NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|281363408|ref|NP_611010|]
View 

parcas [Drosophila melanogaster]

Protein Classification

SH3BP5 family protein( domain architecture ID 11156898)

SH3BP5 family protein similar to human SH3 domain-binding protein 5 (SH3BP5) that functions as guanine nucleotide exchange factor (GEF) with specificity for RAB11A and RAB25

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
SH3BP5 pfam05276
SH3 domain-binding protein 5 (SH3BP5); This family consists of several eukaryotic SH3 ...
8-235 1.13e-118

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: 346.96  E-value: 1.13e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363408    8 ELDPQIQIELENLNSATDEINKLEIELEEANSTFRILLNESTRRLKVSSKKLGNCIEKARPYYEALDKAREAQIECQKAA 87
Cdd:pfam05276   2 ELDPRIQGELEKLNQATDEINKLEIELEEARSTFRELLAESSRKLKALSKKLGSCIDKARPYYEAKRRAKEAQQESQKAA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363408   88 VKFQRANEIHAAAKETVALAEQRFMsNSHEWQFDNAWQEMLNHATQKVMDAETQKADCHAEHQRLTKLFNAAEQKLQQLE 167
Cdd:pfam05276  82 LRFERANSAHAAAKEMVALAEQGLL-NNDEGTFDPAWQEMLNHATQKVMEAENEKTRAEREHQRKTKLCLAAETKVQQLE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281363408  168 DRFRRSINKSRPYFEEKQVCQDQLQTQKNRIQELQQQVAGAKSTYSTALRNLERISEDIHRQRGDFPT 235
Cdd:pfam05276 161 KKLKRSIKKSRPYFELKAQLNKQLEAQKEKVLQLEEEVKEAKARYSTALRNLEQISEEIHEQRRSEKS 228
 
Name Accession Description Interval E-value
SH3BP5 pfam05276
SH3 domain-binding protein 5 (SH3BP5); This family consists of several eukaryotic SH3 ...
8-235 1.13e-118

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: 346.96  E-value: 1.13e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363408    8 ELDPQIQIELENLNSATDEINKLEIELEEANSTFRILLNESTRRLKVSSKKLGNCIEKARPYYEALDKAREAQIECQKAA 87
Cdd:pfam05276   2 ELDPRIQGELEKLNQATDEINKLEIELEEARSTFRELLAESSRKLKALSKKLGSCIDKARPYYEAKRRAKEAQQESQKAA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363408   88 VKFQRANEIHAAAKETVALAEQRFMsNSHEWQFDNAWQEMLNHATQKVMDAETQKADCHAEHQRLTKLFNAAEQKLQQLE 167
Cdd:pfam05276  82 LRFERANSAHAAAKEMVALAEQGLL-NNDEGTFDPAWQEMLNHATQKVMEAENEKTRAEREHQRKTKLCLAAETKVQQLE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281363408  168 DRFRRSINKSRPYFEEKQVCQDQLQTQKNRIQELQQQVAGAKSTYSTALRNLERISEDIHRQRGDFPT 235
Cdd:pfam05276 161 KKLKRSIKKSRPYFELKAQLNKQLEAQKEKVLQLEEEVKEAKARYSTALRNLEQISEEIHEQRRSEKS 228
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4-226 1.29e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363408     4 AEDGELDPQIQIELENLNSATDEINKLEIELEEanstfrilLNESTRRLKVSSKKLGNCIEkarpyyEALDKAREAQIEC 83
Cdd:TIGR02168  274 LEVSELEEEIEELQKELYALANEISRLEQQKQI--------LRERLANLERQLEELEAQLE------ELESKLDELAEEL 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363408    84 QKAAVKFQRANEIHAAAKETVA-LAEQRFMSNSHEwqfdNAWQEMLNHATQKVMDAETQKADCHAEHQRLtklfnaaEQK 162
Cdd:TIGR02168  340 AELEEKLEELKEELESLEAELEeLEAELEELESRL----EELEEQLETLRSKVAQLELQIASLNNEIERL-------EAR 408
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281363408   163 LQQLEDrfRRSINKSRPYFEEKQVCQDQLQTQKNRIQELQQQVAGAKSTYSTALRNLERISEDI 226
Cdd:TIGR02168  409 LERLED--RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
64-226 7.56e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 7.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363408  64 EKARPYYEALDKAREAQIEcqKAAVKFQRANEIHAAAKETVALAEQRfmsnshewqfdnawqemLNHATQKVMDAETQKA 143
Cdd:COG1196  210 EKAERYRELKEELKELEAE--LLLLKLRELEAELEELEAELEELEAE-----------------LEELEAELAELEAELE 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363408 144 DCHAEHQRLTKLFNAAEQKLQQLEDRFRRSINKSRPYFEEKQVCQDQLQTQKNRIQELQQQVAGAKSTYSTALRNLERIS 223
Cdd:COG1196  271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350

                 ...
gi 281363408 224 EDI 226
Cdd:COG1196  351 EEL 353
 
Name Accession Description Interval E-value
SH3BP5 pfam05276
SH3 domain-binding protein 5 (SH3BP5); This family consists of several eukaryotic SH3 ...
8-235 1.13e-118

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: 346.96  E-value: 1.13e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363408    8 ELDPQIQIELENLNSATDEINKLEIELEEANSTFRILLNESTRRLKVSSKKLGNCIEKARPYYEALDKAREAQIECQKAA 87
Cdd:pfam05276   2 ELDPRIQGELEKLNQATDEINKLEIELEEARSTFRELLAESSRKLKALSKKLGSCIDKARPYYEAKRRAKEAQQESQKAA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363408   88 VKFQRANEIHAAAKETVALAEQRFMsNSHEWQFDNAWQEMLNHATQKVMDAETQKADCHAEHQRLTKLFNAAEQKLQQLE 167
Cdd:pfam05276  82 LRFERANSAHAAAKEMVALAEQGLL-NNDEGTFDPAWQEMLNHATQKVMEAENEKTRAEREHQRKTKLCLAAETKVQQLE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281363408  168 DRFRRSINKSRPYFEEKQVCQDQLQTQKNRIQELQQQVAGAKSTYSTALRNLERISEDIHRQRGDFPT 235
Cdd:pfam05276 161 KKLKRSIKKSRPYFELKAQLNKQLEAQKEKVLQLEEEVKEAKARYSTALRNLEQISEEIHEQRRSEKS 228
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4-226 1.29e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363408     4 AEDGELDPQIQIELENLNSATDEINKLEIELEEanstfrilLNESTRRLKVSSKKLGNCIEkarpyyEALDKAREAQIEC 83
Cdd:TIGR02168  274 LEVSELEEEIEELQKELYALANEISRLEQQKQI--------LRERLANLERQLEELEAQLE------ELESKLDELAEEL 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363408    84 QKAAVKFQRANEIHAAAKETVA-LAEQRFMSNSHEwqfdNAWQEMLNHATQKVMDAETQKADCHAEHQRLtklfnaaEQK 162
Cdd:TIGR02168  340 AELEEKLEELKEELESLEAELEeLEAELEELESRL----EELEEQLETLRSKVAQLELQIASLNNEIERL-------EAR 408
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281363408   163 LQQLEDrfRRSINKSRPYFEEKQVCQDQLQTQKNRIQELQQQVAGAKSTYSTALRNLERISEDI 226
Cdd:TIGR02168  409 LERLED--RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
64-226 7.56e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 7.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363408  64 EKARPYYEALDKAREAQIEcqKAAVKFQRANEIHAAAKETVALAEQRfmsnshewqfdnawqemLNHATQKVMDAETQKA 143
Cdd:COG1196  210 EKAERYRELKEELKELEAE--LLLLKLRELEAELEELEAELEELEAE-----------------LEELEAELAELEAELE 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363408 144 DCHAEHQRLTKLFNAAEQKLQQLEDRFRRSINKSRPYFEEKQVCQDQLQTQKNRIQELQQQVAGAKSTYSTALRNLERIS 223
Cdd:COG1196  271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350

                 ...
gi 281363408 224 EDI 226
Cdd:COG1196  351 EEL 353
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
12-230 8.70e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 8.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363408    12 QIQIELENLNSATDEINKLEIELEEANStfriLLNESTRRLKVSSKKLgNCIEKARpyYEALDKAREAQIECQKAAVKFQ 91
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEE----ELEELTAELQELEEKL-EELRLEV--SELEEEIEELQKELYALANEIS 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363408    92 RANEIHAAAKETVALAEQRFMSNSHEWQfdnAWQEMLNHATQKVMDAETQKADCHAEHQRLTKLFNAAEQKLQQLEDRFR 171
Cdd:TIGR02168  299 RLEQQKQILRERLANLERQLEELEAQLE---ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 281363408   172 RsinksrpyfeekqvCQDQLQTQKNRIQELQQQVAGAKSTYSTALRNLERISEDIHRQR 230
Cdd:TIGR02168  376 E--------------LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ 420
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH