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Conserved domains on  [gi|1079631853|emb|SCW41461|]
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Flavorubredoxin [Ruminococcaceae bacterium YRB3002]

Protein Classification

FprA family A-type flavoprotein; flavin reductase family protein( domain architecture ID 11418014)

FprA family A-type flavoprotein contains an MBL fold metallo-hydrolase domain having a binuclear iron center, and a flavodoxin-like domain containing one FMN moiety; similar to Desulfovibrio gigas rubredoxin-oxygen oxidoreductase, which catalyzes the four-electron reduction of one oxygen molecule to two water molecules; flavin reductase family protein containing an N-terminal NAD(P) binding domain of flavin oxidoreductase-like proteins and a C-terminal 2Fe-2S iron-sulfur cluster binding domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NorV COG0426
Flavorubredoxin [Energy production and conversion];
3-384 3.37e-151

Flavorubredoxin [Energy production and conversion];


:

Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 440.42  E-value: 3.37e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853   3 ISNDITYAGVNDHKIDLFEGQYVVPNGMAYNSYVIRGGKIAVMDTVDKNFTHEWLDNLQHILGDSKPDYLVVQHMEPDHS 82
Cdd:COG0426     5 IAHGVYWVGVLDWDRRLFEGEYPTPRGTTYNSYLIVDEKTALIDTVGESFFEEFLENLSKVIDPKKIDYIIVNHQEPDHS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853  83 ANIENFMKNYPEAVIVSSAKAFTMMKNFFGTEfEDRRIVVGEGDTLELGTHTLTFVAAPMVHWPEVIMTYDSTDKVLFSA 162
Cdd:COG0426    85 GSLPELLELAPNAKIVCSKKAARFLPHFYGIP-DFRFIVVKEGDTLDLGGHTLQFIPAPMLHWPDTMFTYDPEDKILFSG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 163 DGFGKFGALD------VEEDWACEARRYYIGIVGKYGAQVQAVLKKAANLEIKTICPLHGPVLTGDLSPYLKLYDTWSSY 236
Cdd:COG0426   164 DAFGSHGASDelfddeVDEHLEEEARRYYANIMMPFSKQVLKALKKVRGLDIDMIAPSHGPIWRGNPKEILDWYRKWSSY 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 237 GVEtEGIAIFYTSVYGHTKAAVELLADKLKNNGCpKVVVNDLAREDMAECVEDAFRYGRIVLATTTYNADIFPFMKEFIN 316
Cdd:COG0426   244 QPE-KKVVIVYASMYGNTEKMAEAIAEGLTEEGV-KVKLYDLEKTDPSEIITEIFDAKGIVIGSPTYNGGAFPPIADLLG 321

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1079631853 317 HLTERGFQNKTVAMIENGSWAPQAIKTMKAMLEKSKnITYTETNVKIMSALNDDSKAQVDALAKELCQ 384
Cdd:COG0426   322 YLKGLAPKNKLAGAFGSYGWSGEAVKLLEEKLEDAG-FEVVFEPLRVKFKPTEEDLKKCEELGTDLAQ 388
Flavin_Reduct pfam01613
Flavin reductase like domain; This is a flavin reductase family consisting of enzymes known to ...
 402-553 2.26e-27

Flavin reductase like domain; This is a flavin reductase family consisting of enzymes known to be flavin reductases as well as various oxidoreductase and monooxygenase components. VlmR is a flavin reductase that functions in a two-component enzyme system to provide isobutylamine N-hydroxylase with reduced flavin and may be involved in the synthesis of valanimycin. SnaC is a flavin reductase that provides reduced flavin for the oxidation of pristinamycin IIB to pristinamycin IIA as catalyzed by SnaA, SnaB heterodimer. This flavin reductase region characterized by enzymes of the family is present in the C-terminus of potential FMN proteins from Synechocystis sp. suggesting it is a flavin reductase domain.


:

Pssm-ID: 460266  Cd Length: 149  Bit Score: 107.75  E-value: 2.26e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 402 LFNIGYGLYVVTSNDGRKDNGLIVNTVTQVTNTPNRIAVTINKQNYSHHVIQQTGIMNVNCLSvEAPFKVFENFGFQSGR 481
Cdd:pfam01613   1 MRRFPTGVAVVTTDDGGEPNGMTVSSFTSVSLDPPLVLVSINRSSSTHDAIEASGEFVVNVLA-EDQEELARRFAGRSGR 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1079631853 482 nvDKFAECEnILRSDNGLVFLPKYInSFMSLKVEDYVDLDTHGMFICSVTEARVLSDKETMTYTYYQKNVKP 553
Cdd:pfam01613  80 --DKFAGIT-WVEGKVGAPLLKGAL-AALECRVVDTVDVGDHTLFIGEVVDVRVDEDADGEPLLYYRRRYRS 147
rubredoxin_like cd00350
Rubredoxin_like; nonheme iron binding domain containing a [Fe(SCys)4] center. The family ...
 563-596 6.93e-11

Rubredoxin_like; nonheme iron binding domain containing a [Fe(SCys)4] center. The family includes rubredoxins, a small electron transfer protein, and a slightly smaller modular rubredoxin domain present in rubrerythrin and nigerythrin and detected either N- or C-terminal to such proteins as flavin reductase, NAD(P)H-nitrite reductase, and ferredoxin-thioredoxin reductase. In rubredoxin, the iron atom is coordinated by four cysteine residues (Fe(S-Cys)4), but iron can also be replaced by cobalt, nickel or zinc and believed to be involved in electron transfer. Rubrerythrins and nigerythrins are small homodimeric proteins, generally consisting of 2 domains: a rubredoxin domain C-terminal to a non-sulfur, oxo-bridged diiron site in the N-terminal rubrerythrin domain. Rubrerythrins and nigerythrins have putative peroxide activity.


