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Conserved domains on  [gi|351051008|emb|CCD73373|]
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Thioredoxin domain-containing protein [Caenorhabditis elegans]

Protein Classification

thioredoxin family protein( domain architecture ID 11459707)

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
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 7-107 1.79e-14

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: 63.69  E-value: 1.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351051008   7 LTDEDFLQKSEHGiGKKAIYYFYGERCPSCESIKPLFDDLCKKYEKTALVYTYPCYNDDQLTGdAFAVNAVPTFVVMNNG 86
Cdd:COG3118    5 LTDENFEEEVLES-DKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAA-QFGVRSIPTLLLFKDG 82

                         90       100
                 ....*....|....*....|..
gi 351051008  87 EEVTRHVGA-EAEKVQELFEKY 107
Cdd:COG3118   83 QPVDRFVGAlPKEQLREFLDKV 104
 
Name Accession Description Interval E-value
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 7-107 1.79e-14

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: 63.69  E-value: 1.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351051008   7 LTDEDFLQKSEHGiGKKAIYYFYGERCPSCESIKPLFDDLCKKYEKTALVYTYPCYNDDQLTGdAFAVNAVPTFVVMNNG 86
Cdd:COG3118    5 LTDENFEEEVLES-DKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAA-QFGVRSIPTLLLFKDG 82

                         90       100
                 ....*....|....*....|..
gi 351051008  87 EEVTRHVGA-EAEKVQELFEKY 107
Cdd:COG3118   83 QPVDRFVGAlPKEQLREFLDKV 104
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 21-105 2.50e-14

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: 62.96  E-value: 2.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351051008  21 GKKAIYYFYGERCPSCESIKPLFDDLCKKYEKTALVYtypcYNDDQL--TGDAFAVNAVPTFVVMNNGEEVTRHVGA-EA 97
Cdd:cd02947   10 AKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVK----VDVDENpeLAEEYGVRSIPTFLFFKNGKEVDRVVGAdPK 85


                 ....*...
gi 351051008  98 EKVQELFE 105
Cdd:cd02947   86 EELEEFLE 93
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 7-108 4.21e-08

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


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 46.90  E-value: 4.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351051008    7 LTDEDF---LQKSEhgigKKAIYYFYGERCPSCESIKPLFDDLCKKYEKTALVY---TypcyNDDQLTGDAFAVNAVPTF 80
Cdd:TIGR01068   1 LTDANFdetIASSD----KPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVklnV----DENPDIAAKYGIRSIPTL 72

                          90       100
                  ....*....|....*....|....*....
gi 351051008   81 VVMNNGEEVTRHVGA-EAEKVQELFEKYA 108
Cdd:TIGR01068  73 LLFKNGKEVDRSVGAlPKAALKQLINKNL 101
PTZ00051 PTZ00051
thioredoxin; Provisional
 28-103 3.42e-07

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 44.48  E-value: 3.42e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 351051008  28 FYGERCPSCESIKPLFDDLCKKYEKTALVYTypcyNDDQLT--GDAFAVNAVPTFVVMNNGEEVTRHVGAEAEKVQEL 103
Cdd:PTZ00051  25 FYAEWCGPCKRIAPFYEECSKEYTKMVFVKV----DVDELSevAEKENITSMPTFKVFKNGSVVDTLLGANDEALKQL 98
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 6-95 3.54e-06

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: 42.22  E-value: 3.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351051008    6 CLTDEDF---LQKSEhgigKKAIYYFYGERCPSCESIKPLFDDLCKKYEKTALVYtypcyNDD----QLTGDAFAVNAVP 78
Cdd:pfam00085   4 VLTDANFdevVQKSS----KPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFA-----KVDvdenPDLASKYGVRGYP 74

                          90
                  ....*....|....*..
gi 351051008   79 TFVVMNNGEEVTRHVGA 95
Cdd:pfam00085  75 TLIFFKNGQPVDDYVGA 91
 
Name Accession Description Interval E-value
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 7-107 1.79e-14

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: 63.69  E-value: 1.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351051008   7 LTDEDFLQKSEHGiGKKAIYYFYGERCPSCESIKPLFDDLCKKYEKTALVYTYPCYNDDQLTGdAFAVNAVPTFVVMNNG 86
Cdd:COG3118    5 LTDENFEEEVLES-DKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAA-QFGVRSIPTLLLFKDG 82

                         90       100
                 ....*....|....*....|..
gi 351051008  87 EEVTRHVGA-EAEKVQELFEKY 107
Cdd:COG3118   83 QPVDRFVGAlPKEQLREFLDKV 104
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 21-105 2.50e-14

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: 62.96  E-value: 2.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351051008  21 GKKAIYYFYGERCPSCESIKPLFDDLCKKYEKTALVYtypcYNDDQL--TGDAFAVNAVPTFVVMNNGEEVTRHVGA-EA 97
Cdd:cd02947   10 AKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVK----VDVDENpeLAEEYGVRSIPTFLFFKNGKEVDRVVGAdPK 85


                 ....*...
gi 351051008  98 EKVQELFE 105
Cdd:cd02947   86 EELEEFLE 93
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 21-107 5.11e-11

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 55.47  E-value: 5.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351051008  21 GKKAIYYFYGERCPSCESIKPLFDDLCKKYEKTALV-------------------YTYPCYND-DQLTGDAFAVNAVPTF 80
Cdd:COG0526   28 GKPVLVNFWATWCPPCRAEMPVLKELAEEYGGVVFVgvdvdenpeavkaflkelgLPYPVLLDpDGELAKAYGVRGIPTT 107

