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Conserved domains on  [gi|323310282|gb|EGA63472|]
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Bud14p [Saccharomyces cerevisiae FostersO]

Protein Classification

SH3_1 domain-containing protein( domain architecture ID 10439896)

SH3_1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 266-312 2.64e-08

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


:

Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 50.28  E-value: 2.64e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 323310282  266 ALYAFNGHDSSHCQLGQDEPCILLNDQDAYWWLVKRITdGKIGFAPA 312
Cdd:pfam00018   2 ALYDYTAQEPDELSFKKGDIIIVLEKSEDGWWKGRNKG-GKEGLIPS 47
 
Name Accession Description Interval E-value
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 266-312 2.64e-08

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 50.28  E-value: 2.64e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 323310282  266 ALYAFNGHDSSHCQLGQDEPCILLNDQDAYWWLVKRITdGKIGFAPA 312
Cdd:pfam00018   2 ALYDYTAQEPDELSFKKGDIIIVLEKSEDGWWKGRNKG-GKEGLIPS 47
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 260-316 9.54e-07

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 45.99  E-value: 9.54e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 323310282   260 DPDKLYALYAFNGHDSSHCQLGQDEPCILLNDQDAYWWLVKRItDGKIGFAPAEILE 316
Cdd:smart00326   1 EGPQVRALYDYTAQDPDELSFKKGDIITVLEKSDDGWWKGRLG-RGKEGLFPSNYVE 56
SH3_SPIN90 cd11849
Src homology 3 domain of SH3 protein interacting with Nck, 90 kDa (SPIN90); SPIN90 is also ...
 264-316 1.93e-06

Src homology 3 domain of SH3 protein interacting with Nck, 90 kDa (SPIN90); SPIN90 is also called NCK interacting protein with SH3 domain (NCKIPSD), Dia-interacting protein (DIP), 54 kDa vimentin-interacting protein (VIP54), or WASP-interacting SH3-domain protein (WISH). It is an F-actin binding protein that regulates actin polymerization and endocytosis. It associates with the Arp2/3 complex near actin filaments and determines filament localization at the leading edge of lamellipodia. SPIN90 is expressed in the early stages of neuronal differentiation and plays a role in regulating growth cone dynamics and neurite outgrowth. It also interacts with IRSp53 and regulates cell motility by playing a role in the formation of membrane protrusions. SPIN90 contains an N-terminal SH3 domain, a proline-rich domain, and a C-terminal VCA (verprolin-homology and cofilin-like acidic) domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212783 [Multi-domain]  Cd Length: 53  Bit Score: 45.00  E-value: 1.93e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 323310282 264 LYALYAFNGHDSSHCQLGQDEPCILLNDQDAYWWLVKRITdGKIGFAPAEILE 316
Cdd:cd11849    2 YRALYDFKSAEPNTLSFSEGETFLLLERSNAHWWLVTNHS-GETGYVPANYVK 53
 
Name Accession Description Interval E-value
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 266-312 2.64e-08

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 50.28  E-value: 2.64e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 323310282  266 ALYAFNGHDSSHCQLGQDEPCILLNDQDAYWWLVKRITdGKIGFAPA 312
Cdd:pfam00018   2 ALYDYTAQEPDELSFKKGDIIIVLEKSEDGWWKGRNKG-GKEGLIPS 47
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 260-316 9.54e-07

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 45.99  E-value: 9.54e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 323310282   260 DPDKLYALYAFNGHDSSHCQLGQDEPCILLNDQDAYWWLVKRItDGKIGFAPAEILE 316
Cdd:smart00326   1 EGPQVRALYDYTAQDPDELSFKKGDIITVLEKSDDGWWKGRLG-RGKEGLFPSNYVE 56
SH3_SPIN90 cd11849
Src homology 3 domain of SH3 protein interacting with Nck, 90 kDa (SPIN90); SPIN90 is also ...
 264-316 1.93e-06

Src homology 3 domain of SH3 protein interacting with Nck, 90 kDa (SPIN90); SPIN90 is also called NCK interacting protein with SH3 domain (NCKIPSD), Dia-interacting protein (DIP), 54 kDa vimentin-interacting protein (VIP54), or WASP-interacting SH3-domain protein (WISH). It is an F-actin binding protein that regulates actin polymerization and endocytosis. It associates with the Arp2/3 complex near actin filaments and determines filament localization at the leading edge of lamellipodia. SPIN90 is expressed in the early stages of neuronal differentiation and plays a role in regulating growth cone dynamics and neurite outgrowth. It also interacts with IRSp53 and regulates cell motility by playing a role in the formation of membrane protrusions. SPIN90 contains an N-terminal SH3 domain, a proline-rich domain, and a C-terminal VCA (verprolin-homology and cofilin-like acidic) domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212783 [Multi-domain]  Cd Length: 53  Bit Score: 45.00  E-value: 1.93e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 323310282 264 LYALYAFNGHDSSHCQLGQDEPCILLNDQDAYWWLVKRITdGKIGFAPAEILE 316
Cdd:cd11849    2 YRALYDFKSAEPNTLSFSEGETFLLLERSNAHWWLVTNHS-GETGYVPANYVK 53
SH3_Myosin-I_fungi cd11858
Src homology 3 domain of Type I fungal Myosins; Type I myosins (myosin-I) are actin-dependent ...
 266-316 1.78e-05

Src homology 3 domain of Type I fungal Myosins; Type I myosins (myosin-I) are actin-dependent motors in endocytic actin structures and actin patches. They play roles in membrane traffic in endocytic and secretory pathways, cell motility, and mechanosensing. Saccharomyces cerevisiae has two myosins-I, Myo3 and Myo5, which are involved in endocytosis and the polarization of the actin cytoskeleton. Myosin-I contains an N-terminal actin-activated ATPase, a phospholipid-binding TH1 (tail homology 1) domain, and a C-terminal extension which includes an F-actin-binding TH2 domain, an SH3 domain, and an acidic peptide that participates in activating the Arp2/3complex. The SH3 domain of myosin-I is required for myosin-I-induced actin polymerization. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212792 [Multi-domain]  Cd Length: 55  Bit Score: 42.37  E-value: 1.78e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 323310282 266 ALYAFNGHDSSHCQLGQDEPCILLNDQDAYWWLVKRITDGKIGFAPAEILE 316
Cdd:cd11858    4 ALYDFAGSVANELSLKKDDIVYIVQKEDNGWWLAKKLDESKEGWVPAAYLE 54
 
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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