NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2546810924|ref|WP_301350662|]
View 

TlpA disulfide reductase family protein [uncultured Muribaculum sp.]

Protein Classification

TlpA family protein disulfide reductase( domain architecture ID 10001660)

TlpA family protein disulfide reductase such as Bradyrhizobium japonicum thiol:disulfide interchange protein TlpA, an unusual thioredoxin which has been implicated in the biogenesis of cytochrome aa3 and also characterized as a reductant for the copper metallochaperone ScoI, and similar to ResA and DsbE, which are essential proteins in cytochrome c maturation

CATH:  3.40.30.10
Gene Ontology:  GO:0016491
PubMed:  11531338|15667290

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 331-451 1.02e-23

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


:

Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 96.30  E-value: 1.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546810924 331 TSTGSDLPPMKLIDSEGRELSLDSFKGKPVLLDFWSIGCGPCLEEFRQMDEFKKALGDkadnLQVVTVCCGNpDNQRWKN 410
Cdd:COG0526     2 KAVGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYGG----VVFVGVDVDE-NPEAVKA 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2546810924 411 MITRYNLNDVNTVIMHNESAPIYSTIGYPTYILVGPDGKIV 451
Cdd:COG0526    77 FLKELGLPYPVLLDPDGELAKAYGVRGIPTTVLIDKDGKIV 117
 
Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 331-451 1.02e-23

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 96.30  E-value: 1.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546810924 331 TSTGSDLPPMKLIDSEGRELSLDSFKGKPVLLDFWSIGCGPCLEEFRQMDEFKKALGDkadnLQVVTVCCGNpDNQRWKN 410
Cdd:COG0526     2 KAVGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYGG----VVFVGVDVDE-NPEAVKA 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2546810924 411 MITRYNLNDVNTVIMHNESAPIYSTIGYPTYILVGPDGKIV 451
Cdd:COG0526    77 FLKELGLPYPVLLDPDGELAKAYGVRGIPTTVLIDKDGKIV 117
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 342-452 4.40e-21

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: 88.45  E-value: 4.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546810924 342 LIDSEGRELSLDSFKGKPVLLDFWSIGCGPCLEEFRQMDEFKKALGDkaDNLQVVTVCCGNPDNQRWKNMITRYNLNDVN 421
Cdd:cd02966     4 LPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKD--DGVEVVGVNVDDDDPAAVKAFLKKYGITFPV 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2546810924 422 TVIMHNESAPIYSTIGYPTYILVGPDGKIVE 452
Cdd:cd02966    82 LLDPDGELAKAYGVRGLPTTFLIDRDGRIRA 112
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
334-452 1.59e-12

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 65.79  E-value: 1.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546810924 334 GSDLPPMKLIDSEGRELSLDSFKGKPVLLDFWSIGCGPCLEEFRQMDEFKKALGDKAdnLQVVTVCCGNPdNQRWKNMIT 413
Cdd:PRK03147   38 GKEAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKG--VEIIAVNVDET-ELAVKNFVN 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2546810924 414 RYNLN-----DVNTVIMHnesapIYSTIGYPTYILVGPDGKIVE 452
Cdd:PRK03147  115 RYGLTfpvaiDKGRQVID-----AYGVGPLPTTFLIDKDGKVVK 153
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 334-452 3.89e-11

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: 60.32  E-value: 3.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546810924 334 GSDLPPMKLIDSEGRELSLDSFKGKPVLLDFW-SIGCGPCLEEFRQMDEFKKALgdKADNLQVVTVCCGNPDNQrwKNMI 412
Cdd:pfam00578   2 GDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYpADWTPVCTTELPALADLYEEF--KKLGVEVLGVSVDSPESH--KAFA 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2546810924 413 TRYNLN-----DVNTVIMHNESAPIY-STIGYPTYILVGPDGKIVE 452
Cdd:pfam00578  78 EKYGLPfpllsDPDGEVARAYGVLNEeEGGALRATFVIDPDGKVRY 123
 
Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 331-451 1.02e-23

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 96.30  E-value: 1.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546810924 331 TSTGSDLPPMKLIDSEGRELSLDSFKGKPVLLDFWSIGCGPCLEEFRQMDEFKKALGDkadnLQVVTVCCGNpDNQRWKN 410
Cdd:COG0526     2 KAVGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYGG----VVFVGVDVDE-NPEAVKA 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2546810924 411 MITRYNLNDVNTVIMHNESAPIYSTIGYPTYILVGPDGKIV 451
Cdd:COG0526    77 FLKELGLPYPVLLDPDGELAKAYGVRGIPTTVLIDKDGKIV 117
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 342-452 4.40e-21

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: 88.45  E-value: 4.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546810924 342 LIDSEGRELSLDSFKGKPVLLDFWSIGCGPCLEEFRQMDEFKKALGDkaDNLQVVTVCCGNPDNQRWKNMITRYNLNDVN 421
Cdd:cd02966     4 LPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKD--DGVEVVGVNVDDDDPAAVKAFLKKYGITFPV 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2546810924 422 TVIMHNESAPIYSTIGYPTYILVGPDGKIVE 452
Cdd:cd02966    82 LLDPDGELAKAYGVRGLPTTFLIDRDGRIRA 112
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
338-451 3.51e-19

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 83.76  E-value: 3.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546810924 338 PPMKLIDSEGRELSLDSFKGKPVLLDFWSIGCGPCLEEFRQMDEFKKALGDKadNLQVVTVccgNPDN-QRWKNMITRYN 416
Cdd:COG1225     2 PDFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDK--GVEVLGV---SSDSdEAHKKFAEKYG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2546810924 417 LN-----DVntvimHNESAPIYSTIGYPTYILVGPDGKIV 451
Cdd:COG1225    77 LPfpllsDP-----DGEVAKAYGVRGTPTTFLIDPDGKIR 111
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
334-452 1.59e-12

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 65.79  E-value: 1.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546810924 334 GSDLPPMKLIDSEGRELSLDSFKGKPVLLDFWSIGCGPCLEEFRQMDEFKKALGDKAdnLQVVTVCCGNPdNQRWKNMIT 413
Cdd:PRK03147   38 GKEAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKG--VEIIAVNVDET-ELAVKNFVN 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2546810924 414 RYNLN-----DVNTVIMHnesapIYSTIGYPTYILVGPDGKIVE 452
Cdd:PRK03147  115 RYGLTfpvaiDKGRQVID-----AYGVGPLPTTFLIDKDGKVVK 153
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 334-452 3.89e-11

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: 60.32  E-value: 3.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546810924 334 GSDLPPMKLIDSEGRELSLDSFKGKPVLLDFW-SIGCGPCLEEFRQMDEFKKALgdKADNLQVVTVCCGNPDNQrwKNMI 412
Cdd:pfam00578   2 GDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYpADWTPVCTTELPALADLYEEF--KKLGVEVLGVSVDSPESH--KAFA 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2546810924 413 TRYNLN-----DVNTVIMHNESAPIY-STIGYPTYILVGPDGKIVE 452
Cdd:pfam00578  78 EKYGLPfpllsDPDGEVARAYGVLNEeEGGALRATFVIDPDGKVRY 123
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 334-452 2.75e-10

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 58.54  E-value: 2.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546810924 334 GSDLPPMKLID--SEGRELSLDSFKGKPVLLDFW-SIGCGPCLEEFRQMDEFKKALGDKADnlQVVTVCCGNpDNQRWKN 410
Cdd:pfam08534   3 GDKAPDFTLPDaaTDGNTVSLSDFKGKKVVLNFWpGAFCPTCSAEHPYLEKLNELYKEKGV--DVVAVNSDN-DAFFVKR 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2546810924 411 MITRYNLNDvntVIMHNESA------------PIYSTIGYPTYILVGPDGKIVE 452
Cdd:pfam08534  80 FWGKEGLPF---PFLSDGNAaftkalglpieeDASAGLRSPRYAVIDEDGKVVY 130
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 357-450 7.14e-09

