd10276 142 KVVWnRTSTAPELSLRGGAAPVGAYDVVFVGDGNGTVVAlNTGTGVDIWEFSVSEPRGRTELPRmidssvtyvvVGGYLY 221
|
250 260
....*....|....*....|
gi 1304137069 282 SV------LALDPDSGKIKT 295
Cdd:cd10276 222 STsyqgylVALDFESGQFLW 241
|
|
| assembly_YfgL |
TIGR03300 |
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
75-217 |
2.36e-16 |
|
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: 81.13 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 75 VWtfSTGVLEGHEAP-----PIVNNGVMFVATPMGQVIALNAKTGEEYWRykRQLPDDLfqlhptSRGVGLWEDKLYLAT 149
Cdd:TIGR03300 43 VW--SASVGDGVGHYylrlqPAVAGGKVYAADADGTVAALDAETGKRLWR--VDLDERL------SGGVGADGGLVFVGT 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1304137069 150 TDDHVVALDAKTGKVLWDTKVQdykkGQYMTlMPLVVDGKVIVGGSggefgvRGYVVAFDAGSGKELW 217
Cdd:TIGR03300 113 EKGEVIALDAEDGKELWRAKLS----SEVLS-PPLVANGLVVVRTN------DGRLTALDAATGERLW 169
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
73-293 |
4.06e-16 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 77.83 E-value: 4.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 73 KPVWTFSTGVLEGHEAPpiVNNGVMFVATPMGQVIALNAKTGEEYWRYKrqlpddlfqlhPTSRGVG---LWEDKLYLAT 149
Cdd:pfam13360 14 AELWRVDLETGLGGGVA--VDGGRLFVATGGGQLVALDAATGKLLWRQT-----------LSGEVLGaplVAGGRVFVVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 150 TDDHVVALDAKTGKVLWDTKVQDYKKGQYMTLMPLVVDGKVIVGGSGGEfgvrgyVVAFDAGSGKELW-RTFTIPGEGEP 228
Cdd:pfam13360 81 GDGSLIALDAADGRRLWSYQRSGEPLALRSSGSPAVVGDTVVAGFSSGK------LVALDPATGKVRWeAPLAAPRGTNE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1304137069 229 GHET---------WSGDDWKSGGGAAwmTGTYDKDTKTVYWGIGNASPwPGSMHPGDNLYTSS----VLALDPDSGKI 293
Cdd:pfam13360 155 LERLvditgtpvvAGGRVFASAYQGR--LVAFDAATGRRLWTREISGP-NGPILDGDLLYVVSddgeLYALDRATGAV 229
|
|
| PRK11138 |
PRK11138 |
outer membrane biogenesis protein BamB; Provisional |
58-246 |
2.64e-15 |
|
outer membrane biogenesis protein BamB; Provisional
Pssm-ID: 236857 [Multi-domain] Cd Length: 394 Bit Score: 78.05 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 58 FSPLDQINtsNVKDLKPVWTFSTGVLEGH---EAPPIVNNGVMFVATPMGQVIALNAKTGEEYWRYKRQLPDDLFQLHPT 134
Cdd:PRK11138 32 MSPLPQVE--NQFTPTTVWSTSVGDGVGDyysRLHPAVAYNKVYAADRAGLVKALDADTGKEIWSVDLSEKDGWFSKNKS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 135 SR---GVGLWEDKLYLATTDDHVVALDAKTGKVLWDTKVqdykKGQYMTlMPLVVDGKVIVGGSggefgvRGYVVAFDAG 211
Cdd:PRK11138 110 ALlsgGVTVAGGKVYIGSEKGQVYALNAEDGEVAWQTKV----AGEALS-RPVVSDGLVLVHTS------NGMLQALNES 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1304137069 212 SGKELWR------TFTIPGEGEP----GHETWSGDDWK------SGGGAAW 246
Cdd:PRK11138 179 DGAVKWTvnldvpSLTLRGESAPatafGGAIVGGDNGRvsavlmEQGQLIW 229
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
68-218 |
4.35e-14 |
|
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: 74.08 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 68 NVKDLKPVW--TFSTGVLegheAPPIVNNGVMFVATPMGQVIALNAKTGEEYWRYKRQLPddlfQLhpTSRGVG---LWE 142
Cdd:COG1520 113 DADDGEELWraRLSSEVL----AAPAVAGGRVVVRTGDGRVYALDAATGERLWSYQRPVP----AL--TLRGTSspvIVG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 143 DKLYLATTDDHVVALDAKTGKVLWDTKVQdykkgqymtlMP--------LV-VDGKVIVggSGGEFGVRGY---VVAFDA 210
Cdd:COG1520 183 GAVLVGFANGKLVALDLANGQPLWEQRVA----------QPrgrtelerLVdVDGTPVV--DGGVVYAVAYqgrLAALDL 250
|
....*...
