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Conserved domains on  [gi|767924637|ref|XP_011532553|]
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SH3 domain-binding protein 5 isoform X2 [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 ...
 5-229 5.11e-104

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: 307.29  E-value: 5.11e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637    5 IQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELVKKIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQR 84
Cdd:pfam05276   7 IQGELEKLNQATDEINKLEIELEEARSTFRELLAESSRKLKALSKKLGSCIDKARPYYEAKRRAKEAQQESQKAALRFER 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637   85 ATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKRA 164
Cdd:pfam05276  87 ANSAHAAAKEMVALAEQGLLNNDEGTFDPAWQEMLNHATQKVMEAENEKTRAEREHQRKTKLCLAAETKVQQLEKKLKRS 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767924637  165 INKSKPYFELKAKYYVQLEQLKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIHERRRSSAMGPR 229
Cdd:pfam05276 167 IKKSRPYFELKAQLNKQLEAQKEKVLQLEEEVKEAKARYSTALRNLEQISEEIHEQRRSEKSEPP 231
 
Name Accession Description Interval E-value
SH3BP5 pfam05276
SH3 domain-binding protein 5 (SH3BP5); This family consists of several eukaryotic SH3 ...
 5-229 5.11e-104

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: 307.29  E-value: 5.11e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637    5 IQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELVKKIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQR 84
Cdd:pfam05276   7 IQGELEKLNQATDEINKLEIELEEARSTFRELLAESSRKLKALSKKLGSCIDKARPYYEAKRRAKEAQQESQKAALRFER 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637   85 ATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKRA 164
Cdd:pfam05276  87 ANSAHAAAKEMVALAEQGLLNNDEGTFDPAWQEMLNHATQKVMEAENEKTRAEREHQRKTKLCLAAETKVQQLEKKLKRS 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767924637  165 INKSKPYFELKAKYYVQLEQLKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIHERRRSSAMGPR 229
Cdd:pfam05276 167 IKKSRPYFELKAQLNKQLEAQKEKVLQLEEEVKEAKARYSTALRNLEQISEEIHEQRRSEKSEPP 231
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
17-224 9.23e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 9.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637   17 DDINRRETELEDARQKFR--SVLVEATVKLDELVKKIGK--AVEDSKPYWEARRVARQAQLEAQKATQDFQRATEVLRAA 92
Cdd:COG4913   235 DDLERAHEALEDAREQIEllEPIRELAERYAAARERLAEleYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637   93 KETISLAEQRLleddkrqfDSAWQEMLNHATQRVMEAEQtktrsELVHKE-TAARYNAAMGRMRQLEKKLKRAINKSKPY 171
Cdd:COG4913   315 EARLDALREEL--------DELEAQIRGNGGDRLEQLER-----EIERLErELEERERRRARLEALLAALGLPLPASAEE 381

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767924637  172 F-ELKAKYYVQLEQLKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIH--ERRRSS 224
Cdd:COG4913   382 FaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslERRKSN 437
PTZ00121 PTZ00121
MAEBL; Provisional
 39-222 2.99e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637   39 EATVKLDELVK-KIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQRATEVlRAAKETISLAEQRLLEDDKRQFDSAWQE 117
Cdd:PTZ00121 1507 EAKKKADEAKKaEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL-KKAEEKKKAEEAKKAEEDKNMALRKAEE 1585

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637  118 MLNHATQRVMEA-----EQTKTRSELVHKETAARYNAAMGR--------MRQLEKKLKRAINKSKPYFELKAKYYVQLEQ 184
Cdd:PTZ00121 1586 AKKAEEARIEEVmklyeEEKKMKAEEAKKAEEAKIKAEELKkaeeekkkVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767924637  185 LKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIHERRR 222
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 20-222 3.78e-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: 3.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637    20 NRRETE--LEDAR---QKFRSVLVEatvkLDELVKKIGKAVEDSKPYWEARRVARQAQLEAqkATQDFQRATEVLRAAKE 94
Cdd:TIGR02168  173 RRKETErkLERTRenlDRLEDILNE----LERQLKSLERQAEKAERYKELKAELRELELAL--LVLRLEELREELEELQE 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637    95 TISLAEQRL--LEDDKRQFDSAWQEmLNHAtQRVMEAEQTKTRSELvhKETAARYNAAMGRMRQLEKKLKRAINKSKpyf 172
Cdd:TIGR02168  247 ELKEAEEELeeLTAELQELEEKLEE-LRLE-VSELEEEIEELQKEL--YALANEISRLEQQKQILRERLANLERQLE--- 319

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 767924637   173 elkaKYYVQLEQLKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIHERRR 222
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 ...
 5-229 5.11e-104

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: 307.29  E-value: 5.11e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637    5 IQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELVKKIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQR 84
Cdd:pfam05276   7 IQGELEKLNQATDEINKLEIELEEARSTFRELLAESSRKLKALSKKLGSCIDKARPYYEAKRRAKEAQQESQKAALRFER 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637   85 ATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKRA 164
Cdd:pfam05276  87 ANSAHAAAKEMVALAEQGLLNNDEGTFDPAWQEMLNHATQKVMEAENEKTRAEREHQRKTKLCLAAETKVQQLEKKLKRS 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767924637  165 INKSKPYFELKAKYYVQLEQLKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIHERRRSSAMGPR 229
Cdd:pfam05276 167 IKKSRPYFELKAQLNKQLEAQKEKVLQLEEEVKEAKARYSTALRNLEQISEEIHEQRRSEKSEPP 231
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
17-224 9.23e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 9.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637   17 DDINRRETELEDARQKFR--SVLVEATVKLDELVKKIGK--AVEDSKPYWEARRVARQAQLEAQKATQDFQRATEVLRAA 92
Cdd:COG4913   235 DDLERAHEALEDAREQIEllEPIRELAERYAAARERLAEleYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637   93 KETISLAEQRLleddkrqfDSAWQEMLNHATQRVMEAEQtktrsELVHKE-TAARYNAAMGRMRQLEKKLKRAINKSKPY 171
Cdd:COG4913   315 EARLDALREEL--------DELEAQIRGNGGDRLEQLER-----EIERLErELEERERRRARLEALLAALGLPLPASAEE 381

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767924637  172 F-ELKAKYYVQLEQLKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIH--ERRRSS 224
Cdd:COG4913   382 FaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslERRKSN 437
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-225 9.64e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 9.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637   2 LLAIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELVKKIGKAVEDskpywEARRVARQAQLEAQKATQD 81
Cdd:COG1196  248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD-----IARLEERRRELEERLEELE 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637  82 FQRATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKL 161
Cdd:COG1196  323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767924637 162 KRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIHERRRSSA 225
Cdd:COG1196  403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-200 1.24e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637   2 LLAIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELVKKIGKAVEDSKPYWEARRVARQAQLEAQKATQD 81
Cdd:COG1196  318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637  82 FQRATEVLRAAKETISLAEQRLLEDDKRQFDS--AWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEK 159
Cdd:COG1196  398 LAAQLEELEEAEEALLERLERLEEELEELEEAlaELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767924637 160 KLKRAINKSKpyfELKAKYYVQLEQLKKTVDDLQAKLTLAK 200
Cdd:COG1196  478 ALAELLEELA---EAAARLLLLLEAEADYEGFLEGVKAALL 515
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 8-162 1.45e-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: 40.88  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637    8 ELEKLNQStddinRRETELEDARQKFRSVLVEATVKLDELVKKIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQRATE 87
Cdd:pfam17380 349 ELERIRQE-----ERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEME 423

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637   88 VLRAAKETISLAEQRLLEDDK-RQFDSAWQEMLNHATQ----RVMEAEQTKTRSELvHKETAARYNAAMGRMRQLEKKLK 162
Cdd:pfam17380 424 QIRAEQEEARQREVRRLEEERaREMERVRLEEQERQQQverlRQQEEERKRKKLEL-EKEKRDRKRAEEQRRKILEKELE 502
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
8-223 1.95e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637   8 ELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELVKKIGKAVEDSKPYWEARRVARQAQLEAQKAT-------- 79
Cdd:COG4717  303 EAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllaeagve 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637  80 --QDFQRATEVLRAAKETisLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELvhKETAARYNAAMGRMRQL 157
Cdd:COG4717  383 deEELRAALEQAEEYQEL--KEELEELEEQLEELLGELEELLEALDEEELEEELEELEEEL--EELEEELEELREELAEL 458

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767924637 158 EKKLKRAINkSKPYFELKAKYYVQLEQLKKTVDDLQAkltlakgeYKMALKNLEMISDEIHERRRS 223
Cdd:COG4717  459 EAELEQLEE-DGELAELLQELEELKAELRELAEEWAA--------LKLALELLEEAREEYREERLP 515
PTZ00121 PTZ00121
MAEBL; Provisional
 39-222 2.99e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637   39 EATVKLDELVK-KIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQRATEVlRAAKETISLAEQRLLEDDKRQFDSAWQE 117
Cdd:PTZ00121 1507 EAKKKADEAKKaEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL-KKAEEKKKAEEAKKAEEDKNMALRKAEE 1585

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637  118 MLNHATQRVMEA-----EQTKTRSELVHKETAARYNAAMGR--------MRQLEKKLKRAINKSKPYFELKAKYYVQLEQ 184
Cdd:PTZ00121 1586 AKKAEEARIEEVmklyeEEKKMKAEEAKKAEEAKIKAEELKkaeeekkkVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767924637  185 LKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIHERRR 222
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 2-167 3.43e-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: 3.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637   2 LLAIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELVKKIGKAVEDSKPYwEARRVARQAQLEAQKATQD 81
Cdd:COG1579   12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV-EARIKKYEEQLGNVRNNKE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637  82 FQRATEVLRAAKETISLAEQRLLEDDKRqfdsawqemLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKL 161
Cdd:COG1579   91 YEALQKEIESLKRRISDLEDEILELMER---------IEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161


                 ....*.
gi 767924637 162 KRAINK 167
Cdd:COG1579  162 EAEREE 167
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 20-222 3.78e-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: 3.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637    20 NRRETE--LEDAR---QKFRSVLVEatvkLDELVKKIGKAVEDSKPYWEARRVARQAQLEAqkATQDFQRATEVLRAAKE 94
Cdd:TIGR02168  173 RRKETErkLERTRenlDRLEDILNE----LERQLKSLERQAEKAERYKELKAELRELELAL--LVLRLEELREELEELQE 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637    95 TISLAEQRL--LEDDKRQFDSAWQEmLNHAtQRVMEAEQTKTRSELvhKETAARYNAAMGRMRQLEKKLKRAINKSKpyf 172
Cdd:TIGR02168  247 ELKEAEEELeeLTAELQELEEKLEE-LRLE-VSELEEEIEELQKEL--YALANEISRLEQQKQILRERLANLERQLE--- 319

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 767924637   173 elkaKYYVQLEQLKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIHERRR 222
Cdd:TIGR02168  320 ----ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-221 3.84e-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: 3.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637     2 LLAIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELVKKIGKAVEDSKpywEARRVARQAQLEAQKATQD 81
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS---ALRKDLARLEAEVEQLEER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637    82 FQRAT-EVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNhATQRVMEAEQTKTRSEL-----VHKETAARYNAAMGRMR 155
Cdd:TIGR02168  749 IAQLSkELTELEAEIEELEERLEEAEEELAEAEAEIEELE-AQIEQLKEELKALREALdelraELTLLNEEAANLRERLE 827

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767924637   156 QLEKKLKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIHERR 221
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 2-145 3.89e-03

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 38.82  E-value: 3.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637    2 LLAIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELVKKIGKAVEDSKPYWEARRVARQAQLEAQKATQD 81
Cdd:pfam12795  87 LLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQAELAALKAQID 166

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767924637   82 FQRA--------TEVLRAAKEtisLAEQRLLEDDKRQfdSAWQEMLNhaTQRVMEAEQTKTRSELVHKETAA 145
Cdd:pfam12795 167 MLEQellsnnnrQDLLKARRD---LLTLRIQRLEQQL--QALQELLN--EKRLQEAEQAVAQTEQLAEEAAG 231
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
4-164 8.43e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.21  E-value: 8.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637   4 AIQGELEKLNQSTDDINRRETELEDARQKFRSVL---------VEATVKLDELVKKIGKAVEDSKPYwearrvaRQAQLE 74
Cdd:COG4717   92 ELQEELEELEEELEELEAELEELREELEKLEKLLqllplyqelEALEAELAELPERLEELEERLEEL-------RELEEE 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924637  75 AQKATQDFQRATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHatqrvmEAEQTKTRSELVHKETAARYNAAMGRM 154
Cdd:COG4717  165 LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL------EEELEEAQEELEELEEELEQLENELEA 238

                        170
                 ....*....|
gi 767924637 155 RQLEKKLKRA 164
Cdd:COG4717  239 AALEERLKEA 248
 
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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