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Conserved domains on  [gi|6320906|ref|NP_010985|]
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Tho1p [Saccharomyces cerevisiae S288C]

Protein Classification

SAP domain-containing protein( domain architecture ID 15877045)

SAP domain-containing protein such as Saccharomyces cerevisiae THO1 protein, a member of the THO complex that is required for mRNA export

CATH:  1.10.720.30
Gene Ontology:  GO:0003676
PubMed:  26073259|10694879

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tho1_MOS11_C pfam18592
Tho1/MOS11 C-terminal domain; THO is a multi-protein complex involved in the formation of ...
 127-164 1.67e-09

Tho1/MOS11 C-terminal domain; THO is a multi-protein complex involved in the formation of messenger ribonuclear particles (mRNPs) by coupling transcription with mRNA processing and export. Some studies show that Tho1, like Sub2, can assemble onto the nascent mRNA during transcription and that Tho1 and Sub2 can provide alternative pathways for mRNP biogenesis in the absence of a functional THO complex. This is the C-terminal domain found in Tho1 and MOS11 proteins. The C-terminal region of Tho1 from Saccharomyces cerevisiae, adopts a helical fold similar to that of the WHEP RNA-binding domains of metazoan aminoacyl-tRNA synthetases.


:

Pssm-ID: 465813 [Multi-domain]  Cd Length: 37  Bit Score: 51.66  E-value: 1.67e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 6320906    127 AKALDLLNKKLHRANKFGQDqADIDSLQRQINRVEKFG 164
Cdd:pfam18592   1 TAAIEELEKRKARAKKFGIE-AEIDEAEKQLERAEKFG 37
SAP pfam02037
SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding ...
 4-38 2.38e-08

SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding domain found in diverse nuclear and cytoplasmic proteins.


:

Pssm-ID: 460424 [Multi-domain]  Cd Length: 35  Bit Score: 48.17  E-value: 2.38e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 6320906      4 YSSLTVVQLKDLLTKRNLSVGGLKNELVQRLIKDD 38
Cdd:pfam02037   1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
LGT super family cl00478
Prolipoprotein diacylglyceryl transferase;
39-109 3.46e-03

Prolipoprotein diacylglyceryl transferase;


The actual alignment was detected with superfamily member PRK13108:

Pssm-ID: 469786 [Multi-domain]  Cd Length: 460  Bit Score: 38.04  E-value: 3.46e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6320906    39 EESKGESEVSPQEQNQEQGSEPaaiEEPASQNITEKKEVSSEPKETNEPKEE-NKDVQKPSDGPSATASENE 109
Cdd:PRK13108 377 GDLAGQAPAAHQVDAEAASAAP---EEPAALASEAHDETEPEVPEKAAPIPDpAKPDELAVAGPGDDPAEPD 445
 
Name Accession Description Interval E-value
Tho1_MOS11_C pfam18592
Tho1/MOS11 C-terminal domain; THO is a multi-protein complex involved in the formation of ...
 127-164 1.67e-09

Tho1/MOS11 C-terminal domain; THO is a multi-protein complex involved in the formation of messenger ribonuclear particles (mRNPs) by coupling transcription with mRNA processing and export. Some studies show that Tho1, like Sub2, can assemble onto the nascent mRNA during transcription and that Tho1 and Sub2 can provide alternative pathways for mRNP biogenesis in the absence of a functional THO complex. This is the C-terminal domain found in Tho1 and MOS11 proteins. The C-terminal region of Tho1 from Saccharomyces cerevisiae, adopts a helical fold similar to that of the WHEP RNA-binding domains of metazoan aminoacyl-tRNA synthetases.


Pssm-ID: 465813 [Multi-domain]  Cd Length: 37  Bit Score: 51.66  E-value: 1.67e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 6320906    127 AKALDLLNKKLHRANKFGQDqADIDSLQRQINRVEKFG 164
Cdd:pfam18592   1 TAAIEELEKRKARAKKFGIE-AEIDEAEKQLERAEKFG 37
SAP pfam02037
SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding ...
 4-38 2.38e-08

SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding domain found in diverse nuclear and cytoplasmic proteins.


Pssm-ID: 460424 [Multi-domain]  Cd Length: 35  Bit Score: 48.17  E-value: 2.38e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 6320906      4 YSSLTVVQLKDLLTKRNLSVGGLKNELVQRLIKDD 38
Cdd:pfam02037   1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
4-36 1.08e-07

Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 46.71  E-value: 1.08e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 6320906       4 YSSLTVVQLKDLLTKRNLSVGGLKNELVQRLIK 36
Cdd:smart00513   1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLLE 33
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 39-109 3.46e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 38.04  E-value: 3.46e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6320906    39 EESKGESEVSPQEQNQEQGSEPaaiEEPASQNITEKKEVSSEPKETNEPKEE-NKDVQKPSDGPSATASENE 109
Cdd:PRK13108 377 GDLAGQAPAAHQVDAEAASAAP---EEPAALASEAHDETEPEVPEKAAPIPDpAKPDELAVAGPGDDPAEPD 445
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 2-74 6.93e-03

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 37.12  E-value: 6.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6320906     2 ADYSSLTVVQLKDLLTKRNLSVGGLKNELVQRLIKDDE-ESKGESEVSPQEQNQEQGSEPAAIEEPASQNITEK 74
Cdd:PLN03124  77 DEVKGMTVRELREAASERGLATTGRKKDLLERLCAALEsDVKVGSANGTGEDEKEKGGDEEREKEEKIVTATKK 150
 
Name Accession Description Interval E-value
Tho1_MOS11_C pfam18592
Tho1/MOS11 C-terminal domain; THO is a multi-protein complex involved in the formation of ...
 127-164 1.67e-09

Tho1/MOS11 C-terminal domain; THO is a multi-protein complex involved in the formation of messenger ribonuclear particles (mRNPs) by coupling transcription with mRNA processing and export. Some studies show that Tho1, like Sub2, can assemble onto the nascent mRNA during transcription and that Tho1 and Sub2 can provide alternative pathways for mRNP biogenesis in the absence of a functional THO complex. This is the C-terminal domain found in Tho1 and MOS11 proteins. The C-terminal region of Tho1 from Saccharomyces cerevisiae, adopts a helical fold similar to that of the WHEP RNA-binding domains of metazoan aminoacyl-tRNA synthetases.


Pssm-ID: 465813 [Multi-domain]  Cd Length: 37  Bit Score: 51.66  E-value: 1.67e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 6320906    127 AKALDLLNKKLHRANKFGQDqADIDSLQRQINRVEKFG 164
Cdd:pfam18592   1 TAAIEELEKRKARAKKFGIE-AEIDEAEKQLERAEKFG 37
SAP pfam02037
SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding ...
 4-38 2.38e-08

SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding domain found in diverse nuclear and cytoplasmic proteins.


Pssm-ID: 460424 [Multi-domain]  Cd Length: 35  Bit Score: 48.17  E-value: 2.38e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 6320906      4 YSSLTVVQLKDLLTKRNLSVGGLKNELVQRLIKDD 38
Cdd:pfam02037   1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEYL 35
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
4-36 1.08e-07

Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 46.71  E-value: 1.08e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 6320906       4 YSSLTVVQLKDLLTKRNLSVGGLKNELVQRLIK 36
Cdd:smart00513   1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLLE 33
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 39-109 3.46e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 38.04  E-value: 3.46e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6320906    39 EESKGESEVSPQEQNQEQGSEPaaiEEPASQNITEKKEVSSEPKETNEPKEE-NKDVQKPSDGPSATASENE 109
Cdd:PRK13108 377 GDLAGQAPAAHQVDAEAASAAP---EEPAALASEAHDETEPEVPEKAAPIPDpAKPDELAVAGPGDDPAEPD 445
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 5-78 6.51e-03

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 37.12  E-value: 6.51e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6320906     5 SSLTVVQLKDLLTKRNLSVGGLKNELVQRL----IKDDEESKGESEVSPQEQNQEQGSEPAAIEEPASQNITEKKEVS 78
Cdd:PLN03124   3 NKLKVDELRAALAKRGLDTTGLKAALVRRLddaiAEDAKTASKSGTKSSAGRKKRRERQDDGDDEPVSPKRIAIDEVK 80
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 2-74 6.93e-03

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 37.12  E-value: 6.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6320906     2 ADYSSLTVVQLKDLLTKRNLSVGGLKNELVQRLIKDDE-ESKGESEVSPQEQNQEQGSEPAAIEEPASQNITEK 74
Cdd:PLN03124  77 DEVKGMTVRELREAASERGLATTGRKKDLLERLCAALEsDVKVGSANGTGEDEKEKGGDEEREKEEKIVTATKK 150
 
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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