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Conserved domains on  [gi|334187564|ref|NP_001190269|]
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nuclear matrix protein-like protein [Arabidopsis thaliana]

Protein Classification

THO complex subunit THO1/HPR1( domain architecture ID 10571685)

THO complex subunit THO1/HPR1 acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
efThoc1 pfam11957
THO complex subunit 1 transcription elongation factor; The THO complex plays a role in ...
87-512 4.00e-99

THO complex subunit 1 transcription elongation factor; The THO complex plays a role in coupling transcription elongation to mRNA export. It is composed of subunits THP2, HPR1, THO2 and MFT1. The THO complex is a nuclear complex that is required for transcription elongation through genes containing tandemly repeated DNA sequences. The THO complex is also part of the TREX (TRanscription EXport) complex that is involved in coupling transcription to export of mRNAs to the cytoplasm.


:

Pssm-ID: 463412  Cd Length: 464  Bit Score: 309.70  E-value: 4.00e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187564   87 LLDVVLYLCEKEHVEGGMIFQLLEDLTEMSTMKNCKDVFGYIESKQDILgKQELFA--RGKLVMLRTCNQLLRRLSKAND 164
Cdd:pfam11957   2 LLDFCFHLSDDPLCWPTLPFVLLEDVLDSLTPDGCLKFWPYVESRIEWF-KMKGFSykQPLSVLLRTCNELLRRLSRPED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187564  165 VVFCGRILMFLAHFFPLSERSAVNIKGVFNTSNETKYEKDPPKG-----ISVDFNFYKTFWSLQEYFCNPASLTSaSTKW 239
Cdd:pfam11957  81 TVFCGKILLFLSQLFPLSERSNLNLRGEFSTENVTEFEEEEEEKdedtkKPIDYNLYPTFWSLQKFFSNPLSLYF-SPKF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187564  240 QKFSSSLAVVLNTF----------------DAQPLSEEEGEANSLEEEAA-----TFNIKYLTSSKLMGLELKDSSFRRH 298
Cdd:pfam11957 160 KSFEKYLESVLDAFleleeefyrrspikkkTKKKRAIKEKLNDNYQESWKnflenLFNPKYLTSPKLLDLQLSDPNFRKQ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187564  299 ILLQCLIMFDYLRAPGKNDKD--------LPSETMEELKSCEDRVKKLL-EITPPKGKEFLRAVEHILEREKNWVWWKRD 369
Cdd:pfam11957 240 VLLQFLILFQFLLSLTYKTKVkkksetsvLSDEDAKWIKSTCKKVYERLkEFYPPRGPQFYRMVNHLLSSEENWLKWKNE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187564  370 GCPPFEK------QPIDKKSPNAGQKKRRQRWR--LGNKELSQLWRWADQNPNALTDSQRVRTPDIADYWKPL-AEDMDP 440
Cdd:pfam11957 320 GCPEFEKppvsedELSEAPEKDKSFKKKRLFGFikMGNKALNRLWKICETGLDDLKKEERNPLPSLESYLEEIkLDEKDP 399
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334187564  441 SAGIEDEYHHKNNRVYCWKGLRFTARQDLEGFSrftemGIEGVVPVELLPPEvrSKYQAKPNEKAKRAKKEE 512
Cdd:pfam11957 400 EAAVEEEYKIDDKIVKQWRALRLLRRQYLFFFD-----KVDETTGLKGLFDY--SEDSESKEEKEKLDEELE 464
 
Name Accession Description Interval E-value
efThoc1 pfam11957
THO complex subunit 1 transcription elongation factor; The THO complex plays a role in ...
87-512 4.00e-99

THO complex subunit 1 transcription elongation factor; The THO complex plays a role in coupling transcription elongation to mRNA export. It is composed of subunits THP2, HPR1, THO2 and MFT1. The THO complex is a nuclear complex that is required for transcription elongation through genes containing tandemly repeated DNA sequences. The THO complex is also part of the TREX (TRanscription EXport) complex that is involved in coupling transcription to export of mRNAs to the cytoplasm.


