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Conserved domains on  [gi|1039749058|ref|XP_017172153|]
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syntabulin isoform X7 [Mus musculus]

Protein Classification

syntaphilin domain-containing protein( domain architecture ID 10633823)

syntaphilin domain-containing protein similar to Homo sapiens syntaphilin, a syntaxin-1 clamp that controls SNARE assembly, and syntabulin, a microtubule-associated protein implicated in syntaxin transport in neurons

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Syntaphilin pfam15290
Golgi-localized syntaxin-1-binding clamp; Syntaphilin or Syntabulin is a family of eukaryotic ...
 180-471 1.81e-176

Golgi-localized syntaxin-1-binding clamp; Syntaphilin or Syntabulin is a family of eukaryotic proteins. Syntaphilin binds to syntaxin-1 thereby inhibiting SNARE complex formation by absorbing free syntaxin-1. So it is a syntaxin-1 clamp that controls SNARE assembly.


:

Pssm-ID: 464617 [Multi-domain]  Cd Length: 305  Bit Score: 502.73  E-value: 1.81e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 180 NPLSPSNIHPSYAPSSPSSSN-SGSYKGSDCSPVMRRSGRYMSCGENHGVKPPNPEQYLTPLQQKEVTVRHLRTKLKESE 258
Cdd:pfam15290   1 NQGSPVNNRDAYGPSSLSSSSnSGSCKGSDSSPTRRRSGRYHSCGDNHGIKPPNPEQYLTPLQQKEVTIRHLKTKLKESE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 259 RRLHERESEIMELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKL 338
Cdd:pfam15290  81 NRLQDRETEIEELKSQLSRMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMKSSLAEKDKGIQKYFVDINIQNKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 339 ESLLQSMEMAHNSSLRDELCLDFSFDSPEKSLPLSSTFDKLPDGLS-------LEEQITEEGADSELLVGDSMAEGTDLL 411
Cdd:pfam15290 161 ESLLQSMELAQNGSLRDEGTLEFACDSPAKSLTRSSTYTKLSDQLAaeengleLEDQSAEEMADSGLLANDEMANRTDLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039749058 412 DEMVTATTTESSGLEFVHST-----PGPQALKALPLVSHEEGIAVMEQAVQTDVVPFSPAISELI 471
Cdd:pfam15290 241 EEVFMSTAVEAGDLAPFSSTyeklmGSQKSVEALPSCSEEKQQMVEEQAIQTDVVPYSPDLDTLL 305
 
Name Accession Description Interval E-value
Syntaphilin pfam15290
Golgi-localized syntaxin-1-binding clamp; Syntaphilin or Syntabulin is a family of eukaryotic ...
 180-471 1.81e-176

Golgi-localized syntaxin-1-binding clamp; Syntaphilin or Syntabulin is a family of eukaryotic proteins. Syntaphilin binds to syntaxin-1 thereby inhibiting SNARE complex formation by absorbing free syntaxin-1. So it is a syntaxin-1 clamp that controls SNARE assembly.


Pssm-ID: 464617 [Multi-domain]  Cd Length: 305  Bit Score: 502.73  E-value: 1.81e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 180 NPLSPSNIHPSYAPSSPSSSN-SGSYKGSDCSPVMRRSGRYMSCGENHGVKPPNPEQYLTPLQQKEVTVRHLRTKLKESE 258
Cdd:pfam15290   1 NQGSPVNNRDAYGPSSLSSSSnSGSCKGSDSSPTRRRSGRYHSCGDNHGIKPPNPEQYLTPLQQKEVTIRHLKTKLKESE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 259 RRLHERESEIMELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKL 338
Cdd:pfam15290  81 NRLQDRETEIEELKSQLSRMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMKSSLAEKDKGIQKYFVDINIQNKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 339 ESLLQSMEMAHNSSLRDELCLDFSFDSPEKSLPLSSTFDKLPDGLS-------LEEQITEEGADSELLVGDSMAEGTDLL 411
Cdd:pfam15290 161 ESLLQSMELAQNGSLRDEGTLEFACDSPAKSLTRSSTYTKLSDQLAaeengleLEDQSAEEMADSGLLANDEMANRTDLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039749058 412 DEMVTATTTESSGLEFVHST-----PGPQALKALPLVSHEEGIAVMEQAVQTDVVPFSPAISELI 471
Cdd:pfam15290 241 EEVFMSTAVEAGDLAPFSSTyeklmGSQKSVEALPSCSEEKQQMVEEQAIQTDVVPYSPDLDTLL 305
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
247-346 5.66e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.76  E-value: 5.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 247 VRHLRTKLKESERRLHERESEIMELKSQLARMREdwIEEEchrVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQK 326
Cdd:PRK03918  254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKE--LKEK---AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE 328