gi 1304137069 211 GSGKELWR 218
Cdd:COG1520 251 RSGRVLWS 258
|
|
| assembly_YfgL |
TIGR03300 |
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
88-217 |
1.09e-12 |
|
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: 69.58 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 88 APPIVNNGVMFVATPMGQVIALNAKTGEEYWRYKRQLPddlfQLhpTSRGVG---LWEDKLYLATTDDHVVALDAKTGKV 164
Cdd:TIGR03300 139 SPPLVANGLVVVRTNDGRLTALDAATGERLWTYSRVTP----PL--TLRGSAspvIADGGVLVGFAGGKLVALDLQTGQP 212
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1304137069 165 LWDTKVQdYKKGQyMTLMPLV-VDGKVIVGGsGGEFGV--RGYVVAFDAGSGKELW 217
Cdd:TIGR03300 213 LWEQRVA-LPKGR-TELERLVdVDGDPVVDG-GQVYAVsyQGRVAALDLRSGRVLW 265
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
102-218 |
1.93e-11 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 63.96 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 102 PMGQVIALNAKTGEEYWRYKRQLPddlfqlhpTSRGVGLWEDKLYLATTDDHVVALDAKTGKVLWDTKVQDYKKGQymtl 181
Cdd:pfam13360 1 ADGVVTALDAATGAELWRVDLETG--------LGGGVAVDGGRLFVATGGGQLVALDAATGKLLWRQTLSGEVLGA---- 68
|
90 100 110
....*....|....*....|....*....|....*..
gi 1304137069 182 mPLVVDGKVIVGGSGgefgvrGYVVAFDAGSGKELWR 218
Cdd:pfam13360 69 -PLVAGGRVFVVAGD------GSLIALDAADGRRLWS 98
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
88-219 |
3.98e-11 |
|
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: 64.83 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 88 APPIVNNGVMFVATPMGQVIALNAKTGEEYWryKRQLPddlfqlhpTSRGVGLWEDKLYLATTDDHVVALDAKTGKVLWd 167
Cdd:COG1520 227 GTPVVDGGVVYAVAYQGRLAALDLRSGRVLW--SRDLS--------SYTGLAVDGNNLYVTDDDGRVWALDRRNGAELW- 295
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1304137069 168 tkVQDYKKGQYMTlMPLVVDGKVIVGGSggefgvRGYVVAFDAGSGKELWRT 219
Cdd:COG1520 296 --KQDALLYRGLT-APVVLGDYVVVGDF------EGYLHWLSRDDGSLVARL 338
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
126-225 |
1.78e-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: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 126 DDLFQLHPTsrgvgLWEDKLYLATTDDHVVALDAKTGKVLWDTKVQDYKKGqymtlmPLVVDG-KVIVGGSGGEfgvrgy 204
Cdd:COG1520 46 KGYSRLAPA-----VAGDRVYAADADGRVAALDAATGKELWRVDLGEPLSG------GVGADGgLVVVGTEDGE------ 108
|
90 100
....*....|....*....|.
