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Conserved domains on  [gi|109134336|ref|NP_004835|]
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SH3 domain-binding protein 5 isoform a [Homo sapiens]

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

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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 ...
41-269 9.16e-107

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: 315.76  E-value: 9.16e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336   41 VDPRIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELVKKIGKAVEDSKPYWEARRVARQAQLEAQKATQ 120
Cdd:pfam05276   3 LDPRIQGELEKLNQATDEINKLEIELEEARSTFRELLAESSRKLKALSKKLGSCIDKARPYYEAKRRAKEAQQESQKAAL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336  121 DFQRATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKK 200
Cdd:pfam05276  83 RFERANSAHAAAKEMVALAEQGLLNNDEGTFDPAWQEMLNHATQKVMEAENEKTRAEREHQRKTKLCLAAETKVQQLEKK 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109134336  201 LKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIHERRRSSAMGPR 269
Cdd:pfam05276 163 LKRSIKKSRPYFELKAQLNKQLEAQKEKVLQLEEEVKEAKARYSTALRNLEQISEEIHEQRRSEKSEPP 231
 
Name Accession Description Interval E-value
SH3BP5 pfam05276
SH3 domain-binding protein 5 (SH3BP5); This family consists of several eukaryotic SH3 ...
41-269 9.16e-107

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: 315.76  E-value: 9.16e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336   41 VDPRIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELVKKIGKAVEDSKPYWEARRVARQAQLEAQKATQ 120
Cdd:pfam05276   3 LDPRIQGELEKLNQATDEINKLEIELEEARSTFRELLAESSRKLKALSKKLGSCIDKARPYYEAKRRAKEAQQESQKAAL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336  121 DFQRATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKK 200
Cdd:pfam05276  83 RFERANSAHAAAKEMVALAEQGLLNNDEGTFDPAWQEMLNHATQKVMEAENEKTRAEREHQRKTKLCLAAETKVQQLEKK 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109134336  201 LKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIHERRRSSAMGPR 269
Cdd:pfam05276 163 LKRSIKKSRPYFELKAQLNKQLEAQKEKVLQLEEEVKEAKARYSTALRNLEQISEEIHEQRRSEKSEPP 231
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
42-264 7.62e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 7.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336   42 DPRIQGELEKLNQSTDDINRRETELEDARQKFR--SVLVEATVKLDELVKKIGK--AVEDSKPYWEARRVARQAQLEAQK 117
Cdd:COG4913   220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAEleYLRAALRLWFAQRRLELLEAELEE 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336  118 ATQDFQRATEVLRAAKETISLAEQRLleddkrqfDSAWQEMLNHATQRVMEAEQtktrsELVHKE-TAARYNAAMGRMRQ 196
Cdd:COG4913   300 LRAELARLEAELERLEARLDALREEL--------DELEAQIRGNGGDRLEQLER-----EIERLErELEERERRRARLEA 366
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109134336  197 LEKKLKRAINKSKPYF-ELKAKYYVQLEQLKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIH--ERRRSS 264
Cdd:COG4913   367 LLAALGLPLPASAEEFaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslERRKSN 437
PTZ00121 PTZ00121
MAEBL; Provisional
79-262 3.90e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336   79 EATVKLDELVK-KIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQRATEVlRAAKETISLAEQRLLEDDKRQFDSAWQE 157
Cdd:PTZ00121 1507 EAKKKADEAKKaEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL-KKAEEKKKAEEAKKAEEDKNMALRKAEE 1585
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336  158 MLNHATQRVMEA-----EQTKTRSELVHKETAARYNAAMGR--------MRQLEKKLKRAINKSKPYFELKAKYYVQLEQ 224
Cdd:PTZ00121 1586 AKKAEEARIEEVmklyeEEKKMKAEEAKKAEEAKIKAEELKkaeeekkkVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 109134336  225 LKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIHERRR 262
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
60-262 4.53e-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: 39.65  E-value: 4.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336    60 NRRETE--LEDAR---QKFRSVLVEatvkLDELVKKIGKAVEDSKPYWEARRVARQAQLEAqkATQDFQRATEVLRAAKE 134
Cdd:TIGR02168  173 RRKETErkLERTRenlDRLEDILNE----LERQLKSLERQAEKAERYKELKAELRELELAL--LVLRLEELREELEELQE 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336   135 TISLAEQRL--LEDDKRQFDSAWQEmLNHAtQRVMEAEQTKTRSELvhKETAARYNAAMGRMRQLEKKLKRAINKSKpyf 212
Cdd:TIGR02168  247 ELKEAEEELeeLTAELQELEEKLEE-LRLE-VSELEEEIEELQKEL--YALANEISRLEQQKQILRERLANLERQLE--- 319
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 109134336   213 elkaKYYVQLEQLKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIHERRR 262
Cdd:TIGR02168  320 ----ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
 