:

Pssm-ID: 238210 [Multi-domain]  Cd Length: 33  Bit Score: 57.18  E-value: 6.93e-11
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1079631853 563 YVCKVCGYVYEGDELPEdiVCPLCKHGAADFEPI 596
Cdd:cd00350     2 YVCPVCGYIYDGEEAPW--VCPVCGAPKDKFEKL 33
 
Name Accession Description Interval E-value
NorV COG0426
Flavorubredoxin [Energy production and conversion];
3-384 3.37e-151

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 440.42  E-value: 3.37e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853   3 ISNDITYAGVNDHKIDLFEGQYVVPNGMAYNSYVIRGGKIAVMDTVDKNFTHEWLDNLQHILGDSKPDYLVVQHMEPDHS 82
Cdd:COG0426     5 IAHGVYWVGVLDWDRRLFEGEYPTPRGTTYNSYLIVDEKTALIDTVGESFFEEFLENLSKVIDPKKIDYIIVNHQEPDHS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853  83 ANIENFMKNYPEAVIVSSAKAFTMMKNFFGTEfEDRRIVVGEGDTLELGTHTLTFVAAPMVHWPEVIMTYDSTDKVLFSA 162
Cdd:COG0426    85 GSLPELLELAPNAKIVCSKKAARFLPHFYGIP-DFRFIVVKEGDTLDLGGHTLQFIPAPMLHWPDTMFTYDPEDKILFSG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 163 DGFGKFGALD------VEEDWACEARRYYIGIVGKYGAQVQAVLKKAANLEIKTICPLHGPVLTGDLSPYLKLYDTWSSY 236
Cdd:COG0426   164 DAFGSHGASDelfddeVDEHLEEEARRYYANIMMPFSKQVLKALKKVRGLDIDMIAPSHGPIWRGNPKEILDWYRKWSSY 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 237 GVEtEGIAIFYTSVYGHTKAAVELLADKLKNNGCpKVVVNDLAREDMAECVEDAFRYGRIVLATTTYNADIFPFMKEFIN 316
Cdd:COG0426   244 QPE-KKVVIVYASMYGNTEKMAEAIAEGLTEEGV-KVKLYDLEKTDPSEIITEIFDAKGIVIGSPTYNGGAFPPIADLLG 321

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1079631853 317 HLTERGFQNKTVAMIENGSWAPQAIKTMKAMLEKSKnITYTETNVKIMSALNDDSKAQVDALAKELCQ 384
Cdd:COG0426   322 YLKGLAPKNKLAGAFGSYGWSGEAVKLLEEKLEDAG-FEVVFEPLRVKFKPTEEDLKKCEELGTDLAQ 388
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 3-234 1.14e-108

catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Some members of this subgroup are single domain.


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 325.98  E-value: 1.14e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853   3 ISNDITYAGVNDHKIDLFEGQYVVPNGMAYNSYVIRGGKIAVMDTVDKNFTHEWLDNLQHILGDSKPDYLVVQHMEPDHS 82
Cdd:cd07709     3 IADDIYWVGVNDWDLRLFEGEYPTPRGTSYNSYLIKDEKTALIDTVKEPFFDEFLENLEEVIDPRKIDYIVVNHQEPDHS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853  83 ANIENFMKNYPEAVIVSSAKAFTMMKNFFGTEfEDRRIVVGEGDTLELGTHTLTFVAAPMVHWPEVIMTYDSTDKVLFSA 162
Cdd:cd07709    83 GSLPELLELAPNAKIVCSKKAARFLKHFYPGI-DERFVVVKDGDTLDLGKHTLKFIPAPMLHWPDTMVTYDPEDKILFSG 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1079631853 163 DGFGKFGAL-----DVEEDWACEARRYYIGIVGKYGAQVQAVLKKAANLEIKTICPLHGPVLTGDLSPYLKLYDTWS 234
Cdd:cd07709   162 DAFGAHGASgelfdDEVEDYLEEARRYYANIMGPFSKQVRKALEKLEALDIKMIAPSHGPIWRKDPGEIIDLYRDWS 238
PRK11921 PRK11921
anaerobic nitric oxide reductase flavorubredoxin;
3-384 5.26e-54

anaerobic nitric oxide reductase flavorubredoxin;


Pssm-ID: 237023 [Multi-domain]  Cd Length: 394  Bit Score: 188.75  E-value: 5.26e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853   3 ISNDITYAGVNDHKIDLFEGQ-YVVPNGMAYNSYVIRGGKIAVMDTVDKNFTHEWLDNLQHILGDSKPDYLVVQHMEPDH 81
Cdd:PRK11921    3 INDNVTWVGKIDWELRKFHGEeYSTHRGSSYNSYLIKDEKTVLIDTVWQPFAKEFVENLKKEIDLDKIDYIVANHGEIDH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853  82 SANIENFMKNYPEAVIVSSAKAFTMMKNFFGTEFEDRriVVGEGDTLELGTHTLTFVAAPMVHWPEVIMTYDSTDKVLFS 161
Cdd:PRK11921   83 SGALPELMKEIPDTPIYCTKNGAKSLKGHYHQDWNFV--VVKTGDRLEIGSNELIFIEAPMLHWPDSMFTYLTGDNILFS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 162 ADGFGKFGA--------LDVEEDWAcEARRYYIGIVGKYGAQVQAVLK--KAANLEIKTICPLHGPVLTGDLSPYLKLYD 231
Cdd:PRK11921  161 NDAFGQHYAselmyndlVDQGELYQ-EAIKYYANILTPFSPLVIKKIEeiLSLNLPVDMICPSHGVIWRDNPLQIVEKYL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 232 TWSSyGVETEGIAIFYTSVYGHTKAAVELLADKLKNNGcPKVVVN--DLAREDMAECVEDAFRYGRIVLATTTYNADIFP 309
Cdd:PRK11921  240 EWAA-NYQENQVTILYDTMWNSTRRMAEAIAEGIKKAN-KDVTVKlyNSAKSDKNDIITEVFKSKAILVGSSTINRGILS 317

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1079631853 310 FMKEFINHLTERGFQNKTVAMIENGSWAPQAIKTMKAMLEKSKnITYTETNVKIMSALNDDSKAQVDALAKELCQ 384
Cdd:PRK11921  318 STAAILEEIKGLGFKNKKAAAFGSYGWSGESVKIITERLKKAG-FEIVNDGIRELWNPDDEALDRCRSFGENFAE 391
Flavin_Reduct pfam01613
Flavin reductase like domain; This is a flavin reductase family consisting of enzymes known to ...
 402-553 2.26e-27

Flavin reductase like domain; This is a flavin reductase family consisting of enzymes known to be flavin reductases as well as various oxidoreductase and monooxygenase components. VlmR is a flavin reductase that functions in a two-component enzyme system to provide isobutylamine N-hydroxylase with reduced flavin and may be involved in the synthesis of valanimycin. SnaC is a flavin reductase that provides reduced flavin for the oxidation of pristinamycin IIB to pristinamycin IIA as catalyzed by SnaA, SnaB heterodimer. This flavin reductase region characterized by enzymes of the family is present in the C-terminus of potential FMN proteins from Synechocystis sp. suggesting it is a flavin reductase domain.


