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Conserved domains on  [gi|447024852|ref|WP_001102108|]
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MULTISPECIES: (Fe-S)-binding protein [Enterobacteriaceae]

Protein Classification

(Fe-S)-binding protein( domain architecture ID 11415541)

(Fe-S)-binding protein may function as an oxidoreductase

EC:  1.5.3.-
Gene Ontology:  GO:0046872|GO:0051536|GO:0016491
PubMed:  30942582

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
5-236 1.71e-44

Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];


:

Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 154.08  E-value: 1.71e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447024852   5 FFVTCIGDALKSRMARDSVLLLEKLGCRVNFPEKQGCCGQPAINSGYIKEAIPGMKNLIAALEDND-DPIISPAGSCTYA 83
Cdd:COG0247  192 LFPGCFTNYFDPEIGKAAVRLLEAAGVEVVLPPEELCCGAPALSKGDLDLARKLARRNIEALERLGvKAIVTTCPSCGLT 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447024852  84 VKS-YPTYLADEpewasraakVAARMQDLTSFIVNKL--GVVDVGaSLQGRAVYHPSCSLARKLGVKDEPLTLLKNVRGL 160
Cdd:COG0247  272 LKDeYPELLGDR---------VAFEVLDISEFLAELIleGKLKLK-PLGEKVTYHDPCHLGRGGGVYDAPRELLKAIPGV 341
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447024852 161 ELLTFAEQDTCCGFGGTFSVKMAEISGEMVKEKVAHLMEVRPEYLIGADVSCLLNISGRLQREGqkVKVMHIAEVL 236
Cdd:COG0247  342 EVVEMPEDSGCCGGAGGYGFEEPELSMRIGERKLEQIRATGADVVVTACPSCRTQLEDGTKEYG--IEVKHPVELL 415
 
Name Accession Description Interval E-value
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
5-236 1.71e-44

Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 154.08  E-value: 1.71e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447024852   5 FFVTCIGDALKSRMARDSVLLLEKLGCRVNFPEKQGCCGQPAINSGYIKEAIPGMKNLIAALEDND-DPIISPAGSCTYA 83
Cdd:COG0247  192 LFPGCFTNYFDPEIGKAAVRLLEAAGVEVVLPPEELCCGAPALSKGDLDLARKLARRNIEALERLGvKAIVTTCPSCGLT 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447024852  84 VKS-YPTYLADEpewasraakVAARMQDLTSFIVNKL--GVVDVGaSLQGRAVYHPSCSLARKLGVKDEPLTLLKNVRGL 160
Cdd:COG0247  272 LKDeYPELLGDR---------VAFEVLDISEFLAELIleGKLKLK-PLGEKVTYHDPCHLGRGGGVYDAPRELLKAIPGV 341
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447024852 161 ELLTFAEQDTCCGFGGTFSVKMAEISGEMVKEKVAHLMEVRPEYLIGADVSCLLNISGRLQREGqkVKVMHIAEVL 236
Cdd:COG0247  342 EVVEMPEDSGCCGGAGGYGFEEPELSMRIGERKLEQIRATGADVVVTACPSCRTQLEDGTKEYG--IEVKHPVELL 415
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
1-236 1.42e-20

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 89.68  E-value: 1.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447024852   1 MNVNFFVTCIGDALKSRMARDSVLLLEKLGCRVNFPEKQGCCGQPAINSGYIKEAIPGMKNLIAALEDND-DPIISPAGS 79
Cdd:PRK06259 261 LRVAFFTGCLVDYRLQEVGKDAIRVLNAHGISVIIPKNQVCCGSPLIRTGQTDVAEELKKKNLEIFNKLDvDTVVTICAG 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447024852  80 CTYAVKS-YPtyladEPEWasraakvaaRMQDLTSFIVnKLGVVDvGASLQGRAVYHPSCSLARKLGVKDEPLTLLKNVR 158
Cdd:PRK06259 341 CGSTLKNdYK-----EKEF---------NVMDITEVLV-EVGLEK-YKPLDITVTYHDPCHLRRGQGIYEEPRKILRSIP 404
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447024852 159 GLELLTFAEQDTCCGFGGTFSVKMAEISGEMVKEKVAHLMEVRPEYLIGADVSCLLNISGRLQREGQKVKVMHIAEVL 236
Cdd:PRK06259 405 GLEFVEMEIPDQCCGAGGGVRSGKPEIAEALGKRKAEMIRETGADYVITVCPFCEYHIRDSLKKYSEDIPVMNIVSLL 482
CCG pfam02754
Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif ...
132-216 8.21e-17

Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif normally found at the C-terminus in archaeal and bacterial Hdr-like proteins. There may be one or two copies, and the motif is probably an iron-sulfur binding cluster. In some instances one of the cysteines is replaced by an aspartate, and aspartate can in principle also function as a ligand of an iron-sulfur cluster. The family includes a subunit from heterodisulphide reductase and a subunit from glycolate oxidase and glycerol-3-phosphate dehydrogenase.


