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Conserved domains on  [gi|402872120|ref|XP_003899983|]
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PREDICTED: glutaredoxin-1 [Papio anubis]

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List of domain hits

Name Accession Description Interval E-value
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
14-96 9.92e-36

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  Cd Length: 82  Bit Score: 118.80  E-value: 9.92e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402872120  14 KVVVFIKPTCPYCRRAQEILSQLPIKQGLLEfVDITAtnHTNEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSMQQSG 93
Cdd:cd03419    1 PVVVFSKSYCPYCKRAKSLLKELGVKPAVVE-LDQHE--DGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSG 77

                 ...
gi 402872120  94 ELL 96
Cdd:cd03419   78 KLV 80
 
Name Accession Description Interval E-value
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
14-96 9.92e-36

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  Cd Length: 82  Bit Score: 118.80  E-value: 9.92e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402872120  14 KVVVFIKPTCPYCRRAQEILSQLPIKQGLLEfVDITAtnHTNEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSMQQSG 93
Cdd:cd03419    1 PVVVFSKSYCPYCKRAKSLLKELGVKPAVVE-LDQHE--DGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSG 77

                 ...
gi 402872120  94 ELL 96
Cdd:cd03419   78 KLV 80
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
15-99 2.66e-43

Glutaredoxin; 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 model represents eukaryotic glutaredoxins and includes sequences from fungi, plants and metazoans as well as viruses.


Pssm-ID: 233765  Cd Length: 84  Bit Score: 138.15  E-value: 2.66e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402872120   15 VVVFIKPTCPYCRRAQEILSQLPIKQGLlEFVDITATNHTNEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSMQQSGE 94
Cdd:TIGR02180   1 VVVFSKSYCPYCKKAKEILAKLNVKPAY-EVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKSGK 79

                  ....*
gi 402872120   95 LLTRL 99
Cdd:TIGR02180  80 LAELL 84
PHA03050 PHA03050
glutaredoxin; Provisional
1-106 1.34e-28

glutaredoxin; Provisional


Pssm-ID: 165343  Cd Length: 108  Bit Score: 101.25  E-value: 1.34e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402872120   1 MAQEFVNGKIQPGKVVVFIKPTCPYCRRAQEILSQLPIKQGLLEFVDITATNHTNEIQDYLQQLTGARTVPRVFIGKDCI 80
Cdd:PHA03050   1 MAEEFVQQRLANNKVTIFVKFTCPFCRNALDILNKFSFKRGAYEIVDIKEFKPENELRDYFEQITGGRTVPRIFFGKTSI 80
                         90       100
                 ....*....|....*....|....*.
gi 402872120  81 GGCSDLVSMQQSGELLTRLKQIGALQ 106
Cdd:PHA03050  81 GGYSDLLEIDNMDALGDILSSIGVLR 106
GrxC COG0695
Glutaredoxin and related proteins [Posttranslational modification, protein turnover, ...
14-96 1.42e-17

Glutaredoxin and related proteins [Posttranslational modification, protein turnover, chaperones]


Pssm-ID: 223767  Cd Length: 80  Bit Score: 71.58  E-value: 1.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402872120  14 KVVVFIKPTCPYCRRAQEILSQLPIkqgllEFVDITATNHTN-EIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSMQQS 92
Cdd:COG0695    2 NVTIYTKPGCPYCKRAKRLLDRKGV-----DYEEIDVDDDEPeEAREMVKRGKGQRTVPQIFIGGKHVGGCDDLDALEAK 76

                 ....
gi 402872120  93 GELL 96
Cdd:COG0695   77 GKLD 80
Glutaredoxin pfam00462
Glutaredoxin;
15-80 5.78e-17

Glutaredoxin;


Pssm-ID: 249878  Cd Length: 60  Bit Score: 69.45  E-value: 5.78e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 402872120   15 VVVFIKPTCPYCRRAQEILSQLPIKqglLEFVDITAtnhTNEIQDYLQQLTGARTVPRVFIGKDCI 80
Cdd:pfam00462   1 VVLFTKPTCPFCKRAKRLLDSLGVK---FEEIDVDE---DPEIREELKELSGWRTVPQVFIGGEHI 60
grxA PRK11200
glutaredoxin 1; Provisional
14-85 4.68e-11

glutaredoxin 1; Provisional


Pssm-ID: 183036  Cd Length: 85  Bit Score: 54.27  E-value: 4.68e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 402872120  14 KVVVFIKPTCPYCRRAQEILSQLPIKQGLLEF--VDITATNHTNEiqDyLQQLTG--ARTVPRVFIGKDCIGGCSD 85
Cdd:PRK11200   2 FVVIFGRPGCPYCVRAKELAEKLSEERDDFDYryVDIHAEGISKA--D-LEKTVGkpVETVPQIFVDQKHIGGCTD 74
PRK12759 PRK12759
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional
14-100 4.24e-05

bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional


Pssm-ID: 139206 [Multi-domain]  Cd Length: 410  Bit Score: 39.62  E-value: 4.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402872120  14 KVVVFIKPTCPYCRRAQEIL--SQLPIKQGLLEfVDITATNHTNEI-QDYLQQLTGARTVPRVFIGKDCIGGCSDLvsMQ 90
Cdd:PRK12759   3 EVRIYTKTNCPFCDLAKSWFgaNDIPFTQISLD-DDVKRAEFYAEVnKNILLVEEHIRTVPQIFVGDVHIGGYDNL--MA 79
                         90
                 ....*....|
gi 402872120  91 QSGELLTRLK 100
Cdd:PRK12759  80 RAGEVIARVK 89
 
Name Accession Description Interval E-value
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
14-96 9.92e-36

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  Cd Length: 82  Bit Score: 118.80  E-value: 9.92e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402872120  14 KVVVFIKPTCPYCRRAQEILSQLPIKQGLLEfVDITAtnHTNEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSMQQSG 93
Cdd:cd03419    1 PVVVFSKSYCPYCKRAKSLLKELGVKPAVVE-LDQHE--DGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSG 77

                 ...
gi 402872120  94 ELL 96
Cdd:cd03419   78 KLV 80
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
15-99 2.66e-43

Glutaredoxin; 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 model represents eukaryotic glutaredoxins and includes sequences from fungi, plants and metazoans as well as viruses.


Pssm-ID: 233765  Cd Length: 84  Bit Score: 138.15  E-value: 2.66e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402872120   15 VVVFIKPTCPYCRRAQEILSQLPIKQGLlEFVDITATNHTNEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSMQQSGE 94
Cdd:TIGR02180   1 VVVFSKSYCPYCKKAKEILAKLNVKPAY-EVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKSGK 79

                  ....*
gi 402872120   95 LLTRL 99
Cdd:TIGR02180  80 LAELL 84
PHA03050 PHA03050
glutaredoxin; Provisional
1-106 1.34e-28

glutaredoxin; Provisional


Pssm-ID: 165343  Cd Length: 108  Bit Score: 101.25  E-value: 1.34e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402872120   1 MAQEFVNGKIQPGKVVVFIKPTCPYCRRAQEILSQLPIKQGLLEFVDITATNHTNEIQDYLQQLTGARTVPRVFIGKDCI 80
Cdd:PHA03050   1 MAEEFVQQRLANNKVTIFVKFTCPFCRNALDILNKFSFKRGAYEIVDIKEFKPENELRDYFEQITGGRTVPRIFFGKTSI 80
                         90       100
                 ....*....|....*....|....*.
gi 402872120  81 GGCSDLVSMQQSGELLTRLKQIGALQ 106
Cdd:PHA03050  81 GGYSDLLEIDNMDALGDILSSIGVLR 106
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
14-91 2.63e-24

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  Cd Length: 72  Bit Score: 89.06  E-value: 2.63e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 402872120  14 KVVVFIKPTCPYCRRAQEILSQLPIKqglLEFVDITATNhtnEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSMQQ 91
Cdd:cd02066    1 KVVVFSKSTCPYCKRAKRLLESLGIE---FEEIDILEDG---ELREELKELSGWPTVPQIFINGEFIGGYDDLKALHE 72
GrxC COG0695
Glutaredoxin and related proteins [Posttranslational modification, protein turnover, ...
14-96 1.42e-17

Glutaredoxin and related proteins [Posttranslational modification, protein turnover, chaperones]