Pssm-ID: 460266  Cd Length: 149  Bit Score: 107.75  E-value: 2.26e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 402 LFNIGYGLYVVTSNDGRKDNGLIVNTVTQVTNTPNRIAVTINKQNYSHHVIQQTGIMNVNCLSvEAPFKVFENFGFQSGR 481
Cdd:pfam01613   1 MRRFPTGVAVVTTDDGGEPNGMTVSSFTSVSLDPPLVLVSINRSSSTHDAIEASGEFVVNVLA-EDQEELARRFAGRSGR 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1079631853 482 nvDKFAECEnILRSDNGLVFLPKYInSFMSLKVEDYVDLDTHGMFICSVTEARVLSDKETMTYTYYQKNVKP 553
Cdd:pfam01613  80 --DKFAGIT-WVEGKVGAPLLKGAL-AALECRVVDTVDVGDHTLFIGEVVDVRVDEDADGEPLLYYRRRYRS 147
RutF COG1853
FMN reductase RutF, DIM6/NTAB family [Energy production and conversion]; FMN reductase RutF, ...
 401-548 4.37e-21

FMN reductase RutF, DIM6/NTAB family [Energy production and conversion]; FMN reductase RutF, DIM6/NTAB family is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 441458  Cd Length: 160  Bit Score: 90.27  E-value: 4.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 401 ALFNIGYGLYVVTSND-GRKDNGLIVNTVTQVTNTPNRIAVTINKQNYSHHVIQQTGIMNVNCLSVEAPfKVFENFGFQS 479
Cdd:COG1853     8 ALGRLAPGVAVVTTRDaDGRPNGMTASSFTSVSLDPPLVLVSVAKSSDTLENIRETGEFVVNVLSEDQA-ELANRFAGRS 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1079631853 480 GRNVDKFAECEniLRSDNGLVFLPKYINSFMSL--KVEDYVDLDTHGMFICSVTEARVLSDKETMTYTYYQ 548
Cdd:COG1853    87 GRGVDKFAGAG--LTTASGEVGAPLLAEAPAWLecRVVDVIELGDHTLFIGEVVAVHVDEDVDGRPLLYLG 155
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 33-215 1.25e-17

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 81.06  E-value: 1.25e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853   33 NSYVIRG-GKIAVMDTVDkNFTHEWLDNLQHiLGDSKPDYLVVQHMEPDHSANIENFMKnYPEAVIVSSAKAFTMMKNF- 110
Cdd:smart00849   1 NSYLVRDdGGAILIDTGP-GEAEDLLAELKK-LGPKKIDAIILTHGHPDHIGGLPELLE-APGAPVYAPEGTAELLKDLl 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853  111 -------FGTEFEDRRIVVGEGDTLELGTHTLTFVAAPMvHWPEVIMTYDSTDKVLFSADGFGkfgaldveedwACEARR 183
Cdd:smart00849  78 allgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTPG-HTPGSIVLYLPEGKILFTGDLLF-----------AGGDGR 145

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1079631853  184 YYIGIVGKYGAQVQAVLKKAANLEIKTICPLH 215
Cdd:smart00849 146 TLVDGGDAAASDALESLLKLLKLLPKLVVPGH 177
Flavin_Reduct smart00903
Flavin reductase like domain; This entry represents the FMN-binding domain found in NAD(P) ...
 405-544 6.52e-16

Flavin reductase like domain; This entry represents the FMN-binding domain found in NAD(P)H-flavin oxidoreductases (flavin reductases), a class of enzymes capable of producing reduced flavin for bacterial bioluminescence and other biological processes. This domain is also found in various other oxidoreductase and monooxygenase enzymes... This domain consists of a beta-barrel with Greek key topology, and is related to the ferredoxin reductase-like FAD-binding domain. The flavin reductases have a different dimerisation mode than that found in the PNP oxidase-like family, which also carries an FMN-binding domain with a similar topology.


Pssm-ID: 214900  Cd Length: 147  Bit Score: 74.89  E-value: 6.52e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853  405 IGYGLYVVTSNDGRKD-NGLIVNTVTQVTNTPNRIAVTINKQNYSHHVIQQTGIMNVNCLSVEAPfKVFENFGFQSGRNV 483
Cdd:smart00903   4 FPTGVAVVTTRDGDGGrVGLTASSFVSVSLDPPLVLVCVAKSSSTHPLIRESGRFVVNVLAEDQA-DLARRFAGKSGADR 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1079631853  484 DKFAECENILRSDNGLVFLPkyiNSFMSL--KVEDYVDLDTHGMFICSVTEARVLSDKETMTY 544
Cdd:smart00903  83 FEGVAWGLTEAGVTGAPILA---GALAWLecRVVQVIEVGDHTIFVGEVVAVHVRDDGEPLVY 142
ODP pfam19583
ODP family beta lactamase; The ODP (Oxygen-binding Di-iron Protein) domain is a distinct ...
 33-216 4.03e-14

ODP family beta lactamase; The ODP (Oxygen-binding Di-iron Protein) domain is a distinct member of the metallo-beta-lactamase superfamily recruited to various bacterial and archaeal signal transduction pathways, including chemotaxis, to function as oxygen and iron sensors (1). ODP was shown to act as a sensor for chemotactic responses to both iron and oxygen in the human pathogen Treponema denticola (Td). The ODP di-iron site binds oxygen at high affinity to reversibly form an unusually stable peroxo adduct.


