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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759068  136 LGGPFSLTTHTGERKTDKDYLGQWLLIYFGFTHCPDVCPEELEKMIQVVDEIDSiTTLPDLTPLFISIDPERDTKEAIAN 215
Cdd:cd02968   1 IGPDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPDVCPTTLANLAQALKQLGA-DGGDDVQVVFISVDPERDTPEVLKA 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4759068  216 YVKEFSPKLVGLTGTREEVDQVARAYRVYYSPGPKDeDEDYIVDHTIIMYLIGPDGEFLDYFG 278
Cdd:cd02968  80 YAKAFGPGWIGLTGTPEEIEALAKAFGVYYEKVPED-DGDYLVDHSAAIYLVDPDGKLVRYYG 141

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759068  136 LGGPFSLTTHTGERKTDKDYLGQWLLIYFGFTHCPDVCPEELEKMIQVVDEIDSiTTLPDLTPLFISIDPERDTKEAIAN 215
Cdd:cd02968   1 IGPDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPDVCPTTLANLAQALKQLGA-DGGDDVQVVFISVDPERDTPEVLKA 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4759068  216 YVKEFSPKLVGLTGTREEVDQVARAYRVYYSPGPKDeDEDYIVDHTIIMYLIGPDGEFLDYFG 278
Cdd:cd02968  80 YAKAFGPGWIGLTGTPEEIEALAKAFGVYYEKVPED-DGDYLVDHSAAIYLVDPDGKLVRYYG 141

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759068  141 SLTTHTGERKTDKDYLGQWLLIYFGFTHCPDVCPEELEKMIQVVDEIDSiTTLPDLTPLFISIDPERDTKEAIANYVKEF 220
Cdd:COG1999   4 TLTDQDGKPVTLADLRGKPVLVFFGYTSCPDVCPTTLANLAQVQEALGE-DGGDDVQVLFISVDPERDTPEVLKAYAEAF 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4759068  221 S-PKLVGLTGTREEVDQVARAYRVYYSpgpKDEDEDYIVDHTIIMYLIGPDGEFLDYFGQNKRKGEIAASIATHMR 295
Cdd:COG1999  83 GaPRWIGLTGDPEEIAALAKAFGVYYE---KVPDGDYTFDHSAAVYLVDPDGRLRGYYPAGEDPEELAADLKALLE 155

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759068  136 LGGPFSLTTHTGERKTDKDYLGQWLLIYFGFTHCPDVCPEELEKMIQVVDEIDSiTTLPDLTPLFISIDPERDTKEAIAN 215
Cdd:cd02968   1 IGPDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPDVCPTTLANLAQALKQLGA-DGGDDVQVVFISVDPERDTPEVLKA 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4759068  216 YVKEFSPKLVGLTGTREEVDQVARAYRVYYSPGPKDeDEDYIVDHTIIMYLIGPDGEFLDYFG 278
Cdd:cd02968  80 YAKAFGPGWIGLTGTPEEIEALAKAFGVYYEKVPED-DGDYLVDHSAAIYLVDPDGKLVRYYG 141

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759068  141 SLTTHTGERKTDKDYLGQWLLIYFGFTHCPDVCPEELEKMIQVVDEIDSiTTLPDLTPLFISIDPERDTKEAIANYVKEF 220
Cdd:COG1999   4 TLTDQDGKPVTLADLRGKPVLVFFGYTSCPDVCPTTLANLAQVQEALGE-DGGDDVQVLFISVDPERDTPEVLKAYAEAF 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4759068  221 S-PKLVGLTGTREEVDQVARAYRVYYSpgpKDEDEDYIVDHTIIMYLIGPDGEFLDYFGQNKRKGEIAASIATHMR 295
Cdd:COG1999  83 GaPRWIGLTGDPEEIAALAKAFGVYYE---KVPDGDYTFDHSAAVYLVDPDGRLRGYYPAGEDPEELAADLKALLE 155

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759068    140 FSLTTHTGERKTDKDYLGQWLLIYF-GFTHCPdVCPEELEKMIQVVDEIDSIttlpDLTPLFISIDPERDTKEAIANYVK 218
Cdd:pfam00578   8 FELPDGDGGTVSLSDYRGKWVVLFFyPADWTP-VCTTELPALADLYEEFKKL----GVEVLGVSVDSPESHKAFAEKYGL 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 4759068    219 EFsPKLVGLTGtreevdQVARAYRVYYSPGPKDEDEDYIVD 259
Cdd:pfam00578  83 PF-PLLSDPDG------EVARAYGVLNEEEGGALRATFVID 116

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4759068  139 PFSLTTHTGERKTDKDYLGQWLLIYFGFTHCPdVCPEELEKMIQVVDEIDSittlPDLTPLFISIDpeRDTKEAIANYVK 218
Cdd:cd02966   1 DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCP-PCRAEMPELEALAKEYKD----DGVEVVGVNVD--DDDPAAVKAFLK 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 4759068  219 EFSPKLVGLTGTReevDQVARAYRVYYSPgpkdededyivdhtiIMYLIGPDGE 272
Cdd:cd02966  74 KYGITFPVLLDPD---GELAKAYGVRGLP---------------TTFLIDRDGR 109

DEXD-box helicase domain of SecA; SecA is a part of the Sec translocase that transports the vast majority of bacterial and ER-exported proteins. SecA binds both the signal sequence and the mature domain of the preprotein emerging from the ribosome. SecA belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4759068  183 VVDEIDSIttLPD--LTPLFISidperDTKEAIA--NYVKEFsPKLVGLTGT-REEVDQVARAYR 242
Cdd:cd17928 166 IVDEVDSI--LIDeaRTPLIIS-----GTLATITfqNYFRLY-PKLAGMTGTaKTEAEEFREIYN 222