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Conserved domains on  [gi|13384656|ref|NP_079575|]
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thioredoxin-like protein 4A isoform a [Mus musculus]

Protein Classification

DIM1 family thioredoxin-like protein( domain architecture ID 10791280)

DIM1 family thioredoxin-like protein similar to human thioredoxin-like protein 4A (TXNL4A or DIM1) that plays a role in pre-mRNA splicing as a component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes that are involved in spliceosome assembly, and as a component of the precatalytic spliceosome

CATH:  3.40.30.10
Gene Ontology:  GO:0000398|GO:0005681|GO:0005682|GO:0046540
PubMed:  15558583|10049365
SCOP:  3000031

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN00410 PLN00410
U5 snRNP protein, DIM1 family; Provisional
 1-142 3.03e-102

U5 snRNP protein, DIM1 family; Provisional


:

Pssm-ID: 215109  Cd Length: 142  Bit Score: 288.63  E-value: 3.03e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13384656    1 MSYMLPHLHNGWQVDQAILSEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEKVKNFAVIYLVDITEVPDFNKMYELYDPCT 80
Cdd:PLN00410   1 MSYLLPHLHSGWAVDQAILAEEERLVVIRFGHDWDETCMQMDEVLASVAETIKNFAVIYLVDITEVPDFNTMYELYDPCT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13384656   81 VMFFFRNKHIMIDLGTGNNNKINWAMEDKQEMVDIIETVYRGARKGRGLVVSPKDYSTKYRY 142
Cdd:PLN00410  81 VMFFFRNKHIMIDLGTGNNNKINWALKDKQEFIDIVETVYRGARKGRGLVISPKDYSTKYRY 142
 
Name Accession Description Interval E-value
PLN00410 PLN00410
U5 snRNP protein, DIM1 family; Provisional
 1-142 3.03e-102

U5 snRNP protein, DIM1 family; Provisional


Pssm-ID: 215109  Cd Length: 142  Bit Score: 288.63  E-value: 3.03e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13384656    1 MSYMLPHLHNGWQVDQAILSEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEKVKNFAVIYLVDITEVPDFNKMYELYDPCT 80
Cdd:PLN00410   1 MSYLLPHLHSGWAVDQAILAEEERLVVIRFGHDWDETCMQMDEVLASVAETIKNFAVIYLVDITEVPDFNTMYELYDPCT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13384656   81 VMFFFRNKHIMIDLGTGNNNKINWAMEDKQEMVDIIETVYRGARKGRGLVVSPKDYSTKYRY 142
Cdd:PLN00410  81 VMFFFRNKHIMIDLGTGNNNKINWALKDKQEFIDIVETVYRGARKGRGLVISPKDYSTKYRY 142
DIM1 pfam02966
Mitosis protein DIM1;
4-136 7.19e-92

Mitosis protein DIM1;


Pssm-ID: 460768  Cd Length: 133  Bit Score: 261.83  E-value: 7.19e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13384656     4 MLPHLHNGWQVDQAILSEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEKVKNFAVIYLVDITEVPDFNKMYELYDPCTVMF 83
Cdd:pfam02966   1 LLPHLRTGWHVDQAILSEEDKLVVIRFGRDEDPVCMQMDEILYKIAEKVSNFAVIYLVDIDEVPDFNKMYELYDPVTIMF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 13384656    84 FFRNKHIMIDLGTGNNNKINWAMEDKQEMVDIIETVYRGARKGRGLVVSPKDY 136
Cdd:pfam02966  81 FYNNKHMMIDFGTGDNNKLNFSFEDKQELIDIIETIYRGAMKGKGLVVSPIDY 133
DIM1 cd02954
Dim1 family; Dim1 is also referred to as U5 small nuclear ribonucleoprotein particle (snRNP) ...
 10-123 4.80e-77

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: 223.71  E-value: 4.80e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13384656  10 NGWQVDQAILSEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEKVKNFAVIYLVDITEVPDFNKMYELYDPCTVMFFFRNKH 89
Cdd:cd02954   1 SGWAVDQAILSEEEKVVVIRFGRDWDPVCMQMDEVLAKIAEDVSNFAVIYLVDIDEVPDFNKMYELYDPPTVMFFFRNKH 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 13384656  90 IMIDLGTGNNNKINWAMEDKQEMVDIIETVYRGA 123
Cdd:cd02954  81 MKIDLGTGNNNKINWVFEDKQEFIDIIETIYRGA 114
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 16-84 9.63e-04

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: 36.34  E-value: 9.63e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13384656  16 QAILSEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEKVKNFAVIYLVDITEVPDFNKMYELYD-PcTVMFF 84
Cdd:COG3118  11 EEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSiP-TLLLF 79
 
Name Accession Description Interval E-value
PLN00410 PLN00410
U5 snRNP protein, DIM1 family; Provisional
 1-142 3.03e-102

