|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
1-847 |
0e+00 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 1701.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 1 MSKVRLVVVGNGMVGHRFIEELIERADPGRYEITVFGAEPRPAYDRVHLSSYFSHHTSEDLSLVKPGFYDKHGIRLLLGE 80
Cdd:PRK14989 1 MSKVRLAIIGNGMVGHRFIEDLLDKADAANFDITVFCEEPRIAYDRVHLSSYFSHHTAEELSLVREGFYEKHGIKVLVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 81 AVKKIDRANREVHSNKGTVVGYDKLVLATGSYPWVPPIQGSQHHECFVYRTIEDLKAIRSAARSGKSGVVIGGGLLGLEA 160
Cdd:PRK14989 81 RAITINRQEKVIHSSAGRTVFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEACARRSKRGAVVGGGLLGLEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 161 AGALKALGLETHVVEFAPVLMAEQLDGQGGQLLRRKIESMGVQVHTSKSTSEILmHGGEQAKHRLAFADGSQLEVDVVVF 240
Cdd:PRK14989 161 AGALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEIV-QEGVEARKTMRFADGSELEVDFIVF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 241 STGIRPQDTLGRYGDLAIAERGGIVIDDHCLTSDPDIYAIGECAAWQGRFFGLVAPGYKMAQITVDHLLGGDSRFEGADM 320
Cdd:PRK14989 240 STGIRPQDKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGECASWNNRVFGLVAPGYKMAQVAVDHLLGSENAFEGADL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 321 SAKLKLLGVSVGSIGDAHGRTPGSHSYVFQDDQAGVYKKIVVSEDNSRLLGAVLVGDVEDYGNLLQMMLNALPLPSHPDT 400
Cdd:PRK14989 320 SAKLKLLGVDVGGIGDAHGRTPGARSYVYLDESKEIYKRLIVSEDNKTLLGAVLVGDTSDYGNLLQLVLNAIELPENPDS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 401 LILPAYAGA-KPTLGVDALPESAQICSCFDVSKGDIAKAVAEGHTTLAAIKQHTKAGTGCGGCVPLISQVLNAELVKQGI 479
Cdd:PRK14989 400 LILPAHAGSgKPSIGVDKLPDSAQICSCFDVTKGDLIAAINKGCHTVAALKAETKAGTGCGGCIPLVTQVLNAELAKQGI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 480 EVNNHLCAHFPHSRQELFHLVKVEGIKSFDELLAKHGQGYGCEVCKPTVGSILASCWNEHVLSPLNTQLQDTNDIFLGNM 559
Cdd:PRK14989 480 EVNNNLCEHFAYSRQELFHLIRVEGIKTFEELLAKHGKGYGCEVCKPTVGSLLASCWNEYILKPQHTPLQDTNDNFLANI 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 560 QKDGSYSVIPRMAGGEVTPEGLLAVAEVARDYKLYTKITGAQRIGLFGAQKDDLPAIWRKLLAAGFETGQAYAKALRMAK 639
Cdd:PRK14989 560 QKDGTYSVIPRSAGGEITPEGLMAVGRIAREFNLYTKITGSQRIGLFGAQKDDLPEIWRQLIEAGFETGHAYAKALRMAK 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 640 TCVGSTWCRFGVQDSVGLGVFLENRYKGIRTPHKMKFGVSGCTRECAEAQGKDVGIIATDAGWNLYVGGNGGMKPRHADL 719
Cdd:PRK14989 640 TCVGSTWCRYGVGDSVGLGVELENRYKGIRTPHKMKFGVSGCTRECAEAQGKDVGIIATEKGWNLYVCGNGGMKPRHADL 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 720 LASDLDRETLIKLIDRFMMFYVTSADKLQRTSVWLGNLEGGVDYLREVIVDDKLGLADTLERDIQTLIDSYECEWSRTLN 799
Cdd:PRK14989 720 LAADLDRETLIKYLDRFMMFYIRTADKLQRTAVWLENLEGGIDYLKAVIIDDKLGLNAQLEEEMARLREAVVCEWTETVN 799
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 498361884 800 EEEALKRFSHFINSDKRDPDVQFVSERDQHRPATPAERIPVYQIEVET 847
Cdd:PRK14989 800 TPSAQTRFKHFINSDKRDPNVQMVPEREQHRPATPYERIPVTLVEENA 847
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
6-799 |
0e+00 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 1060.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 6 LVVVGNGMVGHRFIEELIERADpGRYEITVFGAEPRPAYDRVHLSSYFS-HHTSEDLSLVKPGFYDKHGIRLLLGEAVKK 84
Cdd:TIGR02374 1 LVLVGNGMAGHRCIEEVLKLNR-HMFEITIFGEEPHPNYNRILLSSVLQgEADLDDITLNSKDWYEKHGITLYTGETVIQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 85 IDRANREVHSNKGTVVGYDKLVLATGSYPWVPPIQGSQHHECFVYRTIEDLKAIRSAARSGKSGVVIGGGLLGLEAAGAL 164
Cdd:TIGR02374 80 IDTDQKQVITDAGRTLSYDKLILATGSYPFILPIPGADKKGVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 165 KALGLETHVVEFAPVLMAEQLDGQGGQLLRRKIESMGVQVHTSKSTSEILmhgGEQAKHRLAFADGSQLEVDVVVFSTGI 244
Cdd:TIGR02374 160 QNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIV---GATKADRIRFKDGSSLEADLIVMAAGI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 245 RPQDTLGRYGDLAIAerGGIVIDDHCLTSDPDIYAIGECAAWQGRFFGLVAPGYKMAQITVDHLLGGDSR-FEGADMSAK 323
Cdd:TIGR02374 237 RPNDELAVSAGIKVN--RGIIVNDSMQTSDPDIYAVGECAEHNGRVYGLVAPLYEQAKVLADHICGVECEeYEGSDLSAK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 324 LKLLGVSVGSIGDAHgRTPGSHSYVFQDDQAGVYKKIVVSEDNsrLLGAVLVGDVEDYGNLLQMMLNALPLPSHPdTLIL 403
Cdd:TIGR02374 315 LKLLGVDVWSAGDAQ-ETERTTSIKIYDEQKGIYKKLVLSDDK--LLGAVLFGDTSDYGRLLDMVLKQADISEDP-AIIK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 404 PAYAGA-KPTLGVDALPESAQICSCFDVSKGDIAKAVAEGH-TTLAAIKQHTKAGTGCGGCVPLISQVLNAELVKQGIEV 481
Cdd:TIGR02374 391 PQISGPeAGGPGVEAMPDSEQICSCNTVTKGAIIDAIHTGScTTVEELKACTKAGTSCGGCKPLVEQLLRAELNSQYTAS 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 482 NNHLCAHFPHSRQELFHLVKVEGIKSFDELLAKHGQGY--GCEVCKPTVGSILASCWNEHVLSPLNTQLqdTNDIFLGNM 559
Cdd:TIGR02374 471 TPALCECTDFSRDELFEEIQARGFTTFAEVMNQLGWKTknGCSTCKPAVQYYLAMLYPGFILDEEATSL--SNDHFLANI 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 560 QKDGSYSVIPRMAGGEVTPEGLLAVAEVARDYKL-YTKITGAQRIGLFGAQKDDLPAIWRKLLAAGFEtgQAYAKALRMA 638
Cdd:TIGR02374 549 QKDGTYSVIPRMYGGRTNPEQLRTIANIAEAYSIpYVKITGGQRLDLFGAKKDDLPNIWKDLKMPGYE--HAYGKALRTV 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 639 KTCVGSTWCRFGVQDSVGLGVFLENRYKGIRTPHKMKFGVSGCTRECAEAQGKDVGIIATDAGWNLYVGGNGGMKPRHAD 718
Cdd:TIGR02374 627 KTCVGSQWCRYGNQDSVQLAIQLERRYEGLRTPHKIKIGVSGCERECAEAAGKDVGVIATEKGWNLYVGGNGGTHPRHGD 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 719 LLASDLDRETLIKLIDRFMMFYVTSADKLQRTSVWLGNLegGVDYLREVIVDDKlgLADTLERDIQTLIDSYECEWSRTL 798
Cdd:TIGR02374 707 LLAVDEDEETLIGYIDRFLQYYRETADYLERTAPWLERL--GIDHVREVLFEDD--LRAELEESMQRDLSLIKCPWKETL 782
|
.
gi 498361884 799 N 799
Cdd:TIGR02374 783 E 783
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
5-405 |
1.51e-148 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 442.66 E-value: 1.51e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 5 RLVVVGNGMVGHRFIEELIERADpgRYEITVFGAEPRPAYDRVHLSSYFSHHTS-EDLSLVKPGFYDKHGIRLLLGEAVK 83
Cdd:COG1251 3 RIVIIGAGMAGVRAAEELRKLDP--DGEITVIGAEPHPPYNRPPLSKVLAGETDeEDLLLRPADFYEENGIDLRLGTRVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 84 KIDRANREVHSNKGTVVGYDKLVLATGSYPWVPPIQGSQHHECFVYRTIEDLKAIRSAARSGKSGVVIGGGLLGLEAAGA 163
Cdd:COG1251 81 AIDRAARTVTLADGETLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 164 LKALGLETHVVEFAPVLMAEQLDGQGGQLLRRKIESMGVQVHTSKSTSEILmhgGEQAKHRLAFADGSQLEVDVVVFSTG 243
Cdd:COG1251 161 LRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIE---GDDRVTGVRLADGEELPADLVVVAIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 244 IRPQDTLGRYGDLAIAerGGIVIDDHCLTSDPDIYAIGECAAWQGRFFG-----LVAPGYKMAQITVDHLLGGDSRFEGA 318
Cdd:COG1251 238 VRPNTELARAAGLAVD--RGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGrrvleLVAPAYEQARVAAANLAGGPAAYEGS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 319 DMSAKLKLLGVSVGSIGDAHGrtpGSHSYVFQDDQAGVYKKIVVSEDnsRLLGAVLVGDVEDYGNLLQMMLNALPLPshP 398
Cdd:COG1251 316 VPSTKLKVFGVDVASAGDAEG---DEEVVVRGDPARGVYKKLVLRDG--RLVGAVLVGDTSDAGALRQLIKNGRPLP--P 388
|
....*..
gi 498361884 399 DTLILPA 405
Cdd:COG1251 389 RALLDAA 395
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
25-336 |
7.32e-57 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 198.11 E-value: 7.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 25 RADPGRyEITVFGAEPRPAYDRVHLSSYFSHHTS--EDLSLVKPGFYDKHGIRLLLGEAVKKIDRANREVHSNKGTVVGY 102
Cdd:COG0446 1 RLGPDA-EITVIEKGPHHSYQPCGLPYYVGGGIKdpEDLLVRTPESFERKGIDVRTGTEVTAIDPEAKTVTLRDGETLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 103 DKLVLATGSYPWVPPIQGSQHHECFVYRTIEDLKAIRSAARS--GKSGVVIgggllgleaagalKALGLETHVVEFAPVL 180
Cdd:COG0446 80 DKLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALREALKEfkGKRAVVIgggpiglelaealRKRGLKVTLVERAPRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 181 MAeQLDGQGGQLLRRKIESMGVQVHTSKSTSEILmhggEQAKHRLAFADGSQLEVDVVVFSTGIRPQDTLGRYGDLAIAE 260
Cdd:COG0446 160 LG-VLDPEMAALLEEELREHGVELRLGETVVAID----GDDKVAVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLALGE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 261 RGGIVIDDHCLTSDPDIYAIGECAAWQGRFFG------LVAPGYKMAQITVDHLLGGDSRFEGAdMSAKLKLLGVSVGSI 334
Cdd:COG0446 235 RGWIKVDETLQTSDPDVYAAGDCAEVPHPVTGktvyipLASAANKQGRVAAENILGGPAPFPGL-GTFISKVFDLCIAST 313
|
..
gi 498361884 335 GD 336
Cdd:COG0446 314 GT 315
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
5-283 |
3.82e-38 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 144.38 E-value: 3.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 5 RLVVVGNGMVGHRFIEELIERadpgRYEITVFGAEPRPAYDRVHLSSYFSH--------HTSEDLSLVKPGFYDK--HGI 74
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQL----GGKVTLIEDEGTCPYGGCVLSKALLGaaeapeiaSLWADLYKRKEEVVKKlnNGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 75 RLLLGEAVKKIDRANREVH-----SNKGTVVGYDKLVLATGSYPWVPPIQGSQHHECFVYRTIEDLKAIRSAARSGKSgV 149
Cdd:pfam07992 78 EVLLGTEVVSIDPGAKKVVleelvDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLLPKRV-V 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 150 VIGGGLLGLEAAGALKALGLETHVVEFAPVLMaEQLDGQGGQLLRRKIESMGVQVHTSKSTSEILmhgGEQAKHRLAFAD 229
Cdd:pfam07992 157 VVGGGYIGVELAAALAKLGKEVTLIEALDRLL-RAFDEEISAALEKALEKNGVEVRLGTSVKEII---GDGDGVEVILKD 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 498361884 230 GSQLEVDVVVFSTGIRPQDTLGRYGDLAIAERGGIVIDDHCLTSDPDIYAIGEC 283
Cdd:pfam07992 233 GTEIDADLVVVAIGRRPNTELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDC 286
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
7-325 |
2.25e-29 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 120.79 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 7 VVVGNGMVGHRFIEElIERAD---PgryeITVFGAEPRPAYDRVHLSSYFSH-HTSEDLSLVKPG-FYDKHGIRLLLGEA 81
Cdd:PRK04965 6 VIIGSGFAARQLVKN-IRKQDahiP----ITLITADSGDEYNKPDLSHVFSQgQRADDLTRQSAGeFAEQFNLRLFPHTW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 82 VKKIDRANREVHSNkGTVVGYDKLVLATGSYPWVPPIQGsqhHECFV-------YRTIEDlkAIRSA------------- 141
Cdd:PRK04965 81 VTDIDAEAQVVKSQ-GNQWQYDKLVLATGASAFVPPIPG---RELMLtlnsqqeYRAAET--QLRDAqrvlvvgggligt 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 142 ------ARSGKSgvVIgggllgleaagalkalglethVVEFAPVLMAEQLDGQGGQLLRRKIESMGVQVHTSKSTSEILM 215
Cdd:PRK04965 155 elamdlCRAGKA--VT---------------------LVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 216 HGgeqAKHRLAFADGSQLEVDVVVFSTGIRPQDTLGRYGDLAIAErgGIVIDDHCLTSDPDIYAIGECAAWQGRFFGLVA 295
Cdd:PRK04965 212 TD---SGIRATLDSGRSIEVDAVIAAAGLRPNTALARRAGLAVNR--GIVVDSYLQTSAPDIYALGDCAEINGQVLPFLQ 286
|
330 340 350
....*....|....*....|....*....|
gi 498361884 296 PGYKMAQITVDHLLGGDSRFEGADMSAKLK 325
Cdd:PRK04965 287 PIQLSAMALAKNLLGQNTPLKLPAMLVKVK 316
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
5-339 |
5.01e-26 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 110.99 E-value: 5.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 5 RLVVVGNGMVGHRFIEELiERADPGRYEITVFGAEPRpaydrvHLSSYFSHH------TSEDLSLVKPGFYDKHGIRLLL 78
Cdd:COG1252 3 RIVIVGGGFAGLEAARRL-RKKLGGDAEVTLIDPNPY------HLFQPLLPEvaagtlSPDDIAIPLRELLRRAGVRFIQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 79 GEaVKKIDRANREVHSNKGTVVGYDKLVLATGSYPWVPPIQGSQHHeCFVYRTIEDLKAIRS--------AARSGKSGVV 150
Cdd:COG1252 76 GE-VTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGIPGLAEH-ALPLKTLEDALALRErllaaferAERRRLLTIV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 151 I--------------GGGLLGLEAAGALKALGLETHVVEFAPVLMAEqLDGQGGQLLRRKIESMGVQVHTSKSTSEIlmh 216
Cdd:COG1252 154 VvgggptgvelagelAELLRKLLRYPGIDPDKVRITLVEAGPRILPG-LGEKLSEAAEKELEKRGVEVHTGTRVTEV--- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 217 ggeqAKHRLAFADGSQLEVDVVVFSTGIRPQDTLGRYGdLAIAERGGIVIDDHC-LTSDPDIYAIGECAAWQGRFFGLVA 295
