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Conserved domains on  [gi|1773561390|gb|QGC21958|]
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2Fe-2S iron-sulfur cluster binding domain-containing protein [Bordetella parapertussis]

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

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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 ...
3-101 5.15e-21

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 PLN02593:

Pssm-ID: 444718 [Multi-domain]  Cd Length: 117  Bit Score: 80.53  E-value: 5.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773561390   3 TIIFIASNEARHVVQADDGLSLMECARRANVPgIAAECGGACTCATCHVHVG-QEWMQAVGEPGDMERDMLDFANDVRAE 81
Cdd:PLN02593    2 SVTFVDKDGEERTVKAPVGMSLLEAAHENDIE-LEGACEGSLACSTCHVIVMdEKVYNKLPEPTDEENDMLDLAFGLTET 80
                          90       100
                  ....*....|....*....|
gi 1773561390  82 SRLSCQITVAPALEGLTVRV 101
Cdd:PLN02593   81 SRLGCQVIAKPELDGMRLAL 100
 
Name Accession Description Interval E-value
PLN02593 PLN02593
adrenodoxin-like ferredoxin protein
3-101 5.15e-21

adrenodoxin-like ferredoxin protein


Pssm-ID: 178203 [Multi-domain]  Cd Length: 117  Bit Score: 80.53  E-value: 5.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773561390   3 TIIFIASNEARHVVQADDGLSLMECARRANVPgIAAECGGACTCATCHVHVG-QEWMQAVGEPGDMERDMLDFANDVRAE 81
Cdd:PLN02593    2 SVTFVDKDGEERTVKAPVGMSLLEAAHENDIE-LEGACEGSLACSTCHVIVMdEKVYNKLPEPTDEENDMLDLAFGLTET 80
                          90       100
                  ....*....|....*....|
gi 1773561390  82 SRLSCQITVAPALEGLTVRV 101
Cdd:PLN02593   81 SRLGCQVIAKPELDGMRLAL 100
Fdx COG0633
Ferredoxin [Energy production and conversion];
1-95 1.18e-15

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 66.03  E-value: 1.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773561390   1 MTTIIFIASneaRHVVQADDGLSLMECARRANVPgIAAECGgACTCATCHVHVGQewmqavGEPGDMERDMLDFAnDVRA 80
Cdd:COG0633     1 MPKVTFIPE---GHTVEVPAGESLLEAALRAGID-LPYSCR-SGACGTCHVRVLE------GEVDHREEDALSDE-ERAA 68
                          90
                  ....*....|....*
gi 1773561390  81 ESRLSCQITVAPALE 95
Cdd:COG0633    69 GSRLACQARPTSDLV 83
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
5-100 2.23e-08

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: 47.00  E-value: 2.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773561390   5 IFIASNEARHVVQADDGLSLMECARRANVPgIAAECGGAcTCATCHVHVGQEWmqavgepGDMERDMLDFANDVRAESRL 84
Cdd:cd00207     1 VTINVPGSGVEVEVPEGETLLDAAREAGID-IPYSCRAG-ACGTCKVEVVEGE-------VDQSDPSLLDEEEAEGGYVL 71
                          90
                  ....*....|....*.
gi 1773561390  85 SCQitvAPALEGLTVR 100
Cdd:cd00207    72 ACQ---TRVTDGLVIE 84
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
13-90 1.17e-03

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 34.81  E-value: 1.17e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1773561390  13 RHVVQADDGLSLMECARRANVPGIAAECGGACtCATCHVHVGQEWMQAvgEPGDMERDMLDFandvrAESRLSCQITV 90
Cdd:pfam00111   7 GVTIEVPDGETTLLDAAEEAGIDIPYSCRGGG-CGTCAVKVLEGEDQS--DQSFLEDDELAA-----GYVVLACQTYP 76
 
Name Accession Description Interval E-value
PLN02593 PLN02593
adrenodoxin-like ferredoxin protein
3-101 5.15e-21

adrenodoxin-like ferredoxin protein


Pssm-ID: 178203 [Multi-domain]  Cd Length: 117  Bit Score: 80.53  E-value: 5.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773561390   3 TIIFIASNEARHVVQADDGLSLMECARRANVPgIAAECGGACTCATCHVHVG-QEWMQAVGEPGDMERDMLDFANDVRAE 81
Cdd:PLN02593    2 SVTFVDKDGEERTVKAPVGMSLLEAAHENDIE-LEGACEGSLACSTCHVIVMdEKVYNKLPEPTDEENDMLDLAFGLTET 80
                          90       100
                  ....*....|....*....|
gi 1773561390  82 SRLSCQITVAPALEGLTVRV 101
Cdd:PLN02593   81 SRLGCQVIAKPELDGMRLAL 100
PTZ00490 PTZ00490
Ferredoxin superfamily; Provisional
16-104 4.37e-17

Ferredoxin superfamily; Provisional


Pssm-ID: 185668  Cd Length: 143  Bit Score: 71.05  E-value: 4.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773561390  16 VQADDGLSLMECARRANVPGIAAECGGACTCATCHVHVGQEWMQAVGEPGDMERDMLDFANDVRAESRLSCQITVAPALE 95
Cdd:PTZ00490   50 VEVPVGMSLMHALRDVAKLDVEGTCNGCMQCATCHVYLSAASFKKLGGPSEEEEDVLAKALDVKETSRLACQVDLTPEMD 129

                  ....*....
gi 1773561390  96 GLTVRVAPQ 104
Cdd:PTZ00490  130 GLEVELPSY 138
Fdx COG0633
Ferredoxin [Energy production and conversion];
1-95 1.18e-15

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 66.03  E-value: 1.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773561390   1 MTTIIFIASneaRHVVQADDGLSLMECARRANVPgIAAECGgACTCATCHVHVGQewmqavGEPGDMERDMLDFAnDVRA 80
Cdd:COG0633     1 MPKVTFIPE---GHTVEVPAGESLLEAALRAGID-LPYSCR-SGACGTCHVRVLE------GEVDHREEDALSDE-ERAA 68
                          90
                  ....*....|....*
gi 1773561390  81 ESRLSCQITVAPALE 95
Cdd:COG0633    69 GSRLACQARPTSDLV 83
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
5-100 2.23e-08

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: 47.00  E-value: 2.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773561390   5 IFIASNEARHVVQADDGLSLMECARRANVPgIAAECGGAcTCATCHVHVGQEWmqavgepGDMERDMLDFANDVRAESRL 84
Cdd:cd00207     1 VTINVPGSGVEVEVPEGETLLDAAREAGID-IPYSCRAG-ACGTCKVEVVEGE-------VDQSDPSLLDEEEAEGGYVL 71
                          90
                  ....*....|....*.
gi 1773561390  85 SCQitvAPALEGLTVR 100
Cdd:cd00207    72 ACQ---TRVTDGLVIE 84
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
10-90 1.60e-05

Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and conversion]; Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase


Pssm-ID: 442118 [Multi-domain]  Cd Length: 396  Bit Score: 41.77  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773561390  10 NEARHVVQADDGLSLMECARRANVPgIAAECGGACTCATCHVHVgqewMQAVGEPGDMERDMLDfANDVRAESRLSCQIT 89
Cdd:COG2871    40 NGDGKEIEVEEGQTLLDALLRQGIF-LPSACGGGGTCGQCKVKV----LEGGGDILPTETFHLS-DRERKEGYRLACQVK 113

                  .
gi 1773561390  90 V 90
Cdd:COG2871   114 V 114
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
13-90 1.17e-03

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 34.81  E-value: 1.17e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1773561390  13 RHVVQADDGLSLMECARRANVPGIAAECGGACtCATCHVHVGQEWMQAvgEPGDMERDMLDFandvrAESRLSCQITV 90
Cdd:pfam00111   7 GVTIEVPDGETTLLDAAEEAGIDIPYSCRGGG-CGTCAVKVLEGEDQS--DQSFLEDDELAA-----GYVVLACQTYP 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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