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Conserved domains on  [gi|17564844|ref|NP_503892|]
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protein-disulfide reductase [Caenorhabditis elegans]

Protein Classification

thioredoxin family protein( domain architecture ID 10121823)

thioredoxin family protein may function as a thiol disulfide reductase that catalyzes the reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif; similar to human nucleoredoxin-like protein 2 that may be involved in the maintenance of both the function and the viability of sensory neurons, including photoreceptors and olfactory neurons

CATH:  3.40.30.10
EC:  1.8.-.-
Gene Ontology:  GO:0015036
PubMed:  11441809|12074972|9099998|10049365|15558583|30367780
SCOP:  4000237

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 2-117 7.41e-47

Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.


:

Pssm-ID: 239262 [Multi-domain]  Cd Length: 132  Bit Score: 146.99  E-value: 7.41e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844   2 LDWTLVDATEALAGKIGGFYFSAHWCPPCCMFTPILKKFYEKVYD---DFEIVFVSSDPSESGLKKYMQEcHGDWYYIPF 78
Cdd:cd02964   4 LDGEGVVPVSALEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEegkNFEIVFVSRDRSEESFNEYFSE-MPPWLAVPF 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 17564844  79 GHEA-KQKLCVKYEITGMPTLVIVKPDGTEVKSDGRYDVQ 117
Cdd:cd02964  83 EDEElRELLEKQFKVEGIPTLVVLKPDGDVVTTNARDEVE 122
 
Name Accession Description Interval E-value
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 2-117 7.41e-47

Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.


Pssm-ID: 239262 [Multi-domain]  Cd Length: 132  Bit Score: 146.99  E-value: 7.41e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844   2 LDWTLVDATEALAGKIGGFYFSAHWCPPCCMFTPILKKFYEKVYD---DFEIVFVSSDPSESGLKKYMQEcHGDWYYIPF 78
Cdd:cd02964   4 LDGEGVVPVSALEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEegkNFEIVFVSRDRSEESFNEYFSE-MPPWLAVPF 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 17564844  79 GHEA-KQKLCVKYEITGMPTLVIVKPDGTEVKSDGRYDVQ 117
Cdd:cd02964  83 EDEElRELLEKQFKVEGIPTLVVLKPDGDVVTTNARDEVE 122
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 15-106 4.90e-27

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 95.84  E-value: 4.90e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844    15 GKIGGFYFSAHWCPPCCMFTPILKKFYEKV--YDDFEIVFVSSDPSESGLKKYMQECHGDWYYIPFGHEAKQKLCVKYEI 92
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLkkKKNVEIVFVSLDRDLEEFKDYLKKMPKDWLSVPFDDDERNELKRKYGV 80

                          90
                  ....*....|....
gi 17564844    93 TGMPTLVIVKPDGT 106
Cdd:pfam13905  81 NAIPTLVLLDPNGE 94
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 3-108 7.89e-20

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 78.58  E-value: 7.89e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844   3 DWTLVDAT------EALAGKIGGFYFSAHWCPPCCMFTPILKKFYEKvYDDFEIVFVSSDPSESGLKKYMQECHGDWyyi 76
Cdd:COG0526  10 DFTLTDLDgkplslADLKGKPVLVNFWATWCPPCRAEMPVLKELAEE-YGGVVFVGVDVDENPEAVKAFLKELGLPY--- 85

                        90       100       110
                ....*....|....*....|....*....|..
gi 17564844  77 PFGHEAKQKLCVKYEITGMPTLVIVKPDGTEV 108
Cdd:COG0526  86 PVLLDPDGELAKAYGVRGIPTTVLIDKDGKIV 117
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 22-109 8.19e-08

thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport]


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 46.51  E-value: 8.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844    22 FSAHWCPPCCMFTPILKKFYEKVYDDFEIVFVSSDpsesglkkymqechgdwyyipfgheAKQKLCVKYEITGMPTLVIV 101
Cdd:TIGR01068  21 FWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVD-------------------------ENPDIAAKYGIRSIPTLLLF 75


                  ....*...
gi 17564844   102 KpDGTEVK 109
Cdd:TIGR01068  76 K-NGKEVD 82
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
22-109 1.20e-04

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 39.22  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844   22 FSAHWCPPCCMFTPILKKFYeKVYDD--FEIVFVSSDPSESGLKKYMQEcHGdwYYIPFGHEAKQKLCVKYEITGMPTLV 99
Cdd:PRK03147  68 FWGTWCKPCEKEMPYMNELY-PKYKEkgVEIIAVNVDETELAVKNFVNR-YG--LTFPVAIDKGRQVIDAYGVGPLPTTF 143

                         90
                 ....*....|
gi 17564844  100 IVKPDGTEVK 109
Cdd:PRK03147 144 LIDKDGKVVK 153
 
Name Accession Description Interval E-value
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 2-117 7.41e-47

Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.