Cdd:COG1252 230 ----DADGVTLEDGEEIPADTVIWAAGVKAPPLLADLG-LPTDRRGRVLVDPTLqVPGHPNVFAIGDCAAVPDPDGKPVP 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 498361884 296 P----GYKMAQITVDHLLggdSRFEGADMSA-KLKLLGvSVGSIGDAHG 339
Cdd:COG1252 305 KtaqaAVQQAKVLAKNIA---ALLRGKPLKPfRYRDKG-CLASLGRGAA 349
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
71-376 |
7.47e-26 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 111.67 E-value: 7.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 71 KHGIRLLLGEAVKKIDRANREV---HSNKGTVV--GYDKLVLATGSYPWVPPIQGSQHHECFVYRTIEDLKAIRSAAR-- 143
Cdd:PRK09564 68 KSGIDVKTEHEVVKVDAKNKTItvkNLKTGSIFndTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALKELLKde 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 144 SGKSGVVIGGGLLGLEAAGALKALGLETHVVEFAPVLMAEQLDGQGGQLLRRKIESMGVQVHTSKSTSEILmhgGEQaKH 223
Cdd:PRK09564 148 EIKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLI---GED-KV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 224 RLAFADGSQLEVDVVVFSTGIRPQDTLGRYGDLAIAERGGIVIDDHCLTSDPDIYAIGECAAWQGRFFG------LVAPG 297
Cdd:PRK09564 224 EGVVTDKGEYEADVVIVATGVKPNTEFLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDCATIYNIVSNknvyvpLATTA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 298 YKMAQITVDHLLGGDSRFEGADMSAKLKLLGVSVGSIG----DAHGRTPGSHSYVFQD--------DQAGVYKKIVVSED 365
Cdd:PRK09564 304 NKLGRMVGENLAGRHVSFKGTLGSACIKVLDLEAARTGlteeEAKKLGIDYKTVFIKDknhtnyypGQEDLYVKLIYEAD 383
|
330
....*....|.
gi 498361884 366 NSRLLGAVLVG 376
Cdd:PRK09564 384 TKVILGGQIIG 394
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
1-284 |
8.30e-24 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 104.62 E-value: 8.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 1 MSKVRLVVVGNGMVGHRFIEELIERADPGryEITVFGAEPRPAYDRVHLS-SYFSHHTSEDLSLVKPGFYDKHGIRLLLG 79
Cdd:PRK09754 1 MKEKTIIIVGGGQAAAMAAASLRQQGFTG--ELHLFSDERHLPYERPPLSkSMLLEDSPQLQQVLPANWWQENNVHLHSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 80 EAVKKIDRANREVHSNKGTVVGYDKLVLATGSYPWVPPIQGSQHHECFVYRTIEDLKAIRSAARSGKSGVVIGGGLLGLE 159
Cdd:PRK09754 79 VTIKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 160 AAGALKALGLETHVVEFAPVLMAEQLDGQGGQLLRRKIESMGVQVHTSKStseiLMHGGEQAKHRLAFADGSQLEVDVVV 239
Cdd:PRK09754 159 LAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNA----IEHVVDGEKVELTLQSGETLQADVVI 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 498361884 240 FSTGIRPQDTLGRygDLAIAERGGIVIDDHCLTSDPDIYAIGECA 284
Cdd:PRK09754 235 YGIGISANDQLAR--EANLDTANGIVIDEACRTCDPAIFAGGDVA 277
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
67-391 |
7.57e-21 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 96.31 E-value: 7.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 67 GFYDKHGIRLLLGEAvkKIDRANR-EVhsNKGTVVGYDKLVLATGSYPWVPPIQGSQHHECFVYRTIEDLKAIrsaarsG 145
Cdd:COG1249 99 ELLKKNGVDVIRGRA--RFVDPHTvEV--TGGETLTADHIVIATGSRPRVPPIPGLDEVRVLTSDEALELEEL------P 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 146 KSGVVIgggllgleaagalKALGLETHVVEFAPVLMAeQLDGQGGQLLRRKIESMGVQVHTSKSTSEILMHGGeqaKHRL 225
Cdd:COG1249 169 KSLVVIgggyiglefaqifARLGSEVTLVERGDRLLP-GEDPEISEALEKALEKEGIDILTGAKVTSVEKTGD---GVTV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 226 AFADGS---QLEVDVVVFSTGIRPQ------DTLGrygdLAIAERGGIVIDDHCLTSDPDIYAIGECAawqGRFfgLVAP 296
Cdd:COG1249 245 TLEDGGgeeAVEADKVLVATGRRPNtdglglEAAG----VELDERGGIKVDEYLRTSVPGIYAIGDVT---GGP--QLAH 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 297 -GYKMAQITVDHLLGGDSRfeGADMSAklkllgVS--------VGSIG----DAH--------GRTPGSHSYVFQ--DDQ 353
Cdd:COG1249 316 vASAEGRVAAENILGKKPR--PVDYRA------IPsvvftdpeIASVGlteeEAReagidvkvGKFPFAANGRALalGET 387
|
330 340 350
....*....|....*....|....*....|....*....
gi 498361884 354 AGVYkKIVVSEDNSRLLGAVLVG-DVEDYGNLLQMMLNA 391
Cdd:COG1249 388 EGFV-KLIADAETGRILGAHIVGpHAGELIHEAALAMEM 425
|
|
| NirB_Fer2_BFD-like_1 |
cd19943 |
first bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of the large ... |
419-470 |
9.26e-20 |
|
first bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of the large subunit of the NADH-dependent nitrite reductase; The NADH-dependent nitrite reductase (NirBD) complex comprises a large and a small subunit, and is also known as nitrite reductase (reduced nicotinamide adenine dinucleotide), NADH-nitrite oxidoreductase, and assimilatory nitrite reductase. NirBD uses NADH as electron donor, and FAD, iron-sulfur cluster, and siroheme cofactors, all embedded in the large subunit NirB to catalyze the 6-electron reduction of nitrite to ammonium. NirBD plays a role in regulating nitric oxide homeostasis in Streptomyces coelicolor. In addition to NirB, the BFD-like [2Fe-2S]-binding domain is found in a variety of proteins including bacterioferritin-associated ferredoxin (BFD) and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.
Pssm-ID: 381076 [Multi-domain] Cd Length: 53 Bit Score: 83.43 E-value: 9.26e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 498361884 419 PESAQICSCFDVSKGDIAKAVAE-GHTTLAAIKQHTKAGTGCGGCVPLISQVL 470
Cdd:cd19943 1 PDDAEVCGCNGVSKGAIVQAIQEkGLTTLDEVKACTKASTSCGGCTPLVEQLL 53
|
|
| Fer2_BFD |
pfam04324 |
BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved ... |
424-470 |
3.13e-17 |
|
BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved cysteine residues. This domain occurs alone in small proteins such as Bacterioferritin-associated ferredoxin (BFD). The function of BFD is not known, but it may may be a general redox and/or regulatory component involved in the iron storage or mobilization functions of bacterioferritin in bacteria. This domain is also found in nitrate reductase proteins in association with Nitrite and sulphite reductase 4Fe-4S domain (pfam01077), Nitrite/Sulfite reductase ferredoxin-like half domain (pfam03460) and Pyridine nucleotide-disulphide oxidoreductase (pfam00070). It is also found in NifU nitrogen fixation proteins, in association with NifU-like N terminal domain (pfam01592) and NifU-like domain (pfam01106).
