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Conserved domains on  [gi|115496163|ref|NP_001070132|]
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ferredoxin-2, mitochondrial precursor [Danio rerio]

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
80-195 1.16e-61

adrenodoxin-like ferredoxin protein


:

Pssm-ID: 178203 [Multi-domain]  Cd Length: 117  Bit Score: 187.23  E-value: 1.16e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115496163  80 VNVVYIDRSGRRIPVQARVGDNVLYLAHKHGIDLEGACEASLACSTCHVYVSS-GHYDRLPEPEEREDDMLDMAPLLQEN 158
Cdd:PLN02593   1 ISVTFVDKDGEERTVKAPVGMSLLEAAHENDIELEGACEGSLACSTCHVIVMDeKVYNKLPEPTDEENDMLDLAFGLTET 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 115496163 159 SRLGCQIILTPELDGMELTLPKVTRNFYVDGHVPKPH 195
Cdd:PLN02593  81 SRLGCQVIAKPELDGMRLALPAATRNFAVDGHVPKPH 117
 
Name Accession Description Interval E-value
PLN02593 PLN02593
adrenodoxin-like ferredoxin protein
80-195 1.16e-61

adrenodoxin-like ferredoxin protein


Pssm-ID: 178203 [Multi-domain]  Cd Length: 117  Bit Score: 187.23  E-value: 1.16e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115496163  80 VNVVYIDRSGRRIPVQARVGDNVLYLAHKHGIDLEGACEASLACSTCHVYVSS-GHYDRLPEPEEREDDMLDMAPLLQEN 158
Cdd:PLN02593   1 ISVTFVDKDGEERTVKAPVGMSLLEAAHENDIELEGACEGSLACSTCHVIVMDeKVYNKLPEPTDEENDMLDLAFGLTET 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 115496163 159 SRLGCQIILTPELDGMELTLPKVTRNFYVDGHVPKPH 195
Cdd:PLN02593  81 SRLGCQVIAKPELDGMRLALPAATRNFAVDGHVPKPH 117
Fdx COG0633
Ferredoxin [Energy production and conversion];
83-179 3.26e-15

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 67.57  E-value: 3.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115496163  83 VYIDRSGRRIPVQArvGDNVLYLAHKHGIDLEGACEaSLACSTCHVYVSSGhydrlpEPEEREDDMLDMAPlLQENSRLG 162
Cdd:COG0633    4 VTFIPEGHTVEVPA--GESLLEAALRAGIDLPYSCR-SGACGTCHVRVLEG------EVDHREEDALSDEE-RAAGSRLA 73
                         90
                 ....*....|....*..
gi 115496163 163 CQIILTPELdgmELTLP 179
Cdd:COG0633   74 CQARPTSDL---VVELP 87
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
83-171 3.00e-12

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: 59.72  E-value: 3.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115496163  83 VYIDRSGRRIPVQARVGDNVLYLAHKHGIDLEGACEASlACSTCHVYVSSGHYDRLPEPEEREDDMldmapllQENSRLG 162
Cdd:cd00207    1 VTINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAG-ACGTCKVEVVEGEVDQSDPSLLDEEEA-------EGGYVLA 72

                 ....*....
gi 115496163 163 CQIILTPEL 171
Cdd:cd00207   73 CQTRVTDGL 81
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
83-168 1.58e-07

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 47.13  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115496163   83 VYIDRSGRRIPVQArVGDNVLYLAHKHGIDLEGACEASlACSTCHVYVSSGHYdrLPEPEEREDDMLDmapllQENSRLG 162
Cdd:pfam00111   1 VTINGKGVTIEVPD-GETTLLDAAEEAGIDIPYSCRGG-GCGTCAVKVLEGED--QSDQSFLEDDELA-----AGYVVLA 71

                  ....*.
gi 115496163  163 CQIILT 168
Cdd:pfam00111  72 CQTYPK 77
 
Name Accession Description Interval E-value
PLN02593 PLN02593
adrenodoxin-like ferredoxin protein
80-195 1.16e-61

adrenodoxin-like ferredoxin protein


Pssm-ID: 178203 [Multi-domain]  Cd Length: 117  Bit Score: 187.23  E-value: 1.16e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115496163  80 VNVVYIDRSGRRIPVQARVGDNVLYLAHKHGIDLEGACEASLACSTCHVYVSS-GHYDRLPEPEEREDDMLDMAPLLQEN 158
Cdd:PLN02593   1 ISVTFVDKDGEERTVKAPVGMSLLEAAHENDIELEGACEGSLACSTCHVIVMDeKVYNKLPEPTDEENDMLDLAFGLTET 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 115496163 159 SRLGCQIILTPELDGMELTLPKVTRNFYVDGHVPKPH 195
Cdd:PLN02593  81 SRLGCQVIAKPELDGMRLALPAATRNFAVDGHVPKPH 117
PTZ00490 PTZ00490
Ferredoxin superfamily; Provisional
111-186 4.64e-23

Ferredoxin superfamily; Provisional


Pssm-ID: 185668  Cd Length: 143  Bit Score: 89.54  E-value: 4.64e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115496163 111 IDLEGACEASLACSTCHVYVSSGHYDRLPEPEEREDDMLDMAPLLQENSRLGCQIILTPELDGMELTLPKVTRNFY 186
Cdd:PTZ00490  68 LDVEGTCNGCMQCATCHVYLSAASFKKLGGPSEEEEDVLAKALDVKETSRLACQVDLTPEMDGLEVELPSYVTNRL 143
Fdx COG0633
Ferredoxin [Energy production and conversion];
83-179 3.26e-15

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 67.57  E-value: 3.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115496163  83 VYIDRSGRRIPVQArvGDNVLYLAHKHGIDLEGACEaSLACSTCHVYVSSGhydrlpEPEEREDDMLDMAPlLQENSRLG 162
Cdd:COG0633    4 VTFIPEGHTVEVPA--GESLLEAALRAGIDLPYSCR-SGACGTCHVRVLEG------EVDHREEDALSDEE-RAAGSRLA 73
                         90
                 ....*....|....*..
gi 115496163 163 CQIILTPELdgmELTLP 179
Cdd:COG0633   74 CQARPTSDL---VVELP 87
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
83-171 3.00e-12

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: 59.72  E-value: 3.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115496163  83 VYIDRSGRRIPVQARVGDNVLYLAHKHGIDLEGACEASlACSTCHVYVSSGHYDRLPEPEEREDDMldmapllQENSRLG 162
Cdd:cd00207    1 VTINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAG-ACGTCKVEVVEGEVDQSDPSLLDEEEA-------EGGYVLA 72

                 ....*....
gi 115496163 163 CQIILTPEL 171
Cdd:cd00207   73 CQTRVTDGL 81
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
83-168 1.58e-07

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 47.13  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115496163   83 VYIDRSGRRIPVQArVGDNVLYLAHKHGIDLEGACEASlACSTCHVYVSSGHYdrLPEPEEREDDMLDmapllQENSRLG 162
Cdd:pfam00111   1 VTINGKGVTIEVPD-GETTLLDAAEEAGIDIPYSCRGG-GCGTCAVKVLEGED--QSDQSFLEDDELA-----AGYVVLA 71

                  ....*.
gi 115496163  163 CQIILT 168
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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