Pssm-ID: 239262 [Multi-domain]  Cd Length: 132  Bit Score: 146.99  E-value: 7.41e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844   2 LDWTLVDATEALAGKIGGFYFSAHWCPPCCMFTPILKKFYEKVYD---DFEIVFVSSDPSESGLKKYMQEcHGDWYYIPF 78
Cdd:cd02964   4 LDGEGVVPVSALEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEegkNFEIVFVSRDRSEESFNEYFSE-MPPWLAVPF 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 17564844  79 GHEA-KQKLCVKYEITGMPTLVIVKPDGTEVKSDGRYDVQ 117
Cdd:cd02964  83 EDEElRELLEKQFKVEGIPTLVVLKPDGDVVTTNARDEVE 122
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 11-113 1.82e-35

Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are thioredoxin (TRX)-like protein disulfide oxidoreductases that alter the redox state of target proteins via the reversible oxidation of an active center CXXC motif. TryX is involved in the regulation of oxidative stress in parasitic trypanosomatids by reducing TryX peroxidase, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. TryX derives reducing equivalents from reduced trypanothione, a polyamine peptide conjugate unique to trypanosomatids, which is regenerated by the NADPH-dependent flavoprotein trypanothione reductase. Vertebrate NRX is a 400-amino acid nuclear protein with one redox active TRX domain containing a CPPC active site motif followed by one redox inactive TRX-like domain. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. Plant NRX, longer than the vertebrate NRX by about 100-200 amino acids, is a nuclear protein containing a redox inactive TRX-like domain between two redox active TRX domains. Both vertebrate and plant NRXs show thiol oxidoreductase activity in vitro. Their localization in the nucleus suggests a role in the redox regulation of nuclear proteins such as transcription factors.


Pssm-ID: 239307 [Multi-domain]  Cd Length: 131  Bit Score: 118.16  E-value: 1.82e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844  11 EALAGKIGGFYFSAHWCPPCCMFTPILKKFYEKVYD---DFEIVFVSSDPSESGLKKYMQEChgDWYYIPFG-HEAKQKL 86
Cdd:cd03009  14 SSLEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEsgkNFEIVFISWDRDEESFNDYFSKM--PWLAVPFSdRERRSRL 91

                        90       100
                ....*....|....*....|....*..
gi 17564844  87 CVKYEITGMPTLVIVKPDGTEVKSDGR 113
Cdd:cd03009  92 NRTFKIEGIPTLIILDADGEVVTTDAR 118
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 15-106 4.90e-27

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 95.84  E-value: 4.90e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844    15 GKIGGFYFSAHWCPPCCMFTPILKKFYEKV--YDDFEIVFVSSDPSESGLKKYMQECHGDWYYIPFGHEAKQKLCVKYEI 92
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLkkKKNVEIVFVSLDRDLEEFKDYLKKMPKDWLSVPFDDDERNELKRKYGV 80

                          90
                  ....*....|....
gi 17564844    93 TGMPTLVIVKPDGT 106
Cdd:pfam13905  81 NAIPTLVLLDPNGE 94
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 3-108 7.89e-20

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 78.58  E-value: 7.89e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844   3 DWTLVDAT------EALAGKIGGFYFSAHWCPPCCMFTPILKKFYEKvYDDFEIVFVSSDPSESGLKKYMQECHGDWyyi 76
Cdd:COG0526  10 DFTLTDLDgkplslADLKGKPVLVNFWATWCPPCRAEMPVLKELAEE-YGGVVFVGVDVDENPEAVKAFLKELGLPY--- 85

                        90       100       110
                ....*....|....*....|....*....|..
gi 17564844  77 PFGHEAKQKLCVKYEITGMPTLVIVKPDGTEV 108
Cdd:COG0526  86 PVLLDPDGELAKAYGVRGIPTTVLIDKDGKIV 117
TryX_like_RdCVF cd03008
Tryparedoxin (TryX)-like family, Rod-derived cone viability factor (RdCVF) subfamily; RdCVF is ...
 11-117 4.00e-16

Tryparedoxin (TryX)-like family, Rod-derived cone viability factor (RdCVF) subfamily; RdCVF is a thioredoxin (TRX)-like protein specifically expressed in photoreceptors. RdCVF was isolated and identified as a factor that supports cone survival in retinal cultures. Cone photoreceptor loss is responsible for the visual handicap resulting from the inherited disease, retinitis pigmentosa. RdCVF shows 33% similarity to TRX but does not exhibit any detectable thiol oxidoreductase activity.


Pssm-ID: 239306  Cd Length: 146  Bit Score: 69.46  E-value: 4.00e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844  11 EALAGKIGGFYFSAHWCPPCCMFTPILKKFYEKVYDDFEI--------VFVSSDPSESGLKKYMQECHGDWYYIPFGHEA 82
Cdd:cd03008  21 ARLENRVLLLFFGAVVSPQCQLFAPKLKDFFVRLTDEFYVdrsaqlalVYVSMDQSEQQQESFLKDMPKKWLFLPFEDEF 100

                        90       100       110
                ....*....|....*....|....*....|....*
gi 17564844  83 KQKLCVKYEITGMPTLVIVKPDGTEVKSDGRYDVQ 117
Cdd:cd03008 101 RRELEAQFSVEELPTVVVLKPDGDVLAANAVDEIL 135
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
3-116 1.56e-12

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 59.88  E-value: 1.56e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844   3 DWTLVDAT------EALAGKIGGFYFSAHWCPPCCMFTPILKKFYEKVYD-DFEIVFVSSDPSESgLKKYMQECHGDWyy 75
Cdd:COG1225   3 DFTLPDLDgktvslSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDkGVEVLGVSSDSDEA-HKKFAEKYGLPF-- 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 17564844  76 iPFGHEAKQKLCVKYEITGMPTLVIVKPDGTEVKSD-GRYDV 116
Cdd:COG1225  80 -PLLSDPDGEVAKAYGVRGTPTTFLIDPDGKIRYVWvGPVDP 120
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 2-110 4.39e-12

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: 58.02  E-value: 4.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844   2 LDWTLVDaTEALAGKIGGFYFSAHWCPPCCMFTPILKKFYEK-VYDDFEIVFVSSD-PSESGLKKYMQEcHGdwYYIPFG 79
Cdd:cd02966   7 LDGKPVS-LSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEyKDDGVEVVGVNVDdDDPAAVKAFLKK-YG--ITFPVL 82

                        90       100       110
                ....*....|....*....|....*....|.
gi 17564844  80 HEAKQKLCVKYEITGMPTLVIVKPDGTEVKS 110
Cdd:cd02966  83 LDPDGELAKAYGVRGLPTTFLIDRDGRIRAR 113
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 21-109 2.26e-10

TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 52.95  E-value: 2.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844  21 YFSAHWCPPCCMFTPILKKFYEKvYDDFEIVFVSSDPSesglkkymqechgdwyyipfgheakQKLCVKYEITGMPTLVI 100
Cdd:cd02947  16 DFWAPWCGPCKAIAPVLEELAEE-YPKVKFVKVDVDEN-------------------------PELAEEYGVRSIPTFLF 69


                ....*....
gi 17564844 101 VKpDGTEVK 109
Cdd:cd02947  70 FK-NGKEVD 77
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 21-109 7.05e-09

Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 49.43  E-value: 7.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844  21 YFSAHWCPPCCMFTPILKKFYEKVYDDFEIVFVSSDpsesglkkymqechgdwyyipfgheAKQKLCVKYEITGMPTLVI 100
Cdd:COG3118  24 DFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVD-------------------------ENPELAAQFGVRSIPTLLL 78


                ....*....
gi 17564844 101 VKpDGTEVK 109
Cdd:COG3118  79 FK-DGQPVD 86
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 22-109 8.19e-08

thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport]