Pssm-ID: 461261 [Multi-domain] Cd Length: 50 Bit Score: 76.03 E-value: 3.13e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 498361884 424 ICSCFDVSKGDIAKAVAEGHTTLAAIKQHTKAGTGCGGCVPLISQVL 470
Cdd:pfam04324 2 VCRCFGVTDGEIRDAIREGLTTVEEVKRRTKAGTGCGSCRPAIEEIL 48
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
70-283 |
8.76e-16 |
|
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]
Pssm-ID: 273944 [Multi-domain] Cd Length: 463 Bit Score: 80.93 E-value: 8.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 70 DKHGIRLLLGEAVKKidrANREVHSNKGT-VVGYDKLVLATGSYPWVPPIQGSQHHEcfvYRTIEDLKAIRsaaRSGKSG 148
Cdd:TIGR02053 99 SSYGVDYLRGRARFK---DPKTVKVDLGReVRGAKRFLIATGARPAIPPIPGLKEAG---YLTSEEALALD---RIPESL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 149 VVIGGGLLGLEAAGALKALGLETHVVEFAPVLMAEQlDGQGGQLLRRKIESMGVQVHTSKSTSEILMHGGEQAKHRLAFA 228
Cdd:TIGR02053 170 AVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPRE-EPEISAAVEEALAEEGIEVVTSAQVKAVSVRGGGKIITVEKPG 248
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498361884 229 DGSQLEVDVVVFSTGIRPQ-DTLG-RYGDLAIAERGGIVIDDHCLTSDPDIYAIGEC 283
Cdd:TIGR02053 249 GQGEVEADELLVATGRRPNtDGLGlEKAGVKLDERGGILVDETLRTSNPGIYAAGDV 305
|
|
| Bfd |
COG2906 |
Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism]; |
424-474 |
9.10e-16 |
|
Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism];
Pssm-ID: 442150 [Multi-domain] Cd Length: 54 Bit Score: 71.77 E-value: 9.10e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 498361884 424 ICSCFDVSKGDIAKAVAEGHTTLAAIKQHTKAGTGCGGCVPLISQVLNAEL 474
Cdd:COG2906 3 VCLCNGVTDRQIRAAIAEGATSLEELRAALGAGTQCGSCVPEARELLAEAL 53
|
|
| NirB_Fer2_BFD-like_2 |
cd19944 |
second bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of the large ... |
483-532 |
1.20e-15 |
|
second bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of the large subunit of the NADH-dependent nitrite reductase; The NADH-dependent nitrite reductase (NirBD) complex comprises a large (NirB) and a small (NirD) subunit, and is also known as nitrite reductase (reduced nicotinamide adenine dinucleotide), NADH-nitrite oxidoreductase, and assimilatory nitrite reductase. NirBD uses NADH as electron donor, and FAD, iron-sulfur cluster, and siroheme cofactors, all embedded in the large subunit NirB to catalyze the 6-electron reduction of nitrite to ammonium. Some of the second [2Fe-2S]-binding domains, have one of the Cys residues replaced by a His residue, they may interact with non-Rieske NirD subunits. NirBD plays a role in regulating nitric oxide homeostasis in Streptomyces coelicolor. In addition to NirB, the BFD-like [2Fe-2S]-binding domain is found in a variety of proteins including bacterioferritin-associated ferredoxin (BFD) and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.
Pssm-ID: 381077 [Multi-domain] Cd Length: 52 Bit Score: 71.45 E-value: 1.20e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 498361884 483 NHLCAHFPHSRQELFHLVKVEGIKSFDELLAKHGQGY--GCEVCKPTVGSIL 532
Cdd:cd19944 1 KTLCSCTDLSHDEVREAIQEHGLTSFEEVMAALGWKTpdGCEKCRPALNYYL 52
|
|
| NIR_SIR |
pfam01077 |
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ... |
632-734 |
1.58e-14 |
|
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the biosynthetic assimilation of sulphur and nitrogen, respectfully. They are also both important for the dissimilation of oxidized anions for energy transduction.
Pssm-ID: 426031 [Multi-domain] Cd Length: 153 Bit Score: 71.53 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 632 AKALRMAKTCVGSTWCRFGVQDSVGLGVFLENRYKGI----RTPHKMKFGVSGCTRECAEAQGKDVGIIATD-----AGW 702
Cdd:pfam01077 1 GDNVRNVTLCPGAGLCPEELLDTRPLAKAIEDEFEPDygfpYLPRKFKIAVSGCPNNCVAAHANDIGFVGVWkdggeIGF 80
|
90 100 110
....*....|....*....|....*....|....
gi 498361884 703 NLYVGGNGGMKPRHADLLASD--LDRETLIKLID 734
Cdd:pfam01077 81 NILVGGGLGRTPGAAATLKVVpfVPEEDVLEVIE 114
|
|
| CysI |
COG0155 |
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ... |
561-734 |
1.80e-13 |
|
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; Sulfite reductase, beta subunit (hemoprotein) is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439925 [Multi-domain] Cd Length: 519 Bit Score: 74.00 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 561 KDGSYSVIPRMAGGEVTPEGLLAVAEVARDY-KLYTKITGAQRIGLFGAQKDDLPAIWRKLLAAGFETGQA--------- 630
Cdd:COG0155 51 PDGAFMLRVRIPGGVLTPEQLRALADIAREYgRGYLHLTTRQNIQLHWILLEDLPEILRELAEVGLTTIGAcgdvvrnvt 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 631 -----------------YAKALRmaktcvgsTWcrfgvqdsvglgvFLENR-YKGIrtPHKMKFGVSGCTRECAEAQGKD 692
Cdd:COG0155 131 asplagvdpdelfdvrpYAEAIS--------QH-------------LLGHPeYTYL--PRKFKIAFSGPPEDDADVEIND 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 498361884 693 VGIIAT-----DAGWNLYVGGNGGMKPRHADLLASDLDRETLIKLID 734
Cdd:COG0155 188 LGFIAVvkedgLVGFNVLVGGGLGRTPRLADVLGEFVPPEDLLDVAE 234
|
|
| CysI |
COG0155 |
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ... |
560-741 |
4.85e-13 |
|
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; Sulfite reductase, beta subunit (hemoprotein) is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439925 [Multi-domain] Cd Length: 519 Bit Score: 72.46 E-value: 4.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 560 QK-DGSYSVIPRMAGGEVTPEGLLAVAEVARDY-KLYTKITGAQRIGLFGAQKDDLPAIWRKLLAAGFETgqAYAKALRM 637
Cdd:COG0155 300 QKqDGLYYVGLSVENGRITDEQLRALADLAERYgSGEIRLTPNQNLILADVPEEDLPALEAALRALGLAT--PPSGLRRD 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 638 AKTCVGSTWCRFGVQDSVGLGV----FLENRYKGIRTPHKMKFGVSGCTRECAEAQGKDVGIIATDA-----GWNLYVGG 708
Cdd:COG0155 378 SIACPGLPTCKLAIAESKRLAPaladRLEEDLDGLHDDEPIRIRISGCPNSCGRHYIADIGLVGKAKkgvveAYQLYLGG 457
|
170 180 190
....*....|....*....|....*....|...
gi 498361884 709 NGGMKPRHADLLASDLDRETLIKLIDRFMMFYV 741
Cdd:COG0155 458 GLGGDARLGRKYGPKVPADEIPDALERLLEAYL 490
|
|
| NIR_SIR_ferr |
pfam03460 |
Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key ... |
560-623 |
3.36e-12 |
|
Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key to both biosynthetic assimilation of sulfur and nitrogen and dissimilation of oxidized anions for energy transduction. Two copies of this repeat are found in Nitrite and Sulfite reductases and form a single structural domain.
