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Conserved domains on  [gi|489744298|ref|WP_003648332|]
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MULTISPECIES: thioredoxin family protein [Lactobacillus]

Protein Classification

thioredoxin family protein( domain architecture ID 10121244)

thioredoxin family protein may function as a thiol disulfide reductase that catalyzes the reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

CATH:  3.40.30.10
EC:  1.8.-.-
Gene Ontology:  GO:0015035
PubMed:  11441809|15558583|12074972|30367780

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 13-103 1.24e-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: 94.16  E-value: 1.24e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298  13 KEITKNGKVVLLFSAAWCPDCRFLDPFLPQIEKDNSDAKFYKVDRDGSVDVAKELNIFGIPSFVVYQDGKEIGRLVNKDr 92
Cdd:cd02947    5 ELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVVGAD- 83

                         90
                 ....*....|.
gi 489744298  93 kTKEEVENFLN 103
Cdd:cd02947   84 -PKEELEEFLE 93
 
Name Accession Description Interval E-value
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 13-103 1.24e-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: 94.16  E-value: 1.24e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298  13 KEITKNGKVVLLFSAAWCPDCRFLDPFLPQIEKDNSDAKFYKVDRDGSVDVAKELNIFGIPSFVVYQDGKEIGRLVNKDr 92
Cdd:cd02947    5 ELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVVGAD- 83

                         90
                 ....*....|.
gi 489744298  93 kTKEEVENFLN 103
Cdd:cd02947   84 -PKEELEEFLE 93
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 4-105 5.27e-24

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: 87.57  E-value: 5.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298   4 IKELTSEKLKE--ITKNGKVVLLFSAAWCPDCRFLDPFLPQIEKDNSD-AKFYKVDRDGSVDVAKELNIFGIPSFVVYQD 80
Cdd:COG3118    2 VVELTDENFEEevLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGkVKFVKVDVDENPELAAQFGVRSIPTLLLFKD 81

                         90       100
                 ....*....|....*....|....*
gi 489744298  81 GKEIGRLVNKdrKTKEEVENFLNSL 105
Cdd:COG3118   82 GQPVDRFVGA--LPKEQLREFLDKV 104
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 3-104 2.75e-13

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: 60.32  E-value: 2.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298    3 EIKELTSEKLKEITKNGK--VVLLFSAAWCPDCRFLDPFLPQIEKDNS-DAKFYKVDRDGSVDVAKELNIFGIPSFVVYQ 79
Cdd:pfam00085   1 VVVVLTDANFDEVVQKSSkpVLVDFYAPWCGPCKMLAPEYEELAQEYKgNVVFAKVDVDENPDLASKYGVRGYPTLIFFK 80

                          90       100
                  ....*....|....*....|....*
gi 489744298   80 DGKEIGRLVNkdRKTKEEVENFLNS 104
Cdd:pfam00085  81 NGQPVDDYVG--ARPKDALAAFLKA 103
PTZ00051 PTZ00051
thioredoxin; Provisional
 4-92 2.59e-11

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 55.27  E-value: 2.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298   4 IKELTSEKL--KEITKNGKVVLLFSAAWCPDCRFLDPFLPQIEKDNSDAKFYKVDRDGSVDVAKELNIFGIPSFVVYQDG 81
Cdd:PTZ00051   2 VHIVTSQAEfeSTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDELSEVAEKENITSMPTFKVFKNG 81

                         90
                 ....*....|...
gi 489744298  82 KEIGRLV--NKDR 92
Cdd:PTZ00051  82 SVVDTLLgaNDEA 94
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 2-82 1.10e-04

protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs).


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 39.66  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298    2 EEIKELTSEKLKEITKNGKVVLL-FSAAWCPDCRFLDP----FLPQIEKDNSDAKFYKVDRDGSVDVAKELNIFGIPSFV 76
Cdd:TIGR01130   1 EDVLVLTKDNFDDFIKSHEFVLVeFYAPWCGHCKSLAPeyekAADELKKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLK 80


                  ....*.
gi 489744298   77 VYQDGK 82
Cdd:TIGR01130  81 IFRNGE 86
 
Name Accession Description Interval E-value
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 13-103 1.24e-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: 94.16  E-value: 1.24e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298  13 KEITKNGKVVLLFSAAWCPDCRFLDPFLPQIEKDNSDAKFYKVDRDGSVDVAKELNIFGIPSFVVYQDGKEIGRLVNKDr 92
Cdd:cd02947    5 ELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVVGAD- 83

                         90
                 ....*....|.
gi 489744298  93 kTKEEVENFLN 103
Cdd:cd02947   84 -PKEELEEFLE 93
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 4-105 5.27e-24

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: 87.57  E-value: 5.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298   4 IKELTSEKLKE--ITKNGKVVLLFSAAWCPDCRFLDPFLPQIEKDNSD-AKFYKVDRDGSVDVAKELNIFGIPSFVVYQD 80
Cdd:COG3118    2 VVELTDENFEEevLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGkVKFVKVDVDENPELAAQFGVRSIPTLLLFKD 81

                         90       100
                 ....*....|....*....|....*
gi 489744298  81 GKEIGRLVNKdrKTKEEVENFLNSL 105
Cdd:COG3118   82 GQPVDRFVGA--LPKEQLREFLDKV 104
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 5-105 1.45e-16

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 69.72  E-value: 1.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298   5 KELTSEKLKeitknGKVVLL-FSAAWCPDCRFLDPFLPQIEKDNSDAKFYKVDRDGSVD--------------------- 62
Cdd:COG0526   19 KPLSLADLK-----GKPVLVnFWATWCPPCRAEMPVLKELAEEYGGVVFVGVDVDENPEavkaflkelglpypvlldpdg 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489744298  63 -VAKELNIFGIPSFVVY-QDGKEIGRLVNkdRKTKEEVENFLNSL 105
Cdd:COG0526   94 eLAKAYGVRGIPTTVLIdKDGKIVARHVG--PLSPEELEEALEKL 136
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 3-104 2.75e-13

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: 60.32  E-value: 2.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298    3 EIKELTSEKLKEITKNGK--VVLLFSAAWCPDCRFLDPFLPQIEKDNS-DAKFYKVDRDGSVDVAKELNIFGIPSFVVYQ 79
Cdd:pfam00085   1 VVVVLTDANFDEVVQKSSkpVLVDFYAPWCGPCKMLAPEYEELAQEYKgNVVFAKVDVDENPDLASKYGVRGYPTLIFFK 80

                          90       100
                  ....*....|....*....|....*
gi 489744298   80 DGKEIGRLVNkdRKTKEEVENFLNS 104
Cdd:pfam00085  81 NGQPVDDYVG--ARPKDALAAFLKA 103
PTZ00051 PTZ00051
thioredoxin; Provisional
 4-92 2.59e-11

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 55.27  E-value: 2.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298   4 IKELTSEKL--KEITKNGKVVLLFSAAWCPDCRFLDPFLPQIEKDNSDAKFYKVDRDGSVDVAKELNIFGIPSFVVYQDG 81
Cdd:PTZ00051   2 VHIVTSQAEfeSTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDELSEVAEKENITSMPTFKVFKNG 81

                         90
                 ....*....|...
gi 489744298  82 KEIGRLV--NKDR 92
Cdd:PTZ00051  82 SVVDTLLgaNDEA 94
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 2-87 3.78e-09

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: 49.58  E-value: 3.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298   2 EEIKELTSEKLKEITkngkvVLLFSAAWCPDCRFLDPFLPQIEKD-NSDAKFYKVDRDGSVDVAKELNIFGIPSFVVYQD 80
Cdd:cd02984    3 EEFEELLKSDASKLL-----VLHFWAPWAEPCKQMNQVFEELAKEaFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRN 77