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 46.51  E-value: 8.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844    22 FSAHWCPPCCMFTPILKKFYEKVYDDFEIVFVSSDpsesglkkymqechgdwyyipfgheAKQKLCVKYEITGMPTLVIV 101
Cdd:TIGR01068  21 FWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVD-------------------------ENPDIAAKYGIRSIPTLLLF 75


                  ....*...
gi 17564844   102 KpDGTEVK 109
Cdd:TIGR01068  76 K-NGKEVD 82
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 10-105 4.91e-07

TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE homolog subfamily; composed of ScsD, the DsbE homolog of Mycobacterium tuberculosis (MtbDsbE) and similar proteins, all containing a redox-active CXXC motif. The Salmonella typhimurium ScsD is a thioredoxin-like protein which confers copper tolerance to copper-sensitive mutants of E. coli. MtbDsbE has been characterized as an oxidase in vitro, catalyzing the disulfide bond formation of substrates like hirudin. The reduced form of MtbDsbE is more stable than its oxidized form, consistent with an oxidase function. This is in contrast to the function of DsbE from gram-negative bacteria which is a specific reductase of apocytochrome c.


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 44.98  E-value: 4.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844  10 TEALAGKIGGFYFSAHWCPPCCMFTPILkkfyEKVYDDFEIVFVS-SDPSESGLKKYMQECHGDWYYIPfghEAKQKLCV 88
Cdd:cd03011  15 LESLSGKPVLVYFWATWCPVCRFTSPTV----NQLAADYPVVSVAlRSGDDGAVARFMQKKGYGFPVIN---DPDGVISA 87

                        90
                ....*....|....*..
gi 17564844  89 KYEITGMPTLVIVKPDG 105
Cdd:cd03011  88 RWGVSVTPAIVIVDPGG 104
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 21-113 5.08e-06

Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 41.83  E-value: 5.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844    21 YFSAHWCPPCCMFTPILKKFYEKVYDDFEIVFVSSDPSESglkkymqechgdwyyipfgheakqkLCVKYEITGMPTLVI 100
Cdd:pfam00085  24 DFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPD-------------------------LASKYGVRGYPTLIF 78

                          90
                  ....*....|...
gi 17564844   101 VKPDGTEVKSDGR 113
Cdd:pfam00085  79 FKNGQPVDDYVGA 91
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 20-109 9.86e-05

Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI and PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5, PDIR, ERp46 and the transmembrane PDIs. PDI, ERp57, ERp72, P5, PDIR and ERp46 are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins usually contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and may also contain one or more redox inactive TRX-like (b) domains. Only one a domain is required for the oxidase function but multiple copies are necessary for the isomerase function. The different types of PDIs may show different substrate specificities and tissue-specific expression, or may be induced by stress. PDIs are in their reduced form at steady state and are oxidized to the active form by Ero1, which is localized in the ER through ERp44. Some members of this family also contain a DnaJ domain in addition to the redox active a domains; examples are ERdj5 and Pfj2. Also included in the family is the redox inactive N-terminal TRX-like domain of ERp29.


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 38.75  E-value: 9.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844  20 FYfsAHWCPPCCMFTPILKKFYEKVYDDFEIVFVSSDpsesglkkymqeCHgdwyyipfgheAKQKLCVKYEITGMPTLV 99
Cdd:cd02961  22 FY--APWCGHCKALAPEYEKLAKELKGDGKVVVAKVD------------CT-----------ANNDLCSEYGVRGYPTIK 76

                        90
                ....*....|
gi 17564844 100 IVKPDGTEVK 109
Cdd:cd02961  77 LFPNGSKEPV 86
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
22-109 1.20e-04

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 39.22  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844   22 FSAHWCPPCCMFTPILKKFYeKVYDD--FEIVFVSSDPSESGLKKYMQEcHGdwYYIPFGHEAKQKLCVKYEITGMPTLV 99
Cdd:PRK03147  68 FWGTWCKPCEKEMPYMNELY-PKYKEkgVEIIAVNVDETELAVKNFVNR-YG--LTFPVAIDKGRQVIDAYGVGPLPTTF 143

                         90
                 ....*....|
gi 17564844  100 IVKPDGTEVK 109
Cdd:PRK03147 144 LIDKDGKVVK 153
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 20-106 2.47e-04

