NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15235586|ref|NP_192454|]
View 

mitochondrial ferredoxin 1 [Arabidopsis thaliana]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PLN02593 PLN02593
adrenodoxin-like ferredoxin protein
81-197 6.36e-87

adrenodoxin-like ferredoxin protein


:

Pssm-ID: 178203 [Multi-domain]  Cd Length: 117  Bit Score: 251.18  E-value: 6.36e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235586   81 ITIIFVDKDGEEIPVKVPIGMSVLEAAHENDIDLEGACEASLACSTCHVIVMDTEYYNKLEEPTDEENDMLDLAFGLTET 160
Cdd:PLN02593   1 ISVTFVDKDGEERTVKAPVGMSLLEAAHENDIELEGACEGSLACSTCHVIVMDEKVYNKLPEPTDEENDMLDLAFGLTET 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 15235586  161 SRLGCQVIARPELDGVRLAIPSATRNFAVDGFVPKPH 197
Cdd:PLN02593  81 SRLGCQVIAKPELDGMRLALPAATRNFAVDGHVPKPH 117
 
Name Accession Description Interval E-value
PLN02593 PLN02593
adrenodoxin-like ferredoxin protein
81-197 6.36e-87

adrenodoxin-like ferredoxin protein


Pssm-ID: 178203 [Multi-domain]  Cd Length: 117  Bit Score: 251.18  E-value: 6.36e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235586   81 ITIIFVDKDGEEIPVKVPIGMSVLEAAHENDIDLEGACEASLACSTCHVIVMDTEYYNKLEEPTDEENDMLDLAFGLTET 160
Cdd:PLN02593   1 ISVTFVDKDGEERTVKAPVGMSLLEAAHENDIELEGACEGSLACSTCHVIVMDEKVYNKLPEPTDEENDMLDLAFGLTET 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 15235586  161 SRLGCQVIARPELDGVRLAIPSATRNFAVDGFVPKPH 197
Cdd:PLN02593  81 SRLGCQVIAKPELDGMRLALPAATRNFAVDGHVPKPH 117
Fdx COG0633
Ferredoxin [Energy production and conversion];
80-173 2.34e-16

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 70.65  E-value: 2.34e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235586  80 KITIIfvdkdGEEIPVKVPIGMSVLEAAHENDIDLEGACEaSLACSTCHVIVMDteyynklEEPTDEENDMLDlAFGLTE 159
Cdd:COG0633   3 KVTFI-----PEGHTVEVPAGESLLEAALRAGIDLPYSCR-SGACGTCHVRVLE-------GEVDHREEDALS-DEERAA 68
                        90
                ....*....|....
gi 15235586 160 TSRLGCQVIARPEL 173
Cdd:COG0633  69 GSRLACQARPTSDL 82
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
84-173 7.42e-14

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: 63.95  E-value: 7.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235586  84 IFVDKDGEEIPVKVPIGMSVLEAAHENDIDLEGACEASlACSTCHVIVMDTEYynkleeptDEENDMLDLAFGLTETSRL 163
Cdd:cd00207   1 VTINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAG-ACGTCKVEVVEGEV--------DQSDPSLLDEEEAEGGYVL 71
                        90
                ....*....|
gi 15235586 164 GCQVIARPEL 173
Cdd:cd00207  72 ACQTRVTDGL 81
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
84-170 2.62e-09

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 51.76  E-value: 2.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235586    84 IFVDKDGEEIPVKVPiGMSVLEAAHENDIDLEGACEASlACSTCHVIVMDTEYynkLEEPTDEENDMLDLAFGLtetsrL 163
Cdd:pfam00111   1 VTINGKGVTIEVPDG-ETTLLDAAEEAGIDIPYSCRGG-GCGTCAVKVLEGED---QSDQSFLEDDELAAGYVV-----L 70

                  ....*..
gi 15235586   164 GCQVIAR 170
Cdd:pfam00111  71 ACQTYPK 77
 
Name Accession Description Interval E-value
PLN02593 PLN02593
adrenodoxin-like ferredoxin protein
81-197 6.36e-87

adrenodoxin-like ferredoxin protein


Pssm-ID: 178203 [Multi-domain]  Cd Length: 117  Bit Score: 251.18  E-value: 6.36e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235586   81 ITIIFVDKDGEEIPVKVPIGMSVLEAAHENDIDLEGACEASLACSTCHVIVMDTEYYNKLEEPTDEENDMLDLAFGLTET 160
Cdd:PLN02593   1 ISVTFVDKDGEERTVKAPVGMSLLEAAHENDIELEGACEGSLACSTCHVIVMDEKVYNKLPEPTDEENDMLDLAFGLTET 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 15235586  161 SRLGCQVIARPELDGVRLAIPSATRNFAVDGFVPKPH 197
Cdd:PLN02593  81 SRLGCQVIAKPELDGMRLALPAATRNFAVDGHVPKPH 117
PTZ00490 PTZ00490
Ferredoxin superfamily; Provisional
63-186 1.58e-25

Ferredoxin superfamily; Provisional


Pssm-ID: 185668  Cd Length: 143  Bit Score: 96.09  E-value: 1.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235586   63 FCTSSTTSSENGdeeteKITIIFVDKDGEEIPVKVPIGMSVLEAAHE-NDIDLEGACEASLACSTCHVIVMDTEYyNKLE 141
Cdd:PTZ00490  23 LSTSRALYSTPG-----KVKVCVKKRDGTHCDVEVPVGMSLMHALRDvAKLDVEGTCNGCMQCATCHVYLSAASF-KKLG 96
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 15235586  142 EPTDEENDMLDLAFGLTETSRLGCQVIARPELDGVRLAIPSATRN 186
Cdd:PTZ00490  97 GPSEEEEDVLAKALDVKETSRLACQVDLTPEMDGLEVELPSYVTN 141
Fdx COG0633
Ferredoxin [Energy production and conversion];
80-173 2.34e-16

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 70.65  E-value: 2.34e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235586  80 KITIIfvdkdGEEIPVKVPIGMSVLEAAHENDIDLEGACEaSLACSTCHVIVMDteyynklEEPTDEENDMLDlAFGLTE 159
Cdd:COG0633   3 KVTFI-----PEGHTVEVPAGESLLEAALRAGIDLPYSCR-SGACGTCHVRVLE-------GEVDHREEDALS-DEERAA 68
                        90
                ....*....|....
gi 15235586 160 TSRLGCQVIARPEL 173
Cdd:COG0633  69 GSRLACQARPTSDL 82
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
84-173 7.42e-14

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: 63.95  E-value: 7.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235586  84 IFVDKDGEEIPVKVPIGMSVLEAAHENDIDLEGACEASlACSTCHVIVMDTEYynkleeptDEENDMLDLAFGLTETSRL 163
Cdd:cd00207   1 VTINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAG-ACGTCKVEVVEGEV--------DQSDPSLLDEEEAEGGYVL 71
                        90
                ....*....|
gi 15235586 164 GCQVIARPEL 173
Cdd:cd00207  72 ACQTRVTDGL 81
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
84-170 2.62e-09

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 51.76  E-value: 2.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235586    84 IFVDKDGEEIPVKVPiGMSVLEAAHENDIDLEGACEASlACSTCHVIVMDTEYynkLEEPTDEENDMLDLAFGLtetsrL 163
Cdd:pfam00111   1 VTINGKGVTIEVPDG-ETTLLDAAEEAGIDIPYSCRGG-GCGTCAVKVLEGED---QSDQSFLEDDELAAGYVV-----L 70

                  ....*..
gi 15235586   164 GCQVIAR 170
Cdd:pfam00111  71 ACQTYPK 77
petF CHL00134
ferredoxin; Validated
78-127 3.11e-04

ferredoxin; Validated


Pssm-ID: 177056 [Multi-domain]  Cd Length: 99  Bit Score: 38.55  E-value: 3.11e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 15235586   78 TEKITIIfVDKDGEEIPVKVPIGMSVLEAAHENDIDLEGACEASlACSTC 127
Cdd:CHL00134   3 TYKVTLL-SEEEGIDVTIDCPDDVYILDAAEEQGIDLPYSCRAG-ACSTC 50
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
74-136 2.70e-03

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 37.77  E-value: 2.70e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15235586   74 GDEETEKITIIFVDKDGEeipVKVPIGMSVLEAAHENDIDLEGACEASLaCSTCHVIVMDTEY 136
Cdd:PRK10684 242 AEAATSGLTFTKLQPARE---FYAPVGTTLLEALESNKVPVVAACRAGV-CGCCKTKVVSGEY 300
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH