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Conserved domains on  [gi|498361884|ref|WP_010676040|]
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MULTISPECIES: nitrite reductase large subunit NirB [Aeromonas]

Protein Classification

nitrite reductase large subunit( domain architecture ID 11487548)

nitrite reductase NAD(P)H large subunit similar to NirB, part of the NirBD complex that catalyzes the reduction of nitrite to ammonia

Graphical summary

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List of domain hits

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
 
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
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
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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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