Name Accession Description Interval E-value
SH3BP5 pfam05276
SH3 domain-binding protein 5 (SH3BP5); This family consists of several eukaryotic SH3 ...
41-269 9.16e-107

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: 315.76  E-value: 9.16e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336   41 VDPRIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELVKKIGKAVEDSKPYWEARRVARQAQLEAQKATQ 120
Cdd:pfam05276   3 LDPRIQGELEKLNQATDEINKLEIELEEARSTFRELLAESSRKLKALSKKLGSCIDKARPYYEAKRRAKEAQQESQKAAL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336  121 DFQRATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKK 200
Cdd:pfam05276  83 RFERANSAHAAAKEMVALAEQGLLNNDEGTFDPAWQEMLNHATQKVMEAENEKTRAEREHQRKTKLCLAAETKVQQLEKK 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109134336  201 LKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIHERRRSSAMGPR 269
Cdd:pfam05276 163 LKRSIKKSRPYFELKAQLNKQLEAQKEKVLQLEEEVKEAKARYSTALRNLEQISEEIHEQRRSEKSEPP 231
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
42-264 7.62e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 7.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336   42 DPRIQGELEKLNQSTDDINRRETELEDARQKFR--SVLVEATVKLDELVKKIGK--AVEDSKPYWEARRVARQAQLEAQK 117
Cdd:COG4913   220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAEleYLRAALRLWFAQRRLELLEAELEE 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336  118 ATQDFQRATEVLRAAKETISLAEQRLleddkrqfDSAWQEMLNHATQRVMEAEQtktrsELVHKE-TAARYNAAMGRMRQ 196
Cdd:COG4913   300 LRAELARLEAELERLEARLDALREEL--------DELEAQIRGNGGDRLEQLER-----EIERLErELEERERRRARLEA 366
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109134336  197 LEKKLKRAINKSKPYF-ELKAKYYVQLEQLKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIH--ERRRSS 264
Cdd:COG4913   367 LLAALGLPLPASAEEFaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslERRKSN 437
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
44-265 1.14e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336  44 RIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDE-------LVKKIGKAVEDskpywEARRVARQAQLEAQ 116
Cdd:COG1196  243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEaqaeeyeLLAELARLEQD-----IARLEERRRELEER 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336 117 KATQDFQRATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQ 196
Cdd:COG1196  318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109134336 197 LEKKLKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIHERRRSSA 265
Cdd:COG1196  398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
44-240 9.03e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 9.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336  44 RIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELVKKIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQ 123
Cdd:COG1196  327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336 124 RATEVLRAAKETISLAEQRLLEDDKRQfdsawQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKR 203
Cdd:COG1196  407 EAEEALLERLERLEEELEELEEALAEL-----EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 109134336 204 AINKSKpyfELKAKYYVQLEQLKKTVDDLQAKLTLAK 240
Cdd:COG1196  482 LLEELA---EAAARLLLLLEAEADYEGFLEGVKAALL 515
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
48-263 2.07e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336  48 ELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELVKKIGKAVEDSKPYWEARRVARQAQLEAQKAT-------- 119
Cdd:COG4717  303 EAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllaeagve 382
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336 120 --QDFQRATEVLRAAKETisLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELvhKETAARYNAAMGRMRQL 197
Cdd:COG4717  383 deEELRAALEQAEEYQEL--KEELEELEEQLEELLGELEELLEALDEEELEEELEELEEEL--EELEEELEELREELAEL 458
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109134336 198 EKKLKRAINkSKPYFELKAKYYVQLEQLKKTVDDLQAkltlakgeYKMALKNLEMISDEIHERRRS 263