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: 53.08  E-value: 7.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546810924 357 GKPVLLDFWSIGCGPCLEEFRQMDEFKKALgDKADNLQVVTVCCGNPDNQrWKNMITRYNL--------NDVNTVIMHNe 428
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKL-KKKKNVEIVFVSLDRDLEE-FKDYLKKMPKdwlsvpfdDDERNELKRK- 77

                          90       100
                  ....*....|....*....|..
gi 2546810924 429 sapiYSTIGYPTYILVGPDGKI 450
Cdd:pfam13905  78 ----YGVNAIPTLVLLDPNGEV 95
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 338-398 3.69e-06

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: 46.44  E-value: 3.69e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2546810924 338 PPMKLIDSEGRELSLDSFKGKPVLLDFwsiG---CgP--CLEEFRQMDEFKKALGDKA-DNLQVVTV 398
Cdd:cd02968     3 PDFTLTDQDGRPVTLSDLKGKPVLVYF---GythC-PdvCPTTLANLAQALKQLGADGgDDVQVVFI 65
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 337-387 5.91e-06

TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, periplasmic TRX-like reductase containing a CXXC motif that specifically donates reducing equivalents to apocytochrome c via CcmH, another cytochrome c maturation (Ccm) factor with a redox active CXXC motif. Assembly of cytochrome c requires the ligation of heme to reduced thiols of the apocytochrome. In bacteria, this assembly occurs in the periplasm. The reductase activity of DsbE in the oxidizing environment of the periplasm is crucial in the maturation of cytochrome c.


Pssm-ID: 239308 [Multi-domain]  Cd Length: 127  Bit Score: 45.65  E-value: 5.91e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2546810924 337 LPPMKL--IDSEGRELSLDSFKGKPVLLDFWSIGCGPCLEEFRQMDEFKKALG 387
Cdd:cd03010     3 APAFSLpaLPGPDKTLTSADLKGKPYLLNVWASWCAPCREEHPVLMALARQGR 55
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 356-451 2.69e-05

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 46.77  E-value: 2.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546810924  356 KGKPVLLDFWSIGCGPCLEEFRQMDEFKKALGDKAdnLQVVTVCCGNPDNQR----WKNMITRYNLND--VNTVIMHnes 429
Cdd:PLN02919   419 KGKVVILDFWTYCCINCMHVLPDLEFLEKKYKDQP--FTVVGVHSAKFDNEKdleaIRNAVLRYNISHpvVNDGDMY--- 493

                           90       100
                   ....*....|....*....|....*
gi 2546810924  430 apIYSTIG---YPTYILVGPDGKIV 451
Cdd:PLN02919   494 --LWRELGvssWPTFAVVSPNGKLI 516
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 337-452 4.31e-05

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.


Pssm-ID: 239315  Cd Length: 140  Bit Score: 43.31  E-value: 4.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546810924 337 LPPMKLIDSEGRELSLDSFKGKPVLLDFW----SIGCGPCLEEFRQ-MDEFKKAlgdkadNLQVVTVCCGNPDNQRwkNM 411
Cdd:cd03017     3 APDFTLPDQDGETVSLSDLRGKPVVLYFYpkddTPGCTKEACDFRDlYEEFKAL------GAVVIGVSPDSVESHA--KF 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2546810924 412 ITRYNLN-----DVN-TVI----MHNESAPIYSTIGYPTYILvGPDGKIVE 452
Cdd:cd03017    75 AEKYGLPfpllsDPDgKLAkaygVWGEKKKKYMGIERSTFLI-DPDGKIVK 124
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
356-450 4.73e-05

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 42.41  E-value: 4.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546810924 356 KGKPVLLDFWSIGCGPC---LEEFRQMDEFKKALGDKADnLQVVTVCCGNPDNQRWKNMITrynlndvntvimHNESAPI 432
Cdd:pfam13098   3 NGKPVLVVFTDPDCPYCkklKKELLEDPDVTVYLGPNFV-FIAVNIWCAKEVAKAFTDILE------------NKELGRK 69

