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Conserved domains on  [gi|300545785|emb|CBU99050|]
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unnamed protein product [Arabidopsis thaliana]

Protein Classification

PICOT family protein( domain architecture ID 10122222)

PICOT (PKC-interacting cousin of thioredoxin) family protein containing thioredoxin-like and glutaredoxin-like domains, may be redox inactive, similar to PICOT that functions as a cytosolic iron-sulfur (Fe-S) cluster assembly factor

CATH:  3.40.30.10
Gene Ontology:  GO:0016226|GO:0051536
PubMed:  18479680|9099998|10049365|15558583|31176019|12074972
SCOP:  3000031

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 157-246 1.72e-57

Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of PICOT and GRX-PICOT-like proteins. The non-PICOT members of this family contain only the GRX-like domain, whereas PICOT contains an N-terminal TRX-like domain followed by one to three GRX-like domains. It is interesting to note that PICOT from plants contain three repeats of the GRX-like domain, metazoan proteins (except for insect) have two repeats, while fungal sequences contain only one copy of the domain. PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli. Both GRX and TRX domains of PICOT are required for its activity. Characterized non-PICOT members of this family include CXIP1, a CAX-interacting protein in Arabidopsis thaliana, and PfGLP-1, a GRX-like protein from Plasmodium falciparum.


:

Pssm-ID: 239326  Cd Length: 90  Bit Score: 185.00  E-value: 1.72e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 157 LEKLTNSHPVMLFMKGIPEEPRCGFSRKVVDILKEVNVDFGSFDILSDNEVREGLKKFSNWPTFPQLYCNGELLGGADIA 236
Cdd:cd03028    1 IKKLIKENPVVLFMKGTPEEPRCGFSRKVVQILNQLGVDFGTFDILEDEEVRQGLKEYSNWPTFPQLYVNGELVGGCDIV 80

                         90
                 ....*....|
gi 300545785 237 IAMHESGELK 246
Cdd:cd03028   81 KEMHESGELQ 90
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 394-483 5.25e-56

Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of PICOT and GRX-PICOT-like proteins. The non-PICOT members of this family contain only the GRX-like domain, whereas PICOT contains an N-terminal TRX-like domain followed by one to three GRX-like domains. It is interesting to note that PICOT from plants contain three repeats of the GRX-like domain, metazoan proteins (except for insect) have two repeats, while fungal sequences contain only one copy of the domain. PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli. Both GRX and TRX domains of PICOT are required for its activity. Characterized non-PICOT members of this family include CXIP1, a CAX-interacting protein in Arabidopsis thaliana, and PfGLP-1, a GRX-like protein from Plasmodium falciparum.


:

Pssm-ID: 239326  Cd Length: 90  Bit Score: 181.15  E-value: 5.25e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 394 LKALINSSEVMLFMKGSPDEPKCGFSSKVVKALRGENVSFGSFDILTDEEVRQGIKNFSNWPTFPQLYYKGELIGGCDII 473
Cdd:cd03028    1 IKKLIKENPVVLFMKGTPEEPRCGFSRKVVQILNQLGVDFGTFDILEDEEVRQGLKEYSNWPTFPQLYVNGELVGGCDIV 80

                         90
                 ....*....|
gi 300545785 474 MELSESGDLK 483
Cdd:cd03028   81 KEMHESGELQ 90
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 287-376 1.04e-54

Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of PICOT and GRX-PICOT-like proteins. The non-PICOT members of this family contain only the GRX-like domain, whereas PICOT contains an N-terminal TRX-like domain followed by one to three GRX-like domains. It is interesting to note that PICOT from plants contain three repeats of the GRX-like domain, metazoan proteins (except for insect) have two repeats, while fungal sequences contain only one copy of the domain. PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli. Both GRX and TRX domains of PICOT are required for its activity. Characterized non-PICOT members of this family include CXIP1, a CAX-interacting protein in Arabidopsis thaliana, and PfGLP-1, a GRX-like protein from Plasmodium falciparum.


:

Pssm-ID: 239326  Cd Length: 90  Bit Score: 177.69  E-value: 1.04e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 287 LEGLVNSKPVMLFMKGRPEEPKCGFSGKVVEILNQEKIEFGSFDILLDDEVRQGLKVYSNWSSYPQLYVKGELMGGSDIV 366
Cdd:cd03028    1 IKKLIKENPVVLFMKGTPEEPRCGFSRKVVQILNQLGVDFGTFDILEDEEVRQGLKEYSNWPTFPQLYVNGELVGGCDIV 80

                         90
                 ....*....|
gi 300545785 367 LEMQKSGELK 376
Cdd:cd03028   81 KEMHESGELQ 90
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 10-102 4.76e-40

TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT contains an N-terminal TRX-like domain, which does not contain the catalytic CXXC motif, followed by one to three glutaredoxin domains. The TRX-like domain is required for interaction with PKC theta. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli.


:

Pssm-ID: 239282 [Multi-domain]  Cd Length: 97  Bit Score: 139.33  E-value: 4.76e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785  10 SKAELDNLRQSGA--PVVLHFWASWCDASKQMDQVFSHLATD-FPRAHFFRVEAEEHPEISEAYSVAAVPYFVFFKDGKT 86
Cdd:cd02984    1 SEEEFEELLKSDAskLLVLHFWAPWAEPCKQMNQVFEELAKEaFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTI 80

                         90
                 ....*....|....*.
gi 300545785  87 VDTLEGADPSSLANKV 102
Cdd:cd02984   81 VDRVSGADPKELAKKV 96
 
Name Accession Description Interval E-value
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 157-246 1.72e-57

Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of PICOT and GRX-PICOT-like proteins. The non-PICOT members of this family contain only the GRX-like domain, whereas PICOT contains an N-terminal TRX-like domain followed by one to three GRX-like domains. It is interesting to note that PICOT from plants contain three repeats of the GRX-like domain, metazoan proteins (except for insect) have two repeats, while fungal sequences contain only one copy of the domain. PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli. Both GRX and TRX domains of PICOT are required for its activity. Characterized non-PICOT members of this family include CXIP1, a CAX-interacting protein in Arabidopsis thaliana, and PfGLP-1, a GRX-like protein from Plasmodium falciparum.


Pssm-ID: 239326  Cd Length: 90  Bit Score: 185.00  E-value: 1.72e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 157 LEKLTNSHPVMLFMKGIPEEPRCGFSRKVVDILKEVNVDFGSFDILSDNEVREGLKKFSNWPTFPQLYCNGELLGGADIA 236
Cdd:cd03028    1 IKKLIKENPVVLFMKGTPEEPRCGFSRKVVQILNQLGVDFGTFDILEDEEVRQGLKEYSNWPTFPQLYVNGELVGGCDIV 80

                         90
                 ....*....|
gi 300545785 237 IAMHESGELK 246
Cdd:cd03028   81 KEMHESGELQ 90
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 394-483 5.25e-56

Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of PICOT and GRX-PICOT-like proteins. The non-PICOT members of this family contain only the GRX-like domain, whereas PICOT contains an N-terminal TRX-like domain followed by one to three GRX-like domains. It is interesting to note that PICOT from plants contain three repeats of the GRX-like domain, metazoan proteins (except for insect) have two repeats, while fungal sequences contain only one copy of the domain. PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli. Both GRX and TRX domains of PICOT are required for its activity. Characterized non-PICOT members of this family include CXIP1, a CAX-interacting protein in Arabidopsis thaliana, and PfGLP-1, a GRX-like protein from Plasmodium falciparum.


Pssm-ID: 239326  Cd Length: 90  Bit Score: 181.15  E-value: 5.25e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 394 LKALINSSEVMLFMKGSPDEPKCGFSSKVVKALRGENVSFGSFDILTDEEVRQGIKNFSNWPTFPQLYYKGELIGGCDII 473
Cdd:cd03028    1 IKKLIKENPVVLFMKGTPEEPRCGFSRKVVQILNQLGVDFGTFDILEDEEVRQGLKEYSNWPTFPQLYVNGELVGGCDIV 80

                         90
                 ....*....|
gi 300545785 474 MELSESGDLK 483
Cdd:cd03028   81 KEMHESGELQ 90
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 287-376 1.04e-54

Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of PICOT and GRX-PICOT-like proteins. The non-PICOT members of this family contain only the GRX-like domain, whereas PICOT contains an N-terminal TRX-like domain followed by one to three GRX-like domains. It is interesting to note that PICOT from plants contain three repeats of the GRX-like domain, metazoan proteins (except for insect) have two repeats, while fungal sequences contain only one copy of the domain. PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli. Both GRX and TRX domains of PICOT are required for its activity. Characterized non-PICOT members of this family include CXIP1, a CAX-interacting protein in Arabidopsis thaliana, and PfGLP-1, a GRX-like protein from Plasmodium falciparum.


Pssm-ID: 239326  Cd Length: 90  Bit Score: 177.69  E-value: 1.04e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 287 LEGLVNSKPVMLFMKGRPEEPKCGFSGKVVEILNQEKIEFGSFDILLDDEVRQGLKVYSNWSSYPQLYVKGELMGGSDIV 366
Cdd:cd03028    1 IKKLIKENPVVLFMKGTPEEPRCGFSRKVVQILNQLGVDFGTFDILEDEEVRQGLKEYSNWPTFPQLYVNGELVGGCDIV 80

                         90
                 ....*....|
gi 300545785 367 LEMQKSGELK 376
Cdd:cd03028   81 KEMHESGELQ 90
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
388-488 3.31e-49

Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440047  Cd Length: 105  Bit Score: 164.13  E-value: 3.31e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 388 QSLEDRLKALINSSEVMLFMKGSPDEPKCGFSSKVVKALRGENVSFGSFDILTDEEVRQGIKNFSNWPTFPQLYYKGELI 467
Cdd:COG0278    2 MDVQERIKQQIKSNPVVLFMKGTPQFPQCGFSARAVQILNACGVDFATVNVLEDPEIRQGLKEYSNWPTIPQLYVKGEFI 81

                         90       100
                 ....*....|....*....|.
gi 300545785 468 GGCDIIMELSESGDLKATLSE 488
Cdd:COG0278   82 GGCDIIREMYESGELQKLLEE 102
TIGR00365 TIGR00365
monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. ...
 391-486 8.91e-49

monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. coli, originally designated ydhD, is now designated grxD. Its protein, Grx4, is a monothiol glutaredoxin similar to Grx5 of yeast, which is involved in iron-sulfur cluster formation. [Energy metabolism, Electron transport]


Pssm-ID: 188046  Cd Length: 97  Bit Score: 162.63  E-value: 8.91e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785  391 EDRLKALINSSEVMLFMKGSPDEPKCGFSSKVVKALRGENVSFGSFDILTDEEVRQGIKNFSNWPTFPQLYYKGELIGGC 470
Cdd:TIGR00365   2 IERIKEQIAENPVVLYMKGTPQFPQCGFSARAVQILNACGVPFAYVNVLEDPEIRQGIKEYSNWPTIPQLYVKGEFVGGC 81

                          90
                  ....*....|....*.
gi 300545785  471 DIIMELSESGDLKATL 486
Cdd:TIGR00365  82 DIIMEMYQSGELQTLL 97
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
150-254 4.68e-48

Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440047  Cd Length: 105  Bit Score: 161.05  E-value: 4.68e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 150 ADALKSRLEKLTNSHPVMLFMKGIPEEPRCGFSRKVVDILKEVNVDFGSFDILSDNEVREGLKKFSNWPTFPQLYCNGEL 229
Cdd:COG0278    1 MMDVQERIKQQIKSNPVVLFMKGTPQFPQCGFSARAVQILNACGVDFATVNVLEDPEIRQGLKEYSNWPTIPQLYVKGEF 80

                         90       100
                 ....*....|....*....|....*
gi 300545785 230 LGGADIAIAMHESGELKDAFKDLGI 254
Cdd:COG0278   81 IGGCDIIREMYESGELQKLLEEAGA 105
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
280-384 1.18e-46

Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440047  Cd Length: 105  Bit Score: 157.20  E-value: 1.18e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 280 SETLRARLEGLVNSKPVMLFMKGRPEEPKCGFSGKVVEILNQEKIEFGSFDILLDDEVRQGLKVYSNWSSYPQLYVKGEL 359
Cdd:COG0278    1 MMDVQERIKQQIKSNPVVLFMKGTPQFPQCGFSARAVQILNACGVDFATVNVLEDPEIRQGLKEYSNWPTIPQLYVKGEF 80

                         90       100
                 ....*....|....*....|....*
gi 300545785 360 MGGSDIVLEMQKSGELKKVLTEKGI 384
Cdd:COG0278   81 IGGCDIIREMYESGELQKLLEEAGA 105
TIGR00365 TIGR00365
monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. ...
 154-249 2.04e-45

monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. coli, originally designated ydhD, is now designated grxD. Its protein, Grx4, is a monothiol glutaredoxin similar to Grx5 of yeast, which is involved in iron-sulfur cluster formation. [Energy metabolism, Electron transport]


Pssm-ID: 188046  Cd Length: 97  Bit Score: 153.77  E-value: 2.04e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785  154 KSRLEKLTNSHPVMLFMKGIPEEPRCGFSRKVVDILKEVNVDFGSFDILSDNEVREGLKKFSNWPTFPQLYCNGELLGGA 233
Cdd:TIGR00365   2 IERIKEQIAENPVVLYMKGTPQFPQCGFSARAVQILNACGVPFAYVNVLEDPEIRQGIKEYSNWPTIPQLYVKGEFVGGC 81

                          90
                  ....*....|....*.
gi 300545785  234 DIAIAMHESGELKDAF 249
Cdd:TIGR00365  82 DIIMEMYQSGELQTLL 97
TIGR00365 TIGR00365
monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. ...
 285-379 1.06e-43

monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. coli, originally designated ydhD, is now designated grxD. Its protein, Grx4, is a monothiol glutaredoxin similar to Grx5 of yeast, which is involved in iron-sulfur cluster formation. [Energy metabolism, Electron transport]


Pssm-ID: 188046  Cd Length: 97  Bit Score: 149.15  E-value: 1.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785  285 ARLEGLVNSKPVMLFMKGRPEEPKCGFSGKVVEILNQEKIEFGSFDILLDDEVRQGLKVYSNWSSYPQLYVKGELMGGSD 364
Cdd:TIGR00365   3 ERIKEQIAENPVVLYMKGTPQFPQCGFSARAVQILNACGVPFAYVNVLEDPEIRQGIKEYSNWPTIPQLYVKGEFVGGCD 82

                          90
                  ....*....|....*
gi 300545785  365 IVLEMQKSGELKKVL 379
Cdd:TIGR00365  83 IIMEMYQSGELQTLL 97
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 10-102 4.76e-40

TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT contains an N-terminal TRX-like domain, which does not contain the catalytic CXXC motif, followed by one to three glutaredoxin domains. The TRX-like domain is required for interaction with PKC theta. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli.


Pssm-ID: 239282 [Multi-domain]  Cd Length: 97  Bit Score: 139.33  E-value: 4.76e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785  10 SKAELDNLRQSGA--PVVLHFWASWCDASKQMDQVFSHLATD-FPRAHFFRVEAEEHPEISEAYSVAAVPYFVFFKDGKT 86
Cdd:cd02984    1 SEEEFEELLKSDAskLLVLHFWAPWAEPCKQMNQVFEELAKEaFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTI 80

                         90
                 ....*....|....*.
gi 300545785  87 VDTLEGADPSSLANKV 102
Cdd:cd02984   81 VDRVSGADPKELAKKV 96
PTZ00062 PTZ00062
glutaredoxin; Provisional
 7-251 7.44e-35

glutaredoxin; Provisional


Pssm-ID: 240250 [Multi-domain]  Cd Length: 204  Bit Score: 129.15  E-value: 7.44e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785   7 DIVSKAELDNLRQS-GAPVVLHFWASWCDASKQMDQVFSHLATDFPRAHFFRVeaeehpeiSEAYSVAAVPYFVFFKDGK 85
Cdd:PTZ00062   2 NFIKKEEKDKLIESnTGKLVLYVKSSKEPEYEQLMDVCNALVEDFPSLEFYVV--------NLADANNEYGVFEFYQNSQ 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785  86 TVDTLEGADPSSLANKVGKVAGSSTSAEpaapaslglaagptileTVKenakaslqdraqpvstadalksRLEKLTNSHP 165
Cdd:PTZ00062  74 LINSLEGCNTSTLVSFIRGWAQKGSSED-----------------TVE----------------------KIERLIRNHK 114

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 166 VMLFMKGIPEEPRCGFSRKVVDILKEVNVDFGSFDILSDNEVREGLKKFSNWPTFPQLYCNGELLGGADIAIAMHESGEL 245
Cdd:PTZ00062 115 ILLFMKGSKTFPFCRFSNAVVNMLNSSGVKYETYNIFEDPDLREELKVYSNWPTYPQLYVNGELIGGHDIIKELYESNSL 194


                 ....*.
gi 300545785 246 KDAFKD 251
Cdd:PTZ00062 195 RKVIPD 200
PTZ00062 PTZ00062
glutaredoxin; Provisional
 276-381 1.60e-30

glutaredoxin; Provisional


Pssm-ID: 240250 [Multi-domain]  Cd Length: 204  Bit Score: 117.59  E-value: 1.60e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 276 NTGLSETLRaRLEGLVNSKPVMLFMKGRPEEPKCGFSGKVVEILNQEKIEFGSFDILLDDEVRQGLKVYSNWSSYPQLYV 355
Cdd:PTZ00062  96 KGSSEDTVE-KIERLIRNHKILLFMKGSKTFPFCRFSNAVVNMLNSSGVKYETYNIFEDPDLREELKVYSNWPTYPQLYV 174

                         90       100
                 ....*....|....*....|....*.
gi 300545785 356 KGELMGGSDIVLEMQKSGELKKVLTE 381
Cdd:PTZ00062 175 NGELIGGHDIIKELYESNSLRKVIPD 200
PTZ00062 PTZ00062
glutaredoxin; Provisional
 385-483 8.62e-29

glutaredoxin; Provisional


Pssm-ID: 240250 [Multi-domain]  Cd Length: 204  Bit Score: 112.58  E-value: 8.62e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 385 TGEQSLEDRLKALINSSEVMLFMKGSPDEPKCGFSSKVVKALRGENVSFGSFDILTDEEVRQGIKNFSNWPTFPQLYYKG 464
Cdd:PTZ00062  97 GSSEDTVEKIERLIRNHKILLFMKGSKTFPFCRFSNAVVNMLNSSGVKYETYNIFEDPDLREELKVYSNWPTYPQLYVNG 176

                         90
                 ....*....|....*....
gi 300545785 465 ELIGGCDIIMELSESGDLK 483
Cdd:PTZ00062 177 ELIGGHDIIKELYESNSLR 195
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 9-105 1.65e-21

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: 89.11  E-value: 1.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785   9 VSKAELDN-LRQSGAPVVLHFWASWCDASKQMDQVFSHLATDF-PRAHFFRVEAEEHPEISEAYSVAAVPYFVFFKDGKT 86
Cdd:COG3118    5 LTDENFEEeVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYgGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQP 84

                         90       100
                 ....*....|....*....|
gi 300545785  87 VDTLEGA-DPSSLANKVGKV 105
Cdd:COG3118   85 VDRFVGAlPKEQLREFLDKV 104
Glutaredoxin pfam00462
Glutaredoxin;
166-229 2.41e-19

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 81.40  E-value: 2.41e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300545785  166 VMLFMKgipeePRCGFSRKVVDILKEVNVDFGSFDILSDNEVREGLKKFSNWPTFPQLYCNGEL 229
Cdd:pfam00462   1 VVLYTK-----PTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKELSGWPTVPQVFIDGEH 59
Glutaredoxin pfam00462
Glutaredoxin;
403-467 1.21e-18

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 79.47  E-value: 1.21e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300545785  403 VMLFMKgspdePKCGFSSKVVKALRGENVSFGSFDILTDEEVRQGIKNFSNWPTFPQLYYKGELI 467
Cdd:pfam00462   1 VVLYTK-----PTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKELSGWPTVPQVFIDGEHI 60
Glutaredoxin pfam00462
Glutaredoxin;
296-359 1.92e-16

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 73.31  E-value: 1.92e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300545785  296 VMLFMKgrpeePKCGFSGKVVEILNQEKIEFGSFDILLDDEVRQGLKVYSNWSSYPQLYVKGEL 359
Cdd:pfam00462   1 VVLYTK-----PTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKELSGWPTVPQVFIDGEH 59
PTZ00051 PTZ00051
thioredoxin; Provisional
 5-100 5.06e-15

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 70.68  E-value: 5.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785   5 VKDIVSKAELDNLRQSGAPVVLHFWASWCDASKQMDQVFSHLATDFPRAHFFRVEAEEHPEISEAYSVAAVPYFVFFKDG 84
Cdd:PTZ00051   2 VHIVTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDELSEVAEKENITSMPTFKVFKNG 81

                         90
                 ....*....|....*.
gi 300545785  85 KTVDTLEGADPSSLAN 100
Cdd:PTZ00051  82 SVVDTLLGANDEALKQ 97
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 9-95 5.07e-15

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


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 70.78  E-value: 5.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785    9 VSKAELDNLRQSG-APVVLHFWASWCDASKQMDQVFSHLATDFP-RAHFFRVEAEEHPEISEAYSVAAVPYFVFFKDGKT 86
Cdd:TIGR01068   1 LTDANFDETIASSdKPVLVDFWAPWCGPCKMIAPILEELAKEYEgKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKE 80


                  ....*....
gi 300545785   87 VDTLEGADP 95
Cdd:TIGR01068  81 VDRSVGALP 89
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 8-95 3.48e-11

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


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 59.94  E-value: 3.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785    8 IVSKAELDN-LRQSGAPVVLHFWASWCDASKQMDQVFSHLATDFP-RAHFFRVEAEEHPEISEAYSVAAVPYFVFFKDGK 85
Cdd:pfam00085   4 VLTDANFDEvVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKgNVVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQ 83

                          90
                  ....*....|
gi 300545785   86 TVDTLEGADP 95
Cdd:pfam00085  84 PVDDYVGARP 93
 
Name Accession Description Interval E-value
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 157-246 1.72e-57

Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of PICOT and GRX-PICOT-like proteins. The non-PICOT members of this family contain only the GRX-like domain, whereas PICOT contains an N-terminal TRX-like domain followed by one to three GRX-like domains. It is interesting to note that PICOT from plants contain three repeats of the GRX-like domain, metazoan proteins (except for insect) have two repeats, while fungal sequences contain only one copy of the domain. PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli. Both GRX and TRX domains of PICOT are required for its activity. Characterized non-PICOT members of this family include CXIP1, a CAX-interacting protein in Arabidopsis thaliana, and PfGLP-1, a GRX-like protein from Plasmodium falciparum.


Pssm-ID: 239326  Cd Length: 90  Bit Score: 185.00  E-value: 1.72e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 157 LEKLTNSHPVMLFMKGIPEEPRCGFSRKVVDILKEVNVDFGSFDILSDNEVREGLKKFSNWPTFPQLYCNGELLGGADIA 236
Cdd:cd03028    1 IKKLIKENPVVLFMKGTPEEPRCGFSRKVVQILNQLGVDFGTFDILEDEEVRQGLKEYSNWPTFPQLYVNGELVGGCDIV 80

                         90
                 ....*....|
gi 300545785 237 IAMHESGELK 246
Cdd:cd03028   81 KEMHESGELQ 90
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 394-483 5.25e-56

Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of PICOT and GRX-PICOT-like proteins. The non-PICOT members of this family contain only the GRX-like domain, whereas PICOT contains an N-terminal TRX-like domain followed by one to three GRX-like domains. It is interesting to note that PICOT from plants contain three repeats of the GRX-like domain, metazoan proteins (except for insect) have two repeats, while fungal sequences contain only one copy of the domain. PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli. Both GRX and TRX domains of PICOT are required for its activity. Characterized non-PICOT members of this family include CXIP1, a CAX-interacting protein in Arabidopsis thaliana, and PfGLP-1, a GRX-like protein from Plasmodium falciparum.


Pssm-ID: 239326  Cd Length: 90  Bit Score: 181.15  E-value: 5.25e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 394 LKALINSSEVMLFMKGSPDEPKCGFSSKVVKALRGENVSFGSFDILTDEEVRQGIKNFSNWPTFPQLYYKGELIGGCDII 473
Cdd:cd03028    1 IKKLIKENPVVLFMKGTPEEPRCGFSRKVVQILNQLGVDFGTFDILEDEEVRQGLKEYSNWPTFPQLYVNGELVGGCDIV 80

                         90
                 ....*....|
gi 300545785 474 MELSESGDLK 483
Cdd:cd03028   81 KEMHESGELQ 90
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 287-376 1.04e-54

Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of PICOT and GRX-PICOT-like proteins. The non-PICOT members of this family contain only the GRX-like domain, whereas PICOT contains an N-terminal TRX-like domain followed by one to three GRX-like domains. It is interesting to note that PICOT from plants contain three repeats of the GRX-like domain, metazoan proteins (except for insect) have two repeats, while fungal sequences contain only one copy of the domain. PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli. Both GRX and TRX domains of PICOT are required for its activity. Characterized non-PICOT members of this family include CXIP1, a CAX-interacting protein in Arabidopsis thaliana, and PfGLP-1, a GRX-like protein from Plasmodium falciparum.


Pssm-ID: 239326  Cd Length: 90  Bit Score: 177.69  E-value: 1.04e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 287 LEGLVNSKPVMLFMKGRPEEPKCGFSGKVVEILNQEKIEFGSFDILLDDEVRQGLKVYSNWSSYPQLYVKGELMGGSDIV 366
Cdd:cd03028    1 IKKLIKENPVVLFMKGTPEEPRCGFSRKVVQILNQLGVDFGTFDILEDEEVRQGLKEYSNWPTFPQLYVNGELVGGCDIV 80

                         90
                 ....*....|
gi 300545785 367 LEMQKSGELK 376
Cdd:cd03028   81 KEMHESGELQ 90
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
388-488 3.31e-49

Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440047  Cd Length: 105  Bit Score: 164.13  E-value: 3.31e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 388 QSLEDRLKALINSSEVMLFMKGSPDEPKCGFSSKVVKALRGENVSFGSFDILTDEEVRQGIKNFSNWPTFPQLYYKGELI 467
Cdd:COG0278    2 MDVQERIKQQIKSNPVVLFMKGTPQFPQCGFSARAVQILNACGVDFATVNVLEDPEIRQGLKEYSNWPTIPQLYVKGEFI 81

                         90       100
                 ....*....|....*....|.
gi 300545785 468 GGCDIIMELSESGDLKATLSE 488
Cdd:COG0278   82 GGCDIIREMYESGELQKLLEE 102
TIGR00365 TIGR00365
monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. ...
 391-486 8.91e-49

monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. coli, originally designated ydhD, is now designated grxD. Its protein, Grx4, is a monothiol glutaredoxin similar to Grx5 of yeast, which is involved in iron-sulfur cluster formation. [Energy metabolism, Electron transport]


Pssm-ID: 188046  Cd Length: 97  Bit Score: 162.63  E-value: 8.91e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785  391 EDRLKALINSSEVMLFMKGSPDEPKCGFSSKVVKALRGENVSFGSFDILTDEEVRQGIKNFSNWPTFPQLYYKGELIGGC 470
Cdd:TIGR00365   2 IERIKEQIAENPVVLYMKGTPQFPQCGFSARAVQILNACGVPFAYVNVLEDPEIRQGIKEYSNWPTIPQLYVKGEFVGGC 81

                          90
                  ....*....|....*.
gi 300545785  471 DIIMELSESGDLKATL 486
Cdd:TIGR00365  82 DIIMEMYQSGELQTLL 97
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
150-254 4.68e-48

Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440047  Cd Length: 105  Bit Score: 161.05  E-value: 4.68e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 150 ADALKSRLEKLTNSHPVMLFMKGIPEEPRCGFSRKVVDILKEVNVDFGSFDILSDNEVREGLKKFSNWPTFPQLYCNGEL 229
Cdd:COG0278    1 MMDVQERIKQQIKSNPVVLFMKGTPQFPQCGFSARAVQILNACGVDFATVNVLEDPEIRQGLKEYSNWPTIPQLYVKGEF 80

                         90       100
                 ....*....|....*....|....*
gi 300545785 230 LGGADIAIAMHESGELKDAFKDLGI 254
Cdd:COG0278   81 IGGCDIIREMYESGELQKLLEEAGA 105
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
280-384 1.18e-46

Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440047  Cd Length: 105  Bit Score: 157.20  E-value: 1.18e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 280 SETLRARLEGLVNSKPVMLFMKGRPEEPKCGFSGKVVEILNQEKIEFGSFDILLDDEVRQGLKVYSNWSSYPQLYVKGEL 359
Cdd:COG0278    1 MMDVQERIKQQIKSNPVVLFMKGTPQFPQCGFSARAVQILNACGVDFATVNVLEDPEIRQGLKEYSNWPTIPQLYVKGEF 80

                         90       100
                 ....*....|....*....|....*
gi 300545785 360 MGGSDIVLEMQKSGELKKVLTEKGI 384
Cdd:COG0278   81 IGGCDIIREMYESGELQKLLEEAGA 105
TIGR00365 TIGR00365
monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. ...
 154-249 2.04e-45

monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. coli, originally designated ydhD, is now designated grxD. Its protein, Grx4, is a monothiol glutaredoxin similar to Grx5 of yeast, which is involved in iron-sulfur cluster formation. [Energy metabolism, Electron transport]


Pssm-ID: 188046  Cd Length: 97  Bit Score: 153.77  E-value: 2.04e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785  154 KSRLEKLTNSHPVMLFMKGIPEEPRCGFSRKVVDILKEVNVDFGSFDILSDNEVREGLKKFSNWPTFPQLYCNGELLGGA 233
Cdd:TIGR00365   2 IERIKEQIAENPVVLYMKGTPQFPQCGFSARAVQILNACGVPFAYVNVLEDPEIRQGIKEYSNWPTIPQLYVKGEFVGGC 81

                          90
                  ....*....|....*.
gi 300545785  234 DIAIAMHESGELKDAF 249
Cdd:TIGR00365  82 DIIMEMYQSGELQTLL 97
TIGR00365 TIGR00365
monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. ...
 285-379 1.06e-43

monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. coli, originally designated ydhD, is now designated grxD. Its protein, Grx4, is a monothiol glutaredoxin similar to Grx5 of yeast, which is involved in iron-sulfur cluster formation. [Energy metabolism, Electron transport]


Pssm-ID: 188046  Cd Length: 97  Bit Score: 149.15  E-value: 1.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785  285 ARLEGLVNSKPVMLFMKGRPEEPKCGFSGKVVEILNQEKIEFGSFDILLDDEVRQGLKVYSNWSSYPQLYVKGELMGGSD 364
Cdd:TIGR00365   3 ERIKEQIAENPVVLYMKGTPQFPQCGFSARAVQILNACGVPFAYVNVLEDPEIRQGIKEYSNWPTIPQLYVKGEFVGGCD 82

                          90
                  ....*....|....*
gi 300545785  365 IVLEMQKSGELKKVL 379
Cdd:TIGR00365  83 IIMEMYQSGELQTLL 97
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 10-102 4.76e-40

TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT contains an N-terminal TRX-like domain, which does not contain the catalytic CXXC motif, followed by one to three glutaredoxin domains. The TRX-like domain is required for interaction with PKC theta. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli.


Pssm-ID: 239282 [Multi-domain]  Cd Length: 97  Bit Score: 139.33  E-value: 4.76e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785  10 SKAELDNLRQSGA--PVVLHFWASWCDASKQMDQVFSHLATD-FPRAHFFRVEAEEHPEISEAYSVAAVPYFVFFKDGKT 86
Cdd:cd02984    1 SEEEFEELLKSDAskLLVLHFWAPWAEPCKQMNQVFEELAKEaFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTI 80

                         90
                 ....*....|....*.
gi 300545785  87 VDTLEGADPSSLANKV 102
Cdd:cd02984   81 VDRVSGADPKELAKKV 96
PTZ00062 PTZ00062
glutaredoxin; Provisional
 7-251 7.44e-35

glutaredoxin; Provisional


Pssm-ID: 240250 [Multi-domain]  Cd Length: 204  Bit Score: 129.15  E-value: 7.44e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785   7 DIVSKAELDNLRQS-GAPVVLHFWASWCDASKQMDQVFSHLATDFPRAHFFRVeaeehpeiSEAYSVAAVPYFVFFKDGK 85
Cdd:PTZ00062   2 NFIKKEEKDKLIESnTGKLVLYVKSSKEPEYEQLMDVCNALVEDFPSLEFYVV--------NLADANNEYGVFEFYQNSQ 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785  86 TVDTLEGADPSSLANKVGKVAGSSTSAEpaapaslglaagptileTVKenakaslqdraqpvstadalksRLEKLTNSHP 165
Cdd:PTZ00062  74 LINSLEGCNTSTLVSFIRGWAQKGSSED-----------------TVE----------------------KIERLIRNHK 114

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 166 VMLFMKGIPEEPRCGFSRKVVDILKEVNVDFGSFDILSDNEVREGLKKFSNWPTFPQLYCNGELLGGADIAIAMHESGEL 245
Cdd:PTZ00062 115 ILLFMKGSKTFPFCRFSNAVVNMLNSSGVKYETYNIFEDPDLREELKVYSNWPTYPQLYVNGELIGGHDIIKELYESNSL 194


                 ....*.
gi 300545785 246 KDAFKD 251
Cdd:PTZ00062 195 RKVIPD 200
PTZ00062 PTZ00062
glutaredoxin; Provisional
 276-381 1.60e-30

glutaredoxin; Provisional


Pssm-ID: 240250 [Multi-domain]  Cd Length: 204  Bit Score: 117.59  E-value: 1.60e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 276 NTGLSETLRaRLEGLVNSKPVMLFMKGRPEEPKCGFSGKVVEILNQEKIEFGSFDILLDDEVRQGLKVYSNWSSYPQLYV 355
Cdd:PTZ00062  96 KGSSEDTVE-KIERLIRNHKILLFMKGSKTFPFCRFSNAVVNMLNSSGVKYETYNIFEDPDLREELKVYSNWPTYPQLYV 174

                         90       100
                 ....*....|....*....|....*.
gi 300545785 356 KGELMGGSDIVLEMQKSGELKKVLTE 381
Cdd:PTZ00062 175 NGELIGGHDIIKELYESNSLRKVIPD 200
PTZ00062 PTZ00062
glutaredoxin; Provisional
 385-483 8.62e-29

glutaredoxin; Provisional


Pssm-ID: 240250 [Multi-domain]  Cd Length: 204  Bit Score: 112.58  E-value: 8.62e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 385 TGEQSLEDRLKALINSSEVMLFMKGSPDEPKCGFSSKVVKALRGENVSFGSFDILTDEEVRQGIKNFSNWPTFPQLYYKG 464
Cdd:PTZ00062  97 GSSEDTVEKIERLIRNHKILLFMKGSKTFPFCRFSNAVVNMLNSSGVKYETYNIFEDPDLREELKVYSNWPTYPQLYVNG 176

                         90
                 ....*....|....*....
gi 300545785 465 ELIGGCDIIMELSESGDLK 483
Cdd:PTZ00062 177 ELIGGHDIIKELYESNSLR 195
PRK10824 PRK10824
Grx4 family monothiol glutaredoxin;
392-488 2.12e-28

Grx4 family monothiol glutaredoxin;


Pssm-ID: 182759  Cd Length: 115  Bit Score: 108.84  E-value: 2.12e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 392 DRLKALINSSEVMLFMKGSPDEPKCGFSSKVVKALRGENVSFGSFDILTDEEVRQGIKNFSNWPTFPQLYYKGELIGGCD 471
Cdd:PRK10824   6 EKIQRQIAENPILLYMKGSPKLPSCGFSAQAVQALSACGERFAYVDILQNPDIRAELPKYANWPTFPQLWVDGELVGGCD 85

                         90
                 ....*....|....*..
gi 300545785 472 IIMELSESGDLKATLSE 488
Cdd:PRK10824  86 IVIEMYQRGELQQLIKE 102
PRK10824 PRK10824
Grx4 family monothiol glutaredoxin;
156-266 4.80e-27

Grx4 family monothiol glutaredoxin;


Pssm-ID: 182759  Cd Length: 115  Bit Score: 104.99  E-value: 4.80e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 156 RLEKLTNSHPVMLFMKGIPEEPRCGFSRKVVDILKEVNVDFGSFDILSDNEVREGLKKFSNWPTFPQLYCNGELLGGADI 235
Cdd:PRK10824   7 KIQRQIAENPILLYMKGSPKLPSCGFSAQAVQALSACGERFAYVDILQNPDIRAELPKYANWPTFPQLWVDGELVGGCDI 86

                         90       100       110
                 ....*....|....*....|....*....|.
gi 300545785 236 AIAMHESGELKDAFKDlgiTTVGSKESQDEA 266
Cdd:PRK10824  87 VIEMYQRGELQQLIKE---TAAKYKSEEPDA 114
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 165-241 2.37e-26

Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, as well as E. coli GRX1 and GRX3, which are members of this family. E. coli GRX2, however, is a 24-kDa protein that belongs to the GSH S-transferase (GST) family.


Pssm-ID: 239017 [Multi-domain]  Cd Length: 72  Bit Score: 101.39  E-value: 2.37e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300545785 165 PVMLFMKGIpeeprCGFSRKVVDILKEVNVDFGSFDILSDNEVREGLKKFSNWPTFPQLYCNGELLGGADIAIAMHE 241
Cdd:cd02066    1 KVVVFSKST-----CPYCKRAKRLLESLGIEFEEIDILEDGELREELKELSGWPTVPQIFINGEFIGGYDDLKALHE 72
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 12-97 4.53e-26

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: 101.48  E-value: 4.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785  12 AELDNLRQSGAPVVLHFWASWCDASKQMDQVFSHLATDFPRAHFFRVEAEEHPEISEAYSVAAVPYFVFFKDGKTVDTLE 91
Cdd:cd02947    1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVV 80


                 ....*.
gi 300545785  92 GADPSS 97
Cdd:cd02947   81 GADPKE 86
PRK10824 PRK10824
Grx4 family monothiol glutaredoxin;
286-381 7.63e-26

Grx4 family monothiol glutaredoxin;


Pssm-ID: 182759  Cd Length: 115  Bit Score: 101.52  E-value: 7.63e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 286 RLEGLVNSKPVMLFMKGRPEEPKCGFSGKVVEILNQEKIEFGSFDILLDDEVRQGLKVYSNWSSYPQLYVKGELMGGSDI 365
Cdd:PRK10824   7 KIQRQIAENPILLYMKGSPKLPSCGFSAQAVQALSACGERFAYVDILQNPDIRAELPKYANWPTFPQLWVDGELVGGCDI 86

                         90
                 ....*....|....*.
gi 300545785 366 VLEMQKSGELKKVLTE 381
Cdd:PRK10824  87 VIEMYQRGELQQLIKE 102
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 403-478 9.62e-26

Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, as well as E. coli GRX1 and GRX3, which are members of this family. E. coli GRX2, however, is a 24-kDa protein that belongs to the GSH S-transferase (GST) family.


Pssm-ID: 239017 [Multi-domain]  Cd Length: 72  Bit Score: 99.85  E-value: 9.62e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300545785 403 VMLFMKGSpdepkCGFSSKVVKALRGENVSFGSFDILTDEEVRQGIKNFSNWPTFPQLYYKGELIGGCDIIMELSE 478
Cdd:cd02066    2 VVVFSKST-----CPYCKRAKRLLESLGIEFEEIDILEDGELREELKELSGWPTVPQIFINGEFIGGYDDLKALHE 72
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 295-371 4.50e-23

Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, as well as E. coli GRX1 and GRX3, which are members of this family. E. coli GRX2, however, is a 24-kDa protein that belongs to the GSH S-transferase (GST) family.


Pssm-ID: 239017 [Multi-domain]  Cd Length: 72  Bit Score: 92.53  E-value: 4.50e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300545785 295 PVMLFMKGRpeepkCGFSGKVVEILNQEKIEFGSFDILLDDEVRQGLKVYSNWSSYPQLYVKGELMGGSDIVLEMQK 371
Cdd:cd02066    1 KVVVFSKST-----CPYCKRAKRLLESLGIEFEEIDILEDGELREELKELSGWPTVPQIFINGEFIGGYDDLKALHE 72
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 9-105 1.65e-21

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: 89.11  E-value: 1.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785   9 VSKAELDN-LRQSGAPVVLHFWASWCDASKQMDQVFSHLATDF-PRAHFFRVEAEEHPEISEAYSVAAVPYFVFFKDGKT 86
Cdd:COG3118    5 LTDENFEEeVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYgGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQP 84

                         90       100
                 ....*....|....*....|
gi 300545785  87 VDTLEGA-DPSSLANKVGKV 105
Cdd:COG3118   85 VDRFVGAlPKEQLREFLDKV 104
Glutaredoxin pfam00462
Glutaredoxin;
166-229 2.41e-19

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 81.40  E-value: 2.41e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300545785  166 VMLFMKgipeePRCGFSRKVVDILKEVNVDFGSFDILSDNEVREGLKKFSNWPTFPQLYCNGEL 229
Cdd:pfam00462   1 VVLYTK-----PTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKELSGWPTVPQVFIDGEH 59
Glutaredoxin pfam00462
Glutaredoxin;
403-467 1.21e-18

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 79.47  E-value: 1.21e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300545785  403 VMLFMKgspdePKCGFSSKVVKALRGENVSFGSFDILTDEEVRQGIKNFSNWPTFPQLYYKGELI 467
Cdd:pfam00462   1 VVLYTK-----PTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKELSGWPTVPQVFIDGEHI 60
Glutaredoxin pfam00462
Glutaredoxin;
296-359 1.92e-16

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 73.31  E-value: 1.92e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300545785  296 VMLFMKgrpeePKCGFSGKVVEILNQEKIEFGSFDILLDDEVRQGLKVYSNWSSYPQLYVKGEL 359
Cdd:pfam00462   1 VVLYTK-----PTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKELSGWPTVPQVFIDGEH 59
PTZ00051 PTZ00051
thioredoxin; Provisional
 5-100 5.06e-15

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 70.68  E-value: 5.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785   5 VKDIVSKAELDNLRQSGAPVVLHFWASWCDASKQMDQVFSHLATDFPRAHFFRVEAEEHPEISEAYSVAAVPYFVFFKDG 84
Cdd:PTZ00051   2 VHIVTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDELSEVAEKENITSMPTFKVFKNG 81

                         90
                 ....*....|....*.
gi 300545785  85 KTVDTLEGADPSSLAN 100
Cdd:PTZ00051  82 SVVDTLLGANDEALKQ 97
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 9-95 5.07e-15

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


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 70.78  E-value: 5.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785    9 VSKAELDNLRQSG-APVVLHFWASWCDASKQMDQVFSHLATDFP-RAHFFRVEAEEHPEISEAYSVAAVPYFVFFKDGKT 86
Cdd:TIGR01068   1 LTDANFDETIASSdKPVLVDFWAPWCGPCKMIAPILEELAKEYEgKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKE 80


                  ....*....
gi 300545785   87 VDTLEGADP 95
Cdd:TIGR01068  81 VDRSVGALP 89
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 23-95 4.52e-14

ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like domain. Its gene has been sequenced from several gammaproteobacteria and actinobacteria.


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 67.68  E-value: 4.52e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300545785  23 PVVLHFWASWCDASKQMDQVFSHLATDFP-RAHFFRVEAEEHPEISEAYSVAAVPYFVFFKDGKTVDTLEGADP 95
Cdd:cd02956   14 PVVVDFWAPRSPPSKELLPLLERLAEEYQgQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVDGFQGAQP 87
PRK10996 PRK10996
thioredoxin 2; Provisional
 10-97 8.87e-13

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 65.48  E-value: 8.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785  10 SKAELDNLRQSGAPVVLHFWASWCDASKQMDQVFSHLATDFP-RAHFFRVEAEEHPEISEAYSVAAVPYFVFFKDGKTVD 88
Cdd:PRK10996  41 TGETLDKLLQDDLPVVIDFWAPWCGPCRNFAPIFEDVAAERSgKVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVD 120


                 ....*....
gi 300545785  89 TLEGADPSS 97
Cdd:PRK10996 121 MLNGAVPKA 129
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 8-95 3.48e-11

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


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 59.94  E-value: 3.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785    8 IVSKAELDN-LRQSGAPVVLHFWASWCDASKQMDQVFSHLATDFP-RAHFFRVEAEEHPEISEAYSVAAVPYFVFFKDGK 85
Cdd:pfam00085   4 VLTDANFDEvVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKgNVVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQ 83

                          90
                  ....*....|
gi 300545785   86 TVDTLEGADP 95
Cdd:pfam00085  84 PVDDYVGARP 93
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 14-108 4.76e-10

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 57.78  E-value: 4.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785  14 LDNLRqsGAPVVLHFWASWCDASKQMDQVFSHLATDFPRAHFFRVEAEEHPE----------------------ISEAYS 71
Cdd:COG0526   23 LADLK--GKPVLVNFWATWCPPCRAEMPVLKELAEEYGGVVFVGVDVDENPEavkaflkelglpypvlldpdgeLAKAYG 100

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 300545785  72 VAAVPYFVFF-KDGKTVDTLEGA-DPSSLANKVGKVAGS 108
Cdd:COG0526  101 VRGIPTTVLIdKDGKIVARHVGPlSPEELEEALEKLLAK 139
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 165-246 8.89e-10

Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, which are members of this subfamily. Also included in this subfamily are the N-terminal GRX domains of proteins similar to human thioredoxin reductase 1 and 3.


Pssm-ID: 239511 [Multi-domain]  Cd Length: 82  Bit Score: 55.24  E-value: 8.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 165 PVMLFMKgipeePRCGFSRKVVDILKEVNVDFGSF--DILSD-NEVREGLKKFSNWPTFPQLYCNGELLGGADIAIAMHE 241
Cdd:cd03419    1 PVVVFSK-----SYCPYCKRAKSLLKELGVKPAVVelDQHEDgSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHK 75


                 ....*
gi 300545785 242 SGELK 246
Cdd:cd03419   76 SGKLV 80
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 9-92 1.81e-07

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


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 49.99  E-value: 1.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785   9 VSKAELDNLRQSGAPVVLHFWASWCDASKQMDQVFSHLATDFP--------------------RAHFFRVEAEEHPEISE 68
Cdd:cd03011    8 LDGEQFDLESLSGKPVLVYFWATWCPVCRFTSPTVNQLAADYPvvsvalrsgddgavarfmqkKGYGFPVINDPDGVISA 87

                         90       100
                 ....*....|....*....|....
gi 300545785  69 AYSVAAVPYFVFFKDGKTVDTLEG 92
Cdd:cd03011   88 RWGVSVTPAIVIVDPGGIVFVTTG 111
Phd_like cd02957
Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as ...
 3-90 4.62e-07

Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as cytosolic regulators of G protein functions. Phd and PhLPs specifically bind G protein betagamma (Gbg)-subunits with high affinity, resulting in the solubilization of Gbg from the plasma membrane and impeding G protein-mediated signal transduction by inhibiting the formation of a functional G protein trimer (G protein alphabetagamma). Phd also inhibits the GTPase activity of G protein alpha. Phd can be phosphorylated by protein kinase A and G protein-coupled receptor kinase 2, leading to its inactivation. Phd was originally isolated from the retina, where it is highly expressed and has been implicated to play an important role in light adaptation. It is also found in the pineal gland, liver, spleen, striated muscle and the brain. The C-terminal domain of Phd adopts a thioredoxin fold, but it does not contain a CXXC motif. Phd interacts with G protein beta mostly through the N-terminal helical domain. Also included in this family is a PhLP characterized as a viral inhibitor of apoptosis (IAP)-associated factor, named VIAF, that functions in caspase activation during apoptosis.


Pssm-ID: 239255 [Multi-domain]  Cd Length: 113  Bit Score: 48.32  E-value: 4.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785   3 GTVKDIVSKAELDNLRQSGA--PVVLHFWASWCDASKQMDQVFSHLATDFPRAHFFRVEAEEhPEISEAYSVAAVPYFVF 80
Cdd:cd02957    4 GEVREISSKEFLEEVTKASKgtRVVVHFYEPGFPRCKILDSHLEELAAKYPETKFVKINAEK-AFLVNYLDIKVLPTLLV 82

                         90
                 ....*....|
gi 300545785  81 FKDGKTVDTL 90
Cdd:cd02957   83 YKNGELIDNI 92
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 3-90 5.87e-07

PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of uncharacterized PDI-like eukaryotic proteins containing only one redox active TRX (a) domain with a CXXS motif, similar to ERp44. CXXS is still a redox active motif; however, the mixed disulfide formed with the substrate is more stable than those formed by CXXC motif proteins. PDI-related proteins are usually involved in the oxidative protein folding in the ER by acting as catalysts and folding assistants. ERp44 is involved in thiol-mediated retention in the ER.


Pssm-ID: 239297 [Multi-domain]  Cd Length: 100  Bit Score: 47.74  E-value: 5.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785   3 GTVKdIVSKAELDNLRQSGAPVVLHFWASWCDASKQMDQVFSHLATDFPRAHFFRVEAEE-HPEISEAYSVAAVPYFVFF 81
Cdd:cd02999    1 PPEE-VLNIALDLMAFNREDYTAVLFYASWCPFSASFRPHFNALSSMFPQIRHLAIEESSiKPSLLSRYGVVGFPTILLF 79

                         90
                 ....*....|....*..
gi 300545785  82 KDG--------KTVDTL 90
Cdd:cd02999   80 NSTprvryngtRTLDSL 96
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 403-483 2.01e-06

Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, which are members of this subfamily. Also included in this subfamily are the N-terminal GRX domains of proteins similar to human thioredoxin reductase 1 and 3.


Pssm-ID: 239511 [Multi-domain]  Cd Length: 82  Bit Score: 45.61  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 403 VMLFMKGSpdepkCGFSSKVVKALRGENVSFGSF--DILTD-EEVRQGIKNFSNWPTFPQLYYKGELIGGCDIIMELSES 479
Cdd:cd03419    2 VVVFSKSY-----CPYCKRAKSLLKELGVKPAVVelDQHEDgSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKS 76


                 ....
gi 300545785 480 GDLK 483
Cdd:cd03419   77 GKLV 80
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
165-250 7.46e-06

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 43.65  E-value: 7.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 165 PVMLFMKgipeePRCGFSRKVVDILKEVNVDFGSFDILSDNEVREGLKKFSNWPTFPQLYCNGELLGGADiaiamheSGE 244
Cdd:COG0695    1 KVTLYTT-----PGCPYCARAKRLLDEKGIPYEEIDVDEDPEAREELRERSGRRTVPVIFIGGEHLGGFD-------EGE 68


                 ....*.
gi 300545785 245 LKDAFK 250
Cdd:COG0695   69 LDALLA 74
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 295-377 2.27e-05

Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, which are members of this subfamily. Also included in this subfamily are the N-terminal GRX domains of proteins similar to human thioredoxin reductase 1 and 3.


Pssm-ID: 239511 [Multi-domain]  Cd Length: 82  Bit Score: 42.53  E-value: 2.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 295 PVMLFMKgrpeePKCGFSGKVVEILNQEKIEFGSFDilLDD-----EVRQGLKVYSNWSSYPQLYVKGELMGGSDIVLEM 369
Cdd:cd03419    1 PVVVFSK-----SYCPYCKRAKSLLKELGVKPAVVE--LDQhedgsEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMAL 73


                 ....*...
gi 300545785 370 QKSGELKK 377
Cdd:cd03419   74 HKSGKLVK 81
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
414-486 3.38e-05

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 41.72  E-value: 3.38e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300545785 414 PKCGFSSKVVKALRGENVSFGSFDILTDEEVRQGIKNFSNWPTFPQLYYKGELIGGCDiimelseSGDLKATL 486
Cdd:COG0695    8 PGCPYCARAKRLLDEKGIPYEEIDVDEDPEAREELRERSGRRTVPVIFIGGEHLGGFD-------EGELDALL 73
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 206-259 3.77e-05

Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of uncharacterized eukaryotic proteins containing a GRX-like domain having only one conserved cysteine, aligning to the C-terminal cysteine of the CXXC motif of GRXs. This subfamily is predominantly composed of plant proteins. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins via a redox active CXXC motif using a similar dithiol mechanism employed by TRXs. GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. Proteins containing only the C-terminal cysteine are generally redox inactive.


Pssm-ID: 239329 [Multi-domain]  Cd Length: 147  Bit Score: 43.76  E-value: 3.77e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 300545785 206 EVREGLKKFSNWPTFPQLYCNGELLGGADIAIAMHESGELKDAFKDLGITTVGS 259
Cdd:cd03031   47 ELRELLGAELKAVSLPRVFVDGRYLGGAEEVLRLNESGELRKLLKGIRARAGGG 100
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 414-486 4.38e-05

Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This family of glutaredoxins includes the E. coli protein GrxC (Grx3) which appears to have a secondary role in reducing ribonucleotide reductase (in the absence of GrxA) possibly indicating a role in the reduction of other protein disulfides. [Energy metabolism, Electron transport]


Pssm-ID: 274017 [Multi-domain]  Cd Length: 79  Bit Score: 41.86  E-value: 4.38e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300545785  414 PKCGFSSKVVKALRGENVSFGSFDILTDEEVRQGIKNFSNWPTFPQLYYKGELIGGCDIIMELSESGDLKATL 486
Cdd:TIGR02181   7 PYCPYCTRAKALLSSKGVTFTEIRVDGDPALRDEMMQRSGRRTVPQIFIGDVHVGGCDDLYALDREGKLDPLL 79
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 11-95 5.17e-05

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 43.35  E-value: 5.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785  11 KAELDNLRQSGAPVVLHFWASWCDASKQMD-QVFSHLAT-DFPRAHFF--RVEAE--------------EHpEISEAYSV 72
Cdd:COG2143   30 EEDLALAKAEGKPILLFFESDWCPYCKKLHkEVFSDPEVaAYLKENFVvvQLDAEgdkevtdfdgetltEK-ELARKYGV 108

                         90       100
                 ....*....|....*....|....
gi 300545785  73 AAVPYFVFF-KDGKTVDTLEGADP 95
Cdd:COG2143  109 RGTPTLVFFdAEGKEIARIPGYLK 132
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 25-84 6.42e-05

Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include TRX, protein disulfide isomerase (PDI), tlpA-like, glutaredoxin, NrdH redoxin, and the bacterial Dsb (DsbA, DsbC, DsbG, DsbE, DsbDgamma) protein families. Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins and glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 41.14  E-value: 6.42e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300545785  25 VLHFWASWCDASKQMDQVFSHLATDFPRAHFFRVEAEEHPEISEA---YSVAAVPYFVFFKDG 84
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELALLNKGVKFEAVDVDEDPALEKElkrYGVGGVPTLVVFGPG 63
Phd_like_Phd cd02987
Phosducin (Phd)-like family, Phd subfamily; Phd is a cytosolic regulator of G protein ...
 3-90 9.28e-05

Phosducin (Phd)-like family, Phd subfamily; Phd is a cytosolic regulator of G protein functions. It specifically binds G protein betagamma (Gbg)-subunits with high affinity, resulting in the solubilization of Gbg from the plasma membrane. This impedes the formation of a functional G protein trimer (G protein alphabetagamma), thereby inhibiting G protein-mediated signal transduction. Phd also inhibits the GTPase activity of G protein alpha. Phd can be phosphorylated by protein kinase A and G protein-coupled receptor kinase 2, leading to its inactivation. Phd was originally isolated from the retina, where it is highly expressed and has been implicated to play an important role in light adaptation. It is also found in the pineal gland, liver, spleen, striated muscle and the brain. The C-terminal domain of Phd adopts a thioredoxin fold, but it does not contain a CXXC motif. Phd interacts with G protein beta mostly through the N-terminal helical domain.


Pssm-ID: 239285  Cd Length: 175  Bit Score: 43.05  E-value: 9.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785   3 GTVKDIVSKAE-LDNLRQSGA--PVVLHFWASWCDASKQMDQVFSHLATDFPRAHFFRVEAEEhPEISEAYSVAAVPYFV 79
Cdd:cd02987   62 GKVYELDSGEQfLDAIDKEGKdtTVVVHIYEPGIPGCAALNSSLLCLAAEYPAVKFCKIRASA-TGASDEFDTDALPALL 140

                         90
                 ....*....|.
gi 300545785  80 FFKDGKTVDTL 90
Cdd:cd02987  141 VYKGGELIGNF 151
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
 12-84 1.28e-04

DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein DsbD. It contains a CXXC motif in a TRX fold and shuttles the reducing potential from the membrane domain (DsbD beta) to the N-terminal periplasmic domain (DsbD alpha). DsbD beta, a transmembrane domain comprising of eight helices, acquires its reducing potential from the cytoplasmic thioredoxin. DsbD alpha transfers the acquired reducing potential from DsbD gamma to target proteins such as the periplasmic protein disulphide isomerases, DsbC and DsbG. This flow of reducing potential from the cytoplasm through DsbD allows DsbC and DsbG to act as isomerases in the oxidizing environment of the bacterial periplasm. DsbD also transfers reducing potential from the cytoplasm to specific reductases in the periplasm which are involved in the maturation of cytochromes.


Pssm-ID: 239251 [Multi-domain]  Cd Length: 104  Bit Score: 41.05  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785  12 AELDNLRQSGAPVVLHFWASWCDASKQMDQ-VFSH------LATDFpraHFFRVEA----EEHPEISEAYSVAAVPYFVF 80
Cdd:cd02953    2 AALAQALAQGKPVFVDFTADWCVTCKVNEKvVFSDpevqaaLKKDV---VLLRADWtkndPEITALLKRFGVFGPPTYLF 78


                 ....
gi 300545785  81 FKDG 84
Cdd:cd02953   79 YGPG 82
Phd_like_TxnDC9 cd02989
Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; ...
 3-92 1.29e-04

Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; composed of predominantly uncharacterized eukaryotic proteins, containing a TRX-like domain without the redox active CXXC motif. The gene name for the human protein is TxnDC9. The two characterized members are described as Phd-like proteins, PLP1 of Saccharomyces cerevisiae and PhLP3 of Dictyostelium discoideum. Gene disruption experiments show that both PLP1 and PhLP3 are non-essential proteins. Unlike Phd and most Phd-like proteins, members of this group do not contain the Phd N-terminal helical domain which is implicated in binding to the G protein betagamma subunit.


Pssm-ID: 239287  Cd Length: 113  Bit Score: 41.41  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785   3 GTVKDIVSKAELDNLRQSGAPVVLHFWASWCDASKQMDQVFSHLATDFPRAHFFRVEAEEHPEISEAYSVAAVPYFVFFK 82
Cdd:cd02989    4 GKYREVSDEKEFFEIVKSSERVVCHFYHPEFFRCKIMDKHLEILAKKHLETKFIKVNAEKAPFLVEKLNIKVLPTVILFK 83

                         90
                 ....*....|
gi 300545785  83 DGKTVDTLEG 92
Cdd:cd02989   84 NGKTVDRIVG 93
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
295-379 1.36e-04

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 40.18  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785 295 PVMLFMKgrpeePKCGFSGKVVEILNQEKIEFGSFDILLDDEVRQGLKVYSNWSSYPQLYVKGELMGGSDivlemqkSGE 374
Cdd:COG0695    1 KVTLYTT-----PGCPYCARAKRLLDEKGIPYEEIDVDEDPEAREELRERSGRRTVPVIFIGGEHLGGFD-------EGE 68


                 ....*
gi 300545785 375 LKKVL 379
Cdd:COG0695   69 LDALL 73
trxA PRK09381
thioredoxin TrxA;
13-93 3.47e-04

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 40.05  E-value: 3.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785  13 ELDNLRQSGAPVVlHFWASWCDASKQMDQVFSHLATDFP-RAHFFRVEAEEHPEISEAYSVAAVPYFVFFKDGKTVDTLE 91
Cdd:PRK09381  14 DTDVLKADGAILV-DFWAEWCGPCKMIAPILDEIADEYQgKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKV 92


                 ..
gi 300545785  92 GA 93
Cdd:PRK09381  93 GA 94
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 335-381 3.83e-04

Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of uncharacterized eukaryotic proteins containing a GRX-like domain having only one conserved cysteine, aligning to the C-terminal cysteine of the CXXC motif of GRXs. This subfamily is predominantly composed of plant proteins. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins via a redox active CXXC motif using a similar dithiol mechanism employed by TRXs. GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. Proteins containing only the C-terminal cysteine are generally redox inactive.


Pssm-ID: 239329 [Multi-domain]  Cd Length: 147  Bit Score: 40.68  E-value: 3.83e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 300545785 335 DEVRQGLKVYSNWSSYPQLYVKGELMGGSDIVLEMQKSGELKKVLTE 381
Cdd:cd03031   46 EELRELLGAELKAVSLPRVFVDGRYLGGAEEVLRLNESGELRKLLKG 92
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 14-92 4.40e-04

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: 39.91  E-value: 4.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785  14 LDNLRqsGAPVVLHFWASWCDASKQ-----------------------MDQVFSHLATDFPRAH--FFRVEAEEHPEISE 68
Cdd:cd02966   14 LSDLK--GKVVLVNFWASWCPPCRAempelealakeykddgvevvgvnVDDDDPAAVKAFLKKYgiTFPVLLDPDGELAK 91

                         90       100
                 ....*....|....*....|....*
gi 300545785  69 AYSVAAVPYFVFF-KDGKTVDTLEG 92
Cdd:cd02966   92 AYGVRGLPTTFLIdRDGRIRARHVG 116
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
18-96 6.09e-04

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 39.33  E-value: 6.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785   18 RQSGAPVVLHFWASWCDASKQMDQVFSHLA--TDFPRAHFFRV---------------EAEEHPEISEAYSVAAVPYFVF 80
Cdd:pfam13098   1 KGNGKPVLVVFTDPDCPYCKKLKKELLEDPdvTVYLGPNFVFIavniwcakevakaftDILENKELGRKYGVRGTPTIVF 80

                          90
                  ....*....|....*..
gi 300545785   81 FkDGKTVDT-LEGADPS 96
Cdd:pfam13098  81 F-DGKGELLrLPGYVPA 96
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 248-449 6.85e-04

threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 272986 [Multi-domain]  Cd Length: 327  Bit Score: 41.60  E-value: 6.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785  248 AFKDLGITTVGSKESQDEAGKGGGVSSGNTGLSETLRARLEGLvnsKPVMLFMKGRPEEpkcgfsGKVVEIL--NQEKIE 325
Cdd:TIGR00260  52 SFKDRGMAVALTKALELGNDTVLCASTGNTGAAAAAYAGKAGL---KVVVLYPAGKISL------GKLAQALgyNAEVVA 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785  326 F-GSFDILLdDEVRQGLKVYSNW-----SSYPqLYVKG---------ELMGGSD---IVLEMQKSGELKKVLT---EKGI 384
Cdd:TIGR00260 123 IdGNFDDAQ-RLVKQLFEDKPALglnsaNSIP-YRLEGqktyafeavEQLGWEApdkVVVPVPNSGNFGAIWKgfkEKKM 200

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300545785  385 TGEQSLEDRLKALINSSEVML--FMKGSPDEPK-----------CGFSSKVVKALRGENVSFGSFDILTDEEVRQGIK 449
Cdd:TIGR00260 201 LGLDSLPVKRGIQAEGAADIVraFLEGGQWEPIetpetlstamdIGNPANWPRALEAFRRSNGYAEDLSDEEILEAIK 278
DsbD COG4232
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ...
 10-107 7.71e-04

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


Pssm-ID: 443376 [Multi-domain]  Cd Length: 416  Bit Score: 41.71  E-value: 7.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785  10 SKAELDNLRQSGAPVVLHFWASWCDASKQMDQ-VFSH------LATDFpraHFFRVEAEEH-PEIS---EAYSVAAVPYF 78
Cdd:COG4232  309 LEAALAEARAEGKPVFVDFTADWCVTCKENERtVFSDpevqaaLADDV---VLLKADVTDNdPEITallKRFGRFGVPTY 385

                         90       100       110
                 ....*....|....*....|....*....|.
gi 300545785  79 VFF-KDGKTVDTL-EGADPSSLANKVGKVAG 107
Cdd:COG4232  386 VFYdPDGEELPRLgFMLTADEFLAALEKAKG 416
PRK10638 PRK10638
glutaredoxin 3; Provisional
 416-487 1.53e-03

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 37.49  E-value: 1.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300545785 416 CGFSSKVVKALRGENVSFGSFDILTDEEVRQGIKNFSNWPTFPQLYYKGELIGGCDIIMELSESGDLKATLS 487
Cdd:PRK10638  12 CPFCHRAKALLNSKGVSFQEIPIDGDAAKREEMIKRSGRTTVPQIFIDAQHIGGCDDLYALDARGGLDPLLK 83
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 414-480 1.65e-03

Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of bacterial GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including E. coli GRX1 and GRX3, which are members of this subfamily.


Pssm-ID: 239510 [Multi-domain]  Cd Length: 75  Bit Score: 37.18  E-value: 1.65e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300545785 414 PKCGFSSKVVKALRGENVSFGSFDILTDEEVRQGIKNFSN-WPTFPQLYYKGELIGGCDIIMELSESG 480
Cdd:cd03418    8 PNCPYCVRAKALLDKKGVDYEEIDVDGDPALREEMINRSGgRRTVPQIFIGDVHIGGCDDLYALERKG 75
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 23-92 1.99e-03

PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide Isomerase Related). PDIR is composed of three redox active TRX (a) domains and an N-terminal redox inactive TRX-like (b) domain. Similar to PDI, it is involved in oxidative protein folding in the endoplasmic reticulum (ER) through its isomerase and chaperone activities. These activities are lower compared to PDI, probably due to PDIR acting only on a subset of proteins. PDIR is preferentially expressed in cells actively secreting proteins and its expression is induced by stress. Similar to PDI, the isomerase and chaperone activities of PDIR are independent; CXXC mutants lacking isomerase activity retain chaperone activity.


Pssm-ID: 239295 [Multi-domain]  Cd Length: 104  Bit Score: 37.68  E-value: 1.99e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300545785  23 PVVLHFWASWCDASKQMDQVFSHLATDF---PRAHFFRVEA--EEHPEISEAYSVAAVPYFVFFKDGKTVDTLEG 92
Cdd:cd02997   19 HVLVMFYAPWCGHCKKMKPEFTKAATELkedGKGVLAAVDCtkPEHDALKEEYNVKGFPTFKYFENGKFVEKYEG 93
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 422-488 2.83e-03

Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of uncharacterized eukaryotic proteins containing a GRX-like domain having only one conserved cysteine, aligning to the C-terminal cysteine of the CXXC motif of GRXs. This subfamily is predominantly composed of plant proteins. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins via a redox active CXXC motif using a similar dithiol mechanism employed by TRXs. GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. Proteins containing only the C-terminal cysteine are generally redox inactive.


Pssm-ID: 239329 [Multi-domain]  Cd Length: 147  Bit Score: 38.37  E-value: 2.83e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300545785 422 VVKALRGENVSFGSFDILTD----EEVRQGIKNFSNWPTFPQLYYKGELIGGCDIIMELSESGDLKATLSE 488
Cdd:cd03031   22 VRAILESFRVKFDERDVSMDsgfrEELRELLGAELKAVSLPRVFVDGRYLGGAEEVLRLNESGELRKLLKG 92
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 19-92 3.05e-03

TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found only in oxygenic photosynthetic organisms containing both TRX and NTR domains. The TRX domain functions as a protein disulfide reductase via the reversible oxidation of an active center dithiol present in a CXXC motif, while the NTR domain functions as a reductant to oxidized TRX. The fusion protein is bifunctional, showing both TRX and NTR activities, but it is not an independent NTR/TRX system. In plants, the protein is found exclusively in shoots and mature leaves and is localized in the chloroplast. It is involved in plant protection against oxidative stress.


Pssm-ID: 239247 [Multi-domain]  Cd Length: 97  Bit Score: 37.10  E-value: 3.05e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300545785  19 QSGAPVVLHFWASWCDASKQMDQVFSHLATDFP-RAHFFRVEAEEHPEISEAYSVAAVPYFVFFKDGKTVDTLEG 92
Cdd:cd02949   11 ESDRLILVLYTSPTCGPCRTLKPILNKVIDEFDgAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELVKEISG 85
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 2-107 4.41e-03

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 39.35  E-value: 4.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300545785   2 SGTVKDIVSKAELdnlrqsgapVVLHFWASWCDASKQMDQVFS----HLATDFPRAHFFRVEAEEHPEISEAYSVAAVPY 77
Cdd:PTZ00102  39 DSTFDKFITENEI---------VLVKFYAPWCGHCKRLAPEYKkaakMLKEKKSEIVLASVDATEEMELAQEFGVRGYPT 109

                         90       100       110
                 ....*....|....*....|....*....|
gi 300545785  78 FVFFKDGKTVDTLEGADPSSLANKVGKVAG 107
Cdd:PTZ00102 110 IKFFNKGNPVNYSGGRTADGIVSWIKKLTG 139
 
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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