Pssm-ID: 437415  Cd Length: 194  Bit Score: 70.97  E-value: 4.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853  33 NSYVIR-GGKIAVMD--------TVdknfthewLDNLQHILGDSKPDYLVVQHMEPDHSANIENFMKNYPEAVIVSSAKA 103
Cdd:pfam19583   4 NQYLIVdGGEAVLIDpggrltfpAV--------LAKVSKYIDPEKIKYIFASHQDPDICSSLPLWLDVIPDAKIVISELW 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 104 ------FTMMK-NFFGTEFEDRRIVVGEGDTLElgthtltFVAAPMVHWPEVIMTYDSTDKVLFSADgfgKFGALDVEED 176
Cdd:pfam19583  76 erflphYGLKKsRFIPIPDEGGRITLGSGRRLE-------FIPAHFLHSPGNFVTYDPVSKILFSGD---IGAALFPGKD 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1079631853 177 WACEA--------------RRYyigIVGKygaqvqAVLKKAAN----LEIKTICPLHG 216
Cdd:pfam19583 146 WSLFVedfdahipymegfhRRY---MPSN------KALRLWVEmvrkLDIEMIAPQHG 194
rubredoxin_like cd00350
Rubredoxin_like; nonheme iron binding domain containing a [Fe(SCys)4] center. The family ...
 563-596 6.93e-11

Rubredoxin_like; nonheme iron binding domain containing a [Fe(SCys)4] center. The family includes rubredoxins, a small electron transfer protein, and a slightly smaller modular rubredoxin domain present in rubrerythrin and nigerythrin and detected either N- or C-terminal to such proteins as flavin reductase, NAD(P)H-nitrite reductase, and ferredoxin-thioredoxin reductase. In rubredoxin, the iron atom is coordinated by four cysteine residues (Fe(S-Cys)4), but iron can also be replaced by cobalt, nickel or zinc and believed to be involved in electron transfer. Rubrerythrins and nigerythrins are small homodimeric proteins, generally consisting of 2 domains: a rubredoxin domain C-terminal to a non-sulfur, oxo-bridged diiron site in the N-terminal rubrerythrin domain. Rubrerythrins and nigerythrins have putative peroxide activity.


Pssm-ID: 238210 [Multi-domain]  Cd Length: 33  Bit Score: 57.18  E-value: 6.93e-11
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1079631853 563 YVCKVCGYVYEGDELPEdiVCPLCKHGAADFEPI 596
Cdd:cd00350     2 YVCPVCGYIYDGEEAPW--VCPVCGAPKDKFEKL 33
NorV COG1773
Flavorubredoxin [Inorganic ion transport and metabolism];
563-597 5.59e-10

Flavorubredoxin [Inorganic ion transport and metabolism];


Pssm-ID: 441379 [Multi-domain]  Cd Length: 53  Bit Score: 55.18  E-value: 5.59e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1079631853 563 YVCKVCGYVY---EGD------------ELPEDIVCPLCKHGAADFEPIE 597
Cdd:COG1773     4 YQCKVCGYVYdpaEGDpengippgtpfeDLPDDWVCPVCGAGKEDFEPVE 53
Rubredoxin pfam00301
Rubredoxin;
563-593 1.02e-06

Rubredoxin;


Pssm-ID: 459752 [Multi-domain]  Cd Length: 46  Bit Score: 45.70  E-value: 1.02e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1079631853 563 YVCKVCGYVY---EGD------------ELPEDIVCPLCKHGAADF 593
Cdd:pfam00301   1 YECKVCGYVYdpaKGDpdngippgtpfeDLPDDWVCPDCGAGKDQF 46
 
Name Accession Description Interval E-value
NorV COG0426
Flavorubredoxin [Energy production and conversion];
3-384 3.37e-151

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 440.42  E-value: 3.37e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853   3 ISNDITYAGVNDHKIDLFEGQYVVPNGMAYNSYVIRGGKIAVMDTVDKNFTHEWLDNLQHILGDSKPDYLVVQHMEPDHS 82
Cdd:COG0426     5 IAHGVYWVGVLDWDRRLFEGEYPTPRGTTYNSYLIVDEKTALIDTVGESFFEEFLENLSKVIDPKKIDYIIVNHQEPDHS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853  83 ANIENFMKNYPEAVIVSSAKAFTMMKNFFGTEfEDRRIVVGEGDTLELGTHTLTFVAAPMVHWPEVIMTYDSTDKVLFSA 162
Cdd:COG0426    85 GSLPELLELAPNAKIVCSKKAARFLPHFYGIP-DFRFIVVKEGDTLDLGGHTLQFIPAPMLHWPDTMFTYDPEDKILFSG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 163 DGFGKFGALD------VEEDWACEARRYYIGIVGKYGAQVQAVLKKAANLEIKTICPLHGPVLTGDLSPYLKLYDTWSSY 236
Cdd:COG0426   164 DAFGSHGASDelfddeVDEHLEEEARRYYANIMMPFSKQVLKALKKVRGLDIDMIAPSHGPIWRGNPKEILDWYRKWSSY 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 237 GVEtEGIAIFYTSVYGHTKAAVELLADKLKNNGCpKVVVNDLAREDMAECVEDAFRYGRIVLATTTYNADIFPFMKEFIN 316
Cdd:COG0426   244 QPE-KKVVIVYASMYGNTEKMAEAIAEGLTEEGV-KVKLYDLEKTDPSEIITEIFDAKGIVIGSPTYNGGAFPPIADLLG 321

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1079631853 317 HLTERGFQNKTVAMIENGSWAPQAIKTMKAMLEKSKnITYTETNVKIMSALNDDSKAQVDALAKELCQ 384
Cdd:COG0426   322 YLKGLAPKNKLAGAFGSYGWSGEAVKLLEEKLEDAG-FEVVFEPLRVKFKPTEEDLKKCEELGTDLAQ 388
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 3-234 1.14e-108

catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Some members of this subgroup are single domain.


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 325.98  E-value: 1.14e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853   3 ISNDITYAGVNDHKIDLFEGQYVVPNGMAYNSYVIRGGKIAVMDTVDKNFTHEWLDNLQHILGDSKPDYLVVQHMEPDHS 82
Cdd:cd07709     3 IADDIYWVGVNDWDLRLFEGEYPTPRGTSYNSYLIKDEKTALIDTVKEPFFDEFLENLEEVIDPRKIDYIVVNHQEPDHS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853  83 ANIENFMKNYPEAVIVSSAKAFTMMKNFFGTEfEDRRIVVGEGDTLELGTHTLTFVAAPMVHWPEVIMTYDSTDKVLFSA 162
Cdd:cd07709    83 GSLPELLELAPNAKIVCSKKAARFLKHFYPGI-DERFVVVKDGDTLDLGKHTLKFIPAPMLHWPDTMVTYDPEDKILFSG 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1079631853 163 DGFGKFGAL-----DVEEDWACEARRYYIGIVGKYGAQVQAVLKKAANLEIKTICPLHGPVLTGDLSPYLKLYDTWS 234
Cdd:cd07709   162 DAFGAHGASgelfdDEVEDYLEEARRYYANIMGPFSKQVRKALEKLEALDIKMIAPSHGPIWRKDPGEIIDLYRDWS 238
PRK11921 PRK11921
anaerobic nitric oxide reductase flavorubredoxin;
3-384 5.26e-54

anaerobic nitric oxide reductase flavorubredoxin;


Pssm-ID: 237023 [Multi-domain]  Cd Length: 394  Bit Score: 188.75  E-value: 5.26e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853   3 ISNDITYAGVNDHKIDLFEGQ-YVVPNGMAYNSYVIRGGKIAVMDTVDKNFTHEWLDNLQHILGDSKPDYLVVQHMEPDH 81
Cdd:PRK11921    3 INDNVTWVGKIDWELRKFHGEeYSTHRGSSYNSYLIKDEKTVLIDTVWQPFAKEFVENLKKEIDLDKIDYIVANHGEIDH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853  82 SANIENFMKNYPEAVIVSSAKAFTMMKNFFGTEFEDRriVVGEGDTLELGTHTLTFVAAPMVHWPEVIMTYDSTDKVLFS 161
Cdd:PRK11921   83 SGALPELMKEIPDTPIYCTKNGAKSLKGHYHQDWNFV--VVKTGDRLEIGSNELIFIEAPMLHWPDSMFTYLTGDNILFS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 162 ADGFGKFGA--------LDVEEDWAcEARRYYIGIVGKYGAQVQAVLK--KAANLEIKTICPLHGPVLTGDLSPYLKLYD 231
Cdd:PRK11921  161 NDAFGQHYAselmyndlVDQGELYQ-EAIKYYANILTPFSPLVIKKIEeiLSLNLPVDMICPSHGVIWRDNPLQIVEKYL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 232 TWSSyGVETEGIAIFYTSVYGHTKAAVELLADKLKNNGcPKVVVN--DLAREDMAECVEDAFRYGRIVLATTTYNADIFP 309
Cdd:PRK11921  240 EWAA-NYQENQVTILYDTMWNSTRRMAEAIAEGIKKAN-KDVTVKlyNSAKSDKNDIITEVFKSKAILVGSSTINRGILS 317

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1079631853 310 FMKEFINHLTERGFQNKTVAMIENGSWAPQAIKTMKAMLEKSKnITYTETNVKIMSALNDDSKAQVDALAKELCQ 384
Cdd:PRK11921  318 STAAILEEIKGLGFKNKKAAAFGSYGWSGESVKIITERLKKAG-FEIVNDGIRELWNPDDEALDRCRSFGENFAE 391
PRK05452 PRK05452
anaerobic nitric oxide reductase flavorubredoxin; Provisional
 3-386 1.16e-39

anaerobic nitric oxide reductase flavorubredoxin; Provisional


Pssm-ID: 235475 [Multi-domain]  Cd Length: 479  Bit Score: 151.45  E-value: 1.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853   3 ISNDITYAGVNDHKIDLFEG-QYVVPNGMAYNSYVIRGGKIAVMDTVDKNFTHEWLDNLQHILGDSKPDYLVVQHMEPDH 81
Cdd:PRK05452    5 VKNNIHWVGQRDWEVRDFHGtEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRNEIDLADIDYIVINHAEEDH 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853  82 SANIENFMKNYPEAVIVSSAKAFTMMK--------NFFgtefedrriVVGEGDTLELGT-HTLTFVAAPMVHWPEVIMTY 152
Cdd:PRK05452   85 AGALTELMAQIPDTPIYCTANAIDSINghhhhpewNFN---------VVKTGDTLDIGNgKQLIFVETPMLHWPDSMMTY 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 153 DSTDKVLFSADGFGK-------FGALDVEEDWACEARRYYIGIVGKYGAQVQAVLKK--AANLEIKTICPLHGPVLTGDL 223
Cdd:PRK05452  156 LTGDAVLFSNDAFGQhycdehlFNDEVDQTELFEQCQRYYANILTPFSRLVTPKITEilGFNLPVDMIATSHGVVWRDNP 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 224 SPYLKLYDTWS-SYgvETEGIAIFYTSVYGHTKAAVELLADKLkNNGCPKVVVN--DLAREDMAECVEDAFRYGRIVLAT 300
Cdd:PRK05452  236 TQIVELYLKWAaDY--QEDRITIFYDTMSNNTRMMADAIAQGI-AEVDPRVAVKifNVARSDKNEILTNVFRSKGVLVGS 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 301 TTYNADIFPFMKEFINHLTERGFQNKTVAMIENGSWAPQAIKTMKAMLeksknityTETNVKIMSALNDDSKAQVDALak 380
Cdd:PRK05452  313 STMNNVMMPKIAGLLEEITGLRFRNKRASAFGSHGWSGGAVDRLSTRL--------QDAGFEMSLSLKAKWRPDQDAL-- 382


                  ....*.
gi 1079631853 381 ELCQDY 386
Cdd:PRK05452  383 ELCREH 388
Flavin_Reduct pfam01613
Flavin reductase like domain; This is a flavin reductase family consisting of enzymes known to ...
 402-553 2.26e-27

Flavin reductase like domain; This is a flavin reductase family consisting of enzymes known to be flavin reductases as well as various oxidoreductase and monooxygenase components. VlmR is a flavin reductase that functions in a two-component enzyme system to provide isobutylamine N-hydroxylase with reduced flavin and may be involved in the synthesis of valanimycin. SnaC is a flavin reductase that provides reduced flavin for the oxidation of pristinamycin IIB to pristinamycin IIA as catalyzed by SnaA, SnaB heterodimer. This flavin reductase region characterized by enzymes of the family is present in the C-terminus of potential FMN proteins from Synechocystis sp. suggesting it is a flavin reductase domain.


Pssm-ID: 460266  Cd Length: 149  Bit Score: 107.75  E-value: 2.26e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 402 LFNIGYGLYVVTSNDGRKDNGLIVNTVTQVTNTPNRIAVTINKQNYSHHVIQQTGIMNVNCLSvEAPFKVFENFGFQSGR 481
Cdd:pfam01613   1 MRRFPTGVAVVTTDDGGEPNGMTVSSFTSVSLDPPLVLVSINRSSSTHDAIEASGEFVVNVLA-EDQEELARRFAGRSGR 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1079631853 482 nvDKFAECEnILRSDNGLVFLPKYInSFMSLKVEDYVDLDTHGMFICSVTEARVLSDKETMTYTYYQKNVKP 553
Cdd:pfam01613  80 --DKFAGIT-WVEGKVGAPLLKGAL-AALECRVVDTVDVGDHTLFIGEVVDVRVDEDADGEPLLYYRRRYRS 147
RutF COG1853
FMN reductase RutF, DIM6/NTAB family [Energy production and conversion]; FMN reductase RutF, ...
 401-548 4.37e-21

FMN reductase RutF, DIM6/NTAB family [Energy production and conversion]; FMN reductase RutF, DIM6/NTAB family is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 441458  Cd Length: 160  Bit Score: 90.27  E-value: 4.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 401 ALFNIGYGLYVVTSND-GRKDNGLIVNTVTQVTNTPNRIAVTINKQNYSHHVIQQTGIMNVNCLSVEAPfKVFENFGFQS 479
Cdd:COG1853     8 ALGRLAPGVAVVTTRDaDGRPNGMTASSFTSVSLDPPLVLVSVAKSSDTLENIRETGEFVVNVLSEDQA-ELANRFAGRS 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1079631853 480 GRNVDKFAECEniLRSDNGLVFLPKYINSFMSL--KVEDYVDLDTHGMFICSVTEARVLSDKETMTYTYYQ 548
Cdd:COG1853    87 GRGVDKFAGAG--LTTASGEVGAPLLAEAPAWLecRVVDVIELGDHTLFIGEVVAVHVDEDVDGRPLLYLG 155
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 33-215 1.25e-17

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 81.06  E-value: 1.25e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853   33 NSYVIRG-GKIAVMDTVDkNFTHEWLDNLQHiLGDSKPDYLVVQHMEPDHSANIENFMKnYPEAVIVSSAKAFTMMKNF- 110
Cdd:smart00849   1 NSYLVRDdGGAILIDTGP-GEAEDLLAELKK-LGPKKIDAIILTHGHPDHIGGLPELLE-APGAPVYAPEGTAELLKDLl 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853  111 -------FGTEFEDRRIVVGEGDTLELGTHTLTFVAAPMvHWPEVIMTYDSTDKVLFSADGFGkfgaldveedwACEARR 183
Cdd:smart00849  78 allgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTPG-HTPGSIVLYLPEGKILFTGDLLF-----------AGGDGR 145

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1079631853  184 YYIGIVGKYGAQVQAVLKKAANLEIKTICPLH 215
Cdd:smart00849 146 TLVDGGDAAASDALESLLKLLKLLPKLVVPGH 177
Flavin_Reduct smart00903
Flavin reductase like domain; This entry represents the FMN-binding domain found in NAD(P) ...
 405-544 6.52e-16

Flavin reductase like domain; This entry represents the FMN-binding domain found in NAD(P)H-flavin oxidoreductases (flavin reductases), a class of enzymes capable of producing reduced flavin for bacterial bioluminescence and other biological processes. This domain is also found in various other oxidoreductase and monooxygenase enzymes... This domain consists of a beta-barrel with Greek key topology, and is related to the ferredoxin reductase-like FAD-binding domain. The flavin reductases have a different dimerisation mode than that found in the PNP oxidase-like family, which also carries an FMN-binding domain with a similar topology.


Pssm-ID: 214900  Cd Length: 147  Bit Score: 74.89  E-value: 6.52e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853  405 IGYGLYVVTSNDGRKD-NGLIVNTVTQVTNTPNRIAVTINKQNYSHHVIQQTGIMNVNCLSVEAPfKVFENFGFQSGRNV 483
Cdd:smart00903   4 FPTGVAVVTTRDGDGGrVGLTASSFVSVSLDPPLVLVCVAKSSSTHPLIRESGRFVVNVLAEDQA-DLARRFAGKSGADR 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1079631853  484 DKFAECENILRSDNGLVFLPkyiNSFMSL--KVEDYVDLDTHGMFICSVTEARVLSDKETMTY 544
Cdd:smart00903  83 FEGVAWGLTEAGVTGAPILA---GALAWLecRVVQVIEVGDHTIFVGEVVAVHVRDDGEPLVY 142
ODP pfam19583
ODP family beta lactamase; The ODP (Oxygen-binding Di-iron Protein) domain is a distinct ...
 33-216 4.03e-14

ODP family beta lactamase; The ODP (Oxygen-binding Di-iron Protein) domain is a distinct member of the metallo-beta-lactamase superfamily recruited to various bacterial and archaeal signal transduction pathways, including chemotaxis, to function as oxygen and iron sensors (1). ODP was shown to act as a sensor for chemotactic responses to both iron and oxygen in the human pathogen Treponema denticola (Td). The ODP di-iron site binds oxygen at high affinity to reversibly form an unusually stable peroxo adduct.


Pssm-ID: 437415  Cd Length: 194  Bit Score: 70.97  E-value: 4.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853  33 NSYVIR-GGKIAVMD--------TVdknfthewLDNLQHILGDSKPDYLVVQHMEPDHSANIENFMKNYPEAVIVSSAKA 103
Cdd:pfam19583   4 NQYLIVdGGEAVLIDpggrltfpAV--------LAKVSKYIDPEKIKYIFASHQDPDICSSLPLWLDVIPDAKIVISELW 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 104 ------FTMMK-NFFGTEFEDRRIVVGEGDTLElgthtltFVAAPMVHWPEVIMTYDSTDKVLFSADgfgKFGALDVEED 176
Cdd:pfam19583  76 erflphYGLKKsRFIPIPDEGGRITLGSGRRLE-------FIPAHFLHSPGNFVTYDPVSKILFSGD---IGAALFPGKD 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1079631853 177 WACEA--------------RRYyigIVGKygaqvqAVLKKAAN----LEIKTICPLHG 216
Cdd:pfam19583 146 WSLFVedfdahipymegfhRRY---MPSN------KALRLWVEmvrkLDIEMIAPQHG 194
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 26-228 8.94e-14