                          90       100
                  ....*....|....*....|
gi 1039749058 327 YFVDINIQNKKLESLLQSME 346
Cdd:PRK03918  329 RIKELEEKEERLEELKKKLK 348
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 240-357 7.53e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.78  E-value: 7.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 240 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLArmrEDWIEE--------ECHRVEAQLALKEARKEIKQLKQVIE 311
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE---QDWNKElkselknqEKKLEEIQNQISQNNKIISQLNEQIS 345

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1039749058 312 TMRSSLADKDKGIQKYFVDINIQNKKLESLLQsmemaHNSSLRDEL 357
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKK-----ENQSYKQEI 386
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
232-357 1.16e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 232 NPEQYLTPLQQKEVTVRHLRTK---LKESERRLHERESEIMELKSQLARMREDW-----------IEEECHRVEAQLA-- 295
Cdd:COG4717    65 KPELNLKELKELEEELKEAEEKeeeYAELQEELEELEEELEELEAELEELREELeklekllqllpLYQELEALEAELAel 144

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039749058 296 ------LKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKK-LESLLQSMEMAHN--SSLRDEL 357
Cdd:COG4717   145 perleeLEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQrlAELEEEL 215
 
Name Accession Description Interval E-value
Syntaphilin pfam15290
Golgi-localized syntaxin-1-binding clamp; Syntaphilin or Syntabulin is a family of eukaryotic ...
 180-471 1.81e-176

Golgi-localized syntaxin-1-binding clamp; Syntaphilin or Syntabulin is a family of eukaryotic proteins. Syntaphilin binds to syntaxin-1 thereby inhibiting SNARE complex formation by absorbing free syntaxin-1. So it is a syntaxin-1 clamp that controls SNARE assembly.


Pssm-ID: 464617 [Multi-domain]  Cd Length: 305  Bit Score: 502.73  E-value: 1.81e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 180 NPLSPSNIHPSYAPSSPSSSN-SGSYKGSDCSPVMRRSGRYMSCGENHGVKPPNPEQYLTPLQQKEVTVRHLRTKLKESE 258
Cdd:pfam15290   1 NQGSPVNNRDAYGPSSLSSSSnSGSCKGSDSSPTRRRSGRYHSCGDNHGIKPPNPEQYLTPLQQKEVTIRHLKTKLKESE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 259 RRLHERESEIMELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKL 338
Cdd:pfam15290  81 NRLQDRETEIEELKSQLSRMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMKSSLAEKDKGIQKYFVDINIQNKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 339 ESLLQSMEMAHNSSLRDELCLDFSFDSPEKSLPLSSTFDKLPDGLS-------LEEQITEEGADSELLVGDSMAEGTDLL 411
Cdd:pfam15290 161 ESLLQSMELAQNGSLRDEGTLEFACDSPAKSLTRSSTYTKLSDQLAaeengleLEDQSAEEMADSGLLANDEMANRTDLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039749058 412 DEMVTATTTESSGLEFVHST-----PGPQALKALPLVSHEEGIAVMEQAVQTDVVPFSPAISELI 471
Cdd:pfam15290 241 EEVFMSTAVEAGDLAPFSSTyeklmGSQKSVEALPSCSEEKQQMVEEQAIQTDVVPYSPDLDTLL 305
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
247-346 5.66e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.76  E-value: