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Conserved domains on  [gi|330443674|ref|NP_013417|]
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Sph1p [Saccharomyces cerevisiae S288C]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GIT smart00555
Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins; Helical ...
 89-119 1.18e-06

Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins; Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins, and in yeast Spa2p and Sph1p (CPP; unpublished results). In p95-APP1 the N-terminal GIT motif might be involved in binding PIX.


:

Pssm-ID: 128828  Cd Length: 31  Bit Score: 44.85  E-value: 1.18e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 330443674    89 AQSKLSRLKDAKFHKLILDIFTEIERRNLHH 119
Cdd:smart00555   1 ARQKLARLSDEQFQKLLTDLNDELKRRENEA 31
GIT smart00555
Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins; Helical ...
 45-73 2.28e-06

Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins; Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins, and in yeast Spa2p and Sph1p (CPP; unpublished results). In p95-APP1 the N-terminal GIT motif might be involved in binding PIX.


:

Pssm-ID: 128828  Cd Length: 31  Bit Score: 44.07  E-value: 2.28e-06
                           10        20
                   ....*....|....*....|....*....
gi 330443674    45 KDLTKLSNVQFWQLTTDVNDELMKRLTDS 73
Cdd:smart00555   3 QKLARLSDEQFQKLLTDLNDELKRRENEA 31
 
Name Accession Description Interval E-value
GIT smart00555
Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins; Helical ...
 89-119 1.18e-06

Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins; Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins, and in yeast Spa2p and Sph1p (CPP; unpublished results). In p95-APP1 the N-terminal GIT motif might be involved in binding PIX.


Pssm-ID: 128828  Cd Length: 31  Bit Score: 44.85  E-value: 1.18e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 330443674    89 AQSKLSRLKDAKFHKLILDIFTEIERRNLHH 119
Cdd:smart00555   1 ARQKLARLSDEQFQKLLTDLNDELKRRENEA 31
GIT smart00555
Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins; Helical ...
 45-73 2.28e-06

Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins; Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins, and in yeast Spa2p and Sph1p (CPP; unpublished results). In p95-APP1 the N-terminal GIT motif might be involved in binding PIX.


Pssm-ID: 128828  Cd Length: 31  Bit Score: 44.07  E-value: 2.28e-06
                           10        20
                   ....*....|....*....|....*....
gi 330443674    45 KDLTKLSNVQFWQLTTDVNDELMKRLTDS 73
Cdd:smart00555   3 QKLARLSDEQFQKLLTDLNDELKRRENEA 31
GIT_SHD pfam08518
Spa2 homology domain (SHD) of GIT; GIT proteins are signaling integrators with ...
 47-71 2.55e-03

Spa2 homology domain (SHD) of GIT; GIT proteins are signaling integrators with GTPase-activating function which may be involved in the organization of the cytoskeletal matrix assembled at active zones (CAZ). The function of the CAZ might be to define sites of neurotransmitter release. Mutations in the Spa2 homology domain (SHD) domain of GIT1 described here interfere with the association of GIT1 with Piccolo, beta-PIX, and focal adhesion kinase.


Pssm-ID: 462506  Cd Length: 29  Bit Score: 35.45  E-value: 2.55e-03
                          10        20
                  ....*....|....*....|....*
gi 330443674   47 LTKLSNVQFWQLTTDVNDELMKRLT 71
Cdd:pfam08518   5 LARLSNQQFEELVTDVYDELDRRQT 29
 
Name Accession Description Interval E-value
GIT smart00555
Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins; Helical ...
 89-119 1.18e-06

Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins; Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins, and in yeast Spa2p and Sph1p (CPP; unpublished results). In p95-APP1 the N-terminal GIT motif might be involved in binding PIX.


Pssm-ID: 128828  Cd Length: 31  Bit Score: 44.85  E-value: 1.18e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 330443674    89 AQSKLSRLKDAKFHKLILDIFTEIERRNLHH 119
Cdd:smart00555   1 ARQKLARLSDEQFQKLLTDLNDELKRRENEA 31
GIT smart00555
Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins; Helical ...
 45-73 2.28e-06

Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins; Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins, and in yeast Spa2p and Sph1p (CPP; unpublished results). In p95-APP1 the N-terminal GIT motif might be involved in binding PIX.


Pssm-ID: 128828  Cd Length: 31  Bit Score: 44.07  E-value: 2.28e-06
                           10        20
                   ....*....|....*....|....*....
gi 330443674    45 KDLTKLSNVQFWQLTTDVNDELMKRLTDS 73
Cdd:smart00555   3 QKLARLSDEQFQKLLTDLNDELKRRENEA 31
GIT_SHD pfam08518
Spa2 homology domain (SHD) of GIT; GIT proteins are signaling integrators with ...
 47-71 2.55e-03

Spa2 homology domain (SHD) of GIT; GIT proteins are signaling integrators with GTPase-activating function which may be involved in the organization of the cytoskeletal matrix assembled at active zones (CAZ). The function of the CAZ might be to define sites of neurotransmitter release. Mutations in the Spa2 homology domain (SHD) domain of GIT1 described here interfere with the association of GIT1 with Piccolo, beta-PIX, and focal adhesion kinase.


Pssm-ID: 462506  Cd Length: 29  Bit Score: 35.45  E-value: 2.55e-03
                          10        20
                  ....*....|....*....|....*
gi 330443674   47 LTKLSNVQFWQLTTDVNDELMKRLT 71
Cdd:pfam08518   5 LARLSNQQFEELVTDVYDELDRRQT 29
 
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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