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Conserved domains on  [gi|737362331|ref|WP_035344518|]
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SCO family protein [Halalkalibacter hemicellulosilyticus]

Protein Classification

SCO family protein( domain architecture ID 11133300)

SCO (Synthesis of Cytochrome c Oxidase) family protein is required for the proper assembly of cytochrome c oxidase

CATH:  3.40.30.10
Gene Ontology:  GO:0046872
PubMed:  10049365|15558583|10954195
SCOP:  3000031

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 43-176 4.87e-47

SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. SCO1 is required for a post-translational step in the accumulation of subunits COXI and COXII of cytochrome c oxidase. SenC is required for optimal cytochrome c oxidase activity and maximal induction of genes encoding the light-harvesting and reaction centre complexes of R. capsulatus.


:

Pssm-ID: 460630  Cd Length: 134  Bit Score: 150.79  E-value: 4.87e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737362331   43 VEPFQFINEAGELFGAEQLAGGYWVANFIFTNCPSVCPLMTPNMLSLQDEMIAADVPVTFISFTVDPERDTPETLQAYGG 122
Cdd:pfam02630   1 GGPFELVDQDGKAVTEADFEGRPSLVFFGFTHCPDVCPTTLPNMAQVLDALGEEGIDVQPVFITVDPERDTPEVLAEYLE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 737362331  123 NIGADLESwhfLTGyDEAEISEFAlDSFLSVVQPSEDD-----IIHPTYFFLIDPEGLI 176
Cdd:pfam02630  81 AFGPRIIG---LTG-SPEQIAAAA-RAFRVYYEKVPDDggdytVDHTASVYLVDPDGRF 134
 
Name Accession Description Interval E-value
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 43-176 4.87e-47

SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. SCO1 is required for a post-translational step in the accumulation of subunits COXI and COXII of cytochrome c oxidase. SenC is required for optimal cytochrome c oxidase activity and maximal induction of genes encoding the light-harvesting and reaction centre complexes of R. capsulatus.


Pssm-ID: 460630  Cd Length: 134  Bit Score: 150.79  E-value: 4.87e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737362331   43 VEPFQFINEAGELFGAEQLAGGYWVANFIFTNCPSVCPLMTPNMLSLQDEMIAADVPVTFISFTVDPERDTPETLQAYGG 122
Cdd:pfam02630   1 GGPFELVDQDGKAVTEADFEGRPSLVFFGFTHCPDVCPTTLPNMAQVLDALGEEGIDVQPVFITVDPERDTPEVLAEYLE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 737362331  123 NIGADLESwhfLTGyDEAEISEFAlDSFLSVVQPSEDD-----IIHPTYFFLIDPEGLI 176
Cdd:pfam02630  81 AFGPRIIG---LTG-SPEQIAAAA-RAFRVYYEKVPDDggdytVDHTASVYLVDPDGRF 134
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 47-195 4.12e-44

Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441602  Cd Length: 156  Bit Score: 144.27  E-value: 4.12e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737362331  47 QFINEAGELFGAEQLAGGYWVANFIFTNCPSVCPLMTPNMLSLQDEMIAADV-PVTFISFTVDPERDTPETLQAYGGNIG 125
Cdd:COG1999    4 TLTDQDGKPVTLADLRGKPVLVFFGYTSCPDVCPTTLANLAQVQEALGEDGGdDVQVLFISVDPERDTPEVLKAYAEAFG 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 737362331 126 ADleSWHFLTGyDEAEISEFAlDSFLSVVQPSED---DIIHPTYFFLIDPEGLIIRKYDGlTTDQGAIIADLK 195
Cdd:COG1999   84 AP--RWIGLTG-DPEEIAALA-KAFGVYYEKVPDgdyTFDHSAAVYLVDPDGRLRGYYPA-GEDPEELAADLK 151
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 43-182 7.90e-42

SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to Sco1, a membrane-anchored protein possessing a soluble domain with a TRX fold. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop. COX, the terminal enzyme in the respiratory chain, is imbedded in the inner mitochondrial membrane of all eukaryotes and in the plasma membrane of some prokaryotes. It is composed of two subunits, COX I and COX II. It has been proposed that Sco1 specifically delivers copper to the CuA site, a dinuclear copper center, of the COX II subunit. Mutations in human Sco1 and Sco2 cause fatal infantile hepatoencephalomyopathy and cardioencephalomyopathy, respectively. Both disorders are associated with severe COX deficiency in affected tissues. More recently, it has been argued that the redox sensitivity of the copper binding properties of Sco1 implies that it participates in signaling events rather than functioning as a chaperone that transfers copper to COX II.


Pssm-ID: 239266  Cd Length: 142  Bit Score: 137.73  E-value: 7.90e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737362331  43 VEPFQFINEAGELFGAEQLAGGYWVANFIFTNCPSVCPLMTPNMLSLQDEMIAADVP-VTFISFTVDPERDTPETLQAYG 121
Cdd:cd02968    2 GPDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPDVCPTTLANLAQALKQLGADGGDdVQVVFISVDPERDTPEVLKAYA 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 737362331 122 GNIGadlESWHFLTGYDEaEIsEFALDSFLSVVQPSEDD-----IIHPTYFFLIDPEGLIIRKYDG 182
Cdd:cd02968   82 KAFG---PGWIGLTGTPE-EI-EALAKAFGVYYEKVPEDdgdylVDHSAAIYLVDPDGKLVRYYGG 142
 
Name Accession Description Interval E-value
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 43-176 4.87e-47

SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. SCO1 is required for a post-translational step in the accumulation of subunits COXI and COXII of cytochrome c oxidase. SenC is required for optimal cytochrome c oxidase activity and maximal induction of genes encoding the light-harvesting and reaction centre complexes of R. capsulatus.


Pssm-ID: 460630  Cd Length: 134  Bit Score: 150.79  E-value: 4.87e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737362331   43 VEPFQFINEAGELFGAEQLAGGYWVANFIFTNCPSVCPLMTPNMLSLQDEMIAADVPVTFISFTVDPERDTPETLQAYGG 122
Cdd:pfam02630   1 GGPFELVDQDGKAVTEADFEGRPSLVFFGFTHCPDVCPTTLPNMAQVLDALGEEGIDVQPVFITVDPERDTPEVLAEYLE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 737362331  123 NIGADLESwhfLTGyDEAEISEFAlDSFLSVVQPSEDD-----IIHPTYFFLIDPEGLI 176
Cdd:pfam02630  81 AFGPRIIG---LTG-SPEQIAAAA-RAFRVYYEKVPDDggdytVDHTASVYLVDPDGRF 134
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 47-195 4.12e-44

Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441602  Cd Length: 156  Bit Score: 144.27  E-value: 4.12e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737362331  47 QFINEAGELFGAEQLAGGYWVANFIFTNCPSVCPLMTPNMLSLQDEMIAADV-PVTFISFTVDPERDTPETLQAYGGNIG 125
Cdd:COG1999    4 TLTDQDGKPVTLADLRGKPVLVFFGYTSCPDVCPTTLANLAQVQEALGEDGGdDVQVLFISVDPERDTPEVLKAYAEAFG 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 737362331 126 ADleSWHFLTGyDEAEISEFAlDSFLSVVQPSED---DIIHPTYFFLIDPEGLIIRKYDGlTTDQGAIIADLK 195
Cdd:COG1999   84 AP--RWIGLTG-DPEEIAALA-KAFGVYYEKVPDgdyTFDHSAAVYLVDPDGRLRGYYPA-GEDPEELAADLK 151
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 43-182 7.90e-42

SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to Sco1, a membrane-anchored protein possessing a soluble domain with a TRX fold. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop. COX, the terminal enzyme in the respiratory chain, is imbedded in the inner mitochondrial membrane of all eukaryotes and in the plasma membrane of some prokaryotes. It is composed of two subunits, COX I and COX II. It has been proposed that Sco1 specifically delivers copper to the CuA site, a dinuclear copper center, of the COX II subunit. Mutations in human Sco1 and Sco2 cause fatal infantile hepatoencephalomyopathy and cardioencephalomyopathy, respectively. Both disorders are associated with severe COX deficiency in affected tissues. More recently, it has been argued that the redox sensitivity of the copper binding properties of Sco1 implies that it participates in signaling events rather than functioning as a chaperone that transfers copper to COX II.


Pssm-ID: 239266  Cd Length: 142  Bit Score: 137.73  E-value: 7.90e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737362331  43 VEPFQFINEAGELFGAEQLAGGYWVANFIFTNCPSVCPLMTPNMLSLQDEMIAADVP-VTFISFTVDPERDTPETLQAYG 121
Cdd:cd02968    2 GPDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPDVCPTTLANLAQALKQLGADGGDdVQVVFISVDPERDTPEVLKAYA 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 737362331 122 GNIGadlESWHFLTGYDEaEIsEFALDSFLSVVQPSEDD-----IIHPTYFFLIDPEGLIIRKYDG 182
Cdd:cd02968   82 KAFG---PGWIGLTGTPE-EI-EALAKAFGVYYEKVPEDdgdylVDHSAAIYLVDPDGKLVRYYGG 142
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 36-199 3.91e-08

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 50.07  E-value: 3.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737362331  36 MSDAGNEVEPFQFINEAGELFGAEQLAGGYWVANFIFTNCPsVCPLMTPNMLSLQDEMiaADVPVTFISFtvdpeRDTPE 115
Cdd:COG0526    1 MKAVGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCP-PCRAEMPVLKELAEEY--GGVVFVGVDV-----DENPE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737362331 116 TLQAYGGNIGADlesWHFLTGYDEAEISEFALDSFlsvvqpseddiihPTyFFLIDPEGLIIRKYDGLTTDqgaiiADLK 195
Cdd:COG0526   73 AVKAFLKELGLP---YPVLLDPDGELAKAYGVRGI-------------PT-TVLIDKDGKIVARHVGPLSP-----EELE 130


                 ....
gi 737362331 196 ETIQ 199
Cdd:COG0526  131 EALE 134
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
46-199 2.55e-06

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 45.24  E-value: 2.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737362331  46 FQFINEAGELFGAEQLAGGYWVANFIFTNCPsVCPLMTPNMLSLQDEMIAADVPVTFISftvdpeRDTPETLQAYggnig 125
Cdd:COG1225    4 FTLPDLDGKTVSLSDLRGKPVVLYFYATWCP-GCTAELPELRDLYEEFKDKGVEVLGVS------SDSDEAHKKF----- 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 737362331 126 ADLESWHFLTGYDEAEisEFAlDSFLSVVQPSeddiihptyFFLIDPEGLIIRKYDGLTTDQGAIIADLKETIQ 199
Cdd:COG1225   72 AEKYGLPFPLLSDPDG--EVA-KAYGVRGTPT---------TFLIDPDGKIRYVWVGPVDPRPHLEEVLEALLA 133
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 45-182 1.21e-05

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 42.99  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737362331  45 PFQFINEAGELFGAEQLAGGYWVANFIFTNCPsVCPLMTPNMLSLQDEMIAADVPVTFISFTVDPERDTPETLQAYGgni 124
Cdd:cd02966    1 DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCP-PCRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAAVKAFLKKYG--- 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 737362331 125 gadlesWHFLTGYDEAeiSEFALDsFLSVVQPSeddiihptyFFLIDPEGLIIRKYDG 182
Cdd:cd02966   77 ------ITFPVLLDPD--GELAKA-YGVRGLPT---------TFLIDRDGRIRARHVG 116
 
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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