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Conserved domains on  [gi|1622910713|ref|XP_028696324|]
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thioredoxin-like protein 4B isoform X6 [Macaca mulatta]

Protein Classification

thioredoxin domain-containing protein( domain architecture ID 144)

thioredoxin domain-containing protein may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 10-96 7.10e-59

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is 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 the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member cd02986:

Pssm-ID: 469754  Cd Length: 114  Bit Score: 176.95  E-value: 7.10e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622910713  10 SKKEVDQAIKSTAEKVLVLRFGRDEDPVCLQLDDILSKTSSDLSKMAAIYLVDVDQTPVYTQYFDISYIPSTVFFFNGQH 89
Cdd:cd02986     1 SKKEVDQAIKSTAEKVLVLRFGRDEDAVCLQLDDILSKTSHDLSKMASIYLVDVDKVPVYTQYFDISYIPSTIFFFNGQH 80


                  ....*..
gi 1622910713  90 MKVDYGT 96
Cdd:cd02986    81 MKVDYGS 87
 
Name Accession Description Interval E-value
DLP cd02986
Dim1 family, Dim1-like protein (DLP) subfamily; DLP is a novel protein which shares 38% ...
 10-96 7.10e-59

Dim1 family, Dim1-like protein (DLP) subfamily; DLP is a novel protein which shares 38% sequence identity to Dim1. Like Dim1, it is also implicated in pre-mRNA splicing and cell cycle progression. DLP is located in the nucleus and has been shown to interact with the U5 small nuclear ribonucleoprotein particle (snRNP)-specific 102kD protein (or Prp6). Dim1 protein, also known as U5 snRNP-specific 15kD protein is a component of U5 snRNP, which pre-assembles with U4/U6 snRNPs to form a [U4/U6:U5] tri-snRNP complex required for pre-mRNA splicing. Dim1 adopts a thioredoxin fold but does not contain the redox active CXXC motif.


Pssm-ID: 239284  Cd Length: 114  Bit Score: 176.95  E-value: 7.10e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622910713  10 SKKEVDQAIKSTAEKVLVLRFGRDEDPVCLQLDDILSKTSSDLSKMAAIYLVDVDQTPVYTQYFDISYIPSTVFFFNGQH 89
Cdd:cd02986     1 SKKEVDQAIKSTAEKVLVLRFGRDEDAVCLQLDDILSKTSHDLSKMASIYLVDVDKVPVYTQYFDISYIPSTIFFFNGQH 80


                  ....*..
gi 1622910713  90 MKVDYGT 96
Cdd:cd02986    81 MKVDYGS 87
DIM1 pfam02966
Mitosis protein DIM1;
4-96 8.97e-47

Mitosis protein DIM1;


Pssm-ID: 460768  Cd Length: 133  Bit Score: 146.66  E-value: 8.97e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622910713   4 LLPKLTSKKEVDQAIKSTAEKVLVLRFGRDEDPVCLQLDDILSKTSSDLSKMAAIYLVDVDQTPVYTQYFDIsYIPSTV- 82
Cdd:pfam02966   1 LLPHLRTGWHVDQAILSEEDKLVVIRFGRDEDPVCMQMDEILYKIAEKVSNFAVIYLVDIDEVPDFNKMYEL-YDPVTIm 79

                          90
                  ....*....|....
gi 1622910713  83 FFFNGQHMKVDYGT 96
Cdd:pfam02966  80 FFYNNKHMMIDFGT 93
PLN00410 PLN00410
U5 snRNP protein, DIM1 family; Provisional
 1-96 1.26e-26

U5 snRNP protein, DIM1 family; Provisional


Pssm-ID: 215109  Cd Length: 142  Bit Score: 96.03  E-value: 1.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622910713   1 MSFLLPKLTSKKEVDQAIKSTAEKVLVLRFGRDEDPVCLQLDDILSKTSSDLSKMAAIYLVDVDQTPVYTQYFDIsYIPS 80
Cdd:PLN00410    1 MSYLLPHLHSGWAVDQAILAEEERLVVIRFGHDWDETCMQMDEVLASVAETIKNFAVIYLVDITEVPDFNTMYEL-YDPC 79

                          90
                  ....*....|....*..
gi 1622910713  81 TV-FFFNGQHMKVDYGT 96
Cdd:PLN00410   80 TVmFFFRNKHIMIDLGT 96
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 10-88 1.25e-07

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: 45.97  E-value: 1.25e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622910713  10 SKKEVDQAIKSTAEKVLVLrFGRDEDPVCLQLDDILSKTSSDLSKMAAIYLVDVDQTPVYTQYFDISYIPSTVFFFNGQ 88
Cdd:COG3118     6 TDENFEEEVLESDKPVLVD-FWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQ 83
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 10-92 2.87e-03

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: 34.57  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622910713  10 SKKEVDQAIKSTAEKVLVLRFGRDEDPvCLQLDDILSKTSSDLSKMAAIYLVDVDQTPVYTQYFDISYIPSTVFFFNGQ- 88
Cdd:TIGR01068   2 TDANFDETIASSDKPVLVDFWAPWCGP-CKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKe 80


                  ....*
gi 1622910713  89 -HMKV 92
Cdd:TIGR01068  81 vDRSV 85
 
Name Accession Description Interval E-value
DLP cd02986
Dim1 family, Dim1-like protein (DLP) subfamily; DLP is a novel protein which shares 38% ...
 10-96 7.10e-59

Dim1 family, Dim1-like protein (DLP) subfamily; DLP is a novel protein which shares 38% sequence identity to Dim1. Like Dim1, it is also implicated in pre-mRNA splicing and cell cycle progression. DLP is located in the nucleus and has been shown to interact with the U5 small nuclear ribonucleoprotein particle (snRNP)-specific 102kD protein (or Prp6). Dim1 protein, also known as U5 snRNP-specific 15kD protein is a component of U5 snRNP, which pre-assembles with U4/U6 snRNPs to form a [U4/U6:U5] tri-snRNP complex required for pre-mRNA splicing. Dim1 adopts a thioredoxin fold but does not contain the redox active CXXC motif.


Pssm-ID: 239284  Cd Length: 114  Bit Score: 176.95  E-value: 7.10e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622910713  10 SKKEVDQAIKSTAEKVLVLRFGRDEDPVCLQLDDILSKTSSDLSKMAAIYLVDVDQTPVYTQYFDISYIPSTVFFFNGQH 89
Cdd:cd02986     1 SKKEVDQAIKSTAEKVLVLRFGRDEDAVCLQLDDILSKTSHDLSKMASIYLVDVDKVPVYTQYFDISYIPSTIFFFNGQH 80


                  ....*..
gi 1622910713  90 MKVDYGT 96
Cdd:cd02986    81 MKVDYGS 87
DIM1 cd02954
Dim1 family; Dim1 is also referred to as U5 small nuclear ribonucleoprotein particle (snRNP) ...
 10-96 1.49e-49

Dim1 family; Dim1 is also referred to as U5 small nuclear ribonucleoprotein particle (snRNP)-specific 15kD protein. It is a component of U5 snRNP, which pre-assembles with U4/U6 snRNPs to form a [U4/U6:U5] tri-snRNP complex required for pre-mRNA splicing. Dim1 interacts with multiple splicing-associated proteins, suggesting that it functions at multiple control points in the splicing of pre-mRNA as part of a large spliceosomal complex involving many protein-protein interactions. U5 snRNP contains seven core proteins (common to all snRNPs) and nine U5-specific proteins, one of which is Dim1. Dim1 adopts a thioredoxin fold but does not contain the redox active CXXC motif. It is essential for G2/M phase transition, as a consequence to its role in pre-mRNA splicing.


Pssm-ID: 239252  Cd Length: 114  Bit Score: 153.22  E-value: 1.49e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622910713  10 SKKEVDQAIKSTAEKVLVLRFGRDEDPVCLQLDDILSKTSSDLSKMAAIYLVDVDQTPVYTQYFDISYIPSTVFFFNGQH 89
Cdd:cd02954     1 SGWAVDQAILSEEEKVVVIRFGRDWDPVCMQMDEVLAKIAEDVSNFAVIYLVDIDEVPDFNKMYELYDPPTVMFFFRNKH 80


                  ....*..
gi 1622910713  90 MKVDYGT 96
Cdd:cd02954    81 MKIDLGT 87
DIM1 pfam02966
Mitosis protein DIM1;
4-96 8.97e-47

Mitosis protein DIM1;


Pssm-ID: 460768  Cd Length: 133  Bit Score: 146.66  E-value: 8.97e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622910713   4 LLPKLTSKKEVDQAIKSTAEKVLVLRFGRDEDPVCLQLDDILSKTSSDLSKMAAIYLVDVDQTPVYTQYFDIsYIPSTV- 82
Cdd:pfam02966   1 LLPHLRTGWHVDQAILSEEDKLVVIRFGRDEDPVCMQMDEILYKIAEKVSNFAVIYLVDIDEVPDFNKMYEL-YDPVTIm 79

