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Conserved domains on  [gi|22945458|gb|AAF51356|]
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RAB3 GTPase activating protein catalytic subunit 1 [Drosophila melanogaster]

Protein Classification

rab3 GTPase-activating protein catalytic subunit( domain architecture ID 10620847)

rab3 GTPase-activating protein catalytic subunit specifically converts active Rab3-GTP to the inactive form Rab3-GDP

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Rab3-GTPase_cat pfam13890
Rab3 GTPase-activating protein catalytic subunit; This family is the probable catalytic ...
578-726 1.01e-72

Rab3 GTPase-activating protein catalytic subunit; This family is the probable catalytic subunit of the GTPase activating protein that has specificity for Rab3 subfamily (RAB3A, RAB3B, RAB3C and RAB3D). It is likely to convert active Rab3-GTP to the inactive form Rab3-GDP. Rab3 proteins are involved in regulated exocytosis of neurotransmitters and hormones. The Rab3 GTPase-activating complex is a heterodimer composed of RAB3GAP and RAB3-GAP150. This complex interacts with DMXL2.


:

Pssm-ID: 464022  Cd Length: 158  Bit Score: 236.00  E-value: 1.01e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22945458   578 KPEGRLRRLNNERLLEEPdEYLYIPDTQEPVPKTEDQLQDDAEVMLKLG---PGSGLTTQMMCTSLLSDMEAFKAANPRG 654
Cdd:pfam13890   4 EREGRLGPVGNLRLLETG-EPLYAPVTQEPPPMTEDMLEERAEALEALGssaSGSHLRAQLQSASLLSDMEAFKAANPGA 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22945458   655 IMEDFIRWYSPKDW--EEVTDELGQVK--HQLSIRMTTEGNTWQKVWEQAQAVPVSRQKRLFDDTNEALKVLHYLE 726
Cdd:pfam13890  83 VLEDFVRWHSPRDWieEEGDDETGKESseGRLSERMREEGNLWQELWERAKPVPASRQKPLFDPTREAEKVLHYLE 158
 
Name Accession Description Interval E-value
Rab3-GTPase_cat pfam13890
Rab3 GTPase-activating protein catalytic subunit; This family is the probable catalytic ...
578-726 1.01e-72

Rab3 GTPase-activating protein catalytic subunit; This family is the probable catalytic subunit of the GTPase activating protein that has specificity for Rab3 subfamily (RAB3A, RAB3B, RAB3C and RAB3D). It is likely to convert active Rab3-GTP to the inactive form Rab3-GDP. Rab3 proteins are involved in regulated exocytosis of neurotransmitters and hormones. The Rab3 GTPase-activating complex is a heterodimer composed of RAB3GAP and RAB3-GAP150. This complex interacts with DMXL2.


Pssm-ID: 464022  Cd Length: 158  Bit Score: 236.00  E-value: 1.01e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22945458   578 KPEGRLRRLNNERLLEEPdEYLYIPDTQEPVPKTEDQLQDDAEVMLKLG---PGSGLTTQMMCTSLLSDMEAFKAANPRG 654
Cdd:pfam13890   4 EREGRLGPVGNLRLLETG-EPLYAPVTQEPPPMTEDMLEERAEALEALGssaSGSHLRAQLQSASLLSDMEAFKAANPGA 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22945458   655 IMEDFIRWYSPKDW--EEVTDELGQVK--HQLSIRMTTEGNTWQKVWEQAQAVPVSRQKRLFDDTNEALKVLHYLE 726
Cdd:pfam13890  83 VLEDFVRWHSPRDWieEEGDDETGKESseGRLSERMREEGNLWQELWERAKPVPASRQKPLFDPTREAEKVLHYLE 158
 
Name Accession Description Interval E-value
Rab3-GTPase_cat pfam13890
Rab3 GTPase-activating protein catalytic subunit; This family is the probable catalytic ...
578-726 1.01e-72

Rab3 GTPase-activating protein catalytic subunit; This family is the probable catalytic subunit of the GTPase activating protein that has specificity for Rab3 subfamily (RAB3A, RAB3B, RAB3C and RAB3D). It is likely to convert active Rab3-GTP to the inactive form Rab3-GDP. Rab3 proteins are involved in regulated exocytosis of neurotransmitters and hormones. The Rab3 GTPase-activating complex is a heterodimer composed of RAB3GAP and RAB3-GAP150. This complex interacts with DMXL2.


Pssm-ID: 464022  Cd Length: 158  Bit Score: 236.00  E-value: 1.01e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22945458   578 KPEGRLRRLNNERLLEEPdEYLYIPDTQEPVPKTEDQLQDDAEVMLKLG---PGSGLTTQMMCTSLLSDMEAFKAANPRG 654
Cdd:pfam13890   4 EREGRLGPVGNLRLLETG-EPLYAPVTQEPPPMTEDMLEERAEALEALGssaSGSHLRAQLQSASLLSDMEAFKAANPGA 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22945458   655 IMEDFIRWYSPKDW--EEVTDELGQVK--HQLSIRMTTEGNTWQKVWEQAQAVPVSRQKRLFDDTNEALKVLHYLE 726
Cdd:pfam13890  83 VLEDFVRWHSPRDWieEEGDDETGKESseGRLSERMREEGNLWQELWERAKPVPASRQKPLFDPTREAEKVLHYLE 158
 
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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