                          90
                  ....*....|....*...
gi 2546810924 433 YSTIGYPTYILVGPDGKI 450
Cdd:pfam13098  70 YGVRGTPTIVFFDGKGEL 87
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 341-398 8.03e-05

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


Pssm-ID: 441602  Cd Length: 156  Bit Score: 42.97  E-value: 8.03e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546810924 341 KLIDSEGRELSLDSFKGKPVLLDFWSIGC-GPCLEEFRQMDEFKKALGDKA-DNLQVVTV 398
Cdd:COG1999     4 TLTDQDGKPVTLADLRGKPVLVFFGYTSCpDVCPTTLANLAQVQEALGEDGgDDVQVLFI 63
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 349-398 2.39e-04

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: 40.19  E-value: 2.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2546810924 349 ELSLDSFK------GKPVLLDFWSIGCGPCleefRQMD-EFKKALGDKADNLQVVTV 398
Cdd:COG3118     4 ELTDENFEeevlesDKPVLVDFWAPWCGPC----KMLApVLEELAAEYGGKVKFVKV 56
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 357-437 3.22e-04

TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium Synechococcus. It is found only in oxygenic photosynthetic organisms. TRX is a small enzyme that participate in redox reactions, via the reversible oxidation of an active site dithiol present in a CXXC motif. Disruption of the txlA gene suggests that the protein is involved in the redox regulation of the structure and function of photosynthetic apparatus. The plant homolog (designated as HCF164) is localized in the chloroplast and is involved in the assembly of the cytochrome b6f complex, which takes a central position in photosynthetic electron transport.


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 40.78  E-value: 3.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546810924 357 GKPVLLDFWSIGCGPCLEEFRQMDEFKKALGDKADnlqVVTVccgNPDNQRWKNMITRYNLNDV-NTVIMHNESAPIYST 435
Cdd:cd02950    20 GKPTLVEFYADWCTVCQEMAPDVAKLKQKYGDQVN---FVML---NVDNPKWLPEIDRYRVDGIpHFVFLDREGNEEGQS 93


                  ..
gi 2546810924 436 IG 437
Cdd:cd02950    94 IG 95
TlpA_like_DipZ_like cd03012
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ...
 349-451 3.69e-04

TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a TlpA-like TRX domain. Some members show domain architectures similar to that of E. coli DipZ protein (also known as DsbD). The only eukaryotic members of the TlpA family belong to this subfamily. TlpA is a disulfide reductase known to have a crucial role in the biogenesis of cytochrome aa3.


Pssm-ID: 239310 [Multi-domain]  Cd Length: 126  Bit Score: 40.37  E-value: 3.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546810924 349 ELSLDSFKGKPVLLDFWSIGCGPCLEEFRQMDEFKKALGDkaDNLQVVTVCCGNPDNQR----WKNMITRYN-----LND 419
Cdd:cd03012    15 PLSLAQLRGKVVLLDFWTYCCINCLHTLPYLTDLEQKYKD--DGLVVIGVHSPEFAFERdlanVKSAVLRYGitypvAND 92

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2546810924 420 VNTVIMHNesapiYSTIGYPTYILVGPDGKIV 451
Cdd:cd03012    93 NDYATWRA-----YGNQYWPALYLIDPTGNVR 119
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 339-464 4.35e-04

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: 39.97  E-value: 4.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546810924 339 PMKLIDseGRELSLDSFKGKPVLLDFWSIGCGPCLEEfrqmdefKKALGDKADNLQVVTVCCGNPDNQRWKNMITRY--- 415
Cdd:cd03011     4 TATTLD--GEQFDLESLSGKPVLVYFWATWCPVCRFT-------SPTVNQLAADYPVVSVALRSGDDGAVARFMQKKgyg 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2546810924 416 --NLNDVNTVIMHNesapiYSTIGYPTYILVGPDGkIVEWNTDRPSTVLLK 464
Cdd:cd03011    75 fpVINDPDGVISAR-----WGVSVTPAIVIVDPGG-IVFVTTGVTSEWGLR 119
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 356-398 7.41e-04