                          90
                  ....*....|....
gi 1622910713  83 FFFNGQHMKVDYGT 96
Cdd:pfam02966  80 FFYNNKHMMIDFGT 93
PLN00410 PLN00410
U5 snRNP protein, DIM1 family; Provisional
 1-96 1.26e-26

U5 snRNP protein, DIM1 family; Provisional


Pssm-ID: 215109  Cd Length: 142  Bit Score: 96.03  E-value: 1.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622910713   1 MSFLLPKLTSKKEVDQAIKSTAEKVLVLRFGRDEDPVCLQLDDILSKTSSDLSKMAAIYLVDVDQTPVYTQYFDIsYIPS 80
Cdd:PLN00410    1 MSYLLPHLHSGWAVDQAILAEEERLVVIRFGHDWDETCMQMDEVLASVAETIKNFAVIYLVDITEVPDFNTMYEL-YDPC 79

                          90
                  ....*....|....*..
gi 1622910713  81 TV-FFFNGQHMKVDYGT 96
Cdd:PLN00410   80 TVmFFFRNKHIMIDLGT 96
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 10-88 1.25e-07

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: 45.97  E-value: 1.25e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622910713  10 SKKEVDQAIKSTAEKVLVLrFGRDEDPVCLQLDDILSKTSSDLSKMAAIYLVDVDQTPVYTQYFDISYIPSTVFFFNGQ 88
Cdd:COG3118     6 TDENFEEEVLESDKPVLVD-FWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQ 83
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 12-88 4.48e-07

TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 44.47  E-value: 4.48e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622910713  12 KEVDQAIKStaEKVLVLRFGRDEDPVCLQLDDILSKTSSDLSKmAAIYLVDVDQTPVYTQYFDISYIPSTVFFFNGQ 88
Cdd:cd02947     1 EEFEELIKS--AKPVVVDFWAPWCGPCKAIAPVLEELAEEYPK-VKFVKVDVDENPELAEEYGVRSIPTFLFFKNGK 74
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 10-88 5.77e-06

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: 41.49  E-value: 5.77e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622910713  10 SKKEVDQAIKSTAEKVLVLRFGRDEDPVCLQLDDILSKTSSDLSKMAAIYLVDVDQTPVYTQYFDISYIPSTVFFFNGQ 88
Cdd:cd02984     1 SEEEFEELLKSDASKLLVLHFWAPWAEPCKQMNQVFEELAKEAFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGT 79
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 15-88 2.42e-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: 37.25  E-value: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622910713  15 DQAIKSTAEKVLVLrFGRDEDPVCLQLDdilsktsSDLSKMAAIY-------LVDVDQTPVYTQYFDISYIPSTVFFFNG 87
Cdd:cd02956     5 QVLQESTQVPVVVD-FWAPRSPPSKELL-------PLLERLAEEYqgqfvlaKVNCDAQPQIAQQFGVQALPTVYLFAAG 76


                  .
gi 1622910713  88 Q 88
Cdd:cd02956    77 Q 77
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 6-99 9.76e-04

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: 35.67  E-value: 9.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622910713   6 PKLTSKKEVDQAIKSTAEKVLVLrFGRDEDPVCLQLDDILSKTSSDLSKMAAIYLVDVDQTPVYTQYFDISYIPSTVFFF 85
Cdd:pfam00085   2 VVVLTDANFDEVVQKSSKPVLVD-FYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFK 80

                          90
                  ....*....|....
gi 1622910713  86 NGQhmKVDYGTEGR 99
Cdd:pfam00085  81 NGQ--PVDDYVGAR 92
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 10-92 2.87e-03

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: 34.57  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622910713  10 SKKEVDQAIKSTAEKVLVLRFGRDEDPvCLQLDDILSKTSSDLSKMAAIYLVDVDQTPVYTQYFDISYIPSTVFFFNGQ- 88
Cdd:TIGR01068   2 TDANFDETIASSDKPVLVDFWAPWCGP-CKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKe 80


                  ....*
gi 1622910713  89 -HMKV 92
Cdd:TIGR01068  81 vDRSV 85
Phd_like_TxnDC9 cd02989
Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; ...
 5-88 8.74e-03

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: 33.32  E-value: 8.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622910713   5 LPKLTSKKEVDQAIKSTaeKVLVLRFGRDEDPVCLQLDdilsktsSDLSKMAAIYL------VDVDQTPVYTQYFDISYI 78
Cdd:cd02989     6 YREVSDEKEFFEIVKSS--ERVVCHFYHPEFFRCKIMD-------KHLEILAKKHLetkfikVNAEKAPFLVEKLNIKVL 76

                          90
                  ....*....|
gi 1622910713  79 PSTVFFFNGQ 88
Cdd:cd02989    77 PTVILFKNGK 86
 
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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