                         90       100
                 ....*....|....*....|....*....
gi 351051008  81 VVMN-NGEEVTRHVGA-EAEKVQELFEKY 107
Cdd:COG0526  108 VLIDkDGKIVARHVGPlSPEELEEALEKL 136
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 7-108 4.21e-08

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


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 46.90  E-value: 4.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351051008    7 LTDEDF---LQKSEhgigKKAIYYFYGERCPSCESIKPLFDDLCKKYEKTALVY---TypcyNDDQLTGDAFAVNAVPTF 80
Cdd:TIGR01068   1 LTDANFdetIASSD----KPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVklnV----DENPDIAAKYGIRSIPTL 72

                          90       100
                  ....*....|....*....|....*....
gi 351051008   81 VVMNNGEEVTRHVGA-EAEKVQELFEKYA 108
Cdd:TIGR01068  73 LLFKNGKEVDRSVGAlPKAALKQLINKNL 101
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 8-101 4.42e-08

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: 46.88  E-value: 4.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351051008   8 TDEDFLQKSEHGIGKKAIYYFYGERCPSCESIKPLFDDLCKKYEKTALVYTYpcyNDDQLTG--DAFAVNAVPTFVVMNN 85
Cdd:cd02984    1 SEEEFEELLKSDASKLLVLHFWAPWAEPCKQMNQVFEELAKEAFPSVLFLSI---EAEELPEisEKFEITAVPTFVFFRN 77

                         90
                 ....*....|....*.
gi 351051008  86 GEEVTRHVGAEAEKVQ 101
Cdd:cd02984   78 GTIVDRVSGADPKELA 93
PTZ00051 PTZ00051
thioredoxin; Provisional
 28-103 3.42e-07

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 44.48  E-value: 3.42e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 351051008  28 FYGERCPSCESIKPLFDDLCKKYEKTALVYTypcyNDDQLT--GDAFAVNAVPTFVVMNNGEEVTRHVGAEAEKVQEL 103
Cdd:PTZ00051  25 FYAEWCGPCKRIAPFYEECSKEYTKMVFVKV----DVDELSevAEKENITSMPTFKVFKNGSVVDTLLGANDEALKQL 98
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 6-95 3.54e-06

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: 42.22  E-value: 3.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351051008    6 CLTDEDF---LQKSEhgigKKAIYYFYGERCPSCESIKPLFDDLCKKYEKTALVYtypcyNDD----QLTGDAFAVNAVP 78
Cdd:pfam00085   4 VLTDANFdevVQKSS----KPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFA-----KVDvdenPDLASKYGVRGYP 74

                          90
                  ....*....|....*..
gi 351051008   79 TFVVMNNGEEVTRHVGA 95
Cdd:pfam00085  75 TLIFFKNGQPVDDYVGA 91
trxA PRK09381
thioredoxin TrxA;
28-95 6.18e-06

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 41.59  E-value: 6.18e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351051008  28 FYGERCPSCESIKPLFDDLCKKYEKTALVYTYpcyNDDQLTGDA--FAVNAVPTFVVMNNGEEVTRHVGA 95
Cdd:PRK09381  28 FWAEWCGPCKMIAPILDEIADEYQGKLTVAKL---NIDQNPGTApkYGIRGIPTLLLFKNGEVAATKVGA 94
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 21-94 1.19e-04

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 38.37  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351051008  21 GKKAIYYFYGERCPSCESIKPLFDDLCKKYEKTALV----------------------YTYPCYND-DQLTGDAFAVNAV 77
Cdd:cd02966   19 GKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEvvgvnvddddpaavkaflkkygITFPVLLDpDGELAKAYGVRGL 98

                         90
                 ....*....|....*...
gi 351051008  78 PTFVVMN-NGEEVTRHVG 94
Cdd:cd02966   99 PTTFLIDrDGRIRARHVG 116
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 10-105 3.05e-04

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: 36.87  E-value: 3.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351051008  10 EDFLQKSEHGIGKKAIYYFYGERCPSCESIKPLFDDLCKKYEKTALVYTYPCYNDDQLTgDAFAVNAVPTFVVMNNGEEV 89
Cdd:cd02956    1 QNFQQVLQESTQVPVVVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIA-QQFGVQALPTVYLFAAGQPV 79

                         90
                 ....*....|....*..
gi 351051008  90 TRHVGA-EAEKVQELFE 105
Cdd:cd02956   80 DGFQGAqPEEQLRQMLD 96
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 21-94 2.57e-03

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


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 34.97  E-value: 2.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351051008  21 GKKAIYYFYGERCPSCESIKPLFDDLCKKY-------------EKTALV----YTYPCYNDDQLT-GDAFAVNAVPTFVV 82
Cdd:cd03011   20 GKPVLVYFWATWCPVCRFTSPTVNQLAADYpvvsvalrsgddgAVARFMqkkgYGFPVINDPDGViSARWGVSVTPAIVI 99

                         90
                 ....*....|..
gi 351051008  83 MNNGEEVTRHVG 94
Cdd:cd03011  100 VDPGGIVFVTTG 111
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 25-90 6.25e-03

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: 33.06  E-value: 6.25e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 351051008  25 IYYFYGERCPSCESIKPLFDDLCKKYEKTALVYTYPCYNDDQL-TGDAFAVNAVPTFVVMNNGEEVT 90
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELALLNKGVKFEAVDVDEDPALEkELKRYGVGGVPTLVVFGPGIGVK 67
 
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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