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Conserved domains on  [gi|1847915294|ref|NP_001371105|]
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thioredoxin-like protein 4A isoform d [Mus musculus]

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 ...
1-51 1.43e-31

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 PLN00410:

Pssm-ID: 469754  Cd Length: 142  Bit Score: 106.43  E-value: 1.43e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1847915294   1 MSYMLPHLHNGWQVDQAILSEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEK 51
Cdd:PLN00410    1 MSYLLPHLHSGWAVDQAILAEEERLVVIRFGHDWDETCMQMDEVLASVAET 51
 
Name Accession Description Interval E-value
PLN00410 PLN00410
U5 snRNP protein, DIM1 family; Provisional
1-51 1.43e-31

U5 snRNP protein, DIM1 family; Provisional


Pssm-ID: 215109  Cd Length: 142  Bit Score: 106.43  E-value: 1.43e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1847915294   1 MSYMLPHLHNGWQVDQAILSEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEK 51
Cdd:PLN00410    1 MSYLLPHLHSGWAVDQAILAEEERLVVIRFGHDWDETCMQMDEVLASVAET 51
DIM1 pfam02966
Mitosis protein DIM1;
4-51 1.79e-29

Mitosis protein DIM1;


Pssm-ID: 460768  Cd Length: 133  Bit Score: 100.82  E-value: 1.79e-29
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1847915294   4 MLPHLHNGWQVDQAILSEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEK 51
Cdd:pfam02966   1 LLPHLRTGWHVDQAILSEEDKLVVIRFGRDEDPVCMQMDEILYKIAEK 48
DIM1 cd02954
Dim1 family; Dim1 is also referred to as U5 small nuclear ribonucleoprotein particle (snRNP) ...
10-51 7.47e-25

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: 88.51  E-value: 7.47e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1847915294  10 NGWQVDQAILSEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEK 51
Cdd:cd02954     1 SGWAVDQAILSEEEKVVVIRFGRDWDPVCMQMDEVLAKIAED 42
 
Name Accession Description Interval E-value
PLN00410 PLN00410
U5 snRNP protein, DIM1 family; Provisional
1-51 1.43e-31

U5 snRNP protein, DIM1 family; Provisional


Pssm-ID: 215109  Cd Length: 142  Bit Score: 106.43  E-value: 1.43e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1847915294   1 MSYMLPHLHNGWQVDQAILSEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEK 51
Cdd:PLN00410    1 MSYLLPHLHSGWAVDQAILAEEERLVVIRFGHDWDETCMQMDEVLASVAET 51
DIM1 pfam02966
Mitosis protein DIM1;
4-51 1.79e-29

Mitosis protein DIM1;


Pssm-ID: 460768  Cd Length: 133  Bit Score: 100.82  E-value: 1.79e-29
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1847915294   4 MLPHLHNGWQVDQAILSEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEK 51
Cdd:pfam02966   1 LLPHLRTGWHVDQAILSEEDKLVVIRFGRDEDPVCMQMDEILYKIAEK 48
DIM1 cd02954
Dim1 family; Dim1 is also referred to as U5 small nuclear ribonucleoprotein particle (snRNP) ...
10-51 7.47e-25

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: 88.51  E-value: 7.47e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1847915294  10 NGWQVDQAILSEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEK 51
Cdd:cd02954     1 SGWAVDQAILSEEEKVVVIRFGRDWDPVCMQMDEVLAKIAED 42
DLP cd02986
Dim1 family, Dim1-like protein (DLP) subfamily; DLP is a novel protein which shares 38% ...
13-45 2.95e-08

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: 45.98  E-value: 2.95e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1847915294  13 QVDQAILSEEDRVVVIRFGHDWDPTCMKMDEVL 45
Cdd:cd02986     4 EVDQAIKSTAEKVLVLRFGRDEDAVCLQLDDIL 36
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
13-53 1.64e-03

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: 33.40  E-value: 1.64e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 1847915294 13 QVDQAILSEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEKAN 53
Cdd:cd02984    4 EFEELLKSDASKLLVLHFWAPWAEPCKQMNQVFEELAKEAF 44
 
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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