Pssm-ID: 463412  Cd Length: 464  Bit Score: 309.70  E-value: 4.00e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187564   87 LLDVVLYLCEKEHVEGGMIFQLLEDLTEMSTMKNCKDVFGYIESKQDILgKQELFA--RGKLVMLRTCNQLLRRLSKAND 164
Cdd:pfam11957   2 LLDFCFHLSDDPLCWPTLPFVLLEDVLDSLTPDGCLKFWPYVESRIEWF-KMKGFSykQPLSVLLRTCNELLRRLSRPED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187564  165 VVFCGRILMFLAHFFPLSERSAVNIKGVFNTSNETKYEKDPPKG-----ISVDFNFYKTFWSLQEYFCNPASLTSaSTKW 239
Cdd:pfam11957  81 TVFCGKILLFLSQLFPLSERSNLNLRGEFSTENVTEFEEEEEEKdedtkKPIDYNLYPTFWSLQKFFSNPLSLYF-SPKF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187564  240 QKFSSSLAVVLNTF----------------DAQPLSEEEGEANSLEEEAA-----TFNIKYLTSSKLMGLELKDSSFRRH 298
Cdd:pfam11957 160 KSFEKYLESVLDAFleleeefyrrspikkkTKKKRAIKEKLNDNYQESWKnflenLFNPKYLTSPKLLDLQLSDPNFRKQ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187564  299 ILLQCLIMFDYLRAPGKNDKD--------LPSETMEELKSCEDRVKKLL-EITPPKGKEFLRAVEHILEREKNWVWWKRD 369
Cdd:pfam11957 240 VLLQFLILFQFLLSLTYKTKVkkksetsvLSDEDAKWIKSTCKKVYERLkEFYPPRGPQFYRMVNHLLSSEENWLKWKNE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187564  370 GCPPFEK------QPIDKKSPNAGQKKRRQRWR--LGNKELSQLWRWADQNPNALTDSQRVRTPDIADYWKPL-AEDMDP 440
Cdd:pfam11957 320 GCPEFEKppvsedELSEAPEKDKSFKKKRLFGFikMGNKALNRLWKICETGLDDLKKEERNPLPSLESYLEEIkLDEKDP 399
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334187564  441 SAGIEDEYHHKNNRVYCWKGLRFTARQDLEGFSrftemGIEGVVPVELLPPEvrSKYQAKPNEKAKRAKKEE 512
Cdd:pfam11957 400 EAAVEEEYKIDDKIVKQWRALRLLRRQYLFFFD-----KVDETTGLKGLFDY--SEDSESKEEKEKLDEELE 464
 
Name Accession Description Interval E-value
efThoc1 pfam11957
THO complex subunit 1 transcription elongation factor; The THO complex plays a role in ...
87-512 4.00e-99

THO complex subunit 1 transcription elongation factor; The THO complex plays a role in coupling transcription elongation to mRNA export. It is composed of subunits THP2, HPR1, THO2 and MFT1. The THO complex is a nuclear complex that is required for transcription elongation through genes containing tandemly repeated DNA sequences. The THO complex is also part of the TREX (TRanscription EXport) complex that is involved in coupling transcription to export of mRNAs to the cytoplasm.


Pssm-ID: 463412  Cd Length: 464  Bit Score: 309.70  E-value: 4.00e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187564   87 LLDVVLYLCEKEHVEGGMIFQLLEDLTEMSTMKNCKDVFGYIESKQDILgKQELFA--RGKLVMLRTCNQLLRRLSKAND 164
Cdd:pfam11957   2 LLDFCFHLSDDPLCWPTLPFVLLEDVLDSLTPDGCLKFWPYVESRIEWF-KMKGFSykQPLSVLLRTCNELLRRLSRPED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187564  165 VVFCGRILMFLAHFFPLSERSAVNIKGVFNTSNETKYEKDPPKG-----ISVDFNFYKTFWSLQEYFCNPASLTSaSTKW 239
Cdd:pfam11957  81 TVFCGKILLFLSQLFPLSERSNLNLRGEFSTENVTEFEEEEEEKdedtkKPIDYNLYPTFWSLQKFFSNPLSLYF-SPKF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187564  240 QKFSSSLAVVLNTF----------------DAQPLSEEEGEANSLEEEAA-----TFNIKYLTSSKLMGLELKDSSFRRH 298
Cdd:pfam11957 160 KSFEKYLESVLDAFleleeefyrrspikkkTKKKRAIKEKLNDNYQESWKnflenLFNPKYLTSPKLLDLQLSDPNFRKQ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187564  299 ILLQCLIMFDYLRAPGKNDKD--------LPSETMEELKSCEDRVKKLL-EITPPKGKEFLRAVEHILEREKNWVWWKRD 369
Cdd:pfam11957 240 VLLQFLILFQFLLSLTYKTKVkkksetsvLSDEDAKWIKSTCKKVYERLkEFYPPRGPQFYRMVNHLLSSEENWLKWKNE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187564  370 GCPPFEK------QPIDKKSPNAGQKKRRQRWR--LGNKELSQLWRWADQNPNALTDSQRVRTPDIADYWKPL-AEDMDP 440
Cdd:pfam11957 320 GCPEFEKppvsedELSEAPEKDKSFKKKRLFGFikMGNKALNRLWKICETGLDDLKKEERNPLPSLESYLEEIkLDEKDP 399
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334187564  441 SAGIEDEYHHKNNRVYCWKGLRFTARQDLEGFSrftemGIEGVVPVELLPPEvrSKYQAKPNEKAKRAKKEE 512
Cdd:pfam11957 400 EAAVEEEYKIDDKIVKQWRALRLLRRQYLFFFD-----KVDETTGLKGLFDY--SEDSESKEEKEKLDEELE 464
 
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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