                 ....*..
gi 489744298  81 GKEIGRL 87
Cdd:cd02984   78 GTIVDRV 84
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 2-84 1.21e-08

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 50.90  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298   2 EEIKELTSEKL-KEITKNGKVVLLFSAAWCPDCRFLDP----FLPQIEKDNSDAKFYKVDRDGSVDVAKELNIFGIPSFV 76
Cdd:PTZ00102  32 EHVTVLTDSTFdKFITENEIVLVKFYAPWCGHCKRLAPeykkAAKMLKEKKSEIVLASVDATEEMELAQEFGVRGYPTIK 111


                 ....*...
gi 489744298  77 VYQDGKEI 84
Cdd:PTZ00102 112 FFNKGNPV 119
DsbD COG4232
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ...
 10-106 1.44e-08

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


Pssm-ID: 443376 [Multi-domain]  Cd Length: 416  Bit Score: 50.57  E-value: 1.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298  10 EKLKEITKNGKVVLL-FSAAWCPDCRFLDPFL---PQIEKD-NSDAKFYKVD--RDGSVDVA--KELNIFGIPSFVVY-Q 79
Cdd:COG4232  311 AALAEARAEGKPVFVdFTADWCVTCKENERTVfsdPEVQAAlADDVVLLKADvtDNDPEITAllKRFGRFGVPTYVFYdP 390

                         90       100
                 ....*....|....*....|....*..
gi 489744298  80 DGKEIGRLVNKdrKTKEEVENFLNSLK 106
Cdd:COG4232  391 DGEELPRLGFM--LTADEFLAALEKAK 415
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 9-88 1.48e-07

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 46.44  E-value: 1.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298   9 SEKLKEITKNGK-VVLLFSAAWCPDCRFLDP-FLPQIE-KDNSDAKFY--KVDRDGSVDV-------------AKELNIF 70
Cdd:COG2143   30 EEDLALAKAEGKpILLFFESDWCPYCKKLHKeVFSDPEvAAYLKENFVvvQLDAEGDKEVtdfdgetltekelARKYGVR 109

                         90
                 ....*....|....*....
gi 489744298  71 GIPSFVVY-QDGKEIGRLV 88
Cdd:COG2143  110 GTPTLVFFdAEGKEIARIP 128
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
 10-88 1.69e-07

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: 45.29  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298  10 EKLKEITKNGKVVLL-FSAAWCPDCR------FLDPflPQIEKDNSDAKFYKVD--RDGSVDVA--KELNIFGIPSFVVY 78
Cdd:cd02953    2 AALAQALAQGKPVFVdFTADWCVTCKvnekvvFSDP--EVQAALKKDVVLLRADwtKNDPEITAllKRFGVFGPPTYLFY 79

                         90
                 ....*....|..
gi 489744298  79 --QDGKEIGRLV 88
Cdd:cd02953   80 gpGGEPEPLRLP 91
Phd_like_TxnDC9 cd02989
Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; ...
 3-102 1.80e-07

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: 45.64  E-value: 1.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298   3 EIKELTSEK--LKEITKNGKVVLLFSAAWCPDCRFLDPFLPQIEKDNSDAKFYKVDRDGSVDVAKELNIFGIPSFVVYQD 80
Cdd:cd02989    5 KYREVSDEKefFEIVKSSERVVCHFYHPEFFRCKIMDKHLEILAKKHLETKFIKVNAEKAPFLVEKLNIKVLPTVILFKN 84

                         90       100
                 ....*....|....*....|....*...
gi 489744298  81 GKEIGRLV------NKDRKTKEEVENFL 102
Cdd:cd02989   85 GKTVDRIVgfeelgGKDDFSTETLEKRL 112
Phd_like cd02957
Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as ...
 3-103 4.18e-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: 44.47  E-value: 4.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298   3 EIKELTSEK-LKEITKNGK---VVLLFSAAWCPDCRFLDPFLPQIEKDNSDAKFYKVDRDGSVdVAKELNIFGIPSFVVY 78
Cdd:cd02957    5 EVREISSKEfLEEVTKASKgtrVVVHFYEPGFPRCKILDSHLEELAAKYPETKFVKINAEKAF-LVNYLDIKVLPTLLVY 83

                         90       100       110
                 ....*....|....*....|....*....|.
gi 489744298  79 QDGKEIGRLV------NKDRKTkEEVENFLN 103
Cdd:cd02957   84 KNGELIDNIVgfeelgGDDFTT-EDLEKFLA 113
TMX2 cd02962
TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related ...
 2-94 1.01e-06

TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related transmembrane protein, identified and characterized through the cloning of its cDNA from a human fetal library. It contains a TRX domain but the redox active CXXC motif is replaced with SXXC. Sequence analysis predicts that TMX2 may be a Type I membrane protein, with its C-terminal half protruding on the luminal side of the endoplasmic reticulum (ER). In addition to the TRX domain, transmembrane region and ER-retention signal, TMX2 also contains a Myb DNA-binding domain repeat signature and a dileucine motif in the tail.


Pssm-ID: 239260 [Multi-domain]  Cd Length: 152  Bit Score: 44.29  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298   2 EEIKELTSEKLK-EITKNGKVVLL--FSAAWCPDCRFLDPFLPQ--IEKDNSDAKFYKVDRDGSVDVAKelnIFGI---- 72
Cdd:cd02962   28 EHIKYFTPKTLEeELERDKRVTWLveFFTTWSPECVNFAPVFAElsLKYNNNNLKFGKIDIGRFPNVAE---KFRVstsp 104

                         90       100
                 ....*....|....*....|....*..
gi 489744298  73 -----PSFVVYQDGKEIGRLVNKDRKT 94
Cdd:cd02962  105 lskqlPTIILFQGGKEVARRPYYNDSK 131
Thioredoxin_9 pfam14595
Thioredoxin;
3-101 1.58e-06

Thioredoxin;


Pssm-ID: 434059 [Multi-domain]  Cd Length: 129  Bit Score: 43.41  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298    3 EIKELTSEKLKEITKNGKVvLLFSAAWCPDCRFLDPFLPQIEKDNSDAKFYKVDRDGSVDVAKELNIFG---IPSFVVY- 78
Cdd:pfam14595  27 ELSEELIEKIKSIEKPLRI-LVITEDWCGDAAQNVPVLAKIAELNPNIELRILLRDENLELMDQYLTGGgraIPTFIFLd 105

                          90       100
                  ....*....|....*....|...
gi 489744298   79 QDGKEIGRLVNKDRKTKEEVENF 101
Cdd:pfam14595 106 EDGEELGVWGPRPKAVQELVDEA 128
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 5-88 7.61e-06

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: 41.45  E-value: 7.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298   5 KELTSEKLKeitknGKVVLL-FSAAWCPDCRFLDPFLPQIEKDNSDAKF-------------------------YKVDRD 58
Cdd:cd02966   10 KPVSLSDLK-----GKVVLVnFWASWCPPCRAEMPELEALAKEYKDDGVevvgvnvddddpaavkaflkkygitFPVLLD 84

                         90       100       110
                 ....*....|....*....|....*....|.
gi 489744298  59 GSVDVAKELNIFGIP-SFVVYQDGKEIGRLV 88
Cdd:cd02966   85 PDGELAKAYGVRGLPtTFLIDRDGRIRARHV 115
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 22-81 1.14e-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: 39.99  E-value: 1.14e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489744298  22 VLLFSAAWCPDCRFLDPFLPQIEKDNSDAKFYKVDRD---GSVDVAKELNIFGIPSFVVYQDG 81
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELALLNKGVKFEAVDVDedpALEKELKRYGVGGVPTLVVFGPG 63
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 18-105 1.71e-05

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


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 40.78  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298  18 NGKVVLL-FSAAWCPDCRFLDPFLPQIE---KDNSDAKFYKVDRDGSVDVAKELNIFGIPSFVVY-QDGKEIGRLVNkdR 92
Cdd:cd02950   19 NGKPTLVeFYADWCTVCQEMAPDVAKLKqkyGDQVNFVMLNVDNPKWLPEIDRYRVDGIPHFVFLdREGNEEGQSIG--L 96

                         90
                 ....*....|...
gi 489744298  93 KTKEEVENFLNSL 105
Cdd:cd02950   97 QPKQVLAQNLDAL 109
PHA02125 PHA02125
thioredoxin-like protein
 21-76 1.92e-05

thioredoxin-like protein


Pssm-ID: 133998 [Multi-domain]  Cd Length: 75  Bit Score: 39.58  E-value: 1.92e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489744298  21 VVLLFSAAWCPDCRFLDPFLPqiekdNSDAKFYKVDRDGSVDVAKELNIFGIPSFV 76
Cdd:PHA02125   1 MIYLFGAEWCANCKMVKPMLA-----NVEYTYVDVDTDEGVELTAKHHIRSLPTLV 51
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
17-88 2.78e-05

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 39.72  E-value: 2.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298   17 KNGK-VVLLFSAAWCPDCRFLDPFLPQIE------KDNSDAKFYKVDRDGSV-----------DVAKELNIFGIPSFVVY 78
Cdd:pfam13098   2 GNGKpVLVVFTDPDCPYCKKLKKELLEDPdvtvylGPNFVFIAVNIWCAKEVakaftdilenkELGRKYGVRGTPTIVFF 81

                          90
                  ....*....|
gi 489744298   79 QDGKEIGRLV 88
Cdd:pfam13098  82 DGKGELLRLP 91
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 3-82 6.40e-05

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


Pssm-ID: 239308 [Multi-domain]  Cd Length: 127  Bit Score: 39.10  E-value: 6.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298   3 EIKELTSEKLKeitknGKVVLL-FSAAWCPDCRFLDPFLPQIE------------KDN-SDAK---------FYKV--DR 57
Cdd:cd03010   14 PDKTLTSADLK-----GKPYLLnVWASWCAPCREEHPVLMALArqgrvpiyginyKDNpENALawlarhgnpYAAVgfDP 88

                         90       100
                 ....*....|....*....|....*.
gi 489744298  58 DGSvdVAKELNIFGIP-SFVVYQDGK 82
Cdd:cd03010   89 DGR--VGIDLGVYGVPeTFLIDGDGI 112
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 5-84 6.49e-05

PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident protein containing three redox active TRX domains. Yeast complementation studies show that ERp46 can substitute for protein disulfide isomerase (PDI) function in vivo. It has been detected in many tissues, however, transcript and protein levels do not correlate in all tissues, suggesting regulation at a posttranscriptional level. An identical protein, named endoPDI, has been identified as an endothelial PDI that is highly expressed in the endothelium of tumors and hypoxic lesions. It has a protective effect on cells exposed to hypoxia.


Pssm-ID: 239303 [Multi-domain]  Cd Length: 102  Bit Score: 38.81  E-value: 6.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298   5 KELTSEKLKEITKNGKVVLLFSAAWCPDCRFLDPFLPQI----EKDNSDAKFYKVDRDGSVDVAKELNIFGIPSFVVYQD 80
Cdd:cd03005    3 LELTEDNFDHHIAEGNHFVKFFAPWCGHCKRLAPTWEQLakkfNNENPSVKIAKVDCTQHRELCSEFQVRGYPTLLLFKD 82


                 ....
gi 489744298  81 GKEI 84
Cdd:cd03005   83 GEKV 86
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 2-82 1.10e-04

protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs).


