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Conserved domains on  [gi|1376820971|gb|PTQ14677|]
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ferredoxin [Vibrio splendidus]

Protein Classification

similar to 2Fe-2S ferredoxin-5( domain architecture ID 10001920)

protein similar to 2Fe-2S ferredoxin-5

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Fdx COG0633
Ferredoxin [Energy production and conversion];
1-88 2.09e-24

Ferredoxin [Energy production and conversion];


:

Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 87.60  E-value: 2.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376820971  1 MSYqVVLYPENISFTVEKGQTVLDAALNSDIYFPNRCQVGACAMCMCRKLEGQVSYHLEPMLTEKEQQQGWIFACQAFAE 80
Cdd:COG0633    1 MPK-VTFIPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQARPT 79


                 ....*...
gi 1376820971 81 SNLVLTFA 88
Cdd:COG0633   80 SDLVVELP 87
 
Name Accession Description Interval E-value
Fdx COG0633
Ferredoxin [Energy production and conversion];
1-88 2.09e-24

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 87.60  E-value: 2.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376820971  1 MSYqVVLYPENISFTVEKGQTVLDAALNSDIYFPNRCQVGACAMCMCRKLEGQVSYHLEPMLTEKEQQQGWIFACQAFAE 80
Cdd:COG0633    1 MPK-VTFIPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQARPT 79


                 ....*...
gi 1376820971 81 SNLVLTFA 88
Cdd:COG0633   80 SDLVVELP 87
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 1-85 6.59e-22

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 86.85  E-value: 6.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376820971   1 MSYQVVLYPENISFTVEKGQTVLDAALNSDIYFPNRCQVGACAMCMCRKLEGQVSY--HLEPMLTEKEQQQGWIFACQAF 78
Cdd:PRK07609    1 MSFQVTLQPSGRQFTAEPDETILDAALRQGIHLPYGCKNGACGSCKGRLLEGEVEQgpHQASALSGEERAAGEALTCCAK 80


                  ....*..
gi 1376820971  79 AESNLVL 85
Cdd:PRK07609   81 PLSDLVL 87
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 4-86 4.75e-18

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: 71.27  E-value: 4.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376820971  4 QVVLYPENISFTVEKGQTVLDAALNSDIYFPNRCQVGACAMCMCRKLEGQVSYHLEPMLTEKEQQQGWIFACQAFAESNL 83
Cdd:cd00207    2 TINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEEAEGGYVLACQTRVTDGL 81


                 ...
gi 1376820971 84 VLT 86
Cdd:cd00207   82 VIE 84
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
5-80 8.80e-10

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 50.22  E-value: 8.80e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1376820971  5 VVLYPENISFTVEKGQT-VLDAALNSDIYFPNRCQVGACAMCMCRKLEGQVSYHLEPMLTEKEQQQGWIFACQAFAE 80
Cdd:pfam00111  1 VTINGKGVTIEVPDGETtLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDQSDQSFLEDDELAAGYVVLACQTYPK 77
fdx_plant TIGR02008
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ...
 2-85 1.51e-07

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: 44.75  E-value: 1.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376820971  2 SYQVVLYPE---NISFTVEKGQTVLDAALNSDIYFPNRCQVGACAMCMCRKLEGQVSYHLEPMLTEKEQQQGWIFACQAF 78
Cdd:TIGR02008  2 TYKVTLVNPdggEETIECPDDQYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVDQSDQSFLDDDQMEAGYVLTCVAY 81


                 ....*..
gi 1376820971 79 AESNLVL 85
Cdd:TIGR02008 82 PTSDCTI 88
 
Name Accession Description Interval E-value
Fdx COG0633
Ferredoxin [Energy production and conversion];
1-88 2.09e-24

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 87.60  E-value: 2.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376820971  1 MSYqVVLYPENISFTVEKGQTVLDAALNSDIYFPNRCQVGACAMCMCRKLEGQVSYHLEPMLTEKEQQQGWIFACQAFAE 80
Cdd:COG0633    1 MPK-VTFIPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQARPT 79


                 ....*...
gi 1376820971 81 SNLVLTFA 88
Cdd:COG0633   80 SDLVVELP 87
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 1-85 6.59e-22

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 86.85  E-value: 6.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376820971   1 MSYQVVLYPENISFTVEKGQTVLDAALNSDIYFPNRCQVGACAMCMCRKLEGQVSY--HLEPMLTEKEQQQGWIFACQAF 78
Cdd:PRK07609    1 MSFQVTLQPSGRQFTAEPDETILDAALRQGIHLPYGCKNGACGSCKGRLLEGEVEQgpHQASALSGEERAAGEALTCCAK 80


                  ....*..
gi 1376820971  79 AESNLVL 85
Cdd:PRK07609   81 PLSDLVL 87
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 4-86 4.75e-18

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: 71.27  E-value: 4.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376820971  4 QVVLYPENISFTVEKGQTVLDAALNSDIYFPNRCQVGACAMCMCRKLEGQVSYHLEPMLTEKEQQQGWIFACQAFAESNL 83
Cdd:cd00207    2 TINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEEAEGGYVLACQTRVTDGL 81


                 ...
gi 1376820971 84 VLT 86
Cdd:cd00207   82 VIE 84
COG3894 COG3894
Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain ...
 1-84 1.96e-13

Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain [Function unknown];


Pssm-ID: 443101 [Multi-domain]  Cd Length: 621  Bit Score: 63.67  E-value: 1.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376820971   1 MS-YQVVLYPENISFTVEKGQTVLDAALNSDIYFPNRCQ-VGACAMCMCRKLEGQVSYHLEP---MLTEKEQQQGWIFAC 75
Cdd:COG3894     1 MPkVKVTFLPSGKRVEVEAGTTLLDAAREAGVDIDAPCGgRGTCGKCKVKVEEGEFSPVTEEerrLLSPEELAEGYRLAC 80


                  ....*....
gi 1376820971  76 QAFAESNLV 84
Cdd:COG3894    81 QARVLGDLV 89
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
5-80 8.80e-10

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 50.22  E-value: 8.80e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1376820971  5 VVLYPENISFTVEKGQT-VLDAALNSDIYFPNRCQVGACAMCMCRKLEGQVSYHLEPMLTEKEQQQGWIFACQAFAE 80
Cdd:pfam00111  1 VTINGKGVTIEVPDGETtLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDQSDQSFLEDDELAAGYVVLACQTYPK 77
PRK05713 PRK05713
iron-sulfur-binding ferredoxin reductase;
13-76 2.07e-08

iron-sulfur-binding ferredoxin reductase;


Pssm-ID: 235575 [Multi-domain]  Cd Length: 312  Bit Score: 49.34  E-value: 2.07e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1376820971  13 SFTVEKGQTVLDAALNSDIYFPNRCQVGACAMCMCRKLEGQVSYHLEPMLTEKEQQQGWIFACQ 76
Cdd:PRK05713   10 RWSVPAGSNLLDALNAAGVAVPYSCRAGSCHACLVRCLQGEPEDALPEALAAEKREQGWRLACQ 73
fdx_plant TIGR02008
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ...
 2-85 1.51e-07

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: 44.75  E-value: 1.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376820971  2 SYQVVLYPE---NISFTVEKGQTVLDAALNSDIYFPNRCQVGACAMCMCRKLEGQVSYHLEPMLTEKEQQQGWIFACQAF 78
Cdd:TIGR02008  2 TYKVTLVNPdggEETIECPDDQYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVDQSDQSFLDDDQMEAGYVLTCVAY 81


                 ....*..
gi 1376820971 79 AESNLVL 85
Cdd:TIGR02008 82 PTSDCTI 88
petF CHL00134
ferredoxin; Validated
 1-82 1.53e-07

ferredoxin; Validated


Pssm-ID: 177056 [Multi-domain]  Cd Length: 99  Bit Score: 44.71  E-value: 1.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376820971  1 MSYQVVLY--PENISFTVE--KGQTVLDAALNSDIYFPNRCQVGACAMCMCRKLEGQVSYHLEPMLTEKEQQQGWIFACQ 76
Cdd:CHL00134   2 ATYKVTLLseEEGIDVTIDcpDDVYILDAAEEQGIDLPYSCRAGACSTCAGKVTEGTVDQSDQSFLDDDQLEAGFVLTCV 81


                 ....*.
gi 1376820971 77 AFAESN 82
Cdd:CHL00134  82 AYPTSD 87
PTZ00038 PTZ00038
ferredoxin; Provisional
 22-85 7.88e-07

ferredoxin; Provisional


Pssm-ID: 240237 [Multi-domain]  Cd Length: 191  Bit Score: 44.44  E-value: 7.88e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1376820971  22 VLDAALNSDIYFPNRCQVGACAMCMCRKLEGQVSYHLEPMLTEKEQQQGWIFACQAFAESNLVL 85
Cdd:PTZ00038  117 ILDAAERQGVELPYSCRGGSCSTCAAKLLEGEVDNEDQSYLDDEQLKKGYCLLCTCYPKSDCTI 180
PLN03136 PLN03136
Ferredoxin; Provisional
 22-85 1.05e-06

Ferredoxin; Provisional


Pssm-ID: 178681 [Multi-domain]  Cd Length: 148  Bit Score: 43.58  E-value: 1.05e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1376820971  22 VLDAALNSDIYFPNRCQVGACAMCMCRKLEGQVSYHLEPMLTEKEQQQGWIFACQAFAESNLVL 85
Cdd:PLN03136   76 VLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSIDQSDQSFLDDEQISEGYVLTCVAYPTSDVVI 139
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
14-87 9.17e-06

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 42.04  E-value: 9.17e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1376820971  14 FTVEKGQTVLDAALNSDIYFPNRCQVGACAMCMCRKLEGQVS--YHLEPMLTEKEQQQGWIFACQAFAESNLVLTF 87
Cdd:PRK11872   17 FPVGKDELLLDAALRNGINLPLDCREGVCGTCQGRCESGIYSqdYVDEDALSERDLAQRKMLACQTRVKSDAAFYF 92
NuoG COG1034
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ...
 11-46 4.48e-04

NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440657 [Multi-domain]  Cd Length: 453  Bit Score: 37.13  E-value: 4.48e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1376820971  11 NISFTVEKGQTVLDAALNSDIYFPNRCQ------VGACAMCM 46
Cdd:COG1034     8 GKEVEVPKGTTVLQAAEKAGIEIPRFCYhpklsiAGACRMCL 49
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 13-85 1.74e-03

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 35.45  E-value: 1.74e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1376820971  13 SFTVEKGQTVLDAALNSDIYFPNRCQVGACAMCMCRKLEGQVSYHLEPMLTEKEQQQGWIFACQAFAESNLVL 85
Cdd:PRK10684  259 EFYAPVGTTLLEALESNKVPVVAACRAGVCGCCKTKVVSGEYTVSSTMTLTPAEIAQGYVLACSCHPQGDLVL 331
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 4-46 2.42e-03

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 35.09  E-value: 2.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1376820971   4 QVVLYPENISFTVEKGQTVLDAALNSDIYFPNRC------QVGACAMCM 46
Cdd:PRK12814    3 TISLTINGRSVTAAPGTSILEAAASAGITIPTLCfhqeleATGSCWMCI 51
PRK10713 PRK10713
2Fe-2S ferredoxin-like protein;
17-75 2.60e-03

2Fe-2S ferredoxin-like protein;


Pssm-ID: 182668 [Multi-domain]  Cd Length: 84  Bit Score: 33.55  E-value: 2.60e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 1376820971 17 EKGQTVLDAALNSDIYFPNRCQVGACAMCMCRKLEGQVSYHLEPMLTekeQQQGWIFAC 75
Cdd:PRK10713  17 DEHPSLLAALESHNVAVEYQCREGYCGSCRTRLVAGQVDWIAEPLAF---IQPGEILPC 72
Fer2_4 pfam13510
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 4-46 5.03e-03

2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which a beta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated. This cluster appears within sarcosine oxidase proteins.


Pssm-ID: 433268 [Multi-domain]  Cd Length: 82  Bit Score: 32.90  E-value: 5.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 1376820971  4 QVVLYPENISFTVEKGQTVLDAALNSDIYFP-------NR---CQVGACAMCM 46
Cdd:pfam13510  3 PVTFTFDGRPVTAPEGDTIAAALLANGVRVPrsckygrPRgifCAMGECRNCL 55
 
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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