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: 38.69  E-value: 7.41e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2546810924 356 KGKPVLLDFWSIGCGPCleefRQMDEFKKALGDKADNLQVVTV 398
Cdd:cd02947     9 SAKPVVVDFWAPWCGPC----KAIAPVLEELAEEYPKVKFVKV 47
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 334-413 3.31e-03

Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing peroxidatic and resolving cysteines, similar to the homodimeric thiol specific antioxidant (TSA) protein also known as TRX-dependent thiol peroxidase (Tpx). Tpx is a bacterial periplasmic peroxidase which differs from other PRXs in that it shows substrate specificity toward alkyl hydroperoxides over hydrogen peroxide. As with all other PRXs, the peroxidatic cysteine (N-terminal) of Tpx is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Tpx is able to resolve this intermediate by forming an intramolecular disulfide bond with a conserved C-terminal cysteine (the resolving cysteine), which can then be reduced by thioredoxin. This differs from the typical 2-cys PRX which resolves the oxidized cysteine by forming an intermolecular disulfide bond with the resolving cysteine from the other subunit of the homodimer. Atypical 2-cys PRX homodimers have a loop-based interface (A-type for alternate), in contrast with the B-type interface of typical 2-cys and 1-cys PRXs.


Pssm-ID: 239312 [Multi-domain]  Cd Length: 143  Bit Score: 37.95  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546810924 334 GSDLPPMKLIDSEGRELSLDSFKGKPVLLD-FWSIGCGPCLEEFRQMDEfkkaLGDKADNLQVVTVCCGNPDNQ-RW--- 408
Cdd:cd03014     3 GDKAPDFTLVTSDLSEVSLADFAGKVKVISvFPSIDTPVCATQTKRFNK----EAAKLDNTVVLTISADLPFAQkRWcga 78


                  ....*...
gi 2546810924 409 ---KNMIT 413
Cdd:cd03014    79 egvDNVTT 86
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 341-451 3.86e-03

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: 37.59  E-value: 3.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546810924 341 KLIDSEGRELSlDSFKGKPVLLDFWSIGCGPCLEEFRQMDEFKKALGDKADNLQVVTVccgNPD------NQRWKNMITR 414
Cdd:cd02964     2 FLLDGEGVVPV-SALEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEEGKNFEIVFV---SRDrseesfNEYFSEMPPW 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2546810924 415 YNL--NDVNTvimHNESAPIYSTIGYPTYILVGPDGKIV 451
Cdd:cd02964    78 LAVpfEDEEL---RELLEKQFKVEGIPTLVVLKPDGDVV 113
DsbD COG4232
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ...
 356-450 4.95e-03

Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443376 [Multi-domain]  Cd Length: 416  Bit Score: 39.02  E-value: 4.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546810924 356 KGKPVLLDFWSIGCGPCLE-E---FRQmDEFKKALGDKADNLQV-VTvccgNPDNQrWKNMITRYNLNdvntvimhnesa 430
Cdd:COG4232   319 EGKPVFVDFTADWCVTCKEnErtvFSD-PEVQAALADDVVLLKAdVT----DNDPE-ITALLKRFGRF------------ 380

                          90       100
                  ....*....|....*....|
gi 2546810924 431 piystiGYPTYILVGPDGKI 450
Cdd:COG4232   381 ------GVPTYVFYDPDGEE 394
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 356-451 8.14e-03

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 36.81  E-value: 8.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546810924 356 KGKPVLLDFWSIGCGPC--LEE--FRQMdEFKKALgdkADNLQVVTVccgNPDNQRwknMITRYNlndvNTVIMHNESAP 431
Cdd:COG2143    39 EGKPILLFFESDWCPYCkkLHKevFSDP-EVAAYL---KENFVVVQL---DAEGDK---EVTDFD----GETLTEKELAR 104

                          90       100
                  ....*....|....*....|
gi 2546810924 432 IYSTIGYPTYILVGPDGKIV 451
Cdd:COG2143   105 KYGVRGTPTLVFFDAEGKEI 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH