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Conserved domains on  [gi|1246742001|ref|NP_001342747|]
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transcriptional regulatory protein Spp41 [Schizosaccharomyces pombe]

Protein Classification

SPP41 family protein( domain architecture ID 10567897)

SPP41 family protein is a DUF3020 domain-containing protein; similar to Saccharomyces cerevisiae protein SPP41, which is a negative regulator of PRP3 and PRP4 genes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF3020 pfam11223
SPP41, DUF3020; This domain is found in the conserved fungal proteins SPP41 (suppressor of ...
 168-216 7.60e-27

SPP41, DUF3020; This domain is found in the conserved fungal proteins SPP41 (suppressor of PrP4, there are four members, 1 to 4). In S. cerevisiae it is conserved towards the C-terminus of HMG domains. The function is not known. However, it has been shown that SPP41 is involved in negative regulation of expression of spliceosome components PRP4 and PRP3 and that it relocalizes to the cytosol in response to hypoxia.


:

Pssm-ID: 402691  Cd Length: 49  Bit Score: 102.70  E-value: 7.60e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1246742001 168 NRERKKRWREQNEERNKDNDLRCRVNKKAKKLFGSEPSIEKTNWIEAEF 216
Cdd:pfam11223   1 NRERKRKWREANKEKNKDNDLRSRVKKRAKKKFGKEDSEEKDAWIEEEF 49
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 366-568 2.36e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.91  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742001 366 SDSAVTNQSHSQSQNSL---HPLISQSETHSIFSALSETPTPVSGNGNVADA-------PPDFSLSQVMPLDLIA----- 430
Cdd:pfam03154 158 SDSSAQQQILQTQPPVLqaqSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQgspatsqPPNQTQSTAAPHTLIQqtptl 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742001 431 ---------PSMQPSAVSSPMSESHVQ------ISSEMPRTGMSALPMRPRSQNVDKHRKFPYYNKRNAVTTPSSPYDGA 495
Cdd:pfam03154 238 hpqrlpsphPPLQPMTQPPPPSQVSPQplpqpsLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAA 317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742001 496 qSGSPQFPPFELPPHNYSQAQSPNLATP-SPSFSSLPDVSLPPIVKPNLMsePTPTNSDEKSHALG---------FPPPP 565
Cdd:pfam03154 318 -PGQSQQRIHTPPSQSQLQSQQPPREQPlPPAPLSMPHIKPPPTTPIPQL--PNPQSHKHPPHLSGpspfqmnsnLPPPP 394


                  ...
gi 1246742001 566 GQK 568
Cdd:pfam03154 395 ALK 397
 
Name Accession Description Interval E-value
DUF3020 pfam11223
SPP41, DUF3020; This domain is found in the conserved fungal proteins SPP41 (suppressor of ...
 168-216 7.60e-27

SPP41, DUF3020; This domain is found in the conserved fungal proteins SPP41 (suppressor of PrP4, there are four members, 1 to 4). In S. cerevisiae it is conserved towards the C-terminus of HMG domains. The function is not known. However, it has been shown that SPP41 is involved in negative regulation of expression of spliceosome components PRP4 and PRP3 and that it relocalizes to the cytosol in response to hypoxia.


Pssm-ID: 402691  Cd Length: 49  Bit Score: 102.70  E-value: 7.60e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1246742001 168 NRERKKRWREQNEERNKDNDLRCRVNKKAKKLFGSEPSIEKTNWIEAEF 216
Cdd:pfam11223   1 NRERKRKWREANKEKNKDNDLRSRVKKRAKKKFGKEDSEEKDAWIEEEF 49
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 366-568 2.36e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.91  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742001 366 SDSAVTNQSHSQSQNSL---HPLISQSETHSIFSALSETPTPVSGNGNVADA-------PPDFSLSQVMPLDLIA----- 430
Cdd:pfam03154 158 SDSSAQQQILQTQPPVLqaqSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQgspatsqPPNQTQSTAAPHTLIQqtptl 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742001 431 ---------PSMQPSAVSSPMSESHVQ------ISSEMPRTGMSALPMRPRSQNVDKHRKFPYYNKRNAVTTPSSPYDGA 495
Cdd:pfam03154 238 hpqrlpsphPPLQPMTQPPPPSQVSPQplpqpsLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAA 317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742001 496 qSGSPQFPPFELPPHNYSQAQSPNLATP-SPSFSSLPDVSLPPIVKPNLMsePTPTNSDEKSHALG---------FPPPP 565
Cdd:pfam03154 318 -PGQSQQRIHTPPSQSQLQSQQPPREQPlPPAPLSMPHIKPPPTTPIPQL--PNPQSHKHPPHLSGpspfqmnsnLPPPP 394


                  ...
gi 1246742001 566 GQK 568
Cdd:pfam03154 395 ALK 397
PHA03247 PHA03247
large tegument protein UL36; Provisional
 396-559 2.91e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 2.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742001  396 SALSETPTPVSGngnvadAPPDFSLSQVMPldliAPSMQPSAVSSPMSEShVQISSEMPRTGMS-------ALPMRPRSQ 468
Cdd:PHA03247  2816 AALPPAASPAGP------LPPPTSAQPTAP----PPPPGPPPPSLPLGGS-VAPGGDVRRRPPSrspaakpAAPARPPVR 2884

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742001  469 NVdkhrkfpyynKRNAVTTPSSPYDGAQSGSPQFPPFELP--PHNYSQAQSPNLATPSPSFSSLPDVSLPPIVKPNLMSE 546
Cdd:PHA03247  2885 RL----------ARPAVSRSTESFALPPDQPERPPQPQAPppPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGE 2954

                          170
                   ....*....|...
gi 1246742001  547 PTPTNSDEKSHAL 559
Cdd:PHA03247  2955 PSGAVPQPWLGAL 2967
 
Name Accession Description Interval E-value
DUF3020 pfam11223
SPP41, DUF3020; This domain is found in the conserved fungal proteins SPP41 (suppressor of ...
 168-216 7.60e-27

SPP41, DUF3020; This domain is found in the conserved fungal proteins SPP41 (suppressor of PrP4, there are four members, 1 to 4). In S. cerevisiae it is conserved towards the C-terminus of HMG domains. The function is not known. However, it has been shown that SPP41 is involved in negative regulation of expression of spliceosome components PRP4 and PRP3 and that it relocalizes to the cytosol in response to hypoxia.


Pssm-ID: 402691  Cd Length: 49  Bit Score: 102.70  E-value: 7.60e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1246742001 168 NRERKKRWREQNEERNKDNDLRCRVNKKAKKLFGSEPSIEKTNWIEAEF 216
Cdd:pfam11223   1 NRERKRKWREANKEKNKDNDLRSRVKKRAKKKFGKEDSEEKDAWIEEEF 49
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 366-568 2.36e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.91  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742001 366 SDSAVTNQSHSQSQNSL---HPLISQSETHSIFSALSETPTPVSGNGNVADA-------PPDFSLSQVMPLDLIA----- 430
Cdd:pfam03154 158 SDSSAQQQILQTQPPVLqaqSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQgspatsqPPNQTQSTAAPHTLIQqtptl 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742001 431 ---------PSMQPSAVSSPMSESHVQ------ISSEMPRTGMSALPMRPRSQNVDKHRKFPYYNKRNAVTTPSSPYDGA 495
Cdd:pfam03154 238 hpqrlpsphPPLQPMTQPPPPSQVSPQplpqpsLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAA 317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742001 496 qSGSPQFPPFELPPHNYSQAQSPNLATP-SPSFSSLPDVSLPPIVKPNLMsePTPTNSDEKSHALG---------FPPPP 565
Cdd:pfam03154 318 -PGQSQQRIHTPPSQSQLQSQQPPREQPlPPAPLSMPHIKPPPTTPIPQL--PNPQSHKHPPHLSGpspfqmnsnLPPPP 394


                  ...
gi 1246742001 566 GQK 568
Cdd:pfam03154 395 ALK 397
PHA03247 PHA03247
large tegument protein UL36; Provisional
 396-559 2.91e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 2.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742001  396 SALSETPTPVSGngnvadAPPDFSLSQVMPldliAPSMQPSAVSSPMSEShVQISSEMPRTGMS-------ALPMRPRSQ 468
Cdd:PHA03247  2816 AALPPAASPAGP------LPPPTSAQPTAP----PPPPGPPPPSLPLGGS-VAPGGDVRRRPPSrspaakpAAPARPPVR 2884

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742001  469 NVdkhrkfpyynKRNAVTTPSSPYDGAQSGSPQFPPFELP--PHNYSQAQSPNLATPSPSFSSLPDVSLPPIVKPNLMSE 546
Cdd:PHA03247  2885 RL----------ARPAVSRSTESFALPPDQPERPPQPQAPppPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGE 2954

                          170
                   ....*....|...
gi 1246742001  547 PTPTNSDEKSHAL 559
Cdd:PHA03247  2955 PSGAVPQPWLGAL 2967
 
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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