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Conserved domains on  [gi|109150410|ref|NP_446463|]
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SH3 domain-binding protein 5 [Rattus norvegicus]

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 ...
 43-271 1.04e-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: 318.46  E-value: 1.04e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410   43 VDPRIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELAKKIGKAVEDSKPYWEARRVARQAQLEAQKATQ 122
Cdd:pfam05276   3 LDPRIQGELEKLNQATDEINKLEIELEEARSTFRELLAESSRKLKALSKKLGSCIDKARPYYEAKRRAKEAQQESQKAAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410  123 DFQRATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKK 202
Cdd:pfam05276  83 RFERANSAHAAAKEMVALAEQGLLNNDEGTFDPAWQEMLNHATQKVMEAENEKTRAEREHQRKTKLCLAAETKVQQLEKK 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109150410  203 LKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLALAKGEYKAALKSLERISDEIHERRRSNAMGPR 271
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 ...
 43-271 1.04e-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: 318.46  E-value: 1.04e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410   43 VDPRIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELAKKIGKAVEDSKPYWEARRVARQAQLEAQKATQ 122
Cdd:pfam05276   3 LDPRIQGELEKLNQATDEINKLEIELEEARSTFRELLAESSRKLKALSKKLGSCIDKARPYYEAKRRAKEAQQESQKAAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410  123 DFQRATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKK 202
Cdd:pfam05276  83 RFERANSAHAAAKEMVALAEQGLLNNDEGTFDPAWQEMLNHATQKVMEAENEKTRAEREHQRKTKLCLAAETKVQQLEKK 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109150410  203 LKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLALAKGEYKAALKSLERISDEIHERRRSNAMGPR 271
Cdd:pfam05276 163 LKRSIKKSRPYFELKAQLNKQLEAQKEKVLQLEEEVKEAKARYSTALRNLEQISEEIHEQRRSEKSEPP 231
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
44-266 5.62e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.31  E-value: 5.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410   44 DPRIQGELEKLNQSTDDINRRETELEDARQKFR--SVLVEATVKLDELAKKIGK--AVEDSKPYWEARRVARQAQLEAQK 119
Cdd:COG4913   220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAEleYLRAALRLWFAQRRLELLEAELEE 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410  120 ATQDFQRATEVLRAAKETISLAEQRLleddkrqfDSAWQEMLNHATQRVMEAEQtktrsELVHKE-TAARYNAAMGRMRQ 198
Cdd:COG4913   300 LRAELARLEAELERLEARLDALREEL--------DELEAQIRGNGGDRLEQLER-----EIERLErELEERERRRARLEA 366

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109150410  199 LEKKLKRAINKSKPYF-ELKAKYYVQLEQLKKTVDDLQAKLALAKGEYKAALKSLERISDEIH--ERRRSN 266
Cdd:COG4913   367 LLAALGLPLPASAEEFaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslERRKSN 437
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 66-266 2.56e-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: 43.51  E-value: 2.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410    66 TELEDARQKFRSVLVEATVKLDELAKKIGKAVEDSKpywearrvarQAQLEAQKATQDFQRATEVLRAAKETISLAEQRL 145
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLE----------ELRLEVSELEEEIEELQKELYALANEISRLEQQK 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410   146 LE-DDKRQFDSAWQEMLNHATQrvmEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKRAINKSKPYFELKAKYYVQL 224
Cdd:TIGR02168  305 QIlRERLANLERQLEELEAQLE---ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 109150410   225 EQLKKTVDDLQAKLALAKGEYKAALKSLERISDEiHERRRSN 266
Cdd:TIGR02168  382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDR-RERLQQE 422
PTZ00121 PTZ00121
MAEBL; Provisional
 50-264 7.33e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 7.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410   50 ELEKLNQSTDDINRRETELEDARQKfrsvlVEATVKLDELAK-KIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQRAT 128
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKA-----AEAKKKADEAKKaEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410  129 EVlRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEA-----EQTKTRSELVHKETAARYNAAMGR-------- 195
Cdd:PTZ00121 1556 EL-KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVmklyeEEKKMKAEEAKKAEEAKIKAEELKkaeeekkk 1634

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109150410  196 MRQLEKKLKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLALAKGEYKAALKSLERISDEIHERRR 264
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703
 
Name Accession Description Interval E-value
SH3BP5 pfam05276
SH3 domain-binding protein 5 (SH3BP5); This family consists of several eukaryotic SH3 ...
 43-271 1.04e-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: 318.46  E-value: 1.04e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410   43 VDPRIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELAKKIGKAVEDSKPYWEARRVARQAQLEAQKATQ 122
Cdd:pfam05276   3 LDPRIQGELEKLNQATDEINKLEIELEEARSTFRELLAESSRKLKALSKKLGSCIDKARPYYEAKRRAKEAQQESQKAAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410  123 DFQRATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKK 202
Cdd:pfam05276  83 RFERANSAHAAAKEMVALAEQGLLNNDEGTFDPAWQEMLNHATQKVMEAENEKTRAEREHQRKTKLCLAAETKVQQLEKK 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109150410  203 LKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLALAKGEYKAALKSLERISDEIHERRRSNAMGPR 271
Cdd:pfam05276 163 LKRSIKKSRPYFELKAQLNKQLEAQKEKVLQLEEEVKEAKARYSTALRNLEQISEEIHEQRRSEKSEPP 231
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
44-266 5.62e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.31  E-value: 5.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410   44 DPRIQGELEKLNQSTDDINRRETELEDARQKFR--SVLVEATVKLDELAKKIGK--AVEDSKPYWEARRVARQAQLEAQK 119
Cdd:COG4913   220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAEleYLRAALRLWFAQRRLELLEAELEE 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410  120 ATQDFQRATEVLRAAKETISLAEQRLleddkrqfDSAWQEMLNHATQRVMEAEQtktrsELVHKE-TAARYNAAMGRMRQ 198
Cdd:COG4913   300 LRAELARLEAELERLEARLDALREEL--------DELEAQIRGNGGDRLEQLER-----EIERLErELEERERRRARLEA 366

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109150410  199 LEKKLKRAINKSKPYF-ELKAKYYVQLEQLKKTVDDLQAKLALAKGEYKAALKSLERISDEIH--ERRRSN 266
Cdd:COG4913   367 LLAALGLPLPASAEEFaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslERRKSN 437
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 50-264 1.48e-04

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: 44.34  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410   50 ELEKLNQStddinRRETELEDARQKFRSVLVEATVKLDELAKKIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQRATE 129
Cdd:pfam17380 349 ELERIRQE-----ERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEME 423

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410  130 VLRAAKETISLAEQRLLEDDK-RQFDSAWQEMLNHATQ----RVMEAEQTKTRSELvHKETAARYNAAMGRMRQLEKKLK 204
Cdd:pfam17380 424 QIRAEQEEARQREVRRLEEERaREMERVRLEEQERQQQverlRQQEEERKRKKLEL-EKEKRDRKRAEEQRRKILEKELE 502

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410  205 RaiNKSKPYFELKAKyyvqlEQLKKTVDDLQAklALAKGEYKAALKSLERISDEIHERRR 264
Cdd:pfam17380 503 E--RKQAMIEEERKR-----KLLEKEMEERQK--AIYEEERRREAEEERRKQQEMEERRR 553
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 37-267 1.71e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410  37 LEeeeevdpRIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELAKKIGKAVEDSKPYWEARrvaRQAQLE 116
Cdd:COG1196  248 LE-------ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR---RELEER 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410 117 AQKATQDFQRATEVLRAAKETISLAEQRLLEDDKRQfdSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRM 196
Cdd:COG1196  318 LEELEEELAELEEELEELEEELEELEEELEEAEEEL--EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109150410 197 RQLEKKLKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLALAKGEYKAALKSLERISDEIHERRRSNA 267
Cdd:COG1196  396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 66-266 2.56e-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: 43.51  E-value: 2.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410    66 TELEDARQKFRSVLVEATVKLDELAKKIGKAVEDSKpywearrvarQAQLEAQKATQDFQRATEVLRAAKETISLAEQRL 145
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLE----------ELRLEVSELEEEIEELQKELYALANEISRLEQQK 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410   146 LE-DDKRQFDSAWQEMLNHATQrvmEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKRAINKSKPYFELKAKYYVQL 224
Cdd:TIGR02168  305 QIlRERLANLERQLEELEAQLE---ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 109150410   225 EQLKKTVDDLQAKLALAKGEYKAALKSLERISDEiHERRRSN 266
Cdd:TIGR02168  382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDR-RERLQQE 422
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 46-242 3.02e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 3.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410  46 RIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELAKKIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQ 125
Cdd:COG1196  327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410 126 RATEVLRAAKETISLAEQRLLEDDKRQfdsawQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKR 205
Cdd:COG1196  407 EAEEALLERLERLEEELEELEEALAEL-----EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 109150410 206 AINKSKpyfELKAKYYVQLEQLKKTVDDLQAKLALAK 242
Cdd:COG1196  482 LLEELA---EAAARLLLLLEAEADYEGFLEGVKAALL 515
PTZ00121 PTZ00121
MAEBL; Provisional
 50-264 7.33e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 7.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410   50 ELEKLNQSTDDINRRETELEDARQKfrsvlVEATVKLDELAK-KIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQRAT 128
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKA-----AEAKKKADEAKKaEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410  129 EVlRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEA-----EQTKTRSELVHKETAARYNAAMGR-------- 195
Cdd:PTZ00121 1556 EL-KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVmklyeEEKKMKAEEAKKAEEAKIKAEELKkaeeekkk 1634