Pssm-ID: 223767  Cd Length: 80  Bit Score: 71.58  E-value: 1.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402872120  14 KVVVFIKPTCPYCRRAQEILSQLPIkqgllEFVDITATNHTN-EIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSMQQS 92
Cdd:COG0695    2 NVTIYTKPGCPYCKRAKRLLDRKGV-----DYEEIDVDDDEPeEAREMVKRGKGQRTVPQIFIGGKHVGGCDDLDALEAK 76

                 ....
gi 402872120  93 GELL 96
Cdd:COG0695   77 GKLD 80
Glutaredoxin pfam00462
Glutaredoxin;
15-80 5.78e-17

Glutaredoxin;


Pssm-ID: 249878  Cd Length: 60  Bit Score: 69.45  E-value: 5.78e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 402872120   15 VVVFIKPTCPYCRRAQEILSQLPIKqglLEFVDITAtnhTNEIQDYLQQLTGARTVPRVFIGKDCI 80
Cdd:pfam00462   1 VVLFTKPTCPFCKRAKRLLDSLGVK---FEEIDVDE---DPEIREELKELSGWRTVPQVFIGGEHI 60
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
15-95 7.06e-17

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: 233766  Cd Length: 79  Bit Score: 69.98  E-value: 7.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402872120   15 VVVFIKPTCPYCRRAQEILSQlpikQGLlEFVDITATNHTNEiQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSMQQSGE 94
Cdd:TIGR02181   1 VTIYTKPYCPYCTRAKALLSS----KGV-TFTEIRVDGDPAL-RDEMMQRSGRRTVPQIFIGDVHVGGCDDLYALDREGK 74

                  .
gi 402872120   95 L 95
Cdd:TIGR02181  75 L 75
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
14-93 1.22e-15

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  Cd Length: 75  Bit Score: 66.46  E-value: 1.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402872120  14 KVVVFIKPTCPYCRRAQEILSqlpiKQGLlEFVDITATNHTNEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSMQQSG 93
Cdd:cd03418    1 KVEIYTKPNCPYCVRAKALLD----KKGV-DYEEIDVDGDPALREEMINRSGGRRTVPQIFIGDVHIGGCDDLYALERKG 75
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
15-105 9.88e-13

Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to plants. Multiple isoforms are found in A. thaliana and O.sativa.


Pssm-ID: 233771  Cd Length: 99  Bit Score: 59.39  E-value: 9.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402872120   15 VVVFIKPTCPYCRRAQEILSQLPIKQGLLEFVDITATNhtnEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSMQQSGE 94
Cdd:TIGR02189  10 VVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPAGK---DIENALSRLGCSPAVPAVFVGGKLVGGLENVMALHISGS 86
                          90
                  ....*....|.
gi 402872120   95 LLTRLKQIGAL 105
Cdd:TIGR02189  87 LVPMLKQAGAL 97
GlrX-dom TIGR02190
Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to ...
12-86 4.69e-12

Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to an N-terminal peroxiredoxin-like domain.


Pssm-ID: 131245  Cd Length: 79  Bit Score: 57.16  E-value: 4.69e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 402872120   12 PGKVVVFIKPTCPYCRRAQEILsqlpiKQGLLEFVDITATNHTNEIQdyLQQLTGARTVPRVFIGKDCIGGCSDL 86
Cdd:TIGR02190   7 PESVVVFTKPGCPFCAKAKATL-----KEKGYDFEEIPLGNDARGRS--LRAVTGATTVPQVFIGGKLIGGSDEL 74
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
15-86 8.48e-12

Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing peroxiredoxin (PRX) and GRX domains, which is found in some pathogenic bacteria and cyanobacteria. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins. PRX-GRX hybrid proteins from Haemophilus influenza and Neisseria meningitis exhibit GSH-dependent peroxidase activity. The flow of reducing equivalents in the catalytic cycle of the hybrid protein goes from NADPH -> GSH reductase -> GSH -> GRX domain of hybrid -> PRX domain of hybrid -> peroxide substrate.


Pssm-ID: 239327  Cd Length: 72  Bit Score: 55.98  E-value: 8.48e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 402872120  15 VVVFIKPTCPYCRRAQEILSQlpikQGLlEFVDITATNHTNEIQdyLQQLTGARTVPRVFIGKDCIGGCSDL 86
Cdd:cd03029    3 VSLFTKPGCPFCARAKAALQE----NGI-SYEEIPLGKDITGRS--LRAVTGAMTVPQVFIDGELIGGSDDL 67
grxA PRK11200
glutaredoxin 1; Provisional
14-85 4.68e-11

glutaredoxin 1; Provisional


Pssm-ID: 183036  Cd Length: 85  Bit Score: 54.27  E-value: 4.68e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 402872120  14 KVVVFIKPTCPYCRRAQEILSQLPIKQGLLEF--VDITATNHTNEiqDyLQQLTG--ARTVPRVFIGKDCIGGCSD 85
Cdd:PRK11200   2 FVVIFGRPGCPYCVRAKELAEKLSEERDDFDYryVDIHAEGISKA--D-LEKTVGkpVETVPQIFVDQKHIGGCTD 74
COG0278 COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones]
4-103 2.09e-10

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


Pssm-ID: 223355  Cd Length: 105  Bit Score: 52.67  E-value: 2.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402872120   4 EFVNGKIQPGKVVVFIK-----PTCPYCRRAQEILSQLPIKQglLEFVDITATNhtnEIQDYLQQLTGARTVPRVFIGKD 78
Cdd:COG0278    6 DRIQKQIKENPVVLFMKgtpefPQCGFSAQAVQILSACGVVD--FAYVDVLQDP---EIRQGLKEYSNWPTFPQLYVNGE 80
                         90       100
                 ....*....|....*....|....*
gi 402872120  79 CIGGCSDLVSMQQSGELLTRLKQIG 103
Cdd:COG0278   81 FVGGCDIVREMYQSGELQTLLKEAG 105
PRK10638 PRK10638
glutaredoxin 3; Provisional
14-100 6.07e-10

glutaredoxin 3; Provisional


Pssm-ID: 182607  Cd Length: 83  Bit Score: 51.36  E-value: 6.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402872120  14 KVVVFIKPTCPYCRRAQEILSQlpikQGLlEFVDItATNHTNEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSMQQSG 93
Cdd:PRK10638   3 NVEIYTKATCPFCHRAKALLNS----KGV-SFQEI-PIDGDAAKREEMIKRSGRTTVPQIFIDAQHIGGCDDLYALDARG 76

                 ....*..
gi 402872120  94 ELLTRLK 100
Cdd:PRK10638  77 GLDPLLK 83
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
14-78 6.38e-09

NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active CXXC motif within a TRX fold, characterized by a glutaredoxin (GRX)-like sequence and TRX-like activity profile. In vitro, it displays protein disulfide reductase activity that is dependent on TRX reductase, not glutathione (GSH). It is part of the NrdHIEF operon, where NrdEF codes for class Ib ribonucleotide reductase (RNR-Ib), an efficient enzyme at low oxygen levels. Under these conditions when GSH is mostly conjugated to spermidine, NrdH can still function and act as a hydrogen donor for RNR-Ib. It has been suggested that the NrdHEF system may be the oldest RNR reducing system, capable of functioning in a microaerophilic environment, where GSH was not yet available. NrdH from Corynebacterium ammoniagenes can form domain-swapped dimers, although it is unknown if this happens in vivo. Domain-swapped dimerization, which results in the blocking of the TRX reductase binding site, could be a mechanism for regulating the oxidation state of the protein.


Pssm-ID: 239274  Cd Length: 73  Bit Score: 47.99  E-value: 6.38e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 402872120  14 KVVVFIKPTCPYCRRAQEILSQLPIkqgllEFVDITATNHTNEIqDYLQQLTGARTVPRVFIGKD 78
Cdd:cd02976    1 EVTVYTKPDCPYCKATKRFLDERGI-----PFEEVDVDEDPEAL-EELKKLNGYRSVPVVVIGDE 59
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
10-95 7.87e-09

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: 48.26  E-value: 7.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402872120  10 IQPGKVVVFIK-----PTCPYCRRAQEILSQLPIKqglLEFVDITATNhtnEIQDYLQQLTGARTVPRVFIGKDCIGGCS 84
Cdd:cd03028    5 IKENPVVLFMKgtpeePRCGFSRKVVQILNQLGVD---FGTFDILEDE---EVRQGLKEYSNWPTFPQLYVNGELVGGCD 78
                         90
                 ....*....|.
gi 402872120  85 DLVSMQQSGEL 95
Cdd:cd03028   79 IVKEMHESGEL 89
GRX_DEP cd03027
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ...
13-89 2.84e-08

Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of uncharacterized proteins containing a GRX domain and additional domains DEP and DUF547, both of which have unknown functions. GRX is a glutathione (GSH) dependent reductase containing a redox active CXXC motif in a TRX fold. It has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. By altering the redox state of target proteins, GRX is involved in many cellular functions.


Pssm-ID: 239325  Cd Length: 73  Bit Score: 46.25  E-value: 2.84e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 402872120  13 GKVVVFIKPTCPYCRRAQEILSQLPIKqglleFVDITATNHTnEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSM 89
Cdd:cd03027    1 GRVTIYSRLGCEDCTAVRLFLREKGLP-----YVEINIDIFP-ERKAELEERTGSSVVPQIFFNEKLVGGLTDLKSL 71
GRXA TIGR02183
Glutaredoxin, GrxA family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
15-85 2.91e-08

Glutaredoxin, GrxA 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 model includes the E. coli glyutaredoxin GrxA which appears to have primary responsibility for the reduction of ribonucleotide reductase.


Pssm-ID: 131238  Cd Length: 86  Bit Score: 46.36  E-value: 2.91e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 402872120   15 VVVFIKPTCPYCRRAQEILSQLPIKQGLLEF--VDITATNHTNEiqdYLQQLTG--ARTVPRVFIGKDCIGGCSD 85
Cdd:TIGR02183   2 VVIFGRPGCPYCVRAKQLAEKLAIERADFEFryIDIHAEGISKA---DLEKTVGkpVETVPQIFVDEKHVGGCTD 73
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
14-82 5.10e-08

Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the conserved CxxC motif and includes the Clostridium pasteurianum protein YruB which has been cloned from a rubredoxin operon. Somewhat related to NrdH, it is unknown whether this protein actually interacts with glutathione/glutathione reducatase, or, like NrdH, some other reductant system.


Pssm-ID: 131251  Cd Length: 74  Bit Score: 45.45  E-value: 5.10e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 402872120   14 KVVVFIKPTCPYCRRAQEILSQLPIKqglLEFVDITAtnhTNEIQDYLQQLTGARTVPRVFIGKDCIGG 82
Cdd:TIGR02196   1 KVKVYTTPWCPPCKKAKEYLTSKGIA---FEEIDVEK---DSAAREEVLKVLGQRGVPVIVIGHKIIVG 63
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
15-81 4.29e-07

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  Cd Length: 69  Bit Score: 43.07  E-value: 4.29e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 402872120  15 VVVFIKPTCPYCRRAQEILSQLPIKQGLLEFVDITATNHTNEIQDYLQQltGARTVPRVFIGKDCIG 81
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELALLNKGVKFEAVDVDEDPALEKELKRY--GVGGVPTLVVFGPGIG 65
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
14-106 5.30e-06

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  Cd Length: 147  Bit Score: 41.07  E-value: 5.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402872120  14 KVVVF------IKPTCPYCRRAQEILSQLPIKqgllefVDITATNHTNEIQDYLQQLTGAR----TVPRVFIGKDCIGGC 83
Cdd:cd03031    1 RVVLYttslrgVRKTFEDCNNVRAILESFRVK------FDERDVSMDSGFREELRELLGAElkavSLPRVFVDGRYLGGA 74
                         90       100
                 ....*....|....*....|...
gi 402872120  84 SDLVSMQQSGELLTRLKQIGALQ 106
Cdd:cd03031   75 EEVLRLNESGELRKLLKGIRARA 97
TIGR00365 TIGR00365
monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. ...
3-99 6.42e-06

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: 39.76  E-value: 6.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402872120    3 QEFVNGKIQPGKVVVFIK-----PTCPYCRRAQEILSQLPIKqglLEFVDITATNhtnEIQDYLQQLTGARTVPRVFIGK 77
Cdd:TIGR00365   2 IERIKEQIAENPVVLYMKgtpqfPQCGFSARAVQILNACGVP---FAYVNVLEDP---EIRQGIKEYSNWPTIPQLYVKG 75
                          90       100
                  ....*....|....*....|..
gi 402872120   78 DCIGGCSDLVSMQQSGELLTRL 99
Cdd:TIGR00365  76 EFVGGCDIIMEMYQSGELQTLL 97
TrxA COG0526
Thiol-disulfide isomerase and thioredoxins [Posttranslational modification, protein turnover, ...
15-78 2.04e-04