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 39.66  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298    2 EEIKELTSEKLKEITKNGKVVLL-FSAAWCPDCRFLDP----FLPQIEKDNSDAKFYKVDRDGSVDVAKELNIFGIPSFV 76
Cdd:TIGR01130   1 EDVLVLTKDNFDDFIKSHEFVLVeFYAPWCGHCKSLAPeyekAADELKKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLK 80


                  ....*.
gi 489744298   77 VYQDGK 82
Cdd:TIGR01130  81 IFRNGE 86
PRK10996 PRK10996
thioredoxin 2; Provisional
 3-84 1.24e-04

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 38.51  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298   3 EIKELTSEKLKEITKNGK-VVLLFSAAWCPDCRFLDPFLPQIEKDNSD-AKFYKVDRDGSVDVAKELNIFGIPSFVVYQD 80
Cdd:PRK10996  36 EVINATGETLDKLLQDDLpVVIDFWAPWCGPCRNFAPIFEDVAAERSGkVRFVKVNTEAERELSARFRIRSIPTIMIFKN 115


                 ....
gi 489744298  81 GKEI 84
Cdd:PRK10996 116 GQVV 119
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 8-40 2.24e-04

Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.


Pssm-ID: 239262 [Multi-domain]  Cd Length: 132  Bit Score: 37.59  E-value: 2.24e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 489744298   8 TSEKLKEITKNGKVVLL-FSAAWCPDCRFLDPFL 40
Cdd:cd02964    6 GEGVVPVSALEGKTVGLyFSASWCPPCRAFTPKL 39
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 9-103 3.34e-04

PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX related transmembrane protein containing one redox active TRX domain at the N-terminus and a classical ER retrieval sequence for type I transmembrane proteins at the C-terminus. The TMX3 transcript is found in a variety of tissues with the highest levels detected in skeletal muscle and the heart. In vitro, TMX3 showed oxidase activity albeit slightly lower than that of protein disulfide isomerase.


Pssm-ID: 239298 [Multi-domain]  Cd Length: 104  Bit Score: 36.66  E-value: 3.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298   9 SEKLKEITKNGKVVLLFSAAWCPDCRFLDPFLPQ----IEKDNSDAKFYKVDRDGSVDVAKELNIFGIPSFVVYQDGKEI 84
Cdd:cd03000    6 DDSFKDVRKEDIWLVDFYAPWCGHCKKLEPVWNEvgaeLKSSGSPVRVGKLDATAYSSIASEFGVRGYPTIKLLKGDLAY 85

                         90
                 ....*....|....*....
gi 489744298  85 GRlvnKDRKTKEEVENFLN 103
Cdd:cd03000   86 NY---RGPRTKDDIVEFAN 101
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 18-54 9.64e-04

Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are thioredoxin (TRX)-like protein disulfide oxidoreductases that alter the redox state of target proteins via the reversible oxidation of an active center CXXC motif. TryX is involved in the regulation of oxidative stress in parasitic trypanosomatids by reducing TryX peroxidase, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. TryX derives reducing equivalents from reduced trypanothione, a polyamine peptide conjugate unique to trypanosomatids, which is regenerated by the NADPH-dependent flavoprotein trypanothione reductase. Vertebrate NRX is a 400-amino acid nuclear protein with one redox active TRX domain containing a CPPC active site motif followed by one redox inactive TRX-like domain. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. Plant NRX, longer than the vertebrate NRX by about 100-200 amino acids, is a nuclear protein containing a redox inactive TRX-like domain between two redox active TRX domains. Both vertebrate and plant NRXs show thiol oxidoreductase activity in vitro. Their localization in the nucleus suggests a role in the redox regulation of nuclear proteins such as transcription factors.