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 70.49  E-value: 8.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853  26 VPNGMAYNSYVIR-GGKIAVMDT-VDKNFTHEWLDNLQHIlgDSKPDYLVVQHMEPDHSANIENFMKNYpEAVIVSSAKA 103
Cdd:COG0491     9 PGAGLGVNSYLIVgGDGAVLIDTgLGPADAEALLAALAAL--GLDIKAVLLTHLHPDHVGGLAALAEAF-GAPVYAHAAE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 104 FTMMKN-----FFGTEFEDRRIVVGEGDTLELGTHTLTFVAAP-------MVHWPEvimtydstDKVLFSAD--GFGKFG 169
Cdd:COG0491    86 AEALEApaagaLFGREPVPPDRTLEDGDTLELGGPGLEVIHTPghtpghvSFYVPD--------EKVLFTGDalFSGGVG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1079631853 170 ALDVEEDWAcearryyigivgkygAQVQAVLKKAANLEIKTICPLHGPVLTGDLSPYLK 228
Cdd:COG0491   158 RPDLPDGDL---------------AQWLASLERLLALPPDLVIPGHGPPTTAEAIDYLE 201
FldA COG0716
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ...
 243-382 2.68e-11

Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440480 [Multi-domain]  Cd Length: 135  Bit Score: 61.46  E-value: 2.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 243 IAIFYTSVYGHTKAAVELLADKLKNNGCPKVVVNDLAREDMAEcvedafrYGRIVLATTTYNADIFPFMKEFINHLTERg 322
Cdd:COG0716     1 ILIVYGSTTGNTEKVAEAIAEALGAAGVDLFEIEDADLDDLED-------YDLLILGTPTWAGELPDDWEDFLEELKED- 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1079631853 323 FQNKTVAMI--ENGSWAPQAIKTMKAMLEKSKNITYTETNVKIMSALN-DDSKAQVDALAKEL 382
Cdd:COG0716    73 LSGKKVALFgtGDSSGYGDALGELKELLEEKGAKVVGGYDFEGSKAPDaEDTEERAEEWLKQL 135
rubredoxin_like cd00350
Rubredoxin_like; nonheme iron binding domain containing a [Fe(SCys)4] center. The family ...
 563-596 6.93e-11

Rubredoxin_like; nonheme iron binding domain containing a [Fe(SCys)4] center. The family includes rubredoxins, a small electron transfer protein, and a slightly smaller modular rubredoxin domain present in rubrerythrin and nigerythrin and detected either N- or C-terminal to such proteins as flavin reductase, NAD(P)H-nitrite reductase, and ferredoxin-thioredoxin reductase. In rubredoxin, the iron atom is coordinated by four cysteine residues (Fe(S-Cys)4), but iron can also be replaced by cobalt, nickel or zinc and believed to be involved in electron transfer. Rubrerythrins and nigerythrins are small homodimeric proteins, generally consisting of 2 domains: a rubredoxin domain C-terminal to a non-sulfur, oxo-bridged diiron site in the N-terminal rubrerythrin domain. Rubrerythrins and nigerythrins have putative peroxide activity.


Pssm-ID: 238210 [Multi-domain]  Cd Length: 33  Bit Score: 57.18  E-value: 6.93e-11
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1079631853 563 YVCKVCGYVYEGDELPEdiVCPLCKHGAADFEPI 596
Cdd:cd00350     2 YVCPVCGYIYDGEEAPW--VCPVCGAPKDKFEKL 33
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
33-215 2.10e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 60.46  E-value: 2.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853  33 NSYVIRGGKIAVM-DT-VDKNFTHEWLDNLQHiLGDSKPDYLVVQHMEPDHSANIENFMKNYPEAVIVSSAKAFTMMKNF 110
Cdd:pfam00753   7 NSYLIEGGGGAVLiDTgGSAEAALLLLLAALG-LGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 111 FGTEFE------------DRRIVVGEGDTLELGTHTLTFVAAPmVHWPEVIMTYDSTDKVLFSADgFGKFGALDVEEDWA 178
Cdd:pfam00753  86 LGLAASrlglpgppvvplPPDVVLEEGDGILGGGLGLLVTHGP-GHGPGHVVVYYGGGKVLFTGD-LLFAGEIGRLDLPL 163

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1079631853 179 CEARRYYIGIVGKYgaqvQAVLKKAANLEIKTICPLH 215
Cdd:pfam00753 164 GGLLVLHPSSAESS----LESLLKLAKLKAAVIVPGH 196
rubredoxin_SM cd00729
Rubredoxin, Small Modular nonheme iron binding domain containing a [Fe(SCys)4] center, present ...
 563-596 5.08e-10

Rubredoxin, Small Modular nonheme iron binding domain containing a [Fe(SCys)4] center, present in rubrerythrin and nigerythrin and detected either N- or C-terminal to such proteins as flavin reductase, NAD(P)H-nitrite reductase, and ferredoxin-thioredoxin reductase. In rubredoxin, the iron atom is coordinated by four cysteine residues (Fe(S-Cys)4), and believed to be involved in electron transfer. Rubrerythrins and nigerythrins are small homodimeric proteins, generally consisting of 2 domains: a rubredoxin domain C-terminal to a non-sulfur, oxo-bridged diiron site in the N-terminal rubrerythrin domain. Rubrerythrins and nigerythrins have putative peroxide activity.


Pssm-ID: 238371 [Multi-domain]  Cd Length: 34  Bit Score: 54.51  E-value: 5.08e-10
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1079631853 563 YVCKVCGYVYEGDELPEdiVCPLCKHGAADFEPI 596
Cdd:cd00729     3 WVCPVCGYIHEGEEAPE--KCPICGAPKEKFEEF 34
NorV COG1773
Flavorubredoxin [Inorganic ion transport and metabolism];
563-597 5.59e-10

Flavorubredoxin [Inorganic ion transport and metabolism];


Pssm-ID: 441379 [Multi-domain]  Cd Length: 53  Bit Score: 55.18  E-value: 5.59e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1079631853 563 YVCKVCGYVY---EGD------------ELPEDIVCPLCKHGAADFEPIE 597
Cdd:COG1773     4 YQCKVCGYVYdpaEGDpengippgtpfeDLPDDWVCPVCGAGKEDFEPVE 53
YotD COG1592
Rubrerythrin [Energy production and conversion];
558-597 3.00e-09

Rubrerythrin [Energy production and conversion];


Pssm-ID: 441200 [Multi-domain]  Cd Length: 180  Bit Score: 56.75  E-value: 3.00e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1079631853 558 EGKKGYVCKVCGYVYEGDELPEdiVCPLCKHGAADFEPIE 597
Cdd:COG1592   143 DEEVVWVCPVCGYIHEGKEAPE--KCPVCGHPKSYFELFA 180
rubredoxin cd00730
Rubredoxin; nonheme iron binding domains containing a [Fe(SCys)4] center. Rubredoxins are ...
 563-596 1.12e-08

Rubredoxin; nonheme iron binding domains containing a [Fe(SCys)4] center. Rubredoxins are small nonheme iron proteins. The iron atom is coordinated by four cysteine residues (Fe(S-Cys)4), but iron can also be replaced by cobalt, nickel or zinc. They are believed to be involved in electron transfer.