Pssm-ID: 377044 [Multi-domain] Cd Length: 67 Bit Score: 62.16 E-value: 3.36e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498361884 560 QKDGSYSVIPRMAGGEVTPEGLLAVAEVARDYKLYT-KITGAQRIGLFGAQKDDLPAIWRKLLAA 623
Cdd:pfam03460 3 QKDGDYMVRVRVPGGRLTAEQLRALADIAEKYGDGEiRLTTRQNLELHGVPEEDLPELLEELAEA 67
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
103-393 |
1.97e-10 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 64.00 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 103 DKLVLATGSYPWVPPIQG---SQHhecfVYrtieDLKAIRSAARSGKSGVVIGGGLLGLEAAGALKALGLETHVVEFAPV 179
Cdd:PRK07251 120 ETIVINTGAVSNVLPIPGladSKH----VY----DSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAAST 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 180 LMAEQLDGQGgQLLRRKIESMGVQVHTSKSTSEILMHGGEQakhrLAFADGSQLEVDVVVFSTGIRPQDT-LG-RYGDLA 257
Cdd:PRK07251 192 ILPREEPSVA-ALAKQYMEEDGITFLLNAHTTEVKNDGDQV----LVVTEDETYRFDALLYATGRKPNTEpLGlENTDIE 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 258 IAERGGIVIDDHCLTSDPDIYAIGEcaawqgrffglVAPGYKMAQITVDHL------LGGDSRFEGADM----------- 320
Cdd:PRK07251 267 LTERGAIKVDDYCQTSVPGVFAVGD-----------VNGGPQFTYISLDDFrivfgyLTGDGSYTLEDRgnvpttmfitp 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 321 ----------SAKLKLLGVSVGSIGDAHgrTPGSHsyvFQDDQAGVYkKIVVSEDNSRLLGAVLVG-DVEDYGNLLQM-M 388
Cdd:PRK07251 336 plsqvgltekEAKEAGLPYAVKELLVAA--MPRAH---VNNDLRGAF-KVVVNTETKEILGATLFGeGSQEIINLITMaM 409
|
....*
gi 498361884 389 LNALP 393
Cdd:PRK07251 410 DNKIP 414
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
71-281 |
4.54e-10 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 62.86 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 71 KHGIRLLLGEAvkKIDRANR-EVHSNKG-TVVGYDKLVLATGSYPWVPP---IQGsqhhecfvyRTIEDLKAIRSAARSG 145
Cdd:PRK06416 104 KNKVDIIRGEA--KLVDPNTvRVMTEDGeQTYTAKNIILATGSRPRELPgieIDG---------RVIWTSDEALNLDEVP 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 146 KSGVVIGGGLLGLEAAGALKALGLETHVVEFAPVLMAEQlDGQGGQLLRRKIESMGVQVHTSKSTSEIlmhggEQAKH-- 223
Cdd:PRK06416 173 KSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGE-DKEISKLAERALKKRGIKIKTGAKAKKV-----EQTDDgv 246
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498361884 224 RLAFADG---SQLEVDVVVFSTGIRPQ-DTLGrYGDLAIA-ERGGIVIDDHCLTSDPDIYAIG 281
Cdd:PRK06416 247 TVTLEDGgkeETLEADYVLVAVGRRPNtENLG-LEELGVKtDRGFIEVDEQLRTNVPNIYAIG 308
|
|
| Fer2_BFD-like |
cd19942 |
[2Fe-2S]-binding domain of bacterioferritin-associated ferredoxin (BFD) and related proteins; ... |
422-469 |
8.48e-10 |
|
[2Fe-2S]-binding domain of bacterioferritin-associated ferredoxin (BFD) and related proteins; The BFD-like [2Fe-2S]-binding domain comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. The Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport. BFD-like [2Fe-2S]-binding domains are found in proteins such as bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, Cu+ chaperone CopZ, anaerobic glycerol 3-phosphate dehydrogenase subunit A, hydrogen cyanide synthase subunit B, nitrogen fixation protein NifU, prokaryotic assimilatory nitrate reductase catalytic subunit NasA, and archaeal proline dehydrogenase PDH1. This superfamily also includes uncharacterized proteins having an N-terminal BFD-like [2Fe-2S]-binding domain and a C-terminal domain belonging to the Ni,Fe-hydrogenase I small subunit family.
Pssm-ID: 381075 [Multi-domain] Cd Length: 49 Bit Score: 54.75 E-value: 8.48e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 498361884 422 AQICSCFDVSKGDIAKAVAEGH-TTLAAIKQHTKAGTGCGGCVPLISQV 469
Cdd:cd19942 1 ALVCECFAVTEKELREAIRKGGlKTVEELLTGTGAGGGCGVCHPHVAQL 49
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
73-289 |
2.57e-09 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 60.58 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 73 GIRLLLGEAvkKIDRANR-EVhsnKGTVVGYDKLVLATGS-YPWVPPIQGSQHHECFVYRTIEDLKAIrsaarsGKSGVV 150
Cdd:PRK06292 106 KIDKIKGTA--RFVDPNTvEV---NGERIEAKNIVIATGSrVPPIPGVWLILGDRLLTSDDAFELDKL------PKSLAV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 151 IGGGLLGLEAAGALKALGLETHVVEFAPVLMAEQlDGQGGQLLRRKIESMgVQVHTSKSTSEILMHGGEQAKHRLAFADG 230
Cdd:PRK06292 175 IGGGVIGLELGQALSRLGVKVTVFERGDRILPLE-DPEVSKQAQKILSKE-FKIKLGAKVTSVEKSGDEKVEELEKGGKT 252
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 231 SQLEVDVVVFSTGIRPQ-DTLG-RYGDLAIAERGGIVIDDHCLTSDPDIYAIGEC---------AAWQGR 289
Cdd:PRK06292 253 ETIEADYVLVATGRRPNtDGLGlENTGIELDERGRPVVDEHTQTSVPGIYAAGDVngkppllheAADEGR 322
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
167-314 |
3.89e-09 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 59.83 E-value: 3.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 167 LGLETHVVEFAPVLMAEQlDGQGGQLLRRKIESMGVQVHTSKSTSEILMHGGEQAKHRLAFADGSQLEVDVVVFSTGIRP 246
Cdd:PRK06370 193 FGSEVTVIERGPRLLPRE-DEDVAAAVREILEREGIDVRLNAECIRVERDGDGIAVGLDCNGGAPEITGSHILVAVGRVP 271
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498361884 247 Q-DTLGrygdLAIA-----ERGGIVIDDHCLTSDPDIYAIGECaawQGRF-FGLVApgYKMAQITVDHLLGGDSR 314
Cdd:PRK06370 272 NtDDLG----LEAAgvetdARGYIKVDDQLRTTNPGIYAAGDC---NGRGaFTHTA--YNDARIVAANLLDGGRR 337
|
|
| Fer2_BFD-like |
cd19942 |
[2Fe-2S]-binding domain of bacterioferritin-associated ferredoxin (BFD) and related proteins; ... |
485-531 |
9.61e-09 |
|
[2Fe-2S]-binding domain of bacterioferritin-associated ferredoxin (BFD) and related proteins; The BFD-like [2Fe-2S]-binding domain comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. The Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport. BFD-like [2Fe-2S]-binding domains are found in proteins such as bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, Cu+ chaperone CopZ, anaerobic glycerol 3-phosphate dehydrogenase subunit A, hydrogen cyanide synthase subunit B, nitrogen fixation protein NifU, prokaryotic assimilatory nitrate reductase catalytic subunit NasA, and archaeal proline dehydrogenase PDH1. This superfamily also includes uncharacterized proteins having an N-terminal BFD-like [2Fe-2S]-binding domain and a C-terminal domain belonging to the Ni,Fe-hydrogenase I small subunit family.
