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Conserved domains on  [gi|84996039|ref|XP_952741|]
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ferredoxin, putative [Theileria annulata]

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
 1-170 9.87e-97

ferredoxin; Provisional


:

Pssm-ID: 240237 [Multi-domain]  Cd Length: 191  Bit Score: 278.26  E-value: 9.87e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84996039    1 MFLFFIHVCYLVFCSV-----------VACITNRRFSTSFINSP----RNFSYSLSNSNLNTFSQPFNKGIERELINSSK 65
Cdd:PTZ00038   7 SFLFLLLTLLGTYSSVsvnymsadlafSICSGRRRSSASFISSSaspnRASCYSLGNSKGNTSRPSSNGVTPGSSPVRSL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84996039   66 FSDRRIPLYYAVKLVLPEGEKVIESAEDEYILESAESQGVELPYSCRGGSCSTCAATLVSGEIDNSEQSYLDDDQVKKGY 145
Cdd:PTZ00038  87 LSLRRNPLFYNITLQTPDGEKVIECDEDEYILDAAERQGVELPYSCRGGSCSTCAAKLLEGEVDNEDQSYLDDEQLKKGY 166

                        170       180
                 ....*....|....*....|....*
gi 84996039  146 CLLCTSYAKSDCTIETHKEDKLHEE 170
Cdd:PTZ00038 167 CLLCTCYPKSDCTIETHKEDELHDE 191
 
Name Accession Description Interval E-value
PTZ00038 PTZ00038
ferredoxin; Provisional
 1-170 9.87e-97

ferredoxin; Provisional


Pssm-ID: 240237 [Multi-domain]  Cd Length: 191  Bit Score: 278.26  E-value: 9.87e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84996039    1 MFLFFIHVCYLVFCSV-----------VACITNRRFSTSFINSP----RNFSYSLSNSNLNTFSQPFNKGIERELINSSK 65
Cdd:PTZ00038   7 SFLFLLLTLLGTYSSVsvnymsadlafSICSGRRRSSASFISSSaspnRASCYSLGNSKGNTSRPSSNGVTPGSSPVRSL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84996039   66 FSDRRIPLYYAVKLVLPEGEKVIESAEDEYILESAESQGVELPYSCRGGSCSTCAATLVSGEIDNSEQSYLDDDQVKKGY 145
Cdd:PTZ00038  87 LSLRRNPLFYNITLQTPDGEKVIECDEDEYILDAAERQGVELPYSCRGGSCSTCAAKLLEGEVDNEDQSYLDDEQLKKGY 166

                        170       180
                 ....*....|....*....|....*
gi 84996039  146 CLLCTSYAKSDCTIETHKEDKLHEE 170
Cdd:PTZ00038 167 CLLCTCYPKSDCTIETHKEDELHDE 191
fdx_plant TIGR02008
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ...
 75-167 2.63e-44

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: 141.82  E-value: 2.63e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84996039    75 YAVKLVLPEG-EKVIESAEDEYILESAESQGVELPYSCRGGSCSTCAATLVSGEIDNSEQSYLDDDQVKKGYCLLCTSYA 153
Cdd:TIGR02008   3 YKVTLVNPDGgEETIECPDDQYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVDQSDQSFLDDDQMEAGYVLTCVAYP 82

                          90
                  ....*....|....
gi 84996039   154 KSDCTIETHKEDKL 167
Cdd:TIGR02008  83 TSDCTIETHKEEDL 96
Fdx COG0633
Ferredoxin [Energy production and conversion];
80-162 5.59e-29

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 102.62  E-value: 5.59e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84996039  80 VLPEGeKVIESAEDEYILESAESQGVELPYSCRGGSCSTCAATLVSGEIDNSEQSYLDDDQVKKGYCLLCTSYAKSDCTI 159
Cdd:COG0633   6 FIPEG-HTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQARPTSDLVV 84


                ...
gi 84996039 160 ETH 162
Cdd:COG0633  85 ELP 87
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 77-160 1.57e-26

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: 96.31  E-value: 1.57e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84996039  77 VKLVLPEGEKVIESAEDEYILESAESQGVELPYSCRGGSCSTCAATLVSGEIDNSEQSYLDDDQVKKGYCLLCTSYAKSD 156
Cdd:cd00207   1 VTINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEEAEGGYVLACQTRVTDG 80


                ....
gi 84996039 157 CTIE 160
Cdd:cd00207  81 LVIE 84
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
85-154 1.37e-15

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 67.93  E-value: 1.37e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 84996039    85 EKVIESAEDEY-ILESAESQGVELPYSCRGGSCSTCAATLVSGEiDNSEQSYLDDDQVKKGYCLL-CTSYAK 154
Cdd:pfam00111   7 GVTIEVPDGETtLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGE-DQSDQSFLEDDELAAGYVVLaCQTYPK 77
 
Name Accession Description Interval E-value
PTZ00038 PTZ00038
ferredoxin; Provisional
 1-170 9.87e-97

ferredoxin; Provisional


Pssm-ID: 240237 [Multi-domain]  Cd Length: 191  Bit Score: 278.26  E-value: 9.87e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84996039    1 MFLFFIHVCYLVFCSV-----------VACITNRRFSTSFINSP----RNFSYSLSNSNLNTFSQPFNKGIERELINSSK 65
Cdd:PTZ00038   7 SFLFLLLTLLGTYSSVsvnymsadlafSICSGRRRSSASFISSSaspnRASCYSLGNSKGNTSRPSSNGVTPGSSPVRSL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84996039   66 FSDRRIPLYYAVKLVLPEGEKVIESAEDEYILESAESQGVELPYSCRGGSCSTCAATLVSGEIDNSEQSYLDDDQVKKGY 145
Cdd:PTZ00038  87 LSLRRNPLFYNITLQTPDGEKVIECDEDEYILDAAERQGVELPYSCRGGSCSTCAAKLLEGEVDNEDQSYLDDEQLKKGY 166

                        170       180
                 ....*....|....*....|....*
gi 84996039  146 CLLCTSYAKSDCTIETHKEDKLHEE 170
Cdd:PTZ00038 167 CLLCTCYPKSDCTIETHKEDELHDE 191
fdx_plant TIGR02008
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ...
 75-167 2.63e-44

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: 141.82  E-value: 2.63e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84996039    75 YAVKLVLPEG-EKVIESAEDEYILESAESQGVELPYSCRGGSCSTCAATLVSGEIDNSEQSYLDDDQVKKGYCLLCTSYA 153
Cdd:TIGR02008   3 YKVTLVNPDGgEETIECPDDQYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVDQSDQSFLDDDQMEAGYVLTCVAYP 82

                          90
                  ....*....|....
gi 84996039   154 KSDCTIETHKEDKL 167
Cdd:TIGR02008  83 TSDCTIETHKEEDL 96
petF CHL00134
ferredoxin; Validated
 75-168 1.94e-42

ferredoxin; Validated


Pssm-ID: 177056 [Multi-domain]  Cd Length: 99  Bit Score: 137.16  E-value: 1.94e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84996039   75 YAVKLVL-PEG-EKVIESAEDEYILESAESQGVELPYSCRGGSCSTCAATLVSGEIDNSEQSYLDDDQVKKGYCLLCTSY 152
Cdd:CHL00134   4 YKVTLLSeEEGiDVTIDCPDDVYILDAAEEQGIDLPYSCRAGACSTCAGKVTEGTVDQSDQSFLDDDQLEAGFVLTCVAY 83

                         90
                 ....*....|....*.
gi 84996039  153 AKSDCTIETHKEDKLH 168
Cdd:CHL00134  84 PTSDCTILTHQEEELY 99
PLN03136 PLN03136
Ferredoxin; Provisional
 75-167 5.10e-36

Ferredoxin; Provisional


Pssm-ID: 178681 [Multi-domain]  Cd Length: 148  Bit Score: 122.55  E-value: 5.10e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84996039   75 YAVKLVLPEGEKVIESAEDEYILESAESQGVELPYSCRGGSCSTCAATLVSGEIDNSEQSYLDDDQVKKGYCLLCTSYAK 154
Cdd:PLN03136  55 YKVKFITPEGEQEVECEEDVYVLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSIDQSDQSFLDDEQISEGYVLTCVAYPT 134

                         90
                 ....*....|...
gi 84996039  155 SDCTIETHKEDKL 167
Cdd:PLN03136 135 SDVVIETHKEEAI 147
Fdx COG0633
Ferredoxin [Energy production and conversion];
80-162 5.59e-29

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 102.62  E-value: 5.59e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84996039  80 VLPEGeKVIESAEDEYILESAESQGVELPYSCRGGSCSTCAATLVSGEIDNSEQSYLDDDQVKKGYCLLCTSYAKSDCTI 159
Cdd:COG0633   6 FIPEG-HTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQARPTSDLVV 84


                ...
gi 84996039 160 ETH 162
Cdd:COG0633  85 ELP 87
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 77-160 1.57e-26

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: 96.31  E-value: 1.57e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84996039  77 VKLVLPEGEKVIESAEDEYILESAESQGVELPYSCRGGSCSTCAATLVSGEIDNSEQSYLDDDQVKKGYCLLCTSYAKSD 156
Cdd:cd00207   1 VTINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEEAEGGYVLACQTRVTDG 80


                ....
gi 84996039 157 CTIE 160
Cdd:cd00207  81 LVIE 84
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 80-160 1.28e-20

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 86.85  E-value: 1.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84996039   80 VLPEGeKVIESAEDEYILESAESQGVELPYSCRGGSCSTCAATLVSGEIDNS--EQSYLDDDQVKKGYCLLCTSYAKSDC 157
Cdd:PRK07609   7 LQPSG-RQFTAEPDETILDAALRQGIHLPYGCKNGACGSCKGRLLEGEVEQGphQASALSGEERAAGEALTCCAKPLSDL 85


                 ...
gi 84996039  158 TIE 160
Cdd:PRK07609  86 VLE 88
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
85-154 1.37e-15

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 67.93  E-value: 1.37e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 84996039    85 EKVIESAEDEY-ILESAESQGVELPYSCRGGSCSTCAATLVSGEiDNSEQSYLDDDQVKKGYCLL-CTSYAK 154
Cdd:pfam00111   7 GVTIEVPDGETtLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGE-DQSDQSFLEDDELAAGYVVLaCQTYPK 77
COG3894 COG3894
Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain ...
 81-169 1.08e-12

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


Pssm-ID: 443101 [Multi-domain]  Cd Length: 621  Bit Score: 65.21  E-value: 1.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84996039  81 LPEGeKVIESAEDEYILESAESQGVELPYSCRG-GSCSTCAATLVSGE---IDNSEQSYLDDDQVKKGYCLLCTSYAKSD 156
Cdd:COG3894   9 LPSG-KRVEVEAGTTLLDAAREAGVDIDAPCGGrGTCGKCKVKVEEGEfspVTEEERRLLSPEELAEGYRLACQARVLGD 87

                        90
                ....*....|...
gi 84996039 157 CTIETHKEDKLHE 169
Cdd:COG3894  88 LVVEVPPESRLDK 100
PRK05713 PRK05713
iron-sulfur-binding ferredoxin reductase;
81-161 7.87e-07

iron-sulfur-binding ferredoxin reductase;


Pssm-ID: 235575 [Multi-domain]  Cd Length: 312  Bit Score: 47.80  E-value: 7.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84996039   81 LPE---GEKVIESAEDEYILESAESQGVELPYSCRGGSCSTCAATLVSGEIDNSEQSYLDDDQVKKGYCLLCTSYAKSDC 157
Cdd:PRK05713   1 MPElrvGERRWSVPAGSNLLDALNAAGVAVPYSCRAGSCHACLVRCLQGEPEDALPEALAAEKREQGWRLACQCRVVGDL 80


                 ....
gi 84996039  158 TIET 161
Cdd:PRK05713  81 RVEV 84
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
92-158 9.04e-06

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 44.73  E-value: 9.04e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 84996039   92 EDEYILESAESQGVELPYSCRGGSCSTCAATLVSGEIdnsEQSYLDDD-----QVKKGYCLLCTSYAKSDCT 158
Cdd:PRK11872  21 KDELLLDAALRNGINLPLDCREGVCGTCQGRCESGIY---SQDYVDEDalserDLAQRKMLACQTRVKSDAA 89
PRK10713 PRK10713
2Fe-2S ferredoxin-like protein;
84-160 1.18e-05

2Fe-2S ferredoxin-like protein;


Pssm-ID: 182668 [Multi-domain]  Cd Length: 84  Bit Score: 42.02  E-value: 1.18e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 84996039   84 GEKVIESAEDEYILESAESQGVELPYSCRGGSCSTCAATLVSGEIDNSEQ--SYLDDDQVkkgycLLCTSYAKSDCTIE 160
Cdd:PRK10713  10 GTQLLCQDEHPSLLAALESHNVAVEYQCREGYCGSCRTRLVAGQVDWIAEplAFIQPGEI-----LPCCCRAKGDIEIE 83
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 96-160 5.58e-05

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 42.39  E-value: 5.58e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 84996039   96 ILESAESQGVELPYSCRGGSCSTCAATLVSGEIDNSEQSYLDDDQVKKGYCLLCTSYAKSDCTIE 160
Cdd:PRK10684 268 LLEALESNKVPVVAACRAGVCGCCKTKVVSGEYTVSSTMTLTPAEIAQGYVLACSCHPQGDLVLA 332
PRK08493 PRK08493
NADH-quinone oxidoreductase subunit G;
86-169 7.72e-03

NADH-quinone oxidoreductase subunit G;


Pssm-ID: 236277 [Multi-domain]  Cd Length: 819  Bit Score: 36.22  E-value: 7.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84996039   86 KVIESAEDEYILESAESQGVELPYSCRGGSCSTCAAT-LVSGEIDNseqsyldddqvKKGYCllCTSYAKSDCTIETHKE 164
Cdd:PRK08493   9 KECEAQEGEYILNVARRNGIFIPAICYLSGCSPTLACrLCMVEADG-----------KRVYS--CNTKAKEGMNILTNTP 75


                 ....*
gi 84996039  165 DKLHE 169
Cdd:PRK08493  76 NLMDE 80
 
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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