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Conserved domains on  [gi|447025444|ref|WP_001102700|]
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MULTISPECIES: class I ribonucleotide reductase maintenance protein YfaE [Gammaproteobacteria]

Protein Classification

2Fe-2S iron-sulfur cluster-binding family protein( domain architecture ID 1376)

2Fe-2S iron-sulfur cluster-binding family protein such as ferredoxin, an iron-sulfur protein transfering electrons in a wide variety of metabolic reactions

Gene Ontology:  GO:0051536

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
fer2 super family cl00159
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 6-74 1.13e-24

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


The actual alignment was detected with superfamily member PRK10713:

Pssm-ID: 444718 [Multi-domain]  Cd Length: 84  Bit Score: 87.48  E-value: 1.13e-24
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447025444  6 QASNNVLLAQIESKGLTVETHCRSGFCGMCRVRLLEGQVAYDETPIAFVKEGEVLVCCAKAKTDVTLEI 74
Cdd:PRK10713 16 QDEHPSLLAALESHNVAVEYQCREGYCGSCRTRLVAGQVDWIAEPLAFIQPGEILPCCCRAKGDIEIEM 84
 
Name Accession Description Interval E-value
PRK10713 PRK10713
2Fe-2S ferredoxin-like protein;
6-74 1.13e-24

2Fe-2S ferredoxin-like protein;


Pssm-ID: 182668 [Multi-domain]  Cd Length: 84  Bit Score: 87.48  E-value: 1.13e-24
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447025444  6 QASNNVLLAQIESKGLTVETHCRSGFCGMCRVRLLEGQVAYDETPIAFVKEGEVLVCCAKAKTDVTLEI 74
Cdd:PRK10713 16 QDEHPSLLAALESHNVAVEYQCREGYCGSCRTRLVAGQVDWIAEPLAFIQPGEILPCCCRAKGDIEIEM 84
Fdx COG0633
Ferredoxin [Energy production and conversion];
12-74 8.94e-13

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 57.17  E-value: 8.94e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447025444 12 LLAQIESKGLTVETHCRSGFCGMCRVRLLEGQVAYDETPI---AFVKEGEVLVCCAKAKTDVTLEI 74
Cdd:COG0633  21 LLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDAlsdEERAAGSRLACQARPTSDLVVEL 86
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 12-73 1.14e-08

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 47.00  E-value: 1.14e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447025444 12 LLAQIESKGLTVETHCRSGFCGMCRVRLLEGQVAYDE---TPIAFVKEGEVLVCCAKAKTDVTLE 73
Cdd:cd00207  20 LLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDpslLDEEEAEGGYVLACQTRVTDGLVIE 84
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
10-67 6.92e-05

2Fe-2S iron-sulfur cluster binding domain;


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 37.12  E-value: 6.92e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447025444  10 NVLLAQIESKGLTVETHCRSGFCGMCRVRLLEGQVAYDETPI---AFVKEGEVLVCCAKAK 67
Cdd:pfam00111 17 TTLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDQSDQSFLeddELAAGYVVLACQTYPK 77
 
Name Accession Description Interval E-value
PRK10713 PRK10713
2Fe-2S ferredoxin-like protein;
6-74 1.13e-24

2Fe-2S ferredoxin-like protein;


Pssm-ID: 182668 [Multi-domain]  Cd Length: 84  Bit Score: 87.48  E-value: 1.13e-24
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447025444  6 QASNNVLLAQIESKGLTVETHCRSGFCGMCRVRLLEGQVAYDETPIAFVKEGEVLVCCAKAKTDVTLEI 74
Cdd:PRK10713 16 QDEHPSLLAALESHNVAVEYQCREGYCGSCRTRLVAGQVDWIAEPLAFIQPGEILPCCCRAKGDIEIEM 84
Fdx COG0633
Ferredoxin [Energy production and conversion];
12-74 8.94e-13

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 57.17  E-value: 8.94e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447025444 12 LLAQIESKGLTVETHCRSGFCGMCRVRLLEGQVAYDETPI---AFVKEGEVLVCCAKAKTDVTLEI 74
Cdd:COG0633  21 LLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDAlsdEERAAGSRLACQARPTSDLVVEL 86
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 4-74 1.31e-11

CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 57.57  E-value: 1.31e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447025444   4 QLQASNNVLLAQIESkGLTVETHCRSGFCGMCRVRLLEGQVAYDETPIAFVKE-----GEVLVCCAKAKTDVTLEI 74
Cdd:PRK07609  15 TAEPDETILDAALRQ-GIHLPYGCKNGACGSCKGRLLEGEVEQGPHQASALSGeeraaGEALTCCAKPLSDLVLEA 89
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 12-73 1.14e-08

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 47.00  E-value: 1.14e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447025444 12 LLAQIESKGLTVETHCRSGFCGMCRVRLLEGQVAYDE---TPIAFVKEGEVLVCCAKAKTDVTLE 73
Cdd:cd00207  20 LLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDpslLDEEEAEGGYVLACQTRVTDGLVIE 84
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 10-74 1.89e-08

Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and conversion]; Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase


Pssm-ID: 442118 [Multi-domain]  Cd Length: 396  Bit Score: 48.71  E-value: 1.89e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447025444  10 NVLLAQieskGLTVETHC-RSGFCGMCRVRLLEGQVAYDETPIAF-----VKEGEVLVCCAKAKTDVTLEI 74
Cdd:COG2871   56 DALLRQ----GIFLPSACgGGGTCGQCKVKVLEGGGDILPTETFHlsdreRKEGYRLACQVKVKSDMEIEV 122
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 12-73 5.82e-07

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 44.70  E-value: 5.82e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447025444  12 LLAQIESKGLTVETHCRSGFCGMCRVRLLEGQV----AYDETPiAFVKEGEVLVCCAKAKTDVTLE 73
Cdd:PRK10684 268 LLEALESNKVPVVAACRAGVCGCCKTKVVSGEYtvssTMTLTP-AEIAQGYVLACSCHPQGDLVLA 332
PTZ00038 PTZ00038
ferredoxin; Provisional
 17-73 2.06e-06

ferredoxin; Provisional


Pssm-ID: 240237 [Multi-domain]  Cd Length: 191  Bit Score: 42.52  E-value: 2.06e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 447025444  17 ESKGLTVETHCRSGFCGMCRVRLLEGQVAYDETPI---AFVKEGEVLVCCAKAKTDVTLE 73
Cdd:PTZ00038 122 ERQGVELPYSCRGGSCSTCAAKLLEGEVDNEDQSYlddEQLKKGYCLLCTCYPKSDCTIE 181
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
10-67 6.92e-05

2Fe-2S iron-sulfur cluster binding domain;


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 37.12  E-value: 6.92e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447025444  10 NVLLAQIESKGLTVETHCRSGFCGMCRVRLLEGQVAYDETPI---AFVKEGEVLVCCAKAK 67
Cdd:pfam00111 17 TTLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDQSDQSFLeddELAAGYVVLACQTYPK 77
PLN03136 PLN03136
Ferredoxin; Provisional
 12-73 1.55e-04

Ferredoxin; Provisional


Pssm-ID: 178681 [Multi-domain]  Cd Length: 148  Bit Score: 37.42  E-value: 1.55e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447025444  12 LLAQIESKGLTVETHCRSGFCGMCRVRLLEGQVayDETPIAF-----VKEGEVLVCCAKAKTDVTLE 73
Cdd:PLN03136  76 VLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSI--DQSDQSFlddeqISEGYVLTCVAYPTSDVVIE 140
PRK05713 PRK05713
iron-sulfur-binding ferredoxin reductase;
7-74 8.00e-04

iron-sulfur-binding ferredoxin reductase;


Pssm-ID: 235575 [Multi-domain]  Cd Length: 312  Bit Score: 35.86  E-value: 8.00e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447025444   7 ASNnvLLAQIESKGLTVETHCRSGFCGMCRVRLLEGQVAyDETPIAFVKE----GEVLVCCAKAKTDVTLEI 74
Cdd:PRK05713  16 GSN--LLDALNAAGVAVPYSCRAGSCHACLVRCLQGEPE-DALPEALAAEkreqGWRLACQCRVVGDLRVEV 84
 
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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