Thiol-disulfide isomerase and thioredoxins [Posttranslational modification, protein turnover, chaperones / Energy production and conversion]


Pssm-ID: 223600  Cd Length: 127  Bit Score: 36.42  E-value: 2.04e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 402872120  15 VVVFIKPTCPYCRRAQEILSQLPIK-QGLLEFVDITATNHTNEIQDYLQQLtgARTVPRVFIGKD 78
Cdd:COG0526   36 LVDFWAPWCPPCRAEAPLLEELAEEyGGDVEVVAVNVDDENPDLAAEFGVA--VRSIPTLLLFKD 98
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
21-87 2.48e-04

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 257742  Cd Length: 75  Bit Score: 35.23  E-value: 2.48e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 402872120   21 PTCPYCRRAQEIL--SQLPIkqgllEFVDITATNHTNEiqdyLQQLTGARTVPRVFIGKDCIGGCSDLV 87
Cdd:pfam13417   5 PTSPYARKVRLALreKGLPY-----EEVEVDPGDKPPE----LLALNPLGKVPVLVDDGEVLTDSLAII 64
DsbA_DsbC_DsbG cd03020
DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ...
12-36 4.69e-04

DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active CXXC motif imbedded in a TRX fold. They function as protein disulfide isomerases and chaperones in the bacterial periplasm to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins. DsbC and DsbG are kept in their reduced state by the cytoplasmic membrane protein DsbD, which utilizes the TRX/TRX reductase system in the cytosol as a source of reducing equivalents. DsbG differ from DsbC in that it has a more limited substrate specificity, and it may preferentially act later in the folding process to catalyze disulfide rearrangements in folded or partially folded proteins. Also included in the alignment is the predicted protein TrbB, whose gene was sequenced from the enterohemorrhagic E. coli type IV pilus gene cluster, which is required for efficient plasmid transfer.


Pssm-ID: 239318 [Multi-domain]  Cd Length: 197  Bit Score: 36.14  E-value: 4.69e-04
                         10        20
                 ....*....|....*....|....*
gi 402872120  12 PGKVVVFIKPTCPYCRRAQEILSQL 36
Cdd:cd03020   78 KRVVYVFTDPDCPYCRKLEKELKPN 102
DUF836 pfam05768
Glutaredoxin-like domain (DUF836); These proteins are related to the pfam00462 family.
14-49 5.12e-04

Glutaredoxin-like domain (DUF836); These proteins are related to the pfam00462 family.


Pssm-ID: 253377  Cd Length: 76  Bit Score: 34.51  E-value: 5.12e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 402872120   14 KVVVFIKPTCPYCRRAQEILSQLPIKQGL-LEFVDIT 49
Cdd:pfam05768   1 TLTLYGKPGCHLCEGAKEVLAELEAALGFdLERIDID 37
Thioredoxin_4 pfam13462
Thioredoxin;
12-46 5.42e-04

Thioredoxin;


Pssm-ID: 257786  Cd Length: 168  Bit Score: 35.78  E-value: 5.42e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 402872120   12 PGKVVVFIKPTCPYCRRAQEILSQLP---IKQGLLEFV 46
Cdd:pfam13462  14 PVTVIEYADFTCPHCARFHEEVKKLLakyIDTGKVKFI 51
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
7-40 2.19e-03

Thioredoxin-like domain;


Pssm-ID: 257499  Cd Length: 102  Bit Score: 33.17  E-value: 2.19e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 402872120    7 NGKIqpgKVVVFIKPTCPYCRRAQEILSQLPIKQ 40
Cdd:pfam13098   4 NGKP---VLVVFTDPDCPYCKKLHKELLKDDVQD 34
GlrX_actino TIGR02200
Glutaredoxin-like protein; This family of glutaredoxin-like proteins is limited to the ...
14-73 2.55e-03

Glutaredoxin-like protein; This family of glutaredoxin-like proteins is limited to the Actinobacteria and contains the conserved CxxC motif.