Pssm-ID: 239307 [Multi-domain]  Cd Length: 131  Bit Score: 36.11  E-value: 9.64e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 489744298  18 NGKVVLL-FSAAWCPDCRFldpFLPQIekdnsdAKFYK 54
Cdd:cd03009   17 EGKTVGLyFSASWCPPCRA---FTPKL------VEFYE 45
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
19-105 1.17e-03

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 35.61  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298  19 GKVVLL-FSAAWCPDCR----FLDPFLPQIEKD-------NSD-----AKF---YKV------DRDGsvDVAKELNIFGI 72
Cdd:COG1225   21 GKPVVLyFYATWCPGCTaelpELRDLYEEFKDKgvevlgvSSDsdeahKKFaekYGLpfpllsDPDG--EVAKAYGVRGT 98

                         90       100       110
                 ....*....|....*....|....*....|....
gi 489744298  73 PSFVVY-QDGKEIGRLVNKdRKTKEEVENFLNSL 105
Cdd:COG1225   99 PTTFLIdPDGKIRYVWVGP-VDPRPHLEEVLEAL 131
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 21-82 1.21e-03

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: 35.33  E-value: 1.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489744298  21 VVLLFSAAWCPDCRFLDPFLPQI-EKDNSDAKFYKVDRDGSVDVAKELNIFGIPSFVVYQDGK 82
Cdd:cd02956   15 VVVDFWAPRSPPSKELLPLLERLaEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQ 77
trxA PRK09381
thioredoxin TrxA;
15-82 2.94e-03

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 34.27  E-value: 2.94e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489744298  15 ITKNGKVVLLFSAAWCPDCRFLDPFLPQI-EKDNSDAKFYKVDRDGSVDVAKELNIFGIPSFVVYQDGK 82
Cdd:PRK09381  18 LKADGAILVDFWAEWCGPCKMIAPILDEIaDEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGE 86
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 21-96 3.21e-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: 34.01  E-value: 3.21e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489744298  21 VVLLFSAAWCPDCRFLDPFLPQ-IEKDNSDAKFYKVDRDGSVDVAKELNIFGIPSFVVYQDgKEIGRLVNKDRKTKE 96
Cdd:cd02949   16 ILVLYTSPTCGPCRTLKPILNKvIDEFDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKD-KELVKEISGVKMKSE 91
TRX_CDSP32 cd02985
TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed ...
 10-88 7.81e-03

TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed of two TRX domains, a C-terminal TRX domain which contains a redox active CXXC motif and an N-terminal TRX-like domain which contains an SXXS sequence instead of the redox active motif. CDSP32 is a stress-inducible TRX, i.e., it acts as a TRX by reducing protein disulfides and is induced by environmental and oxidative stress conditions. It plays a critical role in plastid defense against oxidative damage, a role related to its function as a physiological electron donor to BAS1, a plastidic 2-cys peroxiredoxin. Plants lacking CDSP32 exhibit decreased photosystem II photochemical efficiencies and chlorophyll retention compared to WT controls, as well as an increased proportion of BAS1 in its overoxidized monomeric form.


Pssm-ID: 239283  Cd Length: 103  Bit Score: 33.23  E-value: 7.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298  10 EKLKEITKNGK---VVLLFSAAWCPDCRFLDPFLPQIEKDNSDAKFYKV---DRDGSVDVAKELNIFGIPSFVVYQDGKE 83
Cdd:cd02985    4 EELDEALKKAKgrlVVLEFALKHSGPSVKIYPTMVKLSRTCNDVVFLLVngdENDSTMELCRREKIIEVPHFLFYKDGEK 83


                 ....*
gi 489744298  84 IGRLV 88
Cdd:cd02985   84 IHEEE 88
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 25-106 8.54e-03

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 33.83  E-value: 8.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489744298  25 FSAAWCPDCRFLDPFLPQIEKD-NSDAKFYKVDRDGSVDVAKELNIFGIPSFVVYQDGKeIGRLVNKDRKTKEEVENFLN 103
Cdd:PTZ00443  59 FYAPWCSHCRKMAPAWERLAKAlKGQVNVADLDATRALNLAKRFAIKGYPTLLLFDKGK-MYQYEGGDRSTEKLAAFALG 137


                 ...
gi 489744298 104 SLK 106
Cdd:PTZ00443 138 DFK 140
 
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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