Pssm-ID: 381075 [Multi-domain] Cd Length: 49 Bit Score: 52.06 E-value: 9.61e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 498361884 485 LCAHFPHSRQELFHLVKVEGIKSFDELLAKHGQGYGCEVCKPTVGSI 531
Cdd:cd19942 3 VCECFAVTEKELREAIRKGGLKTVEELLTGTGAGGGCGVCHPHVAQL 49
|
|
| Fer2_BFD |
cd19945 |
bacterioferritin-associated ferredoxin (BFD) [2Fe-2S]-binding domain; This family includes ... |
424-474 |
5.21e-08 |
|
bacterioferritin-associated ferredoxin (BFD) [2Fe-2S]-binding domain; This family includes Escherichia coli and Pseudomonas aeruginosa bacterioferritin-associated ferredoxin BFD which binds an [2Fe-2S] cluster and appears to interact with bacterioferritin (E. coli BFR/YheA and P. aeruginosa BfrB), a dynamic regulator of intracellular iron levels. It has been suggested that BFD and bacterioferritin form an electron transfer complex which may participate in the iron storage or iron immobilization functions of bacterioferritin. For Pseudomonas aeruginosa, it has been shown that mobilization of Fe3+ stored in BfrB requires interaction with BFD, which transfers electrons to reduce Fe3+ in the internal cavity of BfrB for subsequent release of Fe2+. The stability of BFD may be aided by an anion-binding site found within this domain. In addition to BFD, the BFD-like [2Fe-2S]-binding domain is found in a variety of proteins such as the large subunit of NADH-dependent nitrite reductase and the Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.
Pssm-ID: 381078 [Multi-domain] Cd Length: 54 Bit Score: 49.89 E-value: 5.21e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 498361884 424 ICSCFDVSKGDIAKAVAEGHTTLAAIKQHTKAGTGCGGCVPLISQVLNAEL 474
Cdd:cd19945 3 VCLCNGITDKQIRQAVAQGATSLRELREQLGVGSQCGKCARMARQVLEEEL 53
|
|
| NifU_Fer2_BFD-like |
cd19947 |
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of nitrogen fixation ... |
420-470 |
5.57e-08 |
|
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of nitrogen fixation protein NifU and similar proteins; This family includes the BFD-like [2Fe-2S]-binding domain of Azotobacter vinelandii and Klebsiella pneumoniae nitrogen fixation protein NifU. NifU binds one Fe cation per subunit and one [2Fe-2S] cluster per subunit, and is involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins. The BFD-like [2Fe-2S]-binding domain is found in a variety of other proteins including bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.
Pssm-ID: 381080 [Multi-domain] Cd Length: 55 Bit Score: 49.97 E-value: 5.57e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 498361884 420 ESAQICSCFDVSKGDIAKAVAEGH-TTLAAIKQHTKAGTGCGGCVPLISQVL 470
Cdd:cd19947 1 EGAIVCKCFGVTEVMIERAIRENNlTTVEDVTNYTKAGGGCGSCHEKIEDIL 52
|
|
| Rubredoxin_C |
pfam18267 |
Rubredoxin NAD+ reductase C-terminal domain; This is the C-terminal domain of NADH rubredoxin ... |
321-381 |
6.42e-08 |
|
Rubredoxin NAD+ reductase C-terminal domain; This is the C-terminal domain of NADH rubredoxin oxidoreductase present in Clostridium acetobutylicum. The majority of obligatory anaerobes detoxify micro-aerobic environments by consuming O2 via H2O-forming NADH oxidase. This enzyme offers an alternate reaction pathway for scavenging of O2 and reactive oxygen species, wherein the reducing equivalent is obtained from NADH.
Pssm-ID: 408082 [Multi-domain] Cd Length: 70 Bit Score: 50.25 E-value: 6.42e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498361884 321 SAKLKLLGVSVGSIGDAHGrTPGSHSYVFQDDQAGVYKKIVVseDNSRLLGAVLVGDVEDY 381
Cdd:pfam18267 2 STILKVFGIDLFSMGDIEE-NDNAEEIVKVDASNGIYKKLFI--RDGKLVGAILIGDTSES 59
|
|
| NasA-like_Fer2_BFD-like |
cd19948 |
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain at the C-terminus of ... |
424-470 |
1.37e-07 |
|
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain at the C-terminus of prokaryotic assimilatory nitrate reductase catalytic subunit NasA and similar proteins; The BFD-like [2Fe-2S]-binding domain described in this family is found at the C-terminus of prokaryotic assimilatory nitrate reductase catalytic subunit (NasA) such as Rhodobacter capsulatus E1F1 NasA. Nitrate reductase catalyzes the reduction of nitrate to nitrite, the first step of nitrate assimilation. R. capsulatus E1F1 nitrate reductase is composed of this NasA subunit and a small diaphorase subunit with FAD. Note that this [2Fe-2S]-binding domain is not always present; for example, it is absent from the characterized haloaechean Haloferax mediterranei NasA; both, however, have an [4Fe-4S] binding domain at their N-terminus. The BFD-like [2Fe-2S]-binding domain is found in a variety of other proteins including bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.
Pssm-ID: 381081 [Multi-domain] Cd Length: 53 Bit Score: 48.67 E-value: 1.37e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 498361884 424 ICSCFDVSKGDIAKAVA-EGHTTLAAIKQHTKAGTGCGGCVPLISQVL 470
Cdd:cd19948 4 VCACFSVGENTIRRAIAdNGLTSVAQVGTCLKAGTNCGSCVPEIQKLL 51
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
73-322 |
2.84e-07 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 54.00 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 73 GIRLLLGEAVKKiDRANREVHSNKGT--VVGYDKLVLATGSYPWVPPIQGSQhhECFVYRTIEDLKAIRSAARSgksgVV 150
Cdd:PRK13748 203 AITVLHGEARFK-DDQTLIVRLNDGGerVVAFDRCLIATGASPAVPPIPGLK--ETPYWTSTEALVSDTIPERL----AV 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 151 IGGGLLGLEAAGALKALGLETHVVEFAPVLMAEqlDGQGGQLLRRKIESMGVQV--HTskstseilmhggeQAKHrLAFA 228
Cdd:PRK13748 276 IGSSVVALELAQAFARLGSKVTILARSTLFFRE--DPAIGEAVTAAFRAEGIEVleHT-------------QASQ-VAHV 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 229 DGS--------QLEVDVVVFSTGIRP---QDTLGRYGdLAIAERGGIVIDDHCLTSDPDIYAIGECAAwQGRFFGLVAPG 297
Cdd:PRK13748 340 DGEfvlttghgELRADKLLVATGRAPntrSLALDAAG-VTVNAQGAIVIDQGMRTSVPHIYAAGDCTD-QPQFVYVAAAA 417
|
250 260
....*....|....*....|....*
gi 498361884 298 YKMAQItvdHLLGGDSRFEGADMSA 322
Cdd:PRK13748 418 GTRAAI---NMTGGDAALDLTAMPA 439
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
3-285 |
2.98e-07 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 53.62 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 3 KVRLVVVGNGMVGHRFIEELieraDPGRYEITVFgaEPRPAYDRVHLSSYFSHHTSEDLSLVKP--GFYDKHGIRLLLGE 80
Cdd:PTZ00318 10 KPNVVVLGTGWAGAYFVRNL----DPKKYNITVI--SPRNHMLFTPLLPQTTTGTLEFRSICEPvrPALAKLPNRYLRAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 81 AVKkIDRANREV----------HSNKGTVVGYDKLVLATGSYPWVPPIQGSQHHECFVyRTIEDLKAIRS---------- 140
Cdd:PTZ00318 84 VYD-VDFEEKRVkcgvvsksnnANVNTFSVPYDKLVVAHGARPNTFNIPGVEERAFFL-KEVNHARGIRKrivqcieras 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 141 --------AAR--------SGKSGVVIGGGLLGLEAAGALKalgLETHVVEFAPVLMAE---QLDGQGGQLLRRK----I 197
Cdd:PTZ00318 162 lpttsveeRKRllhfvvvgGGPTGVEFAAELADFFRDDVRN---LNPELVEECKVTVLEagsEVLGSFDQALRKYgqrrL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 198 ESMGVQVHTSKSTSEILmhggeqaKHRLAFADGSQLEVDVVVFSTGIRPQdTLGRYGDLAIAERGGIVIDDHCLTSD-PD 276
Cdd:PTZ00318 239 RRLGVDIRTKTAVKEVL-------DKEVVLKDGEVIPTGLVVWSTGVGPG-PLTKQLKVDKTSRGRISVDDHLRVKPiPN 310
|
....*....
