NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1002249911|ref|XP_015629147|]
View 

ferredoxin C 2, chloroplastic [Oryza sativa Japonica Group]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
60-156 1.82e-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 TIGR02008:

Pssm-ID: 444718 [Multi-domain]  Cd Length: 97  Bit Score: 91.36  E-value: 1.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002249911  60 THKVTVHDrQRGVVHEFVVPQDQYILHTAEAQDITLPFACRHGCCTSCAVRIKSGQIRQPEALGISAELKDKGYALLCVG 139
Cdd:TIGR02008   2 TYKVTLVN-PDGGEETIECPDDQYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVDQSDQSFLDDDQMEAGYVLTCVA 80
                          90
                  ....*....|....*..
gi 1002249911 140 FPTSDVEVETQDEDEVY 156
Cdd:TIGR02008  81 YPTSDCTIETHKEEDLY 97
 
Name Accession Description Interval E-value
fdx_plant TIGR02008
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ...
60-156 1.82e-24

ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ferredoxins. In general, these occur as a single domain proteins or with a chloroplast transit peptide. Species tend to be photosynthetic, but several forms may occur in one species and individually may not be associated with photocynthesis. Halobacterial forms differ somewhat in architecture; they score between trusted and noise cutoffs. Sequences scoring below the noise cutoff tend to be ferredoxin-related domains of larger proteins.


Pssm-ID: 273926 [Multi-domain]  Cd Length: 97  Bit Score: 91.36  E-value: 1.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002249911  60 THKVTVHDrQRGVVHEFVVPQDQYILHTAEAQDITLPFACRHGCCTSCAVRIKSGQIRQPEALGISAELKDKGYALLCVG 139
Cdd:TIGR02008   2 TYKVTLVN-PDGGEETIECPDDQYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVDQSDQSFLDDDQMEAGYVLTCVA 80
                          90
                  ....*....|....*..
gi 1002249911 140 FPTSDVEVETQDEDEVY 156
Cdd:TIGR02008  81 YPTSDCTIETHKEEDLY 97
petF CHL00134
ferredoxin; Validated
60-156 6.15e-24

ferredoxin; Validated


Pssm-ID: 177056 [Multi-domain]  Cd Length: 99  Bit Score: 90.16  E-value: 6.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002249911  60 THKVTVHDRQRGVVHEFVVPQDQYILHTAEAQDITLPFACRHGCCTSCAVRIKSGQIRQPEALGISAELKDKGYALLCVG 139
Cdd:CHL00134    3 TYKVTLLSEEEGIDVTIDCPDDVYILDAAEEQGIDLPYSCRAGACSTCAGKVTEGTVDQSDQSFLDDDQLEAGFVLTCVA 82
                          90
                  ....*....|....*..
gi 1002249911 140 FPTSDVEVETQDEDEVY 156
Cdd:CHL00134   83 YPTSDCTILTHQEEELY 99
Fdx COG0633
Ferredoxin [Energy production and conversion];
62-149 7.11e-23

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 87.21  E-value: 7.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002249911  62 KVTVHDRQrgvvHEFVVPQDQYILHTAEAQDITLPFACRHGCCTSCAVRIKSGQIRQPEALGISAELKDKGYALLCVGFP 141
Cdd:COG0633     3 KVTFIPEG----HTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQARP 78

                  ....*...
gi 1002249911 142 TSDVEVET 149
Cdd:COG0633    79 TSDLVVEL 86
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
63-148 7.01e-19

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: 76.66  E-value: 7.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002249911  63 VTVHDRQRGVvhEFVVPQDQYILHTAEAQDITLPFACRHGCCTSCAVRIKSGQIRQPEALGISAELKDKGYALLCVGFPT 142
Cdd:cd00207     1 VTINVPGSGV--EVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEEAEGGYVLACQTRVT 78

                  ....*.
gi 1002249911 143 SDVEVE 148
Cdd:cd00207    79 DGLVIE 84
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
71-142 2.60e-11

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 56.76  E-value: 2.60e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002249911  71 GVVHEFVVPQDQYILHTA-EAQDITLPFACRHGCCTSCAVRIKSGQIRQPEALGISAELKDKGYALLCVGFPT 142
Cdd:pfam00111   5 GKGVTIEVPDGETTLLDAaEEAGIDIPYSCRGGGCGTCAVKVLEGEDQSDQSFLEDDELAAGYVVLACQTYPK 77
 
Name Accession Description Interval E-value
fdx_plant TIGR02008
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ...
60-156 1.82e-24

ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ferredoxins. In general, these occur as a single domain proteins or with a chloroplast transit peptide. Species tend to be photosynthetic, but several forms may occur in one species and individually may not be associated with photocynthesis. Halobacterial forms differ somewhat in architecture; they score between trusted and noise cutoffs. Sequences scoring below the noise cutoff tend to be ferredoxin-related domains of larger proteins.


Pssm-ID: 273926 [Multi-domain]  Cd Length: 97  Bit Score: 91.36  E-value: 1.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002249911  60 THKVTVHDrQRGVVHEFVVPQDQYILHTAEAQDITLPFACRHGCCTSCAVRIKSGQIRQPEALGISAELKDKGYALLCVG 139
Cdd:TIGR02008   2 TYKVTLVN-PDGGEETIECPDDQYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVDQSDQSFLDDDQMEAGYVLTCVA 80
                          90
                  ....*....|....*..
gi 1002249911 140 FPTSDVEVETQDEDEVY 156
Cdd:TIGR02008  81 YPTSDCTIETHKEEDLY 97
petF CHL00134
ferredoxin; Validated
60-156 6.15e-24

ferredoxin; Validated


Pssm-ID: 177056 [Multi-domain]  Cd Length: 99  Bit Score: 90.16  E-value: 6.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002249911  60 THKVTVHDRQRGVVHEFVVPQDQYILHTAEAQDITLPFACRHGCCTSCAVRIKSGQIRQPEALGISAELKDKGYALLCVG 139
Cdd:CHL00134    3 TYKVTLLSEEEGIDVTIDCPDDVYILDAAEEQGIDLPYSCRAGACSTCAGKVTEGTVDQSDQSFLDDDQLEAGFVLTCVA 82
                          90
                  ....*....|....*..
gi 1002249911 140 FPTSDVEVETQDEDEVY 156
Cdd:CHL00134   83 YPTSDCTILTHQEEELY 99
Fdx COG0633
Ferredoxin [Energy production and conversion];
62-149 7.11e-23

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 87.21  E-value: 7.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002249911  62 KVTVHDRQrgvvHEFVVPQDQYILHTAEAQDITLPFACRHGCCTSCAVRIKSGQIRQPEALGISAELKDKGYALLCVGFP 141
Cdd:COG0633     3 KVTFIPEG----HTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQARP 78

                  ....*...
gi 1002249911 142 TSDVEVET 149
Cdd:COG0633    79 TSDLVVEL 86
PTZ00038 PTZ00038
ferredoxin; Provisional
28-156 4.63e-20

ferredoxin; Provisional


Pssm-ID: 240237 [Multi-domain]  Cd Length: 191  Bit Score: 82.96  E-value: 4.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002249911  28 GATTTTKARASGLRQVEGPVSERAYSSSSPAPT-HKVTVH--DRQRgvvhEFVVPQDQYILHTAEAQDITLPFACRHGCC 104
Cdd:PTZ00038   62 GNSKGNTSRPSSNGVTPGSSPVRSLLSLRRNPLfYNITLQtpDGEK----VIECDEDEYILDAAERQGVELPYSCRGGSC 137
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002249911 105 TSCAVRIKSGQIRQPEALGISAELKDKGYALLCVGFPTSDVEVETQDEDEVY 156
Cdd:PTZ00038  138 STCAAKLLEGEVDNEDQSYLDDEQLKKGYCLLCTCYPKSDCTIETHKEDELH 189
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
63-148 7.01e-19

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: 76.66  E-value: 7.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002249911  63 VTVHDRQRGVvhEFVVPQDQYILHTAEAQDITLPFACRHGCCTSCAVRIKSGQIRQPEALGISAELKDKGYALLCVGFPT 142
Cdd:cd00207     1 VTINVPGSGV--EVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEEAEGGYVLACQTRVT 78

                  ....*.
gi 1002249911 143 SDVEVE 148
Cdd:cd00207    79 DGLVIE 84
PLN03136 PLN03136
Ferredoxin; Provisional
26-155 4.80e-16

Ferredoxin; Provisional


Pssm-ID: 178681 [Multi-domain]  Cd Length: 148  Bit Score: 71.32  E-value: 4.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002249911  26 ARGATTTTKARASGLRQVEGPVSERAYSSSSPAPTHKVTVHDRQRGVVH-------EFVVPQ---------DQYILHTAE 89
Cdd:PLN03136    2 ASTALSSAIVSTSFLRRQQTPISLRSLPSANTQSLFGLKSSTARGGRVTamatykvKFITPEgeqeveceeDVYVLDAAE 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002249911  90 AQDITLPFACRHGCCTSCAVRIKSGQIRQPEALGISAELKDKGYALLCVGFPTSDVEVETQDEDEV 155
Cdd:PLN03136   82 EAGIDLPYSCRAGSCSSCAGKVVSGSIDQSDQSFLDDEQISEGYVLTCVAYPTSDVVIETHKEEAI 147
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
60-148 5.98e-13

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 65.66  E-value: 5.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002249911  60 THKVTVhdRQRGvvHEFVVPQDQYILHTAEAQDITLPFACRHGCCTSCAVRIKSGQIRQP--EALGISAELKDKGYALLC 137
Cdd:PRK07609    2 SFQVTL--QPSG--RQFTAEPDETILDAALRQGIHLPYGCKNGACGSCKGRLLEGEVEQGphQASALSGEERAAGEALTC 77
                          90
                  ....*....|.
gi 1002249911 138 VGFPTSDVEVE 148
Cdd:PRK07609   78 CAKPLSDLVLE 88
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
71-142 2.60e-11

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 56.76  E-value: 2.60e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002249911  71 GVVHEFVVPQDQYILHTA-EAQDITLPFACRHGCCTSCAVRIKSGQIRQPEALGISAELKDKGYALLCVGFPT 142
Cdd:pfam00111   5 GKGVTIEVPDGETTLLDAaEEAGIDIPYSCRGGGCGTCAVKVLEGEDQSDQSFLEDDELAAGYVVLACQTYPK 77
PRK05713 PRK05713
iron-sulfur-binding ferredoxin reductase;
74-151 1.95e-05

iron-sulfur-binding ferredoxin reductase;


Pssm-ID: 235575 [Multi-domain]  Cd Length: 312  Bit Score: 43.95  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002249911  74 HEFVVPQDQYILHTAEAQDITLPFACRHGCCTSCAVRIKSGQIR--QPEALgiSAELKDKGYALLCVGFPTSDVEVETQD 151
Cdd:PRK05713    9 RRWSVPAGSNLLDALNAAGVAVPYSCRAGSCHACLVRCLQGEPEdaLPEAL--AAEKREQGWRLACQCRVVGDLRVEVFD 86
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
75-148 8.44e-05

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 42.00  E-value: 8.44e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002249911  75 EFVVPQDQYILHTAEAQDITLPFACRHGCCTSCAVRIKSGQIRQPEALGISAELKDKGYALLCVGFPTSDVEVE 148
Cdd:PRK10684  259 EFYAPVGTTLLEALESNKVPVVAACRAGVCGCCKTKVVSGEYTVSSTMTLTPAEIAQGYVLACSCHPQGDLVLA 332
 
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