Pssm-ID: 397052 [Multi-domain]  Cd Length: 84  Bit Score: 72.73  E-value: 8.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447024852  132 AVYHPSCSLARklGVKDEPLTLLKNVRGLELLTF--AEQDTCCGFGGTFSVKMaEISGEMVKEKVAHLMEVRPEYLIGAD 209
Cdd:pfam02754   1 VAYFDGCHLGR--ALYPEPRKALKKVLGALGVEVviLEKQSCCGAGGGFSGKE-DVAEALAKRNIDTAEETGADAIVTAC 77

                  ....*..
gi 447024852  210 VSCLLNI 216
Cdd:pfam02754  78 PGCLLQL 84
 
Name Accession Description Interval E-value
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
5-236 1.71e-44

Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 154.08  E-value: 1.71e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447024852   5 FFVTCIGDALKSRMARDSVLLLEKLGCRVNFPEKQGCCGQPAINSGYIKEAIPGMKNLIAALEDND-DPIISPAGSCTYA 83
Cdd:COG0247  192 LFPGCFTNYFDPEIGKAAVRLLEAAGVEVVLPPEELCCGAPALSKGDLDLARKLARRNIEALERLGvKAIVTTCPSCGLT 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447024852  84 VKS-YPTYLADEpewasraakVAARMQDLTSFIVNKL--GVVDVGaSLQGRAVYHPSCSLARKLGVKDEPLTLLKNVRGL 160
Cdd:COG0247  272 LKDeYPELLGDR---------VAFEVLDISEFLAELIleGKLKLK-PLGEKVTYHDPCHLGRGGGVYDAPRELLKAIPGV 341
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447024852 161 ELLTFAEQDTCCGFGGTFSVKMAEISGEMVKEKVAHLMEVRPEYLIGADVSCLLNISGRLQREGqkVKVMHIAEVL 236
Cdd:COG0247  342 EVVEMPEDSGCCGGAGGYGFEEPELSMRIGERKLEQIRATGADVVVTACPSCRTQLEDGTKEYG--IEVKHPVELL 415
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
1-236 1.42e-20

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 89.68  E-value: 1.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447024852   1 MNVNFFVTCIGDALKSRMARDSVLLLEKLGCRVNFPEKQGCCGQPAINSGYIKEAIPGMKNLIAALEDND-DPIISPAGS 79
Cdd:PRK06259 261 LRVAFFTGCLVDYRLQEVGKDAIRVLNAHGISVIIPKNQVCCGSPLIRTGQTDVAEELKKKNLEIFNKLDvDTVVTICAG 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447024852  80 CTYAVKS-YPtyladEPEWasraakvaaRMQDLTSFIVnKLGVVDvGASLQGRAVYHPSCSLARKLGVKDEPLTLLKNVR 158
Cdd:PRK06259 341 CGSTLKNdYK-----EKEF---------NVMDITEVLV-EVGLEK-YKPLDITVTYHDPCHLRRGQGIYEEPRKILRSIP 404
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447024852 159 GLELLTFAEQDTCCGFGGTFSVKMAEISGEMVKEKVAHLMEVRPEYLIGADVSCLLNISGRLQREGQKVKVMHIAEVL 236
Cdd:PRK06259 405 GLEFVEMEIPDQCCGAGGGVRSGKPEIAEALGKRKAEMIRETGADYVITVCPFCEYHIRDSLKKYSEDIPVMNIVSLL 482
glcF PRK11274
glycolate oxidase subunit GlcF;
25-236 4.06e-20

glycolate oxidase subunit GlcF;


Pssm-ID: 236890 [Multi-domain]  Cd Length: 407  Bit Score: 88.01  E-value: 4.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447024852  25 LLEKLGCRVNFPEKQGCCGqpAINS--GYIKEAIPGMKNLIAA----LEDNDDPIISPAGSCTYAVKSYPTYLADEPEWA 98
Cdd:PRK11274 191 VLDRLGISLVVAPEAGCCG--AVRYhlNAQEGGLARMRRNIDAwwpaIEAGAEAIVMTASGCGATVKEYGHLLRDDPAYA 268
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447024852  99 SRAAKVAARMQDLTSFIVNK-LGVVDVGASLQGRAVYHPSCSL--ARKLGVKDEP-LTLLknvrGLELLTFAEQDTCCGF 174
Cdd:PRK11274 269 EKAARVSALTRDLSELLPAEpLELLALLGRPDRRVAFHPPCTLqhGQKLRGKVERlLTRL----GFELTLVADSHLCCGS 344
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447024852 175 GGTFSVKMAEISGEMVKEKVAHLMEVRPEYLIGADVSCLLNISGrlqreGQKVKVMHIAEVL 236
Cdd:PRK11274 345 AGTYSLLQPELSYQLRDNKLAALEAGKPEVIVTANIGCQTHLQS-----GTRTPVRHWIELV 401
CCG pfam02754
Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif ...
132-216 8.21e-17

Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif normally found at the C-terminus in archaeal and bacterial Hdr-like proteins. There may be one or two copies, and the motif is probably an iron-sulfur binding cluster. In some instances one of the cysteines is replaced by an aspartate, and aspartate can in principle also function as a ligand of an iron-sulfur cluster. The family includes a subunit from heterodisulphide reductase and a subunit from glycolate oxidase and glycerol-3-phosphate dehydrogenase.


Pssm-ID: 397052 [Multi-domain]  Cd Length: 84  Bit Score: 72.73  E-value: 8.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447024852  132 AVYHPSCSLARklGVKDEPLTLLKNVRGLELLTF--AEQDTCCGFGGTFSVKMaEISGEMVKEKVAHLMEVRPEYLIGAD 209
Cdd:pfam02754   1 VAYFDGCHLGR--ALYPEPRKALKKVLGALGVEVviLEKQSCCGAGGGFSGKE-DVAEALAKRNIDTAEETGADAIVTAC 77

                  ....*..
gi 447024852  210 VSCLLNI 216
Cdd:pfam02754  78 PGCLLQL 84
CCG pfam02754
Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif ...
3-84 9.54e-16

Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif normally found at the C-terminus in archaeal and bacterial Hdr-like proteins. There may be one or two copies, and the motif is probably an iron-sulfur binding cluster. In some instances one of the cysteines is replaced by an aspartate, and aspartate can in principle also function as a ligand of an iron-sulfur cluster. The family includes a subunit from heterodisulphide reductase and a subunit from glycolate oxidase and glycerol-3-phosphate dehydrogenase.


Pssm-ID: 397052 [Multi-domain]  Cd Length: 84  Bit Score: 70.03  E-value: 9.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447024852    3 VNFFVTC-IGDALKSRMARDSVLLLEKLGCRVNFPEKQGCCGQPAINSGYIKEAIPGMKNLIAALED-NDDPIISPAGSC 80
Cdd:pfam02754   1 VAYFDGChLGRALYPEPRKALKKVLGALGVEVVILEKQSCCGAGGGFSGKEDVAEALAKRNIDTAEEtGADAIVTACPGC 80

                  ....
gi 447024852   81 TYAV 84
Cdd:pfam02754  81 LLQL 84
glpC PRK11168
anaerobic glycerol-3-phosphate dehydrogenase subunit C;
2-181 9.23e-15

anaerobic glycerol-3-phosphate dehydrogenase subunit C;


Pssm-ID: 236869 [Multi-domain]  Cd Length: 396  Bit Score: 72.59  E-value: 9.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447024852   2 NVNFFVTCIGDALKSRMARDSVLLLEKLGCRVnFPEKQGCCGQPAINSGYIKEAIPGMKNLIAALE---DNDDPIISPAG 78
Cdd:PRK11168 163 QVAYFHGCYVNYNHPQLGKDLVKVLNAMGYEV-LLPKEKCCGLPLIANGFLDKARKQAEFNVESLReaiEKGIPVIATSS 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447024852  79 SCTYAVK-SYPTYLaDEPEwasraAKVAARMQDLTSFIVNKL--GVVDVGASLQGRAVYHPSCSLaRKLGVKDEPLTLLK 155
Cdd:PRK11168 242 SCTLTLRdEYPELL-GVDN-----AGVRDHIEDATEFLRRLLdqGKLLPLKPLPLKVAYHTPCHL-EKQGWGLYTLELLR 314
                        170       180
                 ....*....|....*....|....*.
gi 447024852 156 NVRGLELLTFAEQdtCCGFGGTFSVK 181
Cdd:PRK11168 315 LIPGLEVVVLDSQ--CCGIAGTYGFK 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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