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Conserved domains on  [gi|1002280094|ref|XP_015644354|]
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protein HOMOLOG OF MAMMALIAN LYST-INTERACTING PROTEIN 5 [Oryza sativa Japonica Group]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Vta1 pfam04652
Vta1 like; Vta1 (VPS20-associated protein 1) is a positive regulator of Vps4. Vps4 is an ...
 16-142 1.05e-57

Vta1 like; Vta1 (VPS20-associated protein 1) is a positive regulator of Vps4. Vps4 is an ATPase that is required in the multivesicular body (MVB) sorting pathway to dissociate the endosomal sorting complex required for transport (ESCRT). Vta1 promotes correct assembly of Vps4 and stimulates its ATPase activity through its conserved Vta1/SBP1/LIP5 region.


:

Pssm-ID: 461380  Cd Length: 133  Bit Score: 187.39  E-value: 1.05e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280094  16 QRADELQKHEPLVAYYCRLYAMEKGMRIPQKERTKTTNSLLISLMNQLEKDKKSL---TLGSDD---HLHVEGFALNVFA 89
Cdd:pfam04652   1 KRAQELEKADPVVAYYCRLYAVQQILKLGLHKKDKEVRAFLTKLLDKLEQFKKELgdnEAITDEvaaQAYVENFALKLFN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1002280094  90 KADKQDRAGRADINTAKTFYAASIFFEILNQFGELQTDVEQKQKYAIWKAAEI 142
Cdd:pfam04652  81 RADKEDRAGRATKQTAKTFYAAATFFEVLQIFGELDEEIAKKIKYAKWKAARI 133
Vta1_C pfam18097
Vta1 C-terminal domain; This is the C-terminal domain of Vta1 proteins pfam04652. Structural ...
 444-481 2.50e-08

Vta1 C-terminal domain; This is the C-terminal domain of Vta1 proteins pfam04652. Structural and functional analysis indicate that this C-terminal domain promotes the ATP-dependent double ring assembly of Vps4. Furthermore, it has been shown that it is necessary and sufficient for protein dimerization. Mutations in Lys-299 and Lys-302 completely abolished the ability of Vta1 to stimulate the ATPase activity of Vps4 while mutation in Lys-322 had no effect.


:

Pssm-ID: 465647  Cd Length: 38  Bit Score: 49.59  E-value: 2.50e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1002280094 444 VEKIAEAHKAARFAVGALAFDDVSVAVDHLKRALDLLT 481
Cdd:pfam18097   1 PDQIAQAQKHAKYAVSALQFDDVETAIKNLLKALKLLT 38
PTZ00395 super family cl33180
Sec24-related protein; Provisional
 267-403 1.89e-04

Sec24-related protein; Provisional


The actual alignment was detected with superfamily member PTZ00395:

Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 44.30  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280094  267 YPSSDVHKPPH---GYSSAPYTSTDY--PTNEvHKPPSN--YSSPPYTRTDYPSSDSYNPQ-SNDKPDIPTYPHTYHQPP 338
Cdd:PTZ00395   409 FSNAGYSNPGNsnpGYNNAPNSNTPYnnPPNS-NTPYSNppNSNPPYSNLPYSNTPYSNAPlSNAPPSSAKDHHSAYHAA 487

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002280094  339 YtiepQHTSQNYYSTETPAApyNYSNFQSYPSFQDSSVPSVPTHQSSFYPASDGTSAVSYSPSGS 403
Cdd:PTZ00395   488 Y----QHRAANQPAANLPTA--NQPAANNFHGAAGNSVGNPFASRPFGSAPYGGNAATTADPNGI 546
 
Name Accession Description Interval E-value
Vta1 pfam04652
Vta1 like; Vta1 (VPS20-associated protein 1) is a positive regulator of Vps4. Vps4 is an ...
 16-142 1.05e-57

Vta1 like; Vta1 (VPS20-associated protein 1) is a positive regulator of Vps4. Vps4 is an ATPase that is required in the multivesicular body (MVB) sorting pathway to dissociate the endosomal sorting complex required for transport (ESCRT). Vta1 promotes correct assembly of Vps4 and stimulates its ATPase activity through its conserved Vta1/SBP1/LIP5 region.


Pssm-ID: 461380  Cd Length: 133  Bit Score: 187.39  E-value: 1.05e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280094  16 QRADELQKHEPLVAYYCRLYAMEKGMRIPQKERTKTTNSLLISLMNQLEKDKKSL---TLGSDD---HLHVEGFALNVFA 89
Cdd:pfam04652   1 KRAQELEKADPVVAYYCRLYAVQQILKLGLHKKDKEVRAFLTKLLDKLEQFKKELgdnEAITDEvaaQAYVENFALKLFN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1002280094  90 KADKQDRAGRADINTAKTFYAASIFFEILNQFGELQTDVEQKQKYAIWKAAEI 142
Cdd:pfam04652  81 RADKEDRAGRATKQTAKTFYAAATFFEVLQIFGELDEEIAKKIKYAKWKAARI 133
Vta1_C pfam18097
Vta1 C-terminal domain; This is the C-terminal domain of Vta1 proteins pfam04652. Structural ...
 444-481 2.50e-08

Vta1 C-terminal domain; This is the C-terminal domain of Vta1 proteins pfam04652. Structural and functional analysis indicate that this C-terminal domain promotes the ATP-dependent double ring assembly of Vps4. Furthermore, it has been shown that it is necessary and sufficient for protein dimerization. Mutations in Lys-299 and Lys-302 completely abolished the ability of Vta1 to stimulate the ATPase activity of Vps4 while mutation in Lys-322 had no effect.


Pssm-ID: 465647  Cd Length: 38  Bit Score: 49.59  E-value: 2.50e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1002280094 444 VEKIAEAHKAARFAVGALAFDDVSVAVDHLKRALDLLT 481
Cdd:pfam18097   1 PDQIAQAQKHAKYAVSALQFDDVETAIKNLLKALKLLT 38
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 267-403 1.89e-04

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 44.30  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280094  267 YPSSDVHKPPH---GYSSAPYTSTDY--PTNEvHKPPSN--YSSPPYTRTDYPSSDSYNPQ-SNDKPDIPTYPHTYHQPP 338
Cdd:PTZ00395   409 FSNAGYSNPGNsnpGYNNAPNSNTPYnnPPNS-NTPYSNppNSNPPYSNLPYSNTPYSNAPlSNAPPSSAKDHHSAYHAA 487

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002280094  339 YtiepQHTSQNYYSTETPAApyNYSNFQSYPSFQDSSVPSVPTHQSSFYPASDGTSAVSYSPSGS 403
Cdd:PTZ00395   488 Y----QHRAANQPAANLPTA--NQPAANNFHGAAGNSVGNPFASRPFGSAPYGGNAATTADPNGI 546
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 275-433 5.24e-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: 39.37  E-value: 5.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280094 275 PPHGYSSAPYTSTDYPTNEVHKPPSNYSSPPYTRTDYP--------SSDSYNPQSNDKPDIPTYPHTYHQPPYTIEPQHT 346
Cdd:pfam03154 187 PPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTaaphtliqQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPL 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280094 347 SQNYYSTETPAAPYnysNFQSYPSFQDSSVPSVPTHQSSfypasdgTSAVSYSPSGSNHPAPTQYHPSADTTTHQVTPPA 426
Cdd:pfam03154 267 PQPSLHGQMPPMPH---SLQTGPSHMQHPVPPQPFPLTP-------QSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQS 336


                  ....*..
gi 1002280094 427 IAPPASQ 433
Cdd:pfam03154 337 QQPPREQ 343
 
Name Accession Description Interval E-value
Vta1 pfam04652
Vta1 like; Vta1 (VPS20-associated protein 1) is a positive regulator of Vps4. Vps4 is an ...
 16-142 1.05e-57

Vta1 like; Vta1 (VPS20-associated protein 1) is a positive regulator of Vps4. Vps4 is an ATPase that is required in the multivesicular body (MVB) sorting pathway to dissociate the endosomal sorting complex required for transport (ESCRT). Vta1 promotes correct assembly of Vps4 and stimulates its ATPase activity through its conserved Vta1/SBP1/LIP5 region.


Pssm-ID: 461380  Cd Length: 133  Bit Score: 187.39  E-value: 1.05e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280094  16 QRADELQKHEPLVAYYCRLYAMEKGMRIPQKERTKTTNSLLISLMNQLEKDKKSL---TLGSDD---HLHVEGFALNVFA 89
Cdd:pfam04652   1 KRAQELEKADPVVAYYCRLYAVQQILKLGLHKKDKEVRAFLTKLLDKLEQFKKELgdnEAITDEvaaQAYVENFALKLFN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1002280094  90 KADKQDRAGRADINTAKTFYAASIFFEILNQFGELQTDVEQKQKYAIWKAAEI 142
Cdd:pfam04652  81 RADKEDRAGRATKQTAKTFYAAATFFEVLQIFGELDEEIAKKIKYAKWKAARI 133
Vta1_C pfam18097
Vta1 C-terminal domain; This is the C-terminal domain of Vta1 proteins pfam04652. Structural ...
 444-481 2.50e-08

Vta1 C-terminal domain; This is the C-terminal domain of Vta1 proteins pfam04652. Structural and functional analysis indicate that this C-terminal domain promotes the ATP-dependent double ring assembly of Vps4. Furthermore, it has been shown that it is necessary and sufficient for protein dimerization. Mutations in Lys-299 and Lys-302 completely abolished the ability of Vta1 to stimulate the ATPase activity of Vps4 while mutation in Lys-322 had no effect.


Pssm-ID: 465647  Cd Length: 38  Bit Score: 49.59  E-value: 2.50e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1002280094 444 VEKIAEAHKAARFAVGALAFDDVSVAVDHLKRALDLLT 481
Cdd:pfam18097   1 PDQIAQAQKHAKYAVSALQFDDVETAIKNLLKALKLLT 38
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 267-403 1.89e-04

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 44.30  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280094  267 YPSSDVHKPPH---GYSSAPYTSTDY--PTNEvHKPPSN--YSSPPYTRTDYPSSDSYNPQ-SNDKPDIPTYPHTYHQPP 338
Cdd:PTZ00395   409 FSNAGYSNPGNsnpGYNNAPNSNTPYnnPPNS-NTPYSNppNSNPPYSNLPYSNTPYSNAPlSNAPPSSAKDHHSAYHAA 487

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002280094  339 YtiepQHTSQNYYSTETPAApyNYSNFQSYPSFQDSSVPSVPTHQSSFYPASDGTSAVSYSPSGS 403
Cdd:PTZ00395   488 Y----QHRAANQPAANLPTA--NQPAANNFHGAAGNSVGNPFASRPFGSAPYGGNAATTADPNGI 546
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 275-433 5.24e-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: 39.37  E-value: 5.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280094 275 PPHGYSSAPYTSTDYPTNEVHKPPSNYSSPPYTRTDYP--------SSDSYNPQSNDKPDIPTYPHTYHQPPYTIEPQHT 346
Cdd:pfam03154 187 PPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTaaphtliqQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPL 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280094 347 SQNYYSTETPAAPYnysNFQSYPSFQDSSVPSVPTHQSSfypasdgTSAVSYSPSGSNHPAPTQYHPSADTTTHQVTPPA 426
Cdd:pfam03154 267 PQPSLHGQMPPMPH---SLQTGPSHMQHPVPPQPFPLTP-------QSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQS 336


                  ....*..
gi 1002280094 427 IAPPASQ 433
Cdd:pfam03154 337 QQPPREQ 343
 
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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