NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|917214240|ref|WP_051820952|]
View 

TlpA disulfide reductase family protein [Mageeibacillus indolicus]

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, ...
 93-246 4.35e-28

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


:

Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 104.00  E-value: 4.35e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917214240  93 GAETPAaYESETKDGKKVTLDQFKGKVVLLTMGATWCPDCQKELKMLNKLYQNYkdnKDVVFLPtylVDgKKETKDTIKA 172
Cdd:COG0526    5 GKPAPD-FTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEY---GGVVFVG---VD-VDENPEAVKA 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917214240 173 FYEKEKLDLPCYYGDKATLRANFQIGWIPTLMVINKEGKcvpmgkddagniEYYRHT-DITPELLTEKISAALEA 246
Cdd:COG0526   77 FLKELGLPYPVLLDPDGELAKAYGVRGIPTTVLIDKDGK------------IVARHVgPLSPEELEEALEKLLAK 139
 
Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 93-246 4.35e-28

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 104.00  E-value: 4.35e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917214240  93 GAETPAaYESETKDGKKVTLDQFKGKVVLLTMGATWCPDCQKELKMLNKLYQNYkdnKDVVFLPtylVDgKKETKDTIKA 172
Cdd:COG0526    5 GKPAPD-FTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEY---GGVVFVG---VD-VDENPEAVKA 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917214240 173 FYEKEKLDLPCYYGDKATLRANFQIGWIPTLMVINKEGKcvpmgkddagniEYYRHT-DITPELLTEKISAALEA 246
Cdd:COG0526   77 FLKELGLPYPVLLDPDGELAKAYGVRGIPTTVLIDKDGK------------IVARHVgPLSPEELEEALEKLLAK 139
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 106-211 2.63e-26

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: 98.85  E-value: 2.63e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917214240 106 DGKKVTLDQFKGKVVLLTMGATWCPDCQKELKMLNKLYQNYKDnKDVVFLptyLVDGKKETKDTIKAFYEKEKLDLPCYY 185
Cdd:cd02966    8 DGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKD-DGVEVV---GVNVDDDDPAAVKAFLKKYGITFPVLL 83

                         90       100
                 ....*....|....*....|....*.
gi 917214240 186 GDKATLRANFQIGWIPTLMVINKEGK 211
Cdd:cd02966   84 DPDGELAKAYGVRGLPTTFLIDRDGR 109
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 117-211 6.85e-13

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: 62.71  E-value: 6.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917214240  117 GKVVLLTMGATWCPDCQKELKMLNKLYQNYKDNKDVVFLPTYLVDGKKETKDTIKAfYEKEKLDLPCYYGDKATLRANFQ 196
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKKKKNVEIVFVSLDRDLEEFKDYLKK-MPKDWLSVPFDDDERNELKRKYG 79

                          90
                  ....*....|....*
gi 917214240  197 IGWIPTLMVINKEGK 211
Cdd:pfam13905  80 VNAIPTLVLLDPNGE 94
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
87-213 3.42e-12

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 62.71  E-value: 3.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917214240  87 KKDIYKGAETPAAYESETKDGKKVTLDQFKGKVVLLTMGATWCPDCQKELKMLNKLYQNYKDnKDVVFLPTYLvdgkKET 166
Cdd:PRK03147  31 DKEKVQVGKEAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKE-KGVEIIAVNV----DET 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 917214240 167 KDTIKAFYEKEKLDLPCYYGDKATLRANFQIGWIPTLMVINKEGKCV 213
Cdd:PRK03147 106 ELAVKNFVNRYGLTFPVAIDKGRQVIDAYGVGPLPTTFLIDKDGKVV 152
 
Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 93-246 4.35e-28

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 104.00  E-value: 4.35e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917214240  93 GAETPAaYESETKDGKKVTLDQFKGKVVLLTMGATWCPDCQKELKMLNKLYQNYkdnKDVVFLPtylVDgKKETKDTIKA 172
Cdd:COG0526    5 GKPAPD-FTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEY---GGVVFVG---VD-VDENPEAVKA 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917214240 173 FYEKEKLDLPCYYGDKATLRANFQIGWIPTLMVINKEGKcvpmgkddagniEYYRHT-DITPELLTEKISAALEA 246
Cdd:COG0526   77 FLKELGLPYPVLLDPDGELAKAYGVRGIPTTVLIDKDGK------------IVARHVgPLSPEELEEALEKLLAK 139
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 106-211 2.63e-26

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: 98.85  E-value: 2.63e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917214240 106 DGKKVTLDQFKGKVVLLTMGATWCPDCQKELKMLNKLYQNYKDnKDVVFLptyLVDGKKETKDTIKAFYEKEKLDLPCYY 185
Cdd:cd02966    8 DGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKD-DGVEVV---GVNVDDDDPAAVKAFLKKYGITFPVLL 83

                         90       100
                 ....*....|....*....|....*.
gi 917214240 186 GDKATLRANFQIGWIPTLMVINKEGK 211
Cdd:cd02966   84 DPDGELAKAYGVRGLPTTFLIDRDGR 109
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
106-247 7.83e-21

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 84.92  E-value: 7.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917214240 106 DGKKVTLDQFKGKVVLLTMGATWCPDCQKELKMLNKLYQNYKDnKDVVFLPtylVDgkKETKDTIKAFYEKEKLDLPCYY 185
Cdd:COG1225   10 DGKTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKD-KGVEVLG---VS--SDSDEAHKKFAEKYGLPFPLLS 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917214240 186 GDKATLRANFQIGWIPTLMVINKEGKcvpmgkddagnIEYYRHTDITPEL-LTEKISAALEAK 247
Cdd:COG1225   84 DPDGEVAKAYGVRGTPTTFLIDPDGK-----------IRYVWVGPVDPRPhLEEVLEALLAEL 135
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 117-211 6.85e-13

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: 62.71  E-value: 6.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917214240  117 GKVVLLTMGATWCPDCQKELKMLNKLYQNYKDNKDVVFLPTYLVDGKKETKDTIKAfYEKEKLDLPCYYGDKATLRANFQ 196
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKKKKNVEIVFVSLDRDLEEFKDYLKK-MPKDWLSVPFDDDERNELKRKYG 79

                          90
                  ....*....|....*
gi 917214240  197 IGWIPTLMVINKEGK 211
Cdd:pfam13905  80 VNAIPTLVLLDPNGE 94
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
87-213 3.42e-12

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 62.71  E-value: 3.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917214240  87 KKDIYKGAETPAAYESETKDGKKVTLDQFKGKVVLLTMGATWCPDCQKELKMLNKLYQNYKDnKDVVFLPTYLvdgkKET 166
Cdd:PRK03147  31 DKEKVQVGKEAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKE-KGVEIIAVNV----DET 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 917214240 167 KDTIKAFYEKEKLDLPCYYGDKATLRANFQIGWIPTLMVINKEGKCV 213
Cdd:PRK03147 106 ELAVKNFVNRYGLTFPVAIDKGRQVIDAYGVGPLPTTFLIDKDGKVV 152
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 106-246 7.42e-11

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


Pssm-ID: 441602  Cd Length: 156  Bit Score: 58.76  E-value: 7.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917214240 106 DGKKVTLDQFKGKVVLLTMGATWCPD-CQKELKMLNKLYQNYKDN--KDVVFLpTYLVDGKKETKDTIKAFyeKEKLDLP 182
Cdd:COG1999    9 DGKPVTLADLRGKPVLVFFGYTSCPDvCPTTLANLAQVQEALGEDggDDVQVL-FISVDPERDTPEVLKAY--AEAFGAP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917214240 183 CY---YGDKATLRA-----NFQIGWIP----------TLMVINKEGKCVpmgkddagniEYYRHTDiTPELLTEKISAAL 244
Cdd:COG1999   86 RWiglTGDPEEIAAlakafGVYYEKVPdgdytfdhsaAVYLVDPDGRLR----------GYYPAGE-DPEELAADLKALL 154


                 ..
gi 917214240 245 EA 246
Cdd:COG1999  155 EE 156
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 106-211 3.29e-10

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: 56.08  E-value: 3.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917214240  106 DGKKVTLDQFKGKVVLLTMGAT-WCPDCQKELKMLNKLYQNYKD-NKDVVFLPTylvdgkkETKDTIKAFYEKEKLDLPC 183
Cdd:pfam00578  14 DGGTVSLSDYRGKWVVLFFYPAdWTPVCTTELPALADLYEEFKKlGVEVLGVSV-------DSPESHKAFAEKYGLPFPL 86

                          90       100       110
                  ....*....|....*....|....*....|....
gi 917214240  184 YYGDKATLRANFQIGW------IPTLMVINKEGK 211
Cdd:pfam00578  87 LSDPDGEVARAYGVLNeeeggaLRATFVIDPDGK 120
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 105-213 1.90e-08

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: 51.52  E-value: 1.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917214240 105 KDGKKVTLDQFKGKVVLLTMGATWCPDCQKELKMLNKLYQNYKD---NKDVVFLPTylvdgkKETKDTIKAFYEKEK-LD 180
Cdd:cd03009    6 NDGGKVPVSSLEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEsgkNFEIVFISW------DRDEESFNDYFSKMPwLA 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 917214240 181 LPcyYGDKAT---LRANFQIGWIPTLMVINKEGKCV 213
Cdd:cd03009   80 VP--FSDRERrsrLNRTFKIEGIPTLIILDADGEVV 113
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 109-213 3.13e-08

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: 51.07  E-value: 3.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917214240 109 KVTLDQFKGKVVLLTMGATWCPDCQKELKMLNKLYQNYKD---NKDVVFLptylvdGKKETKDTIKAFYEKEK--LDLPc 183
Cdd:cd02964    9 VVPVSALEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEegkNFEIVFV------SRDRSEESFNEYFSEMPpwLAVP- 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 917214240 184 yYGDKAT---LRANFQIGWIPTLMVINKEGKCV 213
Cdd:cd02964   82 -FEDEELrelLEKQFKVEGIPTLVVLKPDGDVV 113
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 104-211 4.75e-07

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 48.13  E-value: 4.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917214240  104 TKDGKKVTLDQFKGKVVLLTMGAT-WCPDCQKELKMLNKLYQNYKDNKDVVFLPTYLVDGKketkdTIKAFYEKEKLDLP 182
Cdd:pfam08534  15 ATDGNTVSLSDFKGKKVVLNFWPGaFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNDAF-----FVKRFWGKEGLPFP 89

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 917214240  183 CYY-GDKATLRA--------NFQIGWIPTLMVINKEGK 211
Cdd:pfam08534  90 FLSdGNAAFTKAlglpieedASAGLRSPRYAVIDEDGK 127
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 110-151 1.46e-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: 46.03  E-value: 1.46e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 917214240 110 VTLDQFKGKVVLLTMGATWCPDCQKELKMLNKLYQ---------NYKDNKD 151
Cdd:cd03010   18 LTSADLKGKPYLLNVWASWCAPCREEHPVLMALARqgrvpiygiNYKDNPE 68
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 106-173 2.26e-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: 46.06  E-value: 2.26e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 917214240 106 DGKKVTLDQFKGKVVLLTMGATWCPD-CQKELKMLNKLYQNYKDN--KDVVFLP-TylVDGKKETKDTIKAF 173
Cdd:cd02968   11 DGRPVTLSDLKGKPVLVYFGYTHCPDvCPTTLANLAQALKQLGADggDDVQVVFiS--VDPERDTPEVLKAY 80
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
 80-247 1.95e-05

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 44.07  E-value: 1.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917214240  80 KAAVRGPKKDIYKgaetpaaYESETKDGKKVTLDQFKGKVVLLTMGATWCPDCQKELKMLNKLYQNYKDNK-DVVFLPT- 157
Cdd:PTZ00056   9 TVSKDELRKSIYD-------YTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGlEILAFPTs 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917214240 158 -YLVDGKKETKDtIKAFYEKEKLDLPCY------------------------YGDKATLRAnfqIGWIPTLMVINKEGKC 212
Cdd:PTZ00056  82 qFLNQEFPNTKD-IRKFNDKNKIKYNFFepievngenthelfkflkancdsmHDENGTLKA---IGWNFGKFLVNKSGNV 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 917214240 213 VPmgkddagnieyYRHTDITPELLTEKISAALEAK 247
Cdd:PTZ00056 158 VA-----------YFSPRTEPLELEKKIAELLGVK 181
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 99-148 6.57e-05

Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.


Pssm-ID: 238207 [Multi-domain]  Cd Length: 152  Bit Score: 41.73  E-value: 6.57e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 917214240  99 AYESETKDGKKVTLDQFKGKVVLLTMGATWCPDcQKELKMLNKLYQNYKD 148
Cdd:cd00340    4 DFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGF-TPQYEGLEALYEKYKD 52
PRK15412 PRK15412
thiol:disulfide interchange protein DsbE; Provisional
 116-150 7.21e-05

thiol:disulfide interchange protein DsbE; Provisional


Pssm-ID: 185310 [Multi-domain]  Cd Length: 185  Bit Score: 42.29  E-value: 7.21e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 917214240 116 KGKVVLLTMGATWCPDCQKELKMLNKLYQ--------NYKDNK 150
Cdd:PRK15412  67 QGKPVLLNVWATWCPTCRAEHQYLNQLSAqgirvvgmNYKDDR 109
PLN02412 PLN02412
probable glutathione peroxidase
 95-213 1.65e-04

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 41.13  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917214240  95 ETPAA-YESETKD--GKKVTLDQFKGKVVLLTMGATWCPDCQKELKMLNKLYQNYKDNK-DVVFLPTYLVDGK-----KE 165
Cdd:PLN02412   4 ESPKSiYDFTVKDigGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGfEILAFPCNQFLGQepgsnEE 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917214240 166 TKDTIKAFYEKE-----KLDL------PCYYGDKATLRANF--QIGWIPTLMVINKEGKCV 213
Cdd:PLN02412  84 IQQTVCTRFKAEfpifdKVDVngkntaPLYKYLKAEKGGLFgdAIKWNFTKFLVSKEGKVV 144
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 106-211 3.90e-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: 39.20  E-value: 3.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917214240 106 DGKKVTLDQFKGKVVLLTMGATWCPDCQKELKMLNKLYQNYkdnkdvvflPTYLVDGKKETKDTIKAFYEKEKLDLPCYY 185
Cdd:cd03011    9 DGEQFDLESLSGKPVLVYFWATWCPVCRFTSPTVNQLAADY---------PVVSVALRSGDDGAVARFMQKKGYGFPVIN 79

                         90       100
                 ....*....|....*....|....*.
gi 917214240 186 GDKATLRANFQIGWIPTLMVINKEGK 211
Cdd:cd03011   80 DPDGVISARWGVSVTPAIVIVDPGGI 105
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 106-176 6.39e-04

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: 38.70  E-value: 6.39e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917214240  106 DGKKVTLDQFKGKVVLLTMGATWCPD-CQKELKMLNKLYQNYKDN-KDVVFLpTYLVDGKKETKDTIKAFYEK 176
Cdd:pfam02630  10 DGKAVTEADFEGRPSLVFFGFTHCPDvCPTTLPNMAQVLDALGEEgIDVQPV-FITVDPERDTPEVLAEYLEA 81
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 100-148 2.20e-03

Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 37.75  E-value: 2.20e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 917214240 100 YESETKDGKKVTLDQFKGKVVLL--TmgATWC---PdcQkeLKMLNKLYQNYKD 148
Cdd:COG0386    7 FSVTTLDGEPVSLSDYKGKVLLIvnT--ASKCgftP--Q--YEGLEALYEKYKD 54
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
116-211 3.50e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 36.25  E-value: 3.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917214240  116 KGKVVLLTMGATWCPDCQK---ELKMLNKLYQNYKDNKDVVFLPtylVDGKKETKDTIKAFYEKEKLdlpcyyGDKatlr 192
Cdd:pfam13098   3 NGKPVLVVFTDPDCPYCKKlkkELLEDPDVTVYLGPNFVFIAVN---IWCAKEVAKAFTDILENKEL------GRK---- 69

                          90
                  ....*....|....*....
gi 917214240  193 anFQIGWIPTLMVINKEGK 211
Cdd:pfam13098  70 --YGVRGTPTIVFFDGKGE 86
TlpA_like_DipZ_like cd03012
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ...
 108-153 4.97e-03

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: 36.13  E-value: 4.97e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 917214240 108 KKVTLDQFKGKVVLLTMGATWCPDCQKELKMLNKLYQNYKDNKDVV 153
Cdd:cd03012   14 KPLSLAQLRGKVVLLDFWTYCCINCLHTLPYLTDLEQKYKDDGLVV 59
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 106-147 7.84e-03

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 36.80  E-value: 7.84e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 917214240 106 DGKKVTLDQFKGKVVLLTMGATWCPDCQKELKMLNKLYQNYK 147
Cdd:PLN02399  88 DGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYK 129
 
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