Pssm-ID: 238372 [Multi-domain]  Cd Length: 50  Bit Score: 51.15  E-value: 1.12e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1079631853 563 YVCKVCGYVY---EGDE------------LPEDIVCPLCKHGAADFEPI 596
Cdd:cd00730     2 YECRICGYIYdpaEGDPdegippgtpfedLPDDWVCPVCGAGKDDFEPL 50
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 15-166 2.43e-08

uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 54.81  E-value: 2.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853  15 HKIDLfeGQYVVPNGMAynSYVIRG-GKIAVMDT-VDKNFTHeWLDNLQHI-LGDSKPDYLVVQHMEPDHSANIENFMKN 91
Cdd:cd07726     3 YLIDL--GFLGFPGRIA--SYLLDGeGRPALIDTgPSSSVPR-LLAALEALgIAPEDVDYIILTHIHLDHAGGAGLLAEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853  92 YPEAVIV----------------SSAKAftmmknFFGTEF-----------EDRRIVVGEGDTLELGTHTLTFVAAPMvH 144
Cdd:cd07726    78 LPNAKVYvhprgarhlidpsklwASARA------VYGDEAdrlggeilpvpEERVIVLEDGETLDLGGRTLEVIDTPG-H 150

                         170       180
                  ....*....|....*....|..
gi 1079631853 145 WPEVIMTYDSTDKVLFSADGFG 166
Cdd:cd07726   151 APHHLSFLDEESDGLFTGDAAG 172
Rubredoxin pfam00301
Rubredoxin;
563-593 1.02e-06

Rubredoxin;


Pssm-ID: 459752 [Multi-domain]  Cd Length: 46  Bit Score: 45.70  E-value: 1.02e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1079631853 563 YVCKVCGYVY---EGD------------ELPEDIVCPLCKHGAADF 593
Cdd:pfam00301   1 YECKVCGYVYdpaKGDpdngippgtpfeDLPDDWVCPDCGAGKDQF 46
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 64-222 2.06e-04

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 42.94  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853  64 LGDSKPDYLVVQHMEPDHSANIENFMKNypEAVIVSSAKAFTMMKNFFGTEFEDRR----------------IVVGEGDT 127
Cdd:cd16282    48 VTDKPVRYVVNTHYHGDHTLGNAAFADA--GAPIIAHENTREELAARGEAYLELMRrlggdamagtelvlpdRTFDDGLT 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 128 LELGTHTLTFVAAPMVHWPEVIMTYDSTDKVLFSADgfgkfgaLdVEEDwacearryYIGIVGkyGAQVQ---AVLKKAA 204
Cdd:cd16282   126 LDLGGRTVELIHLGPAHTPGDLVVWLPEEGVLFAGD-------L-VFNG--------RIPFLP--DGSLAgwiAALDRLL 187

                         170
                  ....*....|....*...
gi 1079631853 205 NLEIKTICPLHGPVLTGD 222
Cdd:cd16282   188 ALDATVVVPGHGPVGDKA 205
Flavodoxin_5 pfam12724
Flavodoxin domain; This is a family of flavodoxins. Flavodoxins are electron transfer proteins ...
 245-320 1.08e-03

Flavodoxin domain; This is a family of flavodoxins. Flavodoxins are electron transfer proteins that carry a molecule of non-covalently bound FMN.


Pssm-ID: 463681 [Multi-domain]  Cd Length: 144  Bit Score: 39.55  E-value: 1.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1079631853 245 IFYTSVYGHTKAAVELLADKLKNNGCPKVVVNDLAREDMAEcvedafrYGRIVLATTTYNADIFPFMKEFIN-HLTE 320
Cdd:pfam12724   2 ILYSSRDGQTKKIAERIAEELREEGELVDVEDVEAGEDLSS-------YDAVVIGASIYYGKHLPELRQFVTkHRDE 71
Flavodoxin_1 pfam00258
Flavodoxin;
245-350 1.11e-03

Flavodoxin;


Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 39.66  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 245 IFYTSVYGHTKAAVELLADKLKNNGcPKVVVNDLAREDMA--ECVEDAFrygrIVLATTTYNADIFP--------FMKEF 314
Cdd:pfam00258   1 IFYGSQTGNTEKLAEAIAEGLGEAG-FEVDVVDLDDVDETlsEIEEEDL----LLVVVSTWGEGEPPdnakpfvdWLLLF 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1079631853 315 iNHLTERGFQNKTVAMIENGSWA----PQAIKTMKAMLEK 350
Cdd:pfam00258  76 -GTLEDGDLSGLKYAVFGLGDSGyegfCGAAKKLDEKLSE 114
PRK09267 PRK09267
flavodoxin FldA; Validated
 243-330 2.83e-03

flavodoxin FldA; Validated


Pssm-ID: 236439 [Multi-domain]  Cd Length: 169  Bit Score: 39.04  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631853 243 IAIFYTSVYGHTKAAVELLADKLKNNGCPKVVVNDLAREDMAEcvedafrYGRIVLATTTYNA-DIFPFMKEFINHLTER 321
Cdd:PRK09267    4 IGIFFGSDTGNTEDIAKMIQKKLGKDVADVVDIAKASKEDFEA-------YDLLILGIPTWGYgELQCDWDDFLPELEEI 76


                  ....*....
gi 1079631853 322 GFQNKTVAM 330
Cdd:PRK09267   77 DFSGKKVAL 85
 
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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