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 162329549  90 QGDFSLLDHKGQPRCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVRKLEAEPdLPLVQPVFITVDPERDDVAAMARY 169
Cdd:cd02968    2 GPDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPDVCPTTLANLAQALKQLGADG-GDDVQVVFISVDPERDTPEVLKAY 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162329549 170 VQEFHPRLLGLTGSTEQVAHASRNYRVYYSAGPKDeDQDYIVDHSIAIYLLNPDGLFTDYYG 231
Cdd:cd02968   81 AKAFGPGWIGLTGTPEEIEALAKAFGVYYEKVPED-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 162329549  90 QGDFSLLDHKGQPRCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVRKLEAEPdLPLVQPVFITVDPERDDVAAMARY 169
Cdd:cd02968    2 GPDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPDVCPTTLANLAQALKQLGADG-GDDVQVVFISVDPERDTPEVLKAY 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162329549 170 VQEFHPRLLGLTGSTEQVAHASRNYRVYYSAGPKDeDQDYIVDHSIAIYLLNPDGLFTDYYG 231
Cdd:cd02968   81 AKAFGPGWIGLTGTPEEIEALAKAFGVYYEKVPED-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 162329549  94 SLLDHKGQPRCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVRKLEAEPDLPlVQPVFITVDPERDDVAAMARYVQEF 173
Cdd:COG1999    4 TLTDQDGKPVTLADLRGKPVLVFFGYTSCPDVCPTTLANLAQVQEALGEDGGDD-VQVLFISVDPERDTPEVLKAYAEAF 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162329549 174 H-PRLLGLTGSTEQVAHASRNYRVYYSagpKDEDQDYIVDHSIAIYLLNPDGLFTDYYGRSRSAEQIVESIRRHIAA 249
Cdd:COG1999   83 GaPRWIGLTGDPEEIAALAKAFGVYYE---KVPDGDYTFDHSAAVYLVDPDGRLRGYYPAGEDPEELAADLKALLEE 156

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 162329549  90 QGDFSLLDHKGQPRCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVRKLEAEPdLPLVQPVFITVDPERDDVAAMARY 169
Cdd:cd02968    2 GPDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPDVCPTTLANLAQALKQLGADG-GDDVQVVFISVDPERDTPEVLKAY 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162329549 170 VQEFHPRLLGLTGSTEQVAHASRNYRVYYSAGPKDeDQDYIVDHSIAIYLLNPDGLFTDYYG 231
Cdd:cd02968   81 AKAFGPGWIGLTGTPEEIEALAKAFGVYYEKVPED-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 162329549  94 SLLDHKGQPRCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVRKLEAEPDLPlVQPVFITVDPERDDVAAMARYVQEF 173
Cdd:COG1999    4 TLTDQDGKPVTLADLRGKPVLVFFGYTSCPDVCPTTLANLAQVQEALGEDGGDD-VQVLFISVDPERDTPEVLKAYAEAF 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162329549 174 H-PRLLGLTGSTEQVAHASRNYRVYYSagpKDEDQDYIVDHSIAIYLLNPDGLFTDYYGRSRSAEQIVESIRRHIAA 249
Cdd:COG1999   83 GaPRWIGLTGDPEEIAALAKAFGVYYE---KVPDGDYTFDHSAAVYLVDPDGRLRGYYPAGEDPEELAADLKALLEE 156

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329549  92 DFSLLDHKGQPRCKADFRGQWVLMYFGFTHCPDiCPDELEKLVQVVRKleaepdLPLVQPVFITVDPERDDVAAMARYVQ 171
Cdd:COG0526   10 DFTLTDLDGKPLSLADLKGKPVLVNFWATWCPP-CRAEMPVLKELAEE------YGGVVFVGVDVDENPEAVKAFLKELG 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162329549 172 EFHPRLLGLTGSteqvahASRNYRVYysagpkdedqdyivdhSI-AIYLLNPDGLFTDYYGRSRSAEQIVESIRRHIAA 249
Cdd:COG0526   83 LPYPVLLDPDGE------LAKAYGVR----------------GIpTTVLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139

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 162329549  92 DFSLLDHKGQPRCKADFRGQWVLMYFGFTHCPdICPDELEKLVQVVRKLeAEPDLPlvqpvFITVDPERDDVAAMARYVQ 171
Cdd:cd02966    1 DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCP-PCRAEMPELEALAKEY-KDDGVE-----VVGVNVDDDDPAAVKAFLK 73

                         90       100
                 ....*....|....*....|....*..
gi 162329549 172 EFHPRLLGLTGSTEQVAhasRNYRVYY 198
Cdd:cd02966   74 KYGITFPVLLDPDGELA---KAYGVRG 97

Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of thioredoxin-dependent thiol peroxidases, widely expressed in pathogenic bacteria, that protect cells against toxicity from reactive oxygen species by reducing and detoxifying hydroperoxides. The protein was named BCP based on its electrophoretic mobility before its function was known. BCP shows substrate selectivity toward fatty acid hydroperoxides rather than hydrogen peroxide or alkyl hydroperoxides. BCP contains the peroxidatic cysteine but appears not to possess a resolving cysteine (some sequences, not all, contain a second cysteine but its role is still unknown). Unlike other PRXs, BCP exists as a monomer. The plant homolog of BCP is PRX Q, which is expressed only in leaves and is cellularly localized in the chloroplasts and the guard cells of stomata. Also included in this subfamily is the fungal nuclear protein, Dot5p (for disrupter of telomere silencing protein 5), which functions as an alkyl-hydroperoxide reductase during post-diauxic growth.

                         10        20
                 ....*....|....*....|....*.
gi 162329549  92 DFSLLDHKGQPRCKADFRGQWVLMYF 117
Cdd:cd03017    5 DFTLPDQDGETVSLSDLRGKPVVLYF 30