gi 498361884 277 IYAIGECAA 285
Cdd:PTZ00318 311 VFALGDCAA 319
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
70-283 |
6.56e-07 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 52.85 E-value: 6.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 70 DKHGIRLLLGEAvKKIDraNREVHSNkGTVVGYDKLVLATGSYPWVPPIQGSQHheCFVYRTIEDLKAI-RSAARSGK-- 146
Cdd:PRK06116 104 ENNGVDLIEGFA-RFVD--AHTVEVN-GERYTADHILIATGGRPSIPDIPGAEY--GITSDGFFALEELpKRVAVVGAgy 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 147 -----SGVVigggllgleaagalKALGLETHVV--------EFAPVLmaeqldgqgGQLLRRKIESMGVQVHTSKSTSEI 213
Cdd:PRK06116 178 iavefAGVL--------------NGLGSETHLFvrgdaplrGFDPDI---------RETLVEEMEKKGIRLHTNAVPKAV 234
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498361884 214 lmHGGEQAKHRLAFADGSQLEVDVVVFSTGIRPQ-DTLG-RYGDLAIAERGGIVIDDHCLTSDPDIYAIGEC 283
Cdd:PRK06116 235 --EKNADGSLTLTLEDGETLTVDCLIWAIGREPNtDGLGlENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDV 304
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
90-281 |
3.61e-06 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 50.34 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 90 REVHSNKGTVVGYDKLVLATGSYPWVPPIQGsqhhECFV-YRTIEDlkaIRSAARSGKSGVVIGGGLLGLEAAGALKALG 168
Cdd:PRK07846 117 KTLRTGDGEEITADQVVIAAGSRPVIPPVIA----DSGVrYHTSDT---IMRLPELPESLVIVGGGFIAAEFAHVFSALG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 169 LETHVVEFAPVLMAEQLDgqggQLLRRKIESMGVQ--VHTSKSTSeilmhGGEQA--KHRLAFADGSQLEVDVVVFSTGI 244
Cdd:PRK07846 190 VRVTVVNRSGRLLRHLDD----DISERFTELASKRwdVRLGRNVV-----GVSQDgsGVTLRLDDGSTVEADVLLVATGR 260
|
170 180 190
....*....|....*....|....*....|....*....
gi 498361884 245 RPQ-DTLG-RYGDLAIAERGGIVIDDHCLTSDPDIYAIG 281
Cdd:PRK07846 261 VPNgDLLDaAAAGVDVDEDGRVVVDEYQRTSAEGVFALG 299
|
|
| CopZ-like_Fer2_BFD-like |
cd10141 |
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of Archaeoglobus ... |
424-460 |
6.17e-06 |
|
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of Archaeoglobus fulgidus CopZ, and similar proteins; Archaeoglobus fulgidus CopZ is a fusion of a redox-active domain (containing a mononuclear metal center and an [2Fe-2S] cluster) with a CXXC-containing copper-binding domain. It is a soluble Cu+ chaperone which delivers cytoplasmic Cu+ to the transmembrane metal-binding sites in the Cu+-ATPase CopA; CopA couples the hydrolysis of ATP to the efflux of cytoplasmic Cu+. In addition to CopZ, the BFD-like [2Fe-2S]-binding domain is found in a variety of other proteins including bacterioferritin-associated ferredoxin (BFD), and the large subunit of NADH-dependent nitrite reductase. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.
Pssm-ID: 381074 [Multi-domain] Cd Length: 58 Bit Score: 44.13 E-value: 6.17e-06
10 20 30
....*....|....*....|....*....|....*...
gi 498361884 424 ICSCFDVSKGDIAKAVAEGH-TTLAAIKQHTKAGtGCG 460
Cdd:cd10141 4 VCYCFGVTEEDIIEAVAETGaTTVEEIRATGKAG-RCA 40
|
|
| GlpA-like_Fer2_BFD-like |
cd19946 |
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of anaerobic ... |
424-472 |
9.50e-06 |
|
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of anaerobic glycerol 3-phosphate dehydrogenase subunit A, hydrogen cyanide synthase subunit B, and similar proteins; This subgroup includes the BFD-like [2Fe-2S]-binding domains of subunits of various component dehydrogenase/oxidases, including anaerobic glycerol 3-phosphate dehydrogenase subunit A of GlpABC, hydrogen cyanide synthase subunit HcnB of HcnABC, octopine oxidase subunit A of OoxAB, and nopaline oxidase subunit A of NoxAB. GlpABC catalyzes the conversion of glycerol 3-phosphate to dihydroxyacetone, and participates in the glycerol degradation by glycerol kinase pathway in step 1 of the sub-pathway that synthesizes glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route). HcnABC oxidizes glycine producing hydrogen cyanide and CO2. In Agrobacterium spp, the first enzymic step in the catabolic utilization of octopine and nopaline is the oxidative cleavage into L-arginine and pyruvate or 2-ketoglutarate, respectively; nopaline oxidase (NoxAB) accepts nopaline and octopine while octopine oxidase (OoaB) has high activity with octopine but barely detectable activity with nopaline, both subunits possibly contributing to the substrate specificity. The BFD-like [2Fe-2S]-binding domain is found in a variety of other proteins including bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.
Pssm-ID: 381079 [Multi-domain] Cd Length: 55 Bit Score: 43.68 E-value: 9.50e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 498361884 424 ICSCFDVSKGDIAKAVAEG-HTTLAAIKQHTKAGTG-CGG--CVPLISQVLNA 472
Cdd:cd19946 3 VCRCEEVTEGEIRDAIRRGaARDLDGLKRRTRAGMGrCQGrfCAPRVAELLAR 55
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
103-282 |
9.96e-06 |
|
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.
Pssm-ID: 200098 [Multi-domain] Cd Length: 486 Bit Score: 49.20 E-value: 9.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 103 DKLVLATGSYPWVPPIQGSQH----HECFVYRtiedlKAIRSAARSGksGVVIGggllgleaagalkalglethvVEFAP 178
Cdd:TIGR01423 153 EHILLATGSWPQMLGIPGIEHcissNEAFYLD-----EPPRRVLTVG--GGFIS---------------------VEFAG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 179 VLMAEQLDG-------QGGQLLR-----------RKIESMGVQVHTSKSTSEILMHGgEQAKHrLAFADGSQLEVDVVVF 240
Cdd:TIGR01423 205 IFNAYKPRGgkvtlcyRNNMILRgfdstlrkeltKQLRANGINIMTNENPAKVTLNA-DGSKH-VTFESGKTLDVDVVMM 282
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 498361884 241 STGIRPQD---TLGRYGdLAIAERGGIVIDDHCLTSDPDIYAIGE 282
Cdd:TIGR01423 283 AIGRVPRTqtlQLDKVG-VELTKKGAIQVDEFSRTNVPNIYAIGD 326
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
167-284 |
1.17e-05 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 48.77 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 167 LGLETHVVEFAP-VLMAEqlDGQGGQLLRRKIESMGVQVHTSKSTSEIlmhggEQAKH--RLAFADGS----QLEVDVVV 239
Cdd:PRK06327 205 LGAEVTILEALPaFLAAA--DEQVAKEAAKAFTKQGLDIHLGVKIGEI-----KTGGKgvSVAYTDADgeaqTLEVDKLI 277
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 498361884 240 FSTGIRPQ------DTLGrygdLAIAERGGIVIDDHCLTSDPDIYAIGECA 284
Cdd:PRK06327 278 VSIGRVPNtdglglEAVG----LKLDERGFIPVDDHCRTNVPNVYAIGDVV 324
|
|
| nirA |
PRK09567 |
NirA family protein; |
574-750 |
2.97e-05 |
|
NirA family protein;
Pssm-ID: 236573 [Multi-domain] Cd Length: 593 Bit Score: 47.70 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 574 GEVTPEGLLAVAEVARDYKLYT-KITGAQRIGLFGAQKDDLPAIWRKLLAAGFETGqayAKALRMAK-TCVGSTWCRFGV 651
Cdd:PRK09567 384 GRLTTDQMRGLAKIAARYGDGEiRLTVWQNLLISGVPDADVAAVEAAIEALGLTTE---ASSIRAGLvACTGNAGCKFAA 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 652 QDSVG----LGVFLENRyKGIRTP---HkmkfgVSGCTRECAEAQGKDVGIIA---------TDAGWNLYVGGNGGMKPR 715
Cdd:PRK09567 461 ADTKGhalaIADYCEPR-VALDQPvniH-----LTGCHHSCAQHYIGDIGLIGakvavsegdTVEGYHIVVGGGFGEDAA 534
|
170 180 190
....*....|....*....|....*....|....*
gi 498361884 716 HADLLASDLDRETLIKLIDRFMMFYVTSADKLQRT 750
Cdd:PRK09567 535 IGREVFRDVKAEDAPRLVERLLRAYLAHRQGPDET 569
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
198-284 |
1.69e-04 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 44.34 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 198 ESMGVQVHTSKSTSEILmhgGEQAKHRLAFADG-----SQLEVDVVVFSTGIRPQDTLGRYGDLAIAERGGIVIDDHCLT 272
Cdd:COG0492 188 ANPKIEVLWNTEVTEIE---GDGRVEGVTLKNVktgeeKELEVDGVFVAIGLKPNTELLKGLGLELDEDGYIVVDEDMET 264
|
90
....*....|..
gi 498361884 273 SDPDIYAIGECA 284
Cdd:COG0492 265 SVPGVFAAGDVR 276
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
68-393 |
3.03e-04 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 44.23 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 68 FYDKHGIRlllgeaVKKIDRaNREVHSnkgtvvgyDKLVLATGSYPWVPPIQGSQHHECfVYRTIEDLKAIRSAARSGks 147
Cdd:PRK08010 101 FINNHSLR------VHRPEG-NLEIHG--------EKIFINTGAQTVVPPIPGITTTPG-VYDSTGLLNLKELPGHLG-- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 148 gvVIGGGLLGLEAAGALKALGLETHVVEFAPVLMAEQlDGQGGQLLRRKIESMGVQVHTSKSTSEILMHGGEQAKHrlaf 227
Cdd:PRK08010 163 --ILGGGYIGVEFASMFANFGSKVTILEAASLFLPRE-DRDIADNIATILRDQGVDIILNAHVERISHHENQVQVH---- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 228 ADGSQLEVDVVVFSTGIRPQdTLG---RYGDLAIAERGGIVIDDHCLTSDPDIYAIGEcaawqgrffglVAPGYKMAQIT 304
Cdd:PRK08010 236 SEHAQLAVDALLIASGRQPA-TASlhpENAGIAVNERGAIVVDKYLHTTADNIWAMGD-----------VTGGLQFTYIS 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 305 VDHL------LGGDSRFEGAD---------MSAKLKLLGVSvgsigDAHGRTPGSHSYV------------FQDDQAGVY 357
Cdd:PRK08010 304 LDDYrivrdeLLGEGKRSTDDrknvpysvfMTPPLSRVGMT-----EEQARESGADIQVvtlpvaaiprarVMNDTRGVL 378
|
330 340 350
....*....|....*....|....*....|....*...
gi 498361884 358 KKIvVSEDNSRLLGA-VLVGDVEDYGNLLQMMLNA-LP 393
Cdd:PRK08010 379 KAI-VDNKTQRILGAsLLCVDSHEMINIVKMVMDAgLP 415
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
5-335 |
5.23e-04 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 43.23 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 5 RLVVVGnGMVGHRFIEELIERADPgRYEITVFGAEPRPAYDRVHLSsYFSHHTSEDLSLVKP----GFYDKHGIRLLLGE 80
Cdd:PRK13512 3 KIIVVG-AVAGGATCASQIRRLDK-ESDIIIFEKDRDMSFANCALP-YYIGEVVEDRKYALAytpeKFYDRKQITVKTYH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 81 AVKKIDRANREV-----HSNKGTVVGYDKLVLATGSYPWVPPiqgSQHHECFVYRTIEDLKAIRS--AARSGKSGVVIGG 153
Cdd:PRK13512 80 EVIAINDERQTVtvlnrKTNEQFEESYDKLILSPGASANSLG---FESDITFTLRNLEDTDAIDQfiKANQVDKALVVGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 154 GLLGLEAAGALKALGLETHVVEFAPVLMaEQLDGQGGQLLRRKIESMGVQVHTSKSTSEIlmhggeqAKHRLAFADGSQL 233
Cdd:PRK13512 157 GYISLEVLENLYERGLHPTLIHRSDKIN-KLMDADMNQPILDELDKREIPYRLNEEIDAI-------NGNEVTFKSGKVE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 234 EVDVVVFSTGIRPQDTLGRYGDLAIAERGGIVIDDHCLTSDPDIYAIGECAAWQGRFFGLVAP------GYKMAQITVDH 307
Cdd:PRK13512 229 HYDMIIEGVGTHPNSKFIESSNIKLDDKGFIPVNDKFETNVPNIYAIGDIITSHYRHVDLPASvplawgAHRAASIVAEQ 308
|
330 340
....*....|....*....|....*....
gi 498361884 308 LLGGDS-RFEGADMSAKLKLLGVSVGSIG 335
Cdd:PRK13512 309 IAGNDTiEFKGFLGNNIVKFFDYTFASVG 337
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
67-290 |
2.08e-03 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 41.68 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 67 GFYDKHGIRLLLGEAvKKIDRANREVHSNKGTV--VGYDKLVLATGSYPWVPPIQGSQHHECFVYRTIEDLKAI-RSAAR 143
Cdd:PRK05249 102 GQYERNRVDLIQGRA-RFVDPHTVEVECPDGEVetLTADKIVIATGSRPYRPPDVDFDHPRIYDSDSILSLDHLpRSLII 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 144 SGkSGVV------IGGgllgleaagalkALGLETHVVEFAPVLMaEQLDGQGGQLLRRKIESMGVqvhtskstseiLMHG 217
Cdd:PRK05249 181 YG-AGVIgceyasIFA------------ALGVKVTLINTRDRLL-SFLDDEISDALSYHLRDSGV-----------TIRH 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 218 GEQAKH--------RLAFADGSQLEVDVVVFStgirpqdtLGRYG---DLAIA-------ERGGIVIDDHCLTSDPDIYA 279
Cdd:PRK05249 236 NEEVEKveggddgvIVHLKSGKKIKADCLLYA--------NGRTGntdGLNLEnagleadSRGQLKVNENYQTAVPHIYA 307
|
250 260
....*....|....*....|
gi 498361884 280 IGECAAW---------QGRF 290
Cdd:PRK05249 308 VGDVIGFpslasasmdQGRI 327
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
195-282 |
5.93e-03 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 40.18 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361884 195 RKIESMGVQVHTSKSTSEILMHGGEQakhRLAFADGSQLEVDVVVFSTGIRPQDTLGRYGDLAIA--ERGGIVIDDHCLT 272
Cdd:PLN02507 252 RNLEGRGINLHPRTNLTQLTKTEGGI---KVITDHGEEFVADVVLFATGRAPNTKRLNLEAVGVEldKAGAVKVDEYSRT 328
|
90
....*....|
gi 498361884 273 SDPDIYAIGE 282
Cdd:PLN02507 329 NIPSIWAIGD 338
|
|
|