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Conserved domains on  [gi|1828880501|ref|WP_167728635|]
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MULTISPECIES: thioredoxin family protein [Thermococcus]

Protein Classification

GlrX_arch family protein( domain architecture ID 11493863)

GlrX_arch family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GlrX_arch TIGR02187
Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal ...
 4-224 5.30e-102

Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal domain with homology to bacterial and eukaryotic glutaredoxins, including a CPYC motif. There is an N-terminal domain which has even more distant homology to glutaredoxins. The name "glutaredoxin" may be inappropriate in the sense of working in tandem with glutathione and glutathione reductase which may not be present in the archaea. The overall domain structure appears to be related to bacterial alkylhydroperoxide reductases, but the homology may be distant enough that the function of this family is wholly different.


:

Pssm-ID: 274021 [Multi-domain]  Cd Length: 215  Bit Score: 294.35  E-value: 5.30e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501   4 ISDADKKVIKEEFFSKLTEPVKLMVFI--GKDHCQYCDQLKQLVQELAELSDKLSYEFIDFDTEEGKKKAEEYRIDRAPA 81
Cdd:TIGR02187   1 LSEEDREILKELFLKELKNPVEIVVFTdnDKEGCQYCKETEQLLEELSEVSPKLKLEIYDFDTPEDKEEAEKYGVERVPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501  82 VSITRNGQDVGVRFFGLPAGHEFGAFLEDIVDVSNMTTDLMPESKEALAKIDRDVRILVFVTPTCPYCPLAVRMAHKFAI 161
Cdd:TIGR02187  81 TIILEEGKDGGIRYTGIPAGYEFAALIEDIVRVSQGEPGLSEKTVELLQSLDEPVRIEVFVTPTCPYCPYAVLMAHKFAL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880501 162 ENTnagkgKILGDMVEAIEYPEWADQYSVMAVPKIVIQVDGEDkvqFEGAYPEKMFMEKLLAA 224
Cdd:TIGR02187 161 AND-----KILGEMIEANENPDLAEKYGVMSVPKIVINKGVEE---FVGAYPEEQFLEYILSA 215
 
Name Accession Description Interval E-value
GlrX_arch TIGR02187
Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal ...
 4-224 5.30e-102

Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal domain with homology to bacterial and eukaryotic glutaredoxins, including a CPYC motif. There is an N-terminal domain which has even more distant homology to glutaredoxins. The name "glutaredoxin" may be inappropriate in the sense of working in tandem with glutathione and glutathione reductase which may not be present in the archaea. The overall domain structure appears to be related to bacterial alkylhydroperoxide reductases, but the homology may be distant enough that the function of this family is wholly different.


Pssm-ID: 274021 [Multi-domain]  Cd Length: 215  Bit Score: 294.35  E-value: 5.30e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501   4 ISDADKKVIKEEFFSKLTEPVKLMVFI--GKDHCQYCDQLKQLVQELAELSDKLSYEFIDFDTEEGKKKAEEYRIDRAPA 81
Cdd:TIGR02187   1 LSEEDREILKELFLKELKNPVEIVVFTdnDKEGCQYCKETEQLLEELSEVSPKLKLEIYDFDTPEDKEEAEKYGVERVPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501  82 VSITRNGQDVGVRFFGLPAGHEFGAFLEDIVDVSNMTTDLMPESKEALAKIDRDVRILVFVTPTCPYCPLAVRMAHKFAI 161
Cdd:TIGR02187  81 TIILEEGKDGGIRYTGIPAGYEFAALIEDIVRVSQGEPGLSEKTVELLQSLDEPVRIEVFVTPTCPYCPYAVLMAHKFAL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880501 162 ENTnagkgKILGDMVEAIEYPEWADQYSVMAVPKIVIQVDGEDkvqFEGAYPEKMFMEKLLAA 224
Cdd:TIGR02187 161 AND-----KILGEMIEANENPDLAEKYGVMSVPKIVINKGVEE---FVGAYPEEQFLEYILSA 215
AhpF COG3634
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];
1-223 1.46e-83

Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];


Pssm-ID: 442851 [Multi-domain]  Cd Length: 200  Bit Score: 246.97  E-value: 1.46e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501   1 MGLISDADKKVIKEeFFSKLTEPVKLMVFIgkDHCQYCDQLKQLVQELAELSDKLSYEFIDFDTeegkkkaeeyrIDRAP 80
Cdd:COG3634     1 MAMLDDELKAQLKE-YLEKLKNPVELVLFL--DDCEKSEELRELLEEIASLSDKISLEVYDKDD-----------VERAP 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501  81 AVSITRNGQDVGVRFFGLPAGHEFGAFLEDIVDVSNMTTDLMPESKEALAKIDRDVRILVFVTPTCPYCPLAVRMAHKFA 160
Cdd:COG3634    67 SFAILRDGEDTGIRFAGIPSGHEFTSLVLALLQVSGHPPKLSEETIEQIKALDGPVHFEVFVSLSCPNCPDVVQALNLMA 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880501 161 IENTNagkgkILGDMVEAIEYPEWADQYSVMAVPKIVIqvdgEDKVQFEGAYPEKMFMEKLLA 223
Cdd:COG3634   147 VLNPN-----ITHEMIDGAEFPDEAEKYGVMSVPTVVL----NGEVFFVGRMPEEEILEKLDT 200
PfPDO_like_N cd02975
Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO)-like family, N-terminal TRX-fold ...
 2-115 1.85e-47

Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO)-like family, N-terminal TRX-fold subdomain; composed of proteins with similarity to PfPDO, a redox active thermostable protein believed to be the archaeal counterpart of bacterial DsbA and eukaryotic protein disulfide isomerase (PDI), which are both involved in oxidative protein folding. PfPDO contains two redox active CXXC motifs in two contiguous TRX-fold subdomains. The active site in the N-terminal TRX-fold subdomain is required for isomerase but not for reductase activity of PfPDO. The exclusive presence of PfPDO-like proteins in extremophiles may suggest that they have a special role in adaptation to extreme conditions.


Pssm-ID: 239273 [Multi-domain]  Cd Length: 113  Bit Score: 152.16  E-value: 1.85e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501   2 GLISDADKKVIKEEFFSKLTEPVKLMVFIGKDHCQYCDQLKQLVQELAELSDKLSYEFIDFDteEGKKKAEEYRIDRAPA 81
Cdd:cd02975     1 GLLSDEDRKALKEEFFKEMKNPVDLVVFSSKEGCQYCEVTKQLLEELSELSDKLKLEIYDFD--EDKEKAEKYGVERVPT 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1828880501  82 VSITR-NGQDVGVRFFGLPAGHEFGAFLEDIVDVS 115
Cdd:cd02975    79 TIFLQdGGKDGGIRYYGLPAGYEFASLIEDIVRVS 113
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 17-226 2.21e-19

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 85.98  E-value: 2.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501  17 FSKLTEPVKLMVFIGkDHCQYcDQLKQLVQELAELSDKLSYEFIDFDTeegkkkaeeyridRAPAVSITRNGQDVGVRFF 96
Cdd:PRK15317   14 LELLERPIELVASLD-DSEKS-AELKELLEEIASLSDKITVEEDSLDV-------------RKPSFSITRPGEDTGVRFA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501  97 GLPAGHEFGAFLEDIVDVSNMTTDLMPESKEALAKIDRDVRILVFVTPTCPYCPLAVRMAHKFAIENTNagkgkILGDMV 176
Cdd:PRK15317   79 GIPMGHEFTSLVLALLQVGGHPPKLDQEVIEQIKALDGDFHFETYVSLSCHNCPDVVQALNLMAVLNPN-----ITHTMI 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1828880501 177 EAIEYPEWADQYSVMAVPKIViqVDGEdkvQFEGAypeKMFMEKLLAALE 226
Cdd:PRK15317  154 DGALFQDEVEARNIMAVPTVF--LNGE---EFGQG---RMTLEEILAKLD 195
Thioredoxin_3 pfam13192
Thioredoxin domain;
142-223 5.76e-12

Thioredoxin domain;


Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 59.15  E-value: 5.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501 142 VTPTCPYCPlAVRMAHKFAIENTNagkgkILGDMVEAIEYPEwADQYSVMAVPKIVIqvdgEDKVQFEGAYPEKMFMEKL 221
Cdd:pfam13192   1 LGPGCPKCP-QLEKAVKEAAAELG-----IDAEVEKVTDFPE-IAKYGVMSTPALVI----NGKVVSSGKVPSEEEIRKL 69


                  ..
gi 1828880501 222 LA 223
Cdd:pfam13192  70 LE 71
 
Name Accession Description Interval E-value
GlrX_arch TIGR02187
Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal ...
 4-224 5.30e-102

Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal domain with homology to bacterial and eukaryotic glutaredoxins, including a CPYC motif. There is an N-terminal domain which has even more distant homology to glutaredoxins. The name "glutaredoxin" may be inappropriate in the sense of working in tandem with glutathione and glutathione reductase which may not be present in the archaea. The overall domain structure appears to be related to bacterial alkylhydroperoxide reductases, but the homology may be distant enough that the function of this family is wholly different.


Pssm-ID: 274021 [Multi-domain]  Cd Length: 215  Bit Score: 294.35  E-value: 5.30e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501   4 ISDADKKVIKEEFFSKLTEPVKLMVFI--GKDHCQYCDQLKQLVQELAELSDKLSYEFIDFDTEEGKKKAEEYRIDRAPA 81
Cdd:TIGR02187   1 LSEEDREILKELFLKELKNPVEIVVFTdnDKEGCQYCKETEQLLEELSEVSPKLKLEIYDFDTPEDKEEAEKYGVERVPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501  82 VSITRNGQDVGVRFFGLPAGHEFGAFLEDIVDVSNMTTDLMPESKEALAKIDRDVRILVFVTPTCPYCPLAVRMAHKFAI 161
Cdd:TIGR02187  81 TIILEEGKDGGIRYTGIPAGYEFAALIEDIVRVSQGEPGLSEKTVELLQSLDEPVRIEVFVTPTCPYCPYAVLMAHKFAL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880501 162 ENTnagkgKILGDMVEAIEYPEWADQYSVMAVPKIVIQVDGEDkvqFEGAYPEKMFMEKLLAA 224
Cdd:TIGR02187 161 AND-----KILGEMIEANENPDLAEKYGVMSVPKIVINKGVEE---FVGAYPEEQFLEYILSA 215
AhpF COG3634
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];
1-223 1.46e-83

Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];


Pssm-ID: 442851 [Multi-domain]  Cd Length: 200  Bit Score: 246.97  E-value: 1.46e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501   1 MGLISDADKKVIKEeFFSKLTEPVKLMVFIgkDHCQYCDQLKQLVQELAELSDKLSYEFIDFDTeegkkkaeeyrIDRAP 80
Cdd:COG3634     1 MAMLDDELKAQLKE-YLEKLKNPVELVLFL--DDCEKSEELRELLEEIASLSDKISLEVYDKDD-----------VERAP 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501  81 AVSITRNGQDVGVRFFGLPAGHEFGAFLEDIVDVSNMTTDLMPESKEALAKIDRDVRILVFVTPTCPYCPLAVRMAHKFA 160
Cdd:COG3634    67 SFAILRDGEDTGIRFAGIPSGHEFTSLVLALLQVSGHPPKLSEETIEQIKALDGPVHFEVFVSLSCPNCPDVVQALNLMA 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880501 161 IENTNagkgkILGDMVEAIEYPEWADQYSVMAVPKIVIqvdgEDKVQFEGAYPEKMFMEKLLA 223
Cdd:COG3634   147 VLNPN-----ITHEMIDGAEFPDEAEKYGVMSVPTVVL----NGEVFFVGRMPEEEILEKLDT 200
PfPDO_like_N cd02975
Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO)-like family, N-terminal TRX-fold ...
 2-115 1.85e-47

Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO)-like family, N-terminal TRX-fold subdomain; composed of proteins with similarity to PfPDO, a redox active thermostable protein believed to be the archaeal counterpart of bacterial DsbA and eukaryotic protein disulfide isomerase (PDI), which are both involved in oxidative protein folding. PfPDO contains two redox active CXXC motifs in two contiguous TRX-fold subdomains. The active site in the N-terminal TRX-fold subdomain is required for isomerase but not for reductase activity of PfPDO. The exclusive presence of PfPDO-like proteins in extremophiles may suggest that they have a special role in adaptation to extreme conditions.


Pssm-ID: 239273 [Multi-domain]  Cd Length: 113  Bit Score: 152.16  E-value: 1.85e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501   2 GLISDADKKVIKEEFFSKLTEPVKLMVFIGKDHCQYCDQLKQLVQELAELSDKLSYEFIDFDteEGKKKAEEYRIDRAPA 81
Cdd:cd02975     1 GLLSDEDRKALKEEFFKEMKNPVDLVVFSSKEGCQYCEVTKQLLEELSELSDKLKLEIYDFD--EDKEKAEKYGVERVPT 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1828880501  82 VSITR-NGQDVGVRFFGLPAGHEFGAFLEDIVDVS 115
Cdd:cd02975    79 TIFLQdGGKDGGIRYYGLPAGYEFASLIEDIVRVS 113
TRX_GRX_like cd02973
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins ...
 136-211 2.99e-25

Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins that show similarity to both TRX and GRX, including the C-terminal TRX-fold subdomain of Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). All members contain a redox-active CXXC motif and may function as PDOs. The archaeal proteins Mj0307 and Mt807 show structures more similar to GRX, but activities more similar to TRX. Some members of the family are similar to PfPDO in that they contain a second CXXC motif located in a second TRX-fold subdomain at the N-terminus; the superimposable N- and C-terminal TRX subdomains form a compact structure. PfPDO is postulated to be the archaeal counterpart of bacterial DsbA and eukaryotic protein disulfide isomerase (PDI). The C-terminal CXXC motif of PfPDO is required for its oxidase, reductase and isomerase activities. Also included in the family is the C-terminal TRX-fold subdomain of the N-terminal domain (NTD) of bacterial AhpF, which has a similar fold as PfPDO with two TRX-fold subdomains but without the second CXXC motif.


Pssm-ID: 239271 [Multi-domain]  Cd Length: 67  Bit Score: 93.79  E-value: 2.99e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880501 136 VRILVFVTPTCPYCPLAVRMAHKFAIENtnagkGKILGDMVEAIEYPEWADQYSVMAVPKIVIQvdgeDKVQFEGA 211
Cdd:cd02973     1 VNIEVFVSPTCPYCPDAVQAANRIAALN-----PNISAEMIDAAEFPDLADEYGVMSVPAIVIN----GKVEFVGR 67
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 17-226 2.21e-19

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 85.98  E-value: 2.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501  17 FSKLTEPVKLMVFIGkDHCQYcDQLKQLVQELAELSDKLSYEFIDFDTeegkkkaeeyridRAPAVSITRNGQDVGVRFF 96
Cdd:PRK15317   14 LELLERPIELVASLD-DSEKS-AELKELLEEIASLSDKITVEEDSLDV-------------RKPSFSITRPGEDTGVRFA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501  97 GLPAGHEFGAFLEDIVDVSNMTTDLMPESKEALAKIDRDVRILVFVTPTCPYCPLAVRMAHKFAIENTNagkgkILGDMV 176
Cdd:PRK15317   79 GIPMGHEFTSLVLALLQVGGHPPKLDQEVIEQIKALDGDFHFETYVSLSCHNCPDVVQALNLMAVLNPN-----ITHTMI 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1828880501 177 EAIEYPEWADQYSVMAVPKIViqVDGEdkvQFEGAypeKMFMEKLLAALE 226
Cdd:PRK15317  154 DGALFQDEVEARNIMAVPTVF--LNGE---EFGQG---RMTLEEILAKLD 195
AhpF_NTD_N cd02974
Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) family, N-terminal ...
 17-108 4.42e-14

Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) family, N-terminal TRX-fold subdomain; AhpF is a homodimeric flavoenzyme which catalyzes the NADH-dependent reduction of the peroxiredoxin AhpC, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. AhpF contains an NTD forming two contiguous TRX-fold subdomain similar to Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). It also contains a catalytic core similar to TRX reductase containing FAD and NADH binding domains with an active site disulfide. The proposed mechanism of action of AhpF is similar to a TRX/TRX reductase system. The flow of reducing equivalents goes from NADH -> catalytic core of AhpF -> NTD of AhpF -> AhpC -> peroxide substrates. The N-terminal TRX-fold subdomain of AhpF NTD is redox inactive, but is proposed to contain an important residue that aids in the catalytic function of the redox-active CXXC motif contained in the C-terminal TRX-fold subdomain.


Pssm-ID: 239272 [Multi-domain]  Cd Length: 94  Bit Score: 65.29  E-value: 4.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501  17 FSKLTEPVKLMVFIGkDHCQYCDqLKQLVQELAELSDKLSYEFIDFDTeegkkkaeeyridRAPAVSITRNGQDVGVRFF 96
Cdd:cd02974    14 LERLENPVELVASLD-DSEKSAE-LLELLEEIASLSDKITLEEDNDDE-------------RKPSFSINRPGEDTGIRFA 78

                          90
                  ....*....|..
gi 1828880501  97 GLPAGHEFGAFL 108
Cdd:cd02974    79 GIPMGHEFTSLV 90
Thioredoxin_3 pfam13192
Thioredoxin domain;
142-223 5.76e-12

Thioredoxin domain;


Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 59.15  E-value: 5.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501 142 VTPTCPYCPlAVRMAHKFAIENTNagkgkILGDMVEAIEYPEwADQYSVMAVPKIVIqvdgEDKVQFEGAYPEKMFMEKL 221
Cdd:pfam13192   1 LGPGCPKCP-QLEKAVKEAAAELG-----IDAEVEKVTDFPE-IAKYGVMSTPALVI----NGKVVSSGKVPSEEEIRKL 69


                  ..
gi 1828880501 222 LA 223
Cdd:pfam13192  70 LE 71
redox_disulf_1 TIGR00411
small redox-active disulfide protein 1; This protein is homologous to a family of proteins ...
 136-211 3.58e-08

small redox-active disulfide protein 1; This protein is homologous to a family of proteins that includes thioredoxins, glutaredoxins, protein-disulfide isomerases, and others, some of which have several such domains. The sequence of this protein at the redox-active disufide site, CPYC, matches glutaredoxins rather than thioredoxins, although its overall sequence seems closer to thioredoxins. It is suggested to be a ribonucleotide-reducing system component distinct from thioredoxin or glutaredoxin. [Unknown function, General]


Pssm-ID: 129505 [Multi-domain]  Cd Length: 82  Bit Score: 49.50  E-value: 3.58e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880501 136 VRILVFVTPTCPYCPLAVRMAHKFAIENTNagkgKILGDMVEAIEYPEWADQYSVMAVPKIVIQvdgeDKVQFEGA 211
Cdd:TIGR00411   1 VKIELFTSPTCPYCPAAKRVVEEVAKEMGD----AVEVEYINVMENPQKAMEYGIMAVPAIVIN----GDVEFIGA 68
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 14-109 3.18e-07

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: 46.78  E-value: 3.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501  14 EEFFSKLTEPVKLMVFIGKDHCQYCDQLKQLVQELAELSDKLsyEFIDFDTEEGKKKAEEYRIDRAPAVSITRNGQDVGv 93
Cdd:cd02947     1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKV--KFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVD- 77

                          90
                  ....*....|....*.
gi 1828880501  94 RFFGLPAGHEFGAFLE 109
Cdd:cd02947    78 RVVGADPKEELEEFLE 93
AhpF_NTD_C cd03026
TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) ...
 127-224 5.69e-07

TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) subfamily, C-terminal TRX-fold subdomain; AhpF is a homodimeric flavoenzyme which catalyzes the NADH-dependent reduction of the peroxiredoxin AhpC, which then reduces hydrogen peroxide and organic hydroperoxides. AhpF contains an NTD containing two contiguous TRX-fold subdomains similar to Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). It also contains a catalytic core similar to TRX reductase containing FAD and NADH binding domains with an active site disulfide. The proposed mechanism of action of AhpF is similar to a TRX/TRX reductase system. The flow of reducing equivalents goes from NADH -> catalytic core of AhpF -> NTD of AhpF -> AhpC -> peroxide substrates. The catalytic CXXC motif of the NTD of AhpF is contained in its C-terminal TRX subdomain.


Pssm-ID: 239324 [Multi-domain]  Cd Length: 89  Bit Score: 46.13  E-value: 5.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501 127 EALAKIDRDVRILVFVTPTCPYCPLAVRMAHKFAIENTNagkgkILGDMVEAIEYPEWADQYSVMAVPKIVIqvDGEDKV 206
Cdd:cd03026     5 EQIRRLNGPINFETYVSLSCHNCPDVVQALNLMAVLNPN-----IEHEMIDGALFQDEVEERGIMSVPAIFL--NGELFG 77

                          90
                  ....*....|....*...
gi 1828880501 207 QfegaypEKMFMEKLLAA 224
Cdd:cd03026    78 F------GRMTLEEILAK 89
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 126-221 6.05e-06

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: 43.32  E-value: 6.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501 126 KEALAKIDRDVRILV-FVTPTCPYCPLAVRMAHKFAIENTNAgkgKILgdMVEAIEYPEWADQYSVMAVPKIVIQVDGED 204
Cdd:cd02947     1 EEFEELIKSAKPVVVdFWAPWCGPCKAIAPVLEELAEEYPKV---KFV--KVDVDENPELAEEYGVRSIPTFLFFKNGKE 75

                          90
                  ....*....|....*..
gi 1828880501 205 KVQFEGAYPEKMFMEKL 221
Cdd:cd02947    76 VDRVVGADPKEELEEFL 92
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 132-221 5.42e-05

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: 40.96  E-value: 5.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501 132 IDRDVRILV-FVTPTCPYCplaVRMAHKF-AIENTNAGKGKILgdMVEAIEYPEWADQYSVMAVPKIVIQVDGEDKVQFE 209
Cdd:COG3118    15 LESDKPVLVdFWAPWCGPC---KMLAPVLeELAAEYGGKVKFV--KVDVDENPELAAQFGVRSIPTLLLFKDGQPVDRFV 89

                          90
                  ....*....|..
gi 1828880501 210 GAYPEKMFMEKL 221
Cdd:COG3118    90 GALPKEQLREFL 101
Thioredoxin_9 pfam14595
Thioredoxin;
121-216 6.63e-04

Thioredoxin;


Pssm-ID: 434059 [Multi-domain]  Cd Length: 129  Bit Score: 38.40  E-value: 6.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501 121 LMPESKEALAKIDRDVRILVFVTPTCPYCPLAVRMAHKFAIENTNAGKGKILGDmveaiEYPEWADQYSVM---AVPKIV 197
Cdd:pfam14595  28 LSEELIEKIKSIEKPLRILVITEDWCGDAAQNVPVLAKIAELNPNIELRILLRD-----ENLELMDQYLTGggrAIPTFI 102

                          90
                  ....*....|....*....
gi 1828880501 198 IQVDGEDKVQFEGAYPEKM 216
Cdd:pfam14595 103 FLDEDGEELGVWGPRPKAV 121
SoxW cd02951
SoxW family; SoxW is a bacterial periplasmic TRX, containing a redox active CXXC motif, ...
 26-113 1.11e-03

SoxW family; SoxW is a bacterial periplasmic TRX, containing a redox active CXXC motif, encoded by a genetic locus (sox operon) involved in thiosulfate oxidation. Sulfur bacteria oxidize sulfur compounds to provide reducing equivalents for carbon dioxide fixation during autotrophic growth and the respiratory electron transport chain. It is unclear what the role of SoxW is, since it has been found to be dispensable in the oxidation of thiosulfate to sulfate. SoxW is specifically kept in the reduced state by SoxV, which is essential in thiosulfate oxidation.


Pssm-ID: 239249 [Multi-domain]  Cd Length: 125  Bit Score: 37.68  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501  26 LMVFIGKDHCQYCDQLKQLVQELAELSDKL-------------SYEFIDFDTEE--GKKKAEEYRIDRAPAVSI-TRNGQ 89
Cdd:cd02951    17 LLLLFSQPGCPYCDKLKRDYLNDPAVQAYIrahfvvvyinidgDKEVTDFDGEAlsEKELARKYRVRFTPTVIFlDPEGG 96

                          90       100
                  ....*....|....*....|....
gi 1828880501  90 DVGVRFFGLPAGHEFGAFLEDIVD 113
Cdd:cd02951    97 KEIARLPGYLPPDEFLAYLEYVQE 120
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 8-112 8.82e-03

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: 34.80  E-value: 8.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880501   8 DKKVIKEEffskltEPVklMVFIGKDHCQYCDQLKQLVQELA-ELSDKLsyEFIDFDTEEGKKKAEEYRIDRAPAVSITR 86
Cdd:COG3118    11 EEEVLESD------KPV--LVDFWAPWCGPCKMLAPVLEELAaEYGGKV--KFVKVDVDENPELAAQFGVRSIPTLLLFK 80

                          90       100
                  ....*....|....*....|....*.
gi 1828880501  87 NGQDVGvRFFGLPAGHEFGAFLEDIV 112
Cdd:COG3118    81 DGQPVD-RFVGALPKEQLREFLDKVL 105
 
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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