Pssm-ID: 131255  Cd Length: 77  Bit Score: 32.51  E-value: 2.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 402872120   14 KVVVFIKPTCPYCRRAQEILSQLPIKqglLEFVDItatNHTNEIQDYLQQLT-GARTVPRV 73
Cdd:TIGR02200   1 TITVYGTTWCGYCAQLMRTLDKLGAA---YEWVDI---EEDEGAADRVVSVNnGNMTVPTV 55
redox_disulf_1 TIGR00411
small redox-active disulfide protein 1; This protein is homologous to a family of proteins ...
14-78 3.08e-03

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


Pssm-ID: 129505  Cd Length: 82  Bit Score: 32.55  E-value: 3.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 402872120   14 KVVVFIKPTCPYCRRAQEILSQLPIKQGLLefVDITATNHTNEIQDYLQqlTGARTVPRVFIGKD 78
Cdd:TIGR00411   2 KIELFTSPTCPYCPAAKRVVEEVAKEMGDA--VEVEYINVMENPQKAME--YGIMAVPAIVINGD 62
TRX_GRX_like cd02973
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins ...
14-75 3.50e-03

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


Pssm-ID: 239271  Cd Length: 67  Bit Score: 32.16  E-value: 3.50e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 402872120  14 KVVVFIKPTCPYCRRAQEILSQLPIKQGLLEFVDITATNHTNEIQDYlqqltGARTVPRVFI 75
Cdd:cd02973    2 NIEVFVSPTCPYCPDAVQAANRIAALNPNISAEMIDAAEFPDLADEY-----GVMSVPAIVI 58
PRK10824 PRK10824
glutaredoxin-4; Provisional
21-104 4.01e-03

glutaredoxin-4; Provisional


Pssm-ID: 182759  Cd Length: 115  Bit Score: 32.95  E-value: 4.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402872120  21 PTCPYCRRAQEILSQLPIKqglLEFVDITatnHTNEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSMQQSGELLTRLK 100
Cdd:PRK10824  28 PSCGFSAQAVQALSACGER---FAYVDIL---QNPDIRAELPKYANWPTFPQLWVDGELVGGCDIVIEMYQRGELQQLIK 101

                 ....
gi 402872120 101 QIGA 104
Cdd:PRK10824 102 ETAA 105
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
15-36 5.25e-03

DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) S-transferase kappa (GSTK), 2-hydroxychromene-2-carboxylate (HCCA) isomerase, an oxidoreductase (FrnE) presumed to be involved in frenolicin biosynthesis, a 27-kDa outer membrane protein, and similar proteins. Members of this family contain a redox active CXXC motif (except GSTK and HCCA isomerase) imbedded in a TRX fold, and an alpha helical insert of about 75 residues (shorter in DsbC and DsbG) relative to TRX. DsbA is involved in the oxidative protein folding pathway in prokaryotes, catalyzing disulfide bond formation of proteins secreted into the bacterial periplasm. DsbC and DsbG function as protein disulfide isomerases and chaperones to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins.


Pssm-ID: 239270  Cd Length: 98  Bit Score: 32.38  E-value: 5.25e-03
                         10        20
                 ....*....|....*....|..
gi 402872120  15 VVVFIKPTCPYCRRAQEILSQL 36
Cdd:cd02972    1 IVEFFDPLCPYCYLFEPELEKL 22
PRK12759 PRK12759
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional
14-100 4.24e-05

bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional


Pssm-ID: 139206 [Multi-domain]  Cd Length: 410  Bit Score: 39.62  E-value: 4.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402872120  14 KVVVFIKPTCPYCRRAQEIL--SQLPIKQGLLEfVDITATNHTNEI-QDYLQQLTGARTVPRVFIGKDCIGGCSDLvsMQ 90
Cdd:PRK12759   3 EVRIYTKTNCPFCDLAKSWFgaNDIPFTQISLD-DDVKRAEFYAEVnKNILLVEEHIRTVPQIFVGDVHIGGYDNL--MA 79
                         90
                 ....*....|
gi 402872120  91 QSGELLTRLK 100
Cdd:PRK12759  80 RAGEVIARVK 89
dsbG PRK11657
disulfide isomerase/thiol-disulfide oxidase; Provisional
12-28 4.89e-03

disulfide isomerase/thiol-disulfide oxidase; Provisional


Pssm-ID: 183262 [Multi-domain]  Cd Length: 251  Bit Score: 33.40  E-value: 4.89e-03
                         10
                 ....*....|....*..
gi 402872120  12 PGKVVVFIKPTCPYCRR 28
Cdd:PRK11657 118 PRIVYVFADPNCPYCKQ 134
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.12
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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