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Conserved domains on  [gi|12861729|dbj|BAB32267|]
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unnamed protein product [Mus musculus]

Protein Classification

ferredoxin family 2Fe-2S iron-sulfur cluster binding protein( domain architecture ID 10010834)

ferredoxin family 2Fe-2S iron-sulfur cluster binding protein similar to Homo sapiens mitochondrial ferredoxin-2, which is essential for heme A and Fe/S protein biosynthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02593 PLN02593
adrenodoxin-like ferredoxin protein
59-174 1.57e-57

adrenodoxin-like ferredoxin protein


:

Pssm-ID: 178203 [Multi-domain]  Cd Length: 117  Bit Score: 176.06  E-value: 1.57e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12861729   59 VNVVFVDRSGKRIPVRGKVGDNVLYLAQRHGVDLEGACEASLACSTCHVYVS-EAHLDLLPPPEEREDDMLDMAPLLQEN 137
Cdd:PLN02593   1 ISVTFVDKDGEERTVKAPVGMSLLEAAHENDIELEGACEGSLACSTCHVIVMdEKVYNKLPEPTDEENDMLDLAFGLTET 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 12861729  138 SRLGCQIVLTPELEGVEFALPKITRNFYVDGHIPKPH 174
Cdd:PLN02593  81 SRLGCQVIAKPELDGMRLALPAATRNFAVDGHVPKPH 117
 
Name Accession Description Interval E-value
PLN02593 PLN02593
adrenodoxin-like ferredoxin protein
59-174 1.57e-57

adrenodoxin-like ferredoxin protein


Pssm-ID: 178203 [Multi-domain]  Cd Length: 117  Bit Score: 176.06  E-value: 1.57e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12861729   59 VNVVFVDRSGKRIPVRGKVGDNVLYLAQRHGVDLEGACEASLACSTCHVYVS-EAHLDLLPPPEEREDDMLDMAPLLQEN 137
Cdd:PLN02593   1 ISVTFVDKDGEERTVKAPVGMSLLEAAHENDIELEGACEGSLACSTCHVIVMdEKVYNKLPEPTDEENDMLDLAFGLTET 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 12861729  138 SRLGCQIVLTPELEGVEFALPKITRNFYVDGHIPKPH 174
Cdd:PLN02593  81 SRLGCQVIAKPELDGMRLALPAATRNFAVDGHVPKPH 117
Fdx COG0633
Ferredoxin [Energy production and conversion];
62-151 1.20e-14

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 65.64  E-value: 1.20e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12861729  62 VFVDRSGKRIPVRGkvGDNVLYLAQRHGVDLEGACEaSLACSTCHVYVSEAHldllppPEEREDDMLDMAPlLQENSRLG 141
Cdd:COG0633   4 VTFIPEGHTVEVPA--GESLLEAALRAGIDLPYSCR-SGACGTCHVRVLEGE------VDHREEDALSDEE-RAAGSRLA 73
                        90
                ....*....|
gi 12861729 142 CQIVLTPELE 151
Cdd:COG0633  74 CQARPTSDLV 83
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
62-151 2.35e-11

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: 57.02  E-value: 2.35e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12861729  62 VFVDRSGKRIPVRGKVGDNVLYLAQRHGVDLEGACEASlACSTCHVYVSEAHLDLLPPPEEREDDMldmapllQENSRLG 141
Cdd:cd00207   1 VTINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAG-ACGTCKVEVVEGEVDQSDPSLLDEEEA-------EGGYVLA 72
                        90
                ....*....|
gi 12861729 142 CQIVLTPELE 151
Cdd:cd00207  73 CQTRVTDGLV 82
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
62-147 1.05e-06

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 44.44  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12861729    62 VFVDRSGKRIPVRgKVGDNVLYLAQRHGVDLEGACEASlACSTCHVYVSEAhlDLLPPPEEREDDMLDmapllQENSRLG 141
Cdd:pfam00111   1 VTINGKGVTIEVP-DGETTLLDAAEEAGIDIPYSCRGG-GCGTCAVKVLEG--EDQSDQSFLEDDELA-----AGYVVLA 71

                  ....*.
gi 12861729   142 CQIVLT 147
Cdd:pfam00111  72 CQTYPK 77
 
Name Accession Description Interval E-value
PLN02593 PLN02593
adrenodoxin-like ferredoxin protein
59-174 1.57e-57

adrenodoxin-like ferredoxin protein


Pssm-ID: 178203 [Multi-domain]  Cd Length: 117  Bit Score: 176.06  E-value: 1.57e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12861729   59 VNVVFVDRSGKRIPVRGKVGDNVLYLAQRHGVDLEGACEASLACSTCHVYVS-EAHLDLLPPPEEREDDMLDMAPLLQEN 137
Cdd:PLN02593   1 ISVTFVDKDGEERTVKAPVGMSLLEAAHENDIELEGACEGSLACSTCHVIVMdEKVYNKLPEPTDEENDMLDLAFGLTET 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 12861729  138 SRLGCQIVLTPELEGVEFALPKITRNFYVDGHIPKPH 174
Cdd:PLN02593  81 SRLGCQVIAKPELDGMRLALPAATRNFAVDGHVPKPH 117
PTZ00490 PTZ00490
Ferredoxin superfamily; Provisional
90-165 4.83e-22

Ferredoxin superfamily; Provisional


Pssm-ID: 185668  Cd Length: 143  Bit Score: 86.46  E-value: 4.83e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12861729   90 VDLEGACEASLACSTCHVYVSEAHLDLLPPPEEREDDMLDMAPLLQENSRLGCQIVLTPELEGVEFALPKITRNFY 165
Cdd:PTZ00490  68 LDVEGTCNGCMQCATCHVYLSAASFKKLGGPSEEEEDVLAKALDVKETSRLACQVDLTPEMDGLEVELPSYVTNRL 143
Fdx COG0633
Ferredoxin [Energy production and conversion];
62-151 1.20e-14

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 65.64  E-value: 1.20e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12861729  62 VFVDRSGKRIPVRGkvGDNVLYLAQRHGVDLEGACEaSLACSTCHVYVSEAHldllppPEEREDDMLDMAPlLQENSRLG 141
Cdd:COG0633   4 VTFIPEGHTVEVPA--GESLLEAALRAGIDLPYSCR-SGACGTCHVRVLEGE------VDHREEDALSDEE-RAAGSRLA 73
                        90
                ....*....|
gi 12861729 142 CQIVLTPELE 151
Cdd:COG0633  74 CQARPTSDLV 83
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
62-151 2.35e-11

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: 57.02  E-value: 2.35e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12861729  62 VFVDRSGKRIPVRGKVGDNVLYLAQRHGVDLEGACEASlACSTCHVYVSEAHLDLLPPPEEREDDMldmapllQENSRLG 141
Cdd:cd00207   1 VTINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAG-ACGTCKVEVVEGEVDQSDPSLLDEEEA-------EGGYVLA 72
                        90
                ....*....|
gi 12861729 142 CQIVLTPELE 151
Cdd:cd00207  73 CQTRVTDGLV 82
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
62-147 1.05e-06

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 44.44  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12861729    62 VFVDRSGKRIPVRgKVGDNVLYLAQRHGVDLEGACEASlACSTCHVYVSEAhlDLLPPPEEREDDMLDmapllQENSRLG 141
Cdd:pfam00111   1 VTINGKGVTIEVP-DGETTLLDAAEEAGIDIPYSCRGG-GCGTCAVKVLEG--EDQSDQSFLEDDELA-----AGYVVLA 71

                  ....*.
gi 12861729   142 CQIVLT 147
Cdd:pfam00111  72 CQTYPK 77
 
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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