gi 1304137069 205 VVAFDAGSGKELWRTfTIPGE 225
Cdd:COG1520 109 VIALDADDGEELWRA-RLSSE 128
|
|
| assembly_YfgL |
TIGR03300 |
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
88-221 |
4.61e-10 |
|
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: 61.49 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 88 APPIVNNGVMFVATPMGQVIALNAKTGEEYWRykrqlpddlfqlHPTS--RGVGLWEDKLYLATTDDHVVALDAKTGKVL 165
Cdd:TIGR03300 235 GDPVVDGGQVYAVSYQGRVAALDLRSGRVLWK------------RDASsyQGPAVDDNRLYVTDADGVVVALDRRSGSEL 302
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1304137069 166 WDtkvQDYKKGQYMTlMPLVVDGKVIVGGSggefgvRGYVVAFDAGSGKELWRTFT 221
Cdd:TIGR03300 303 WK---NDELKYRQLT-APAVLGGYLVVGDF------EGYLHWLDRDDGSFVARLKT 348
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
450-523 |
2.19e-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: 56.36 E-value: 2.19e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1304137069 450 ADHFGELQAWDPATGKKVWQHDYKTsQLFGSVTAtAGDLVLAGGTNDRAFrIFNAKTGELLWEQKTNSGIMAMP 523
Cdd:COG1520 63 ADADGRVAALDAATGKELWRVDLGE-PLSGGVGA-DGGLVVVGTEDGEVI-ALDADDGEELWRARLSSEVLAAP 133
|
|
| BamB_YfgL |
cd10276 |
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ... |
450-534 |
2.10e-07 |
|
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: 53.10 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 450 ADHFGELQAWDPATGKKVWQHDYKTSQLFGSvTATAGDLVLAGGTNDRAFRIFNAKTGELLWEQKTNSGIMAMPMSYeVD 529
Cdd:cd10276 44 ADANGQVSAFNATTGKIIWETSLSGKGFLGG-TPAVGNGKIFVGTESGYLYALDAKDGSELWRTEVSDSQLLSPPTY-AD 121
|
....*
gi 1304137069 530 GTQYI 534
Cdd:cd10276 122 GKIYV 126
|
|
| assembly_YfgL |
TIGR03300 |
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
450-523 |
4.24e-07 |
|
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: 52.24 E-value: 4.24e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1304137069 450 ADHFGELQAWDPATGKKVWQHDYKtSQLFGSVTAtAGDLVLAGGTNDRAFrIFNAKTGELLWEQKTNSGIMAMP 523
Cdd:TIGR03300 71 ADADGTVAALDAETGKRLWRVDLD-ERLSGGVGA-DGGLVFVGTEKGEVI-ALDAEDGKELWRAKLSSEVLSPP 141
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
163-219 |
3.48e-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: 49.43 E-value: 3.48e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1304137069 163 KVLWDTKVQDYKKGQYMTLMPLVVDGKVIVGGSGGEfgvrgyVVAFDAGSGKELWRT 219
Cdd:COG1520 33 KQLWSASVGDGVGKGYSRLAPAVAGDRVYAADADGR------VAALDAATGKELWRV 83
|
|
| PRK11138 |
PRK11138 |
outer membrane biogenesis protein BamB; Provisional |
88-218 |
6.29e-06 |
|
outer membrane biogenesis protein BamB; Provisional
Pssm-ID: 236857 [Multi-domain] Cd Length: 394 Bit Score: 48.77 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 88 APPIVNNGVMFVATPMGQVIALNAKTGEEYWRYKRQLP--------------------DDLFQLHPT--SRGVGLWE--- 142
Cdd:PRK11138 154 SRPVVSDGLVLVHTSNGMLQALNESDGAVKWTVNLDVPsltlrgesapatafggaivgGDNGRVSAVlmEQGQLIWQqri 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 143 -----------------------DKLYLATTDDHVVALDAKTGKVLWdtkvqdykKGQYMTLMPLVVDGKVIvggsggeF 199
Cdd:PRK11138 234 sqptgateidrlvdvdttpvvvgGVVYALAYNGNLVALDLRSGQIVW--------KREYGSVNDFAVDGGRI-------Y 298
|
170 180
....*....|....*....|.
gi 1304137069 200 GV--RGYVVAFDAGSGKELWR 218
Cdd:PRK11138 299 LVdqNDRVYALDTRGGVELWS 319
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
32-166 |
6.91e-06 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 47.40 E-value: 6.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 32 PVTSARLENPEPGNWMLYRRTYDGQgFSPLDQintsnvKDLKPVWTFSTGVLEGHEAP---PIVNNGVMFVATPMGQVIA 108
Cdd:pfam13360 60 TLSGEVLGAPLVAGGRVFVVAGDGS-LIALDA------ADGRRLWSYQRSGEPLALRSsgsPAVVGDTVVAGFSSGKLVA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 109 LNAKTGEEYWRYKRQLP--------------------DDLFQLH--------PTSRGVGLWEDK-------------LYL 147
Cdd:pfam13360 133 LDPATGKVRWEAPLAAPrgtnelerlvditgtpvvagGRVFASAyqgrlvafDAATGRRLWTREisgpngpildgdlLYV 212
|
170
....*....|....*....
gi 1304137069 148 ATTDDHVVALDAKTGKVLW 166
Cdd:pfam13360 213 VSDDGELYALDRATGAVVW 231
|
|
| PRK11138 |
PRK11138 |
outer membrane biogenesis protein BamB; Provisional |
450-523 |
1.28e-05 |
|
outer membrane biogenesis protein BamB; Provisional
Pssm-ID: 236857 [Multi-domain] Cd Length: 394 Bit Score: 47.62 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 450 ADHFGELQAWDPATGKKVWQHDY----------KTSQLFGSVTAtAGDLVLAGGTNDRAFrIFNAKTGELLWEQKTNSGI 519
Cdd:PRK11138 75 ADRAGLVKALDADTGKEIWSVDLsekdgwfsknKSALLSGGVTV-AGGKVYIGSEKGQVY-ALNAEDGEVAWQTKVAGEA 152
|
....
gi 1304137069 520 MAMP 523
Cdd:PRK11138 153 LSRP 156
|
|
| assembly_YfgL |
TIGR03300 |
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
161-219 |
1.57e-05 |
|
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: 47.23 E-value: 1.57e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1304137069 161 TGKVLWDTKVQDYKKGQYMTLMPLVVDGKVIVGGSGGEfgvrgyVVAFDAGSGKELWRT 219
Cdd:TIGR03300 39 KVDQVWSASVGDGVGHYYLRLQPAVAGGKVYAADADGT------VAALDAETGKRLWRV 91
|
|
| assembly_YfgL |
TIGR03300 |
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
454-569 |
1.97e-05 |
|
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: 47.23 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 454 GELQAWDPATGKKVWQHDYKTSQL----FGSVTAtAGDLVLAGGTNDRaFRIFNAKTGELLWEQKTNSG----------- 518
Cdd:TIGR03300 155 GRLTALDAATGERLWTYSRVTPPLtlrgSASPVI-ADGGVLVGFAGGK-LVALDLQTGQPLWEQRVALPkgrtelerlvd 232
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1304137069 519 IMAMPMsyeVDGTQYIAVqsgwgvdaqriqdALAGKVAGFEnnVPQGGVIW 569
Cdd:TIGR03300 233 VDGDPV---VDGGQVYAV-------------SYQGRVAALD--LRSGRVLW 265
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
454-544 |
2.47e-05 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 45.86 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 454 GELQAWDPATGKKVWQHDYKTsqLFGSVTATAGDLVLAGGTNDRAFrIFNAKTGELLWEQKTNSGIMAMPmsyEVDGTQY 533
Cdd:pfam13360 3 GVVTALDAATGAELWRVDLET--GLGGGVAVDGGRLFVATGGGQLV-ALDAATGKLLWRQTLSGEVLGAP---LVAGGRV 76
|
90
....*....|....
gi 1304137069 534 IAV---QSGWGVDA 544
Cdd:pfam13360 77 FVVagdGSLIALDA 90
|
|
| PRK11138 |
PRK11138 |
outer membrane biogenesis protein BamB; Provisional |
90-197 |
3.01e-05 |
|
outer membrane biogenesis protein BamB; Provisional
Pssm-ID: 236857 [Multi-domain] Cd Length: 394 Bit Score: 46.46 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 90 PIVNNGVMFVATPMGQVIALNAKTGEEYWryKRQLP--DDLFQLHptsrgvglweDKLYLATTDDHVVALDAKTGKVLWD 167
Cdd:PRK11138 252 PVVVGGVVYALAYNGNLVALDLRSGQIVW--KREYGsvNDFAVDG----------GRIYLVDQNDRVYALDTRGGVELWS 319
|
90 100 110
....*....|....*....|....*....|
gi 1304137069 168 tkvQDYKKGQYMTlMPLVVDGKVIVGGSGG 197
Cdd:PRK11138 320 ---QSDLLHRLLT-APVLYNGYLVVGDSEG 345
|
|
| PQQ_mGDH |
cd10280 |
Membrane-bound PQQ-dependent glucose dehydrogenase; This bacterial subfamily of enzymes ... |
148-208 |
1.10e-04 |
|
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: 45.26 E-value: 1.10e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1304137069 148 ATTDDHVVALDAKTGKVLWDTKVqdyKKGQYMTLMPLVVDGK---VIVGGSGGEFGVR--GYVVAF 208
Cdd:cd10280 552 ATQDNYLRAFDKATGKELWEARL---PAGGQATPMTYEVDGKqyvVIAAGGHGSLGTKrgDSVIAY 614
|
|
| PQQ |
smart00564 |
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline ... |
89-121 |
1.36e-04 |
|
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline quinone (PQQ) as cofactor, in Ire1p-like Ser/Thr kinases, and in prokaryotic dehydrogenases.
Pssm-ID: 128836 [Multi-domain] Cd Length: 33 Bit Score: 39.05 E-value: 1.36e-04
10 20 30
....*....|....*....|....*....|...
gi 1304137069 89 PPIVNNGVMFVATPMGQVIALNAKTGEEYWRYK 121
Cdd:smart00564 1 PVVLSDGTVYVGSTDGTLYALDAKTGEILWTYK 33
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
450-555 |
1.55e-04 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 43.55 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 450 ADHFGELQAWDPATGKKVWQHDYkTSQLFGSVTATAGDLVLAggTNDRAFRIFNAKTGELLWEQKTNSGIMAM--PMSYE 527
Cdd:pfam13360 39 ATGGGQLVALDAATGKLLWRQTL-SGEVLGAPLVAGGRVFVV--AGDGSLIALDAADGRRLWSYQRSGEPLALrsSGSPA 115
|
90 100
....*....|....*....|....*...
gi 1304137069 528 VDGTQYIAVQSGWGVDAQRIQDalaGKV 555
Cdd:pfam13360 116 VVGDTVVAGFSSGKLVALDPAT---GKV 140
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
454-513 |
1.71e-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: 44.03 E-value: 1.71e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1304137069 454 GELQAWDPATGKKVWQHDYKTSQLF---GSVTATAGDLVLAGGTNDRaFRIFNAKTGELLWEQ 513
Cdd:COG1520 147 GRVYALDAATGERLWSYQRPVPALTlrgTSSPVIVGGAVLVGFANGK-LVALDLANGQPLWEQ 208
|
|
| PQQ |
smart00564 |
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline ... |
138-166 |
2.31e-04 |
|
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline quinone (PQQ) as cofactor, in Ire1p-like Ser/Thr kinases, and in prokaryotic dehydrogenases.
Pssm-ID: 128836 [Multi-domain] Cd Length: 33 Bit Score: 38.67 E-value: 2.31e-04
10 20
....*....|....*....|....*....
gi 1304137069 138 VGLWEDKLYLATTDDHVVALDAKTGKVLW 166
Cdd:smart00564 2 VVLSDGTVYVGSTDGTLYALDAKTGEILW 30
|
|
| PQQ |
pfam01011 |
PQQ enzyme repeat; The family represent a single repeat of a beta propeller. This propeller ... |
143-178 |
1.06e-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: 36.79 E-value: 1.06e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1304137069 143 DKLYLATTDDHVVALDAKTGKVLWDTKVQDYKKGQY 178
Cdd:pfam01011 1 GTVYLGSDDGYLYALDAETGKVLWSFKTGGAVLSSP 36
|
|
| Luminal_IRE1_like |
cd09213 |
The Luminal domain, a dimerization domain, of Inositol-requiring protein 1-like proteins; The ... |
87-174 |
1.13e-03 |
|
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: 41.32 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 87 EAPPIV----NNGVMFVATPMGQVIALNAKTGEeYWRYKRQLPDDLFQLHPTSRGVGLWEDK-------LYLATTDDHVV 155
Cdd:cd09213 82 EASPLVsdtnEDDVVVVGSKRTSVFALDAKTGK-IIKTYRADGLPSTGGSDSDGNSTPGPDElqeeeelLYIGRTDYVLQ 160
|
90
....*....|....*....
gi 1304137069 156 ALDAKTGKVLWDTKVQDYK 174
Cdd:cd09213 161 AIDPRSGKELWNVTYGEYE 179
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
454-514 |
3.67e-03 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 39.31 E-value: 3.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1304137069 454 GELQAWDPATGKKVWQHDYKTSQLFGSVTAT---AGDLVLAGGTNDRAfRIFNAKTGELLWEQK 514
Cdd:pfam13360 83 GSLIALDAADGRRLWSYQRSGEPLALRSSGSpavVGDTVVAGFSSGKL-VALDPATGKVRWEAP 145
|
|
| BamB_YfgL |
cd10276 |
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ... |
68-175 |
7.02e-03 |
|
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: 38.85 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304137069 68 NVKDLKPVWTFSTGVLEGH---------EAPPIVNNGVMFVATPMGQVIALNAKTGEEYWRYKrqlpddlfqlHPTSRGV 138
Cdd:cd10276 182 NTGTGVDIWEFSVSEPRGRtelprmidsSVTYVVVGGYLYSTSYQGYLVALDFESGQFLWSRK----------ASGGTST 251
|
90 100 110
....*....|....*....|....*....|....*...
gi 1304137069 139 GL-WEDKLYLATTDDHVVALDAKTGKVLWDTKVQDYKK 175
Cdd:cd10276 252 STdANGRVYVGDGEGSLYCLDASTGDELWSQTVLLGRV 289
|
|
| PQQ |
pfam01011 |
PQQ enzyme repeat; The family represent a single repeat of a beta propeller. This propeller ... |
95-121 |
7.16e-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: 34.47 E-value: 7.16e-03
|
|