U5 snRNP protein, DIM1 family; Provisional


Pssm-ID: 215109  Cd Length: 142  Bit Score: 288.63  E-value: 3.03e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13384656    1 MSYMLPHLHNGWQVDQAILSEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEKVKNFAVIYLVDITEVPDFNKMYELYDPCT 80
Cdd:PLN00410   1 MSYLLPHLHSGWAVDQAILAEEERLVVIRFGHDWDETCMQMDEVLASVAETIKNFAVIYLVDITEVPDFNTMYELYDPCT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13384656   81 VMFFFRNKHIMIDLGTGNNNKINWAMEDKQEMVDIIETVYRGARKGRGLVVSPKDYSTKYRY 142
Cdd:PLN00410  81 VMFFFRNKHIMIDLGTGNNNKINWALKDKQEFIDIVETVYRGARKGRGLVISPKDYSTKYRY 142
DIM1 pfam02966
Mitosis protein DIM1;
4-136 7.19e-92

Mitosis protein DIM1;


Pssm-ID: 460768  Cd Length: 133  Bit Score: 261.83  E-value: 7.19e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13384656     4 MLPHLHNGWQVDQAILSEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEKVKNFAVIYLVDITEVPDFNKMYELYDPCTVMF 83
Cdd:pfam02966   1 LLPHLRTGWHVDQAILSEEDKLVVIRFGRDEDPVCMQMDEILYKIAEKVSNFAVIYLVDIDEVPDFNKMYELYDPVTIMF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 13384656    84 FFRNKHIMIDLGTGNNNKINWAMEDKQEMVDIIETVYRGARKGRGLVVSPKDY 136
Cdd:pfam02966  81 FYNNKHMMIDFGTGDNNKLNFSFEDKQELIDIIETIYRGAMKGKGLVVSPIDY 133
DIM1 cd02954
Dim1 family; Dim1 is also referred to as U5 small nuclear ribonucleoprotein particle (snRNP) ...
 10-123 4.80e-77

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: 223.71  E-value: 4.80e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13384656  10 NGWQVDQAILSEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEKVKNFAVIYLVDITEVPDFNKMYELYDPCTVMFFFRNKH 89
Cdd:cd02954   1 SGWAVDQAILSEEEKVVVIRFGRDWDPVCMQMDEVLAKIAEDVSNFAVIYLVDIDEVPDFNKMYELYDPPTVMFFFRNKH 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 13384656  90 IMIDLGTGNNNKINWAMEDKQEMVDIIETVYRGA 123
Cdd:cd02954  81 MKIDLGTGNNNKINWVFEDKQEFIDIIETIYRGA 114
DLP cd02986
Dim1 family, Dim1-like protein (DLP) subfamily; DLP is a novel protein which shares 38% ...
 13-123 4.30e-28

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: 99.91  E-value: 4.30e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13384656  13 QVDQAILSEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEKVKNFAVIYLVDITEVPDFNKMYEL-YDPCTVmFFFRNKHIM 91
Cdd:cd02986   4 EVDQAIKSTAEKVLVLRFGRDEDAVCLQLDDILSKTSHDLSKMASIYLVDVDKVPVYTQYFDIsYIPSTI-FFFNGQHMK 82

                        90       100       110
                ....*....|....*....|....*....|..
gi 13384656  92 IDLGTGNNNKINWAMEDKQEMVDIIETVYRGA 123
Cdd:cd02986  83 VDYGSPDHTKFVGSFKTKQDFIDLIEVIYRGA 114
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 16-84 2.64e-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: 37.98  E-value: 2.64e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13384656    16 QAILSEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEKVKNFAVIYLVDITEVPDFNKMYELYDPCTVMFF 84
Cdd:pfam00085  11 DEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFF 79
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 13-84 3.22e-04

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: 37.64  E-value: 3.22e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13384656  13 QVDQAILSEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEKVKNFAVIYLVDITEVPDFNKMYELYDPCTVMFF 84
Cdd:cd02984   4 EFEELLKSDASKLLVLHFWAPWAEPCKQMNQVFEELAKEAFPSVLFLSIEAEELPEISEKFEITAVPTFVFF 75
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 16-84 9.63e-04

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: 36.34  E-value: 9.63e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13384656  16 QAILSEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEKVKNFAVIYLVDITEVPDFNKMYELYD-PcTVMFF 84
Cdd:COG3118  11 EEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSiP-TLLLF 79
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 27-93 5.42e-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: 33.83  E-value: 5.42e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13384656  27 VIRFGHDWDPTCMKMDEVLYSIAEKVKNFAVIYlVDITEVPD---FNKMYELYDPCTVMFFFRNKHIMID 93
Cdd:cd01659   1 LVLFYAPWCPFCQALRPVLAELALLNKGVKFEA-VDVDEDPAlekELKRYGVGGVPTLVVFGPGIGVKYG 69
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 13-69 7.00e-03

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: 33.69  E-value: 7.00e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13384656  13 QVDQAIlsEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEKVKNFaVIYLVDITEVPDF 69
Cdd:cd02947   2 EFEELI--KSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKV-KFVKVDVDENPEL 55
 
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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