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109150410  196 MRQLEKKLKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLALAKGEYKAALKSLERISDEIHERRR 264
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 114-264 9.52e-04

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: 41.38  E-value: 9.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410  114 QLEAQKATQDFQRATEVLRAAKETI-SLAEQRLLEDDKRQF----DSAWQEMLNHATQR----VMEAEQTKTRSELVHKE 184
Cdd:pfam06160 248 ENLALLENLELDEAEEALEEIEERIdQLYDLLEKEVDAKKYveknLPEIEDYLEHAEEQnkelKEELERVQQSYTLNENE 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410  185 TAaRYNAAMGRMRQLEKKL----KRAINKSKPYFELKAKY---YVQLEQLKKTVDDLQAKLA-LAKGEyKAALKSLERIS 256
Cdd:pfam06160 328 LE-RVRGLEKQLEELEKRYdeivERLEEKEVAYSELQEELeeiLEQLEEIEEEQEEFKESLQsLRKDE-LEAREKLDEFK 405


                  ....*...
gi 109150410  257 DEIHERRR 264
Cdd:pfam06160 406 LELREIKR 413
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
50-265 1.62e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410  50 ELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELAKKIGKAVEDSKPYWEARRVARQAQLEAQKAT-------- 121
Cdd:COG4717  303 EAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllaeagve 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410 122 --QDFQRATEVLRAAKETisLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELvhKETAARYNAAMGRMRQL 199
Cdd:COG4717  383 deEELRAALEQAEEYQEL--KEELEELEEQLEELLGELEELLEALDEEELEEELEELEEEL--EELEEELEELREELAEL 458

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109150410 200 EKKLKRAINkSKPYFELKAKYYVQLEQLKKTVDDLQAklalakgeYKAALKSLERISDEIHERRRS 265
Cdd:COG4717  459 EAELEQLEE-DGELAELLQELEELKAELRELAEEWAA--------LKLALELLEEAREEYREERLP 515
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 47-263 1.68e-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: 41.20  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410    47 IQGELEKLNQstdDINRRETELEDARQKFRSV---LVEATVKLDELAKKIGKAVEDskpywEARRVARQAQLEAQKATQ- 122
Cdd:TIGR02168  286 LQKELYALAN---EISRLEQQKQILRERLANLerqLEELEAQLEELESKLDELAEE-----LAELEEKLEELKEELESLe 357

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410   123 -DFQRATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEqtKTRSELVHKETAARYNAAMGRMRQLEK 201
Cdd:TIGR02168  358 aELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR--LERLEDRRERLQQEIEELLKKLEEAEL 435

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109150410   202 K-LKRAINKSKPyfelkakyyvQLEQLKKTVDDLQAKLALAKGEYKAALKSLERISDEIHERR 263
Cdd:TIGR02168  436 KeLQAELEELEE----------ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
76-261 3.05e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 3.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410  76 RSVLVEATVK-LDELAKKIGK----AVEDSKPYWEARRVARQAQLEAQKATQDFQRATEVLRAAKETISLAEQRLLE-DD 149
Cdd:COG4717   44 RAMLLERLEKeADELFKPQGRkpelNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEK 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410 150 KRQFDSAWQEMlnHATQRVMEAEQTKTRSelvHKETAARYNAAMGRMRQLEKKLKRAINKSKPYFE-LKAKYYVQLEQLK 228
Cdd:COG4717  124 LLQLLPLYQEL--EALEAELAELPERLEE---LEERLEELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLA 198

                        170       180       190
                 ....*....|....*....|....*....|...
gi 109150410 229 KTVDDLQAKLALAKGEYKAALKSLERISDEIHE 261
Cdd:COG4717  199 EELEELQQRLAELEEELEEAQEELEELEEELEQ 231
PTZ00121 PTZ00121
MAEBL; Provisional
 69-262 3.28e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410   69 EDARQkfrsvLVEATVKLDELAKKIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQRATEV-----LRAAKETISLAEQ 143
Cdd:PTZ00121 1137 EDARK-----AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELrkaedARKAEAARKAEEE 1211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109150410  144 RLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKRAINKSKPYFELKAKYYVQ 223
Cdd:PTZ00121 1212 RKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKK 1291

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 109150410  224 LEQLKKTVDDLQAKLALAKGEYKAALKSLERISDEIHER 262
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKK 1330
 
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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