Cdd:COG4717  459 EAELEQLEE-DGELAELLQELEELKAELRELAEEWAA--------LKLALELLEEAREEYREERLP 515
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
48-202 3.60e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 39.72  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336   48 ELEKLNQStddinRRETELEDARQKFRSVLVEATVKLDELVKKIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQRATE 127
Cdd:pfam17380 349 ELERIRQE-----ERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEME 423
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336  128 VLRAAKETISLAEQRLLEDDK-RQFDSAWQEMLNHATQ----RVMEAEQTKTRSELvHKETAARYNAAMGRMRQLEKKLK 202
Cdd:pfam17380 424 QIRAEQEEARQREVRRLEEERaREMERVRLEEQERQQQverlRQQEEERKRKKLEL-EKEKRDRKRAEEQRRKILEKELE 502
PTZ00121 PTZ00121
MAEBL; Provisional
79-262 3.90e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336   79 EATVKLDELVK-KIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQRATEVlRAAKETISLAEQRLLEDDKRQFDSAWQE 157
Cdd:PTZ00121 1507 EAKKKADEAKKaEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL-KKAEEKKKAEEAKKAEEDKNMALRKAEE 1585
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336  158 MLNHATQRVMEA-----EQTKTRSELVHKETAARYNAAMGR--------MRQLEKKLKRAINKSKPYFELKAKYYVQLEQ 224
Cdd:PTZ00121 1586 AKKAEEARIEEVmklyeEEKKMKAEEAKKAEEAKIKAEELKkaeeekkkVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 109134336  225 LKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIHERRR 262
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
48-207 4.45e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.75  E-value: 4.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336  48 ELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELVKKIGKAVEDSKPYwEARRVARQAQLEAQKATQDFQRATE 127
Cdd:COG1579   18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV-EARIKKYEEQLGNVRNNKEYEALQK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336 128 VLRAAKETISLAEQRLLEDDKRqfdsawqemLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKRAINK 207
Cdd:COG1579   97 EIESLKRRISDLEDEILELMER---------IEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
60-262 4.53e-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: 39.65  E-value: 4.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336    60 NRRETE--LEDAR---QKFRSVLVEatvkLDELVKKIGKAVEDSKPYWEARRVARQAQLEAqkATQDFQRATEVLRAAKE 134
Cdd:TIGR02168  173 RRKETErkLERTRenlDRLEDILNE----LERQLKSLERQAEKAERYKELKAELRELELAL--LVLRLEELREELEELQE 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336   135 TISLAEQRL--LEDDKRQFDSAWQEmLNHAtQRVMEAEQTKTRSELvhKETAARYNAAMGRMRQLEKKLKRAINKSKpyf 212
Cdd:TIGR02168  247 ELKEAEEELeeLTAELQELEEKLEE-LRLE-VSELEEEIEELQKEL--YALANEISRLEQQKQILRERLANLERQLE--- 319
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 109134336   213 elkaKYYVQLEQLKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIHERRR 262
Cdd:TIGR02168  320 ----ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
48-261 5.76e-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: 39.27  E-value: 5.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336    48 ELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELVKKIGKAVEDSKpywEARRVARQAQLEAQKATQDFQRAT- 126
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS---ALRKDLARLEAEVEQLEERIAQLSk 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336   127 EVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNhATQRVMEAEQTKTRSEL-----VHKETAARYNAAMGRMRQLEKKL 201
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELE-AQIEQLKEELKALREALdelraELTLLNEEAANLRERLESLERRI 833
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134336   202 KRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIHERR 261
Cdd:TIGR02168  834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
 
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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