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Conserved domains on  [gi|109134344|ref|NP_001018009|]
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SH3 domain-binding protein 5 isoform b [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SH3BP5 super family cl24176
SH3 domain-binding protein 5 (SH3BP5); This family consists of several eukaryotic SH3 ...
 1-112 2.26e-45

SH3 domain-binding protein 5 (SH3BP5); This family consists of several eukaryotic SH3 domain-binding protein 5 or c-Jun N-terminal kinase (JNK)-interacting proteins (SH3BP5 or Sab). Sab binds to and serves as a substrate for JNK in vitro, and has been found to interact with the Src homology 3 (SH3) domain of Bruton's tyrosine kinase (Btk). Inspection of the sequence of Sab reveals the presence of two putative mitogen-activated protein kinase interaction motifs (KIMs) similar to that found in the JNK docking domain of the c-Jun transcription factor, and four potential serine-proline JNK phosphorylation sites in the C-terminal half of the molecule.


The actual alignment was detected with superfamily member pfam05276:

Pssm-ID: 461608 [Multi-domain]  Cd Length: 231  Bit Score: 153.21  E-value: 2.26e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134344    1 MLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLT 80
Cdd:pfam05276 120 MLNHATQKVMEAENEKTRAEREHQRKTKLCLAAETKVQQLEKKLKRSIKKSRPYFELKAQLNKQLEAQKEKVLQLEEEVK 199

                          90       100       110
                  ....*....|....*....|....*....|..
gi 109134344   81 LAKGEYKMALKNLEMISDEIHERRRSSAMGPR 112
Cdd:pfam05276 200 EAKARYSTALRNLEQISEEIHEQRRSEKSEPP 231
 
Name Accession Description Interval E-value
SH3BP5 pfam05276
SH3 domain-binding protein 5 (SH3BP5); This family consists of several eukaryotic SH3 ...
 1-112 2.26e-45

SH3 domain-binding protein 5 (SH3BP5); This family consists of several eukaryotic SH3 domain-binding protein 5 or c-Jun N-terminal kinase (JNK)-interacting proteins (SH3BP5 or Sab). Sab binds to and serves as a substrate for JNK in vitro, and has been found to interact with the Src homology 3 (SH3) domain of Bruton's tyrosine kinase (Btk). Inspection of the sequence of Sab reveals the presence of two putative mitogen-activated protein kinase interaction motifs (KIMs) similar to that found in the JNK docking domain of the c-Jun transcription factor, and four potential serine-proline JNK phosphorylation sites in the C-terminal half of the molecule.


Pssm-ID: 461608 [Multi-domain]  Cd Length: 231  Bit Score: 153.21  E-value: 2.26e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134344    1 MLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLT 80
Cdd:pfam05276 120 MLNHATQKVMEAENEKTRAEREHQRKTKLCLAAETKVQQLEKKLKRSIKKSRPYFELKAQLNKQLEAQKEKVLQLEEEVK 199

                          90       100       110
                  ....*....|....*....|....*....|..
gi 109134344   81 LAKGEYKMALKNLEMISDEIHERRRSSAMGPR 112
Cdd:pfam05276 200 EAKARYSTALRNLEQISEEIHEQRRSEKSEPP 231
 
Name Accession Description Interval E-value
SH3BP5 pfam05276
SH3 domain-binding protein 5 (SH3BP5); This family consists of several eukaryotic SH3 ...
 1-112 2.26e-45

SH3 domain-binding protein 5 (SH3BP5); This family consists of several eukaryotic SH3 domain-binding protein 5 or c-Jun N-terminal kinase (JNK)-interacting proteins (SH3BP5 or Sab). Sab binds to and serves as a substrate for JNK in vitro, and has been found to interact with the Src homology 3 (SH3) domain of Bruton's tyrosine kinase (Btk). Inspection of the sequence of Sab reveals the presence of two putative mitogen-activated protein kinase interaction motifs (KIMs) similar to that found in the JNK docking domain of the c-Jun transcription factor, and four potential serine-proline JNK phosphorylation sites in the C-terminal half of the molecule.


Pssm-ID: 461608 [Multi-domain]  Cd Length: 231  Bit Score: 153.21  E-value: 2.26e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134344    1 MLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLT 80
Cdd:pfam05276 120 MLNHATQKVMEAENEKTRAEREHQRKTKLCLAAETKVQQLEKKLKRSIKKSRPYFELKAQLNKQLEAQKEKVLQLEEEVK 199

                          90       100       110
                  ....*....|....*....|....*....|..
gi 109134344   81 LAKGEYKMALKNLEMISDEIHERRRSSAMGPR 112
Cdd:pfam05276 200 EAKARYSTALRNLEQISEEIHEQRRSEKSEPP 231
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 1-105 6.85e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 37.91  E-value: 6.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134344    1 MLNHATQR----VMEAEQTKTRSELVHKETAaRYNAAMGRMRQLEKKL----KRAINKSKPYFELKAKY---YVQLEQLK 69
Cdd:pfam06160 299 YLEHAEEQnkelKEELERVQQSYTLNENELE-RVRGLEKQLEELEKRYdeivERLEEKEVAYSELQEELeeiLEQLEEIE 377

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 109134344   70 KTVDDLQAKL-TLAKGEyKMALKNLEMISDEIHERRR 105
Cdd:pfam06160 378 EEQEEFKESLqSLRKDE-LEAREKLDEFKLELREIKR 413
 
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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