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Conserved domains on  [gi|504587111|ref|WP_014774213|]
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c-type cytochrome [Belliella baltica]

Protein Classification

c-type cytochrome( domain architecture ID 10440489)

c-type cytochrome containing cytochrome c (mono- and diheme) and class III cytochrome c (or c3) tetraheme domains

CATH:  1.10.760.10|3.90.10.10
Gene Ontology:  GO:0009055|GO:0020037
PubMed:  12594933|18568041|10395550|16964504|4364940
SCOP:  3000815|3002451

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cytochrom_C pfam00034
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ...
 45-129 1.36e-13

Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and cytochrome c' families are not included. All these are now in a new clan together. The C-terminus of DUF989, pfam06181, has now been merged into this family.


:

Pssm-ID: 459641 [Multi-domain]  Cd Length: 89  Bit Score: 66.02  E-value: 1.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504587111   45 AGKSVFNANCKTCHKLD---QKYTGPALRGVTDRRSIEWAKSFIKNSAALIASGDAQANALYseynNLAMPQHEFLSDTE 121
Cdd:pfam00034   2 RGKKLFAANCAACHGVNgegAGAGGPDLAGLAARYPGDALGAIRENKHAIGGGGVDRAGGPP----GTGMPAFDGLTDEE 77


                  ....*...
gi 504587111  122 LDNLLSYI 129
Cdd:pfam00034  78 IADLVAYL 85
Cytochrom_C3 cd08168
Heme-binding domain of the class III cytochrome C family and related proteins; This alignment ...
 250-378 1.58e-13

Heme-binding domain of the class III cytochrome C family and related proteins; This alignment models heme binding core motifs as encountered in the cytochrome C3 family and related proteins. Cytochrome C3 is a tetraheme protein found in sulfate-reducing bacteria which use either thiosulfate or sulfate as the ultimate electron acceptors. C3 is an integral part of a complex electron transfer chain. The model also contains triheme cytochromes C7 which function in electron transfer during Fe(III) respiration by Geobacter sulfurreducens (PpcA, PpcB, PpcC, PpcD, and PpcE) and four repeated core motifs as found in the 16-heme cytochrome C HmcA of Desulfovibrio vulgaris Hildenborough which plays a role in electron transfer through the membrane following periplasmic oxidation of hydrogen (resulting in sulfate reduction in the cytoplasm).


:

Pssm-ID: 173979 [Multi-domain]  Cd Length: 85  Bit Score: 65.72  E-value: 1.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504587111 250 KQPIAFSHQLHAGQYEIECQYCHTGVEIGKSANIPsaniCMNCHQHIQNvggkegisteiqkiydavdnnqpiewvrihN 329
Cdd:cd08168    1 KGPVPFPHKKHAEALGIDCRTCHHKYEGGKGEPQK----CAECHSHDGT------------------------------D 46

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 504587111 330 LPDLAYFNHSQHVAvggieCQTCHGPIEEMEVvyqhsSLTMGWCIDCHR 378
Cdd:cd08168   47 DPDFVSLKDAFHNS-----CIGCHKEMAKAGK-----KTGPVGCAGCHK 85
 
Name Accession Description Interval E-value
Cytochrom_C pfam00034
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ...
 45-129 1.36e-13

Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and cytochrome c' families are not included. All these are now in a new clan together. The C-terminus of DUF989, pfam06181, has now been merged into this family.


Pssm-ID: 459641 [Multi-domain]  Cd Length: 89  Bit Score: 66.02  E-value: 1.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504587111   45 AGKSVFNANCKTCHKLD---QKYTGPALRGVTDRRSIEWAKSFIKNSAALIASGDAQANALYseynNLAMPQHEFLSDTE 121
Cdd:pfam00034   2 RGKKLFAANCAACHGVNgegAGAGGPDLAGLAARYPGDALGAIRENKHAIGGGGVDRAGGPP----GTGMPAFDGLTDEE 77


                  ....*...
gi 504587111  122 LDNLLSYI 129
Cdd:pfam00034  78 IADLVAYL 85
Cytochrom_C3 cd08168
Heme-binding domain of the class III cytochrome C family and related proteins; This alignment ...
 250-378 1.58e-13

Heme-binding domain of the class III cytochrome C family and related proteins; This alignment models heme binding core motifs as encountered in the cytochrome C3 family and related proteins. Cytochrome C3 is a tetraheme protein found in sulfate-reducing bacteria which use either thiosulfate or sulfate as the ultimate electron acceptors. C3 is an integral part of a complex electron transfer chain. The model also contains triheme cytochromes C7 which function in electron transfer during Fe(III) respiration by Geobacter sulfurreducens (PpcA, PpcB, PpcC, PpcD, and PpcE) and four repeated core motifs as found in the 16-heme cytochrome C HmcA of Desulfovibrio vulgaris Hildenborough which plays a role in electron transfer through the membrane following periplasmic oxidation of hydrogen (resulting in sulfate reduction in the cytoplasm).


Pssm-ID: 173979 [Multi-domain]  Cd Length: 85  Bit Score: 65.72  E-value: 1.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504587111 250 KQPIAFSHQLHAGQYEIECQYCHTGVEIGKSANIPsaniCMNCHQHIQNvggkegisteiqkiydavdnnqpiewvrihN 329
Cdd:cd08168    1 KGPVPFPHKKHAEALGIDCRTCHHKYEGGKGEPQK----CAECHSHDGT------------------------------D 46

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 504587111 330 LPDLAYFNHSQHVAvggieCQTCHGPIEEMEVvyqhsSLTMGWCIDCHR 378
Cdd:cd08168   47 DPDFVSLKDAFHNS-----CIGCHKEMAKAGK-----KTGPVGCAGCHK 85
CccA COG2010
Cytochrome c, mono- and diheme variants [Energy production and conversion];
16-129 9.64e-08

Cytochrome c, mono- and diheme variants [Energy production and conversion];


Pssm-ID: 441613 [Multi-domain]  Cd Length: 169  Bit Score: 51.49  E-value: 9.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504587111  16 TLALMLFLVLGAQSFAANPDVSDsEEAISAGKSVFNANCKTCHKLDQK-YTG--PALRGV-TDRRSIEWAKSFIKNsaal 91
Cdd:COG2010   63 ALALALLLALLLAAAAADAPAAD-AEALARGKALYEQNCAACHGADGKgGLGaaPNLTDDaLYGGDPEALVETILN---- 137

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 504587111  92 iasGDAQAnalyseynnlAMPQHE-FLSDTELDNLLSYI 129
Cdd:COG2010  138 ---GRPGG----------AMPAFGgQLSDEEIAALAAYL 163
Cytochrome_C7 pfam14522
Cytochrome c7 and related cytochrome c; This family includes cytochromes c7 and c7-type. In ...
 334-419 6.77e-06

Cytochrome c7 and related cytochrome c; This family includes cytochromes c7 and c7-type. In cytochromes c7 all three haems are bis-His co-ordinated, while in c7-type the last haem is His-Met co-ordinated. Desulfuromonas acetoxidans and Geobacter metallireducens cytochrome c7 participate in the anaerobic iron respiration, but Geobacter metallireducens cytochrome c7 hasn't a Fe(III) reductase activity. This entry also includes cytochrome c nitrite reductase subunit NrfH from Desulfovibrio vulgaris which forms a complex with cytochrome c nitrite reductase NrfA.


Pssm-ID: 434012 [Multi-domain]  Cd Length: 62  Bit Score: 43.43  E-value: 6.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504587111  334 AYFNHSQHVAVGGiECQTCHGPIEEmEVVYQHSSLTMGW-CIDCHrqtdikaagneyydklvqlhsDSKNALKVKDIGgl 412
Cdd:pfam14522   1 VVFSHDVHLAGGY-NCADCHNKLFA-SKRVTMAEMEKGKsCGACH---------------------DGKTAFSVADKG-- 55


                  ....*..
gi 504587111  413 ECAKCHY 419
Cdd:pfam14522  56 NCGRCHT 62
 
Name Accession Description Interval E-value
Cytochrom_C pfam00034
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ...
 45-129 1.36e-13

Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and cytochrome c' families are not included. All these are now in a new clan together. The C-terminus of DUF989, pfam06181, has now been merged into this family.


Pssm-ID: 459641 [Multi-domain]  Cd Length: 89  Bit Score: 66.02  E-value: 1.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504587111   45 AGKSVFNANCKTCHKLD---QKYTGPALRGVTDRRSIEWAKSFIKNSAALIASGDAQANALYseynNLAMPQHEFLSDTE 121
Cdd:pfam00034   2 RGKKLFAANCAACHGVNgegAGAGGPDLAGLAARYPGDALGAIRENKHAIGGGGVDRAGGPP----GTGMPAFDGLTDEE 77


                  ....*...
gi 504587111  122 LDNLLSYI 129
Cdd:pfam00034  78 IADLVAYL 85
Cytochrom_C3 cd08168
Heme-binding domain of the class III cytochrome C family and related proteins; This alignment ...
 250-378 1.58e-13

Heme-binding domain of the class III cytochrome C family and related proteins; This alignment models heme binding core motifs as encountered in the cytochrome C3 family and related proteins. Cytochrome C3 is a tetraheme protein found in sulfate-reducing bacteria which use either thiosulfate or sulfate as the ultimate electron acceptors. C3 is an integral part of a complex electron transfer chain. The model also contains triheme cytochromes C7 which function in electron transfer during Fe(III) respiration by Geobacter sulfurreducens (PpcA, PpcB, PpcC, PpcD, and PpcE) and four repeated core motifs as found in the 16-heme cytochrome C HmcA of Desulfovibrio vulgaris Hildenborough which plays a role in electron transfer through the membrane following periplasmic oxidation of hydrogen (resulting in sulfate reduction in the cytoplasm).


Pssm-ID: 173979 [Multi-domain]  Cd Length: 85  Bit Score: 65.72  E-value: 1.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504587111 250 KQPIAFSHQLHAGQYEIECQYCHTGVEIGKSANIPsaniCMNCHQHIQNvggkegisteiqkiydavdnnqpiewvrihN 329
Cdd:cd08168    1 KGPVPFPHKKHAEALGIDCRTCHHKYEGGKGEPQK----CAECHSHDGT------------------------------D 46

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 504587111 330 LPDLAYFNHSQHVAvggieCQTCHGPIEEMEVvyqhsSLTMGWCIDCHR 378
Cdd:cd08168   47 DPDFVSLKDAFHNS-----CIGCHKEMAKAGK-----KTGPVGCAGCHK 85
CccA COG2010
Cytochrome c, mono- and diheme variants [Energy production and conversion];
16-129 9.64e-08

Cytochrome c, mono- and diheme variants [Energy production and conversion];


Pssm-ID: 441613 [Multi-domain]  Cd Length: 169  Bit Score: 51.49  E-value: 9.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504587111  16 TLALMLFLVLGAQSFAANPDVSDsEEAISAGKSVFNANCKTCHKLDQK-YTG--PALRGV-TDRRSIEWAKSFIKNsaal 91
Cdd:COG2010   63 ALALALLLALLLAAAAADAPAAD-AEALARGKALYEQNCAACHGADGKgGLGaaPNLTDDaLYGGDPEALVETILN---- 137

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 504587111  92 iasGDAQAnalyseynnlAMPQHE-FLSDTELDNLLSYI 129
Cdd:COG2010  138 ---GRPGG----------AMPAFGgQLSDEEIAALAAYL 163
Cytochrom_C3 cd08168
Heme-binding domain of the class III cytochrome C family and related proteins; This alignment ...
 336-418 2.06e-07

Heme-binding domain of the class III cytochrome C family and related proteins; This alignment models heme binding core motifs as encountered in the cytochrome C3 family and related proteins. Cytochrome C3 is a tetraheme protein found in sulfate-reducing bacteria which use either thiosulfate or sulfate as the ultimate electron acceptors. C3 is an integral part of a complex electron transfer chain. The model also contains triheme cytochromes C7 which function in electron transfer during Fe(III) respiration by Geobacter sulfurreducens (PpcA, PpcB, PpcC, PpcD, and PpcE) and four repeated core motifs as found in the 16-heme cytochrome C HmcA of Desulfovibrio vulgaris Hildenborough which plays a role in electron transfer through the membrane following periplasmic oxidation of hydrogen (resulting in sulfate reduction in the cytoplasm).


Pssm-ID: 173979 [Multi-domain]  Cd Length: 85  Bit Score: 48.39  E-value: 2.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504587111 336 FNHSQHVAVGGIECQTCHGPIEEMEVVYQHssltmgwCIDCHRQTDIKAAGNEYYDKL-----VQLHSDSKNALKVKDIG 410
Cdd:cd08168    6 FPHKKHAEALGIDCRTCHHKYEGGKGEPQK-------CAECHSHDGTDDPDFVSLKDAfhnscIGCHKEMAKAGKKTGPV 78


                 ....*...
gi 504587111 411 GleCAKCH 418
Cdd:cd08168   79 G--CAGCH 84
CytC552 COG4654
Cytochrome c551/c552 [Energy production and conversion];
45-129 2.93e-07

Cytochrome c551/c552 [Energy production and conversion];


Pssm-ID: 443692 [Multi-domain]  Cd Length: 88  Bit Score: 47.97  E-value: 2.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504587111  45 AGKSVFNAN-CKTCHKLDQKYTGPALRGVTDR-RSIEWAKSFIknsAALIASGDAQAnalyseYNNLAMPQHEFLSDTEL 122
Cdd:COG4654    6 AGKALAKKSgCLACHAVDKKLVGPSYKDVAKKyKGKADAVAKL---AKKIKKGGSGV------WGDVPMPPHPQLSDAEA 76


                 ....*..
gi 504587111 123 DNLLSYI 129
Cdd:COG4654   77 KALVKWI 83
Cyc7 COG3474
Cytochrome c2 [Energy production and conversion];
45-95 3.81e-06

Cytochrome c2 [Energy production and conversion];


Pssm-ID: 442697 [Multi-domain]  Cd Length: 101  Bit Score: 45.26  E-value: 3.81e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504587111  45 AGKSVFNANCKTCHKLDQKY---TGPALRGVTDRRSIewAKSFIKNSAALIASG 95
Cdd:COG3474    5 AGEKLFNRKCAACHSVDGGAgnrVGPNLNGVVGRKAG--SVEGFAYSDALKASG 56
Cytochrome_C7 pfam14522
Cytochrome c7 and related cytochrome c; This family includes cytochromes c7 and c7-type. In ...
 334-419 6.77e-06

Cytochrome c7 and related cytochrome c; This family includes cytochromes c7 and c7-type. In cytochromes c7 all three haems are bis-His co-ordinated, while in c7-type the last haem is His-Met co-ordinated. Desulfuromonas acetoxidans and Geobacter metallireducens cytochrome c7 participate in the anaerobic iron respiration, but Geobacter metallireducens cytochrome c7 hasn't a Fe(III) reductase activity. This entry also includes cytochrome c nitrite reductase subunit NrfH from Desulfovibrio vulgaris which forms a complex with cytochrome c nitrite reductase NrfA.


Pssm-ID: 434012 [Multi-domain]  Cd Length: 62  Bit Score: 43.43  E-value: 6.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504587111  334 AYFNHSQHVAVGGiECQTCHGPIEEmEVVYQHSSLTMGW-CIDCHrqtdikaagneyydklvqlhsDSKNALKVKDIGgl 412
Cdd:pfam14522   1 VVFSHDVHLAGGY-NCADCHNKLFA-SKRVTMAEMEKGKsCGACH---------------------DGKTAFSVADKG-- 55


                  ....*..
gi 504587111  413 ECAKCHY 419
Cdd:pfam14522  56 NCGRCHT 62
Cytochrome_CBB3 pfam13442
Cytochrome C oxidase, cbb3-type, subunit III;
41-129 2.33e-04

Cytochrome C oxidase, cbb3-type, subunit III;


Pssm-ID: 463879 [Multi-domain]  Cd Length: 67  Bit Score: 39.31  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504587111   41 EAISAGKSVFNANCKTCHKLDQKytGPALRGVtdrrsiEWAKSFIKNSaalIASGdaqanalyseynNLAMP-QHEFLSD 119
Cdd:pfam13442   1 AAAAAGEALYAANCASCHGTGGA--GPSLAGR------ALPPEALVDI---IRNG------------KGAMPaFGGDLSD 57

                          90
                  ....*....|
gi 504587111  120 TELDNLLSYI 129
Cdd:pfam13442  58 EELEALAAYL 67
 
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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