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


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 37.97  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844    20 FYFSAHWCPPCcmfTPILKKFyEKVYDDF-----EIVFVSSDPSESgLKKYMQEcHGDWYyiPFGHEAKQKLCVKYEI-- 92
Cdd:pfam00578  31 FFYPADWTPVC---TTELPAL-ADLYEEFkklgvEVLGVSVDSPES-HKAFAEK-YGLPF--PLLSDPDGEVARAYGVln 102

                          90
                  ....*....|....*...
gi 17564844    93 ----TGMPTLVIVKPDGT 106
Cdd:pfam00578 103 eeegGALRATFVIDPDGK 120
TraF pfam13728
F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated ...
 8-104 8.16e-04

F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated with export. The 19 amino acids at the amino terminus of the polypeptides appear to constitute a typical membrane leader peptide - not included in this family, while the remainder of the molecule is predicted to be primarily hydrophilic in character. F plasmid TraF and TraH are required for F pilus assembly and F plasmid transfer, and they are both localized to the outer membrane in the presence of the complete F transfer region, especially TraV, the putative anchor.


Pssm-ID: 433436 [Multi-domain]  Cd Length: 224  Bit Score: 37.29  E-value: 8.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844     8 DATEALAGKIGGFYFSAHWCPPCCMFTPILKKFYEKvyDDFEIVFVSSD--PSEsGLKKYMQEchgdwyyipfgHEAKQK 85
Cdd:pfam13728 122 AALKSLAEEFGLIFFYRGDCPYCEAQAPILQAFADK--YGWTVRPVSVDgrPLP-GFPNYRVD-----------NGQAAR 187

                          90
                  ....*....|....*....
gi 17564844    86 LCVKYeitgMPTLVIVKPD 104
Cdd:pfam13728 188 LGVKR----TPALFLVNPP 202
PLN02927 PLN02927
antheraxanthin epoxidase/zeaxanthin epoxidase
 1-104 2.24e-03

antheraxanthin epoxidase/zeaxanthin epoxidase


Pssm-ID: 178515 [Multi-domain]  Cd Length: 668  Bit Score: 36.23  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844    1 MLDWTLVDATEALAGKiggfyfsahwcPPCCMFTpilkkfyEKVYDDFEIVFVSSDPSESGLKkymqechGDWYYIPFGH 80
Cdd:PLN02927 487 MLDWVLGGNSEKLEGR-----------PPSCRLT-------DKADDRLREWFEDDDALERTIK-------GEWYLIPHGD 541

                         90       100
                 ....*....|....*....|....*.
gi 17564844   81 E--AKQKLCVKYEiTGMPTLVIVKPD 104
Cdd:PLN02927 542 DccVSETLCLTKD-EDQPCIVGSEPD 566
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 20-76 5.73e-03

Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 34.65  E-value: 5.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 17564844    20 FYFSAhWCPPCCMFTPILKKFYEKVYD-DFEIVFVSSDPSESGLKKYMQECHGDWYYI 76
Cdd:pfam08534  35 FWPGA-FCPTCSAEHPYLEKLNELYKEkGVDVVAVNSDNDAFFVKRFWGKEGLPFPFL 91
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 2-73 6.11e-03

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: 34.50  E-value: 6.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844   2 LDWTLVDAT------EALAGKIGGFYFSAHWCPPCC-----MFTPILKKFYEKVYDDFEIVFVSSDP----SESgLKKYM 66
Cdd:cd02968   3 PDFTLTDQDgrpvtlSDLKGKPVLVYFGYTHCPDVCpttlaNLAQALKQLGADGGDDVQVVFISVDPerdtPEV-LKAYA 81


                ....*..
gi 17564844  67 QECHGDW 73
Cdd:cd02968  82 KAFGPGW 88
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 21-108 8.40e-03

Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 34.11  E-value: 8.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17564844  21 YFSAHWCPPCcmftpilKKFYEKVYDDFEIvfvssdpsesglKKYMQEcHGDWYYIPF----------GHEAKQK-LCVK 89
Cdd:COG2143  46 FFESDWCPYC-------KKLHKEVFSDPEV------------AAYLKE-NFVVVQLDAegdkevtdfdGETLTEKeLARK 105

                        90
                ....*....|....*....
gi 17564844  90 YEITGMPTLVIVKPDGTEV 108
Cdd:COG2143 106 YGVRGTPTLVFFDAEGKEI 124
 
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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