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Conserved domains on  [gi|221061015|ref|XP_002262077|]
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ferredoxin, putative [Plasmodium knowlesi strain H]

Protein Classification

ferredoxin( domain architecture ID 11487921)

ferredoxin is an iron-sulfur protein transferring electrons in a wide variety of metabolic reactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00038 PTZ00038
ferredoxin; Provisional
 14-196 1.58e-105

ferredoxin; Provisional


:

Pssm-ID: 240237 [Multi-domain]  Cd Length: 191  Bit Score: 300.99  E-value: 1.58e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221061015  14 TEKSSTYRFSnnrtalkyMSGSRGINICAPQRRACSSFINNLVSSKKASCLPVGGDRGVNARNTSSNLSNDGGKRRYFKS 93
Cdd:PTZ00038  17 GTYSSVSVNY--------MSADLAFSICSGRRRSSASFISSSASPNRASCYSLGNSKGNTSRPSSNGVTPGSSPVRSLLS 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221061015  94 VNRNKLFYNITLRTNDGEKKIQCDEDEYILDASERQNVELPYSCRGGSCSTCAAKLIEGEVDNEDQSYLDEEQLKKKYIL 173
Cdd:PTZ00038  89 LRRNPLFYNITLQTPDGEKVIECDEDEYILDAAERQGVELPYSCRGGSCSTCAAKLLEGEVDNEDQSYLDDEQLKKGYCL 168

                        170       180
                 ....*....|....*....|...
gi 221061015 174 LCTCYPKSDCVIETHKEEELHDM 196
Cdd:PTZ00038 169 LCTCYPKSDCTIETHKEDELHDE 191
 
Name Accession Description Interval E-value
PTZ00038 PTZ00038
ferredoxin; Provisional
 14-196 1.58e-105

ferredoxin; Provisional


Pssm-ID: 240237 [Multi-domain]  Cd Length: 191  Bit Score: 300.99  E-value: 1.58e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221061015  14 TEKSSTYRFSnnrtalkyMSGSRGINICAPQRRACSSFINNLVSSKKASCLPVGGDRGVNARNTSSNLSNDGGKRRYFKS 93
Cdd:PTZ00038  17 GTYSSVSVNY--------MSADLAFSICSGRRRSSASFISSSASPNRASCYSLGNSKGNTSRPSSNGVTPGSSPVRSLLS 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221061015  94 VNRNKLFYNITLRTNDGEKKIQCDEDEYILDASERQNVELPYSCRGGSCSTCAAKLIEGEVDNEDQSYLDEEQLKKKYIL 173
Cdd:PTZ00038  89 LRRNPLFYNITLQTPDGEKVIECDEDEYILDAAERQGVELPYSCRGGSCSTCAAKLLEGEVDNEDQSYLDDEQLKKGYCL 168

                        170       180
                 ....*....|....*....|...
gi 221061015 174 LCTCYPKSDCVIETHKEEELHDM 196
Cdd:PTZ00038 169 LCTCYPKSDCTIETHKEDELHDE 191
fdx_plant TIGR02008
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ...
 101-193 1.40e-43

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: 140.67  E-value: 1.40e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221061015  101 YNITLRTNDG-EKKIQCDEDEYILDASERQNVELPYSCRGGSCSTCAAKLIEGEVDNEDQSYLDEEQLKKKYILLCTCYP 179
Cdd:TIGR02008   3 YKVTLVNPDGgEETIECPDDQYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVDQSDQSFLDDDQMEAGYVLTCVAYP 82

                          90
                  ....*....|....
gi 221061015  180 KSDCVIETHKEEEL 193
Cdd:TIGR02008  83 TSDCTIETHKEEDL 96
Fdx COG0633
Ferredoxin [Energy production and conversion];
102-188 2.26e-30

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 106.47  E-value: 2.26e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221061015 102 NITLRTNDGEkkIQCDEDEYILDASERQNVELPYSCRGGSCSTCAAKLIEGEVDNEDQSYLDEEQLKKKYILLCTCYPKS 181
Cdd:COG0633    3 KVTFIPEGHT--VEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQARPTS 80


                 ....*..
gi 221061015 182 DCVIETH 188
Cdd:COG0633   81 DLVVELP 87
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 103-186 2.57e-30

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: 106.33  E-value: 2.57e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221061015 103 ITLRTNDGEKKIQCDEDEYILDASERQNVELPYSCRGGSCSTCAAKLIEGEVDNEDQSYLDEEQLKKKYILLCTCYPKSD 182
Cdd:cd00207    1 VTINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEEAEGGYVLACQTRVTDG 80


                 ....
gi 221061015 183 CVIE 186
Cdd:cd00207   81 LVIE 84
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
108-180 2.19e-16

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 70.25  E-value: 2.19e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221061015  108 NDGEKKIQCDEDEY-ILDASERQNVELPYSCRGGSCSTCAAKLIEGEvDNEDQSYLDEEQLKKKYILL-CTCYPK 180
Cdd:pfam00111   4 NGKGVTIEVPDGETtLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGE-DQSDQSFLEDDELAAGYVVLaCQTYPK 77
 
Name Accession Description Interval E-value
PTZ00038 PTZ00038
ferredoxin; Provisional
 14-196 1.58e-105

ferredoxin; Provisional


Pssm-ID: 240237 [Multi-domain]  Cd Length: 191  Bit Score: 300.99  E-value: 1.58e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221061015  14 TEKSSTYRFSnnrtalkyMSGSRGINICAPQRRACSSFINNLVSSKKASCLPVGGDRGVNARNTSSNLSNDGGKRRYFKS 93
Cdd:PTZ00038  17 GTYSSVSVNY--------MSADLAFSICSGRRRSSASFISSSASPNRASCYSLGNSKGNTSRPSSNGVTPGSSPVRSLLS 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221061015  94 VNRNKLFYNITLRTNDGEKKIQCDEDEYILDASERQNVELPYSCRGGSCSTCAAKLIEGEVDNEDQSYLDEEQLKKKYIL 173
Cdd:PTZ00038  89 LRRNPLFYNITLQTPDGEKVIECDEDEYILDAAERQGVELPYSCRGGSCSTCAAKLLEGEVDNEDQSYLDDEQLKKGYCL 168

                        170       180
                 ....*....|....*....|...
gi 221061015 174 LCTCYPKSDCVIETHKEEELHDM 196
Cdd:PTZ00038 169 LCTCYPKSDCTIETHKEDELHDE 191
petF CHL00134
ferredoxin; Validated
 101-194 8.16e-44

ferredoxin; Validated


Pssm-ID: 177056 [Multi-domain]  Cd Length: 99  Bit Score: 141.40  E-value: 8.16e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221061015 101 YNITL--RTNDGEKKIQCDEDEYILDASERQNVELPYSCRGGSCSTCAAKLIEGEVDNEDQSYLDEEQLKKKYILLCTCY 178
Cdd:CHL00134   4 YKVTLlsEEEGIDVTIDCPDDVYILDAAEEQGIDLPYSCRAGACSTCAGKVTEGTVDQSDQSFLDDDQLEAGFVLTCVAY 83

                         90
                 ....*....|....*.
gi 221061015 179 PKSDCVIETHKEEELH 194
Cdd:CHL00134  84 PTSDCTILTHQEEELY 99
fdx_plant TIGR02008
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ...
 101-193 1.40e-43

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: 140.67  E-value: 1.40e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221061015  101 YNITLRTNDG-EKKIQCDEDEYILDASERQNVELPYSCRGGSCSTCAAKLIEGEVDNEDQSYLDEEQLKKKYILLCTCYP 179
Cdd:TIGR02008   3 YKVTLVNPDGgEETIECPDDQYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVDQSDQSFLDDDQMEAGYVLTCVAYP 82

                          90
                  ....*....|....
gi 221061015  180 KSDCVIETHKEEEL 193
Cdd:TIGR02008  83 TSDCTIETHKEEDL 96
PLN03136 PLN03136
Ferredoxin; Provisional
 101-193 1.50e-36

Ferredoxin; Provisional


Pssm-ID: 178681 [Multi-domain]  Cd Length: 148  Bit Score: 124.48  E-value: 1.50e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221061015 101 YNITLRTNDGEKKIQCDEDEYILDASERQNVELPYSCRGGSCSTCAAKLIEGEVDNEDQSYLDEEQLKKKYILLCTCYPK 180
Cdd:PLN03136  55 YKVKFITPEGEQEVECEEDVYVLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSIDQSDQSFLDDEQISEGYVLTCVAYPT 134

                         90
                 ....*....|...
gi 221061015 181 SDCVIETHKEEEL 193
Cdd:PLN03136 135 SDVVIETHKEEAI 147
Fdx COG0633
Ferredoxin [Energy production and conversion];
102-188 2.26e-30

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 106.47  E-value: 2.26e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221061015 102 NITLRTNDGEkkIQCDEDEYILDASERQNVELPYSCRGGSCSTCAAKLIEGEVDNEDQSYLDEEQLKKKYILLCTCYPKS 181
Cdd:COG0633    3 KVTFIPEGHT--VEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQARPTS 80


                 ....*..
gi 221061015 182 DCVIETH 188
Cdd:COG0633   81 DLVVELP 87
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 103-186 2.57e-30

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: 106.33  E-value: 2.57e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221061015 103 ITLRTNDGEKKIQCDEDEYILDASERQNVELPYSCRGGSCSTCAAKLIEGEVDNEDQSYLDEEQLKKKYILLCTCYPKSD 182
Cdd:cd00207    1 VTINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEEAEGGYVLACQTRVTDG 80


                 ....
gi 221061015 183 CVIE 186
Cdd:cd00207   81 LVIE 84
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 101-186 2.63e-23

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 94.55  E-value: 2.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221061015 101 YNITLRTNDgeKKIQCDEDEYILDASERQNVELPYSCRGGSCSTCAAKLIEGEVDNED--QSYLDEEQLKKKYILLCTCY 178
Cdd:PRK07609   3 FQVTLQPSG--RQFTAEPDETILDAALRQGIHLPYGCKNGACGSCKGRLLEGEVEQGPhqASALSGEERAAGEALTCCAK 80


                 ....*...
gi 221061015 179 PKSDCVIE 186
Cdd:PRK07609  81 PLSDLVLE 88
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
108-180 2.19e-16

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 70.25  E-value: 2.19e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221061015  108 NDGEKKIQCDEDEY-ILDASERQNVELPYSCRGGSCSTCAAKLIEGEvDNEDQSYLDEEQLKKKYILL-CTCYPK 180
Cdd:pfam00111   4 NGKGVTIEVPDGETtLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGE-DQSDQSFLEDDELAAGYVVLaCQTYPK 77
COG3894 COG3894
Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain ...
 110-194 3.62e-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: 67.14  E-value: 3.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221061015 110 GEKKIQCDEDEYILDASERQNVELPYSCRG-GSCSTCAAKLIEGE---VDNEDQSYLDEEQLKKKYILLCTCYPKSDCVI 185
Cdd:COG3894   11 SGKRVEVEAGTTLLDAAREAGVDIDAPCGGrGTCGKCKVKVEEGEfspVTEEERRLLSPEELAEGYRLACQARVLGDLVV 90


                 ....*....
gi 221061015 186 ETHKEEELH 194
Cdd:COG3894   91 EVPPESRLD 99
PRK10713 PRK10713
2Fe-2S ferredoxin-like protein;
103-186 2.67e-10

2Fe-2S ferredoxin-like protein;


Pssm-ID: 182668 [Multi-domain]  Cd Length: 84  Bit Score: 54.73  E-value: 2.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221061015 103 ITLRTNDGEkkIQC-DEDEYILDASERQNVELPYSCRGGSCSTCAAKLIEGEVDnedqsYLDEEQ--LKKKYILLCTCYP 179
Cdd:PRK10713   4 VTLRITGTQ--LLCqDEHPSLLAALESHNVAVEYQCREGYCGSCRTRLVAGQVD-----WIAEPLafIQPGEILPCCCRA 76


                 ....*..
gi 221061015 180 KSDCVIE 186
Cdd:PRK10713  77 KGDIEIE 83
PRK05713 PRK05713
iron-sulfur-binding ferredoxin reductase;
110-187 1.38e-07

iron-sulfur-binding ferredoxin reductase;


Pssm-ID: 235575 [Multi-domain]  Cd Length: 312  Bit Score: 50.49  E-value: 1.38e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221061015 110 GEKKIQCDEDEYILDASERQNVELPYSCRGGSCSTCAAKLIEGEVDNEDQSYLDEEQLKKKYILLCTCYPKSDCVIET 187
Cdd:PRK05713   7 GERRWSVPAGSNLLDALNAAGVAVPYSCRAGSCHACLVRCLQGEPEDALPEALAAEKREQGWRLACQCRVVGDLRVEV 84
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
118-182 3.34e-07

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 49.36  E-value: 3.34e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221061015 118 EDEYILDASERQNVELPYSCRGGSCSTCAAKLIEG--EVDNEDQSYLDEEQLKKKYILLCTCYPKSD 182
Cdd:PRK11872  21 KDELLLDAALRNGINLPLDCREGVCGTCQGRCESGiySQDYVDEDALSERDLAQRKMLACQTRVKSD 87
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 122-186 9.67e-07

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 47.78  E-value: 9.67e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221061015 122 ILDASERQNVELPYSCRGGSCSTCAAKLIEGEVDNEDQSYLDEEQLKKKYILLCTCYPKSDCVIE 186
Cdd:PRK10684 268 LLEALESNKVPVVAACRAGVCGCCKTKVVSGEYTVSSTMTLTPAEIAQGYVLACSCHPQGDLVLA 332
PRK08493 PRK08493
NADH-quinone oxidoreductase subunit G;
103-191 1.68e-03

NADH-quinone oxidoreductase subunit G;


Pssm-ID: 236277 [Multi-domain]  Cd Length: 819  Bit Score: 38.53  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221061015 103 ITLRTNDgeKKIQCDEDEYILDASERQNVELPYSCRGGSCSTCAA-KLIEGEVDNedqsyldeeqlkkKYILLCTCYPKS 181
Cdd:PRK08493   2 ITITING--KECEAQEGEYILNVARRNGIFIPAICYLSGCSPTLAcRLCMVEADG-------------KRVYSCNTKAKE 66

                         90
                 ....*....|
gi 221061015 182 DCVIETHKEE 191
Cdd:PRK08493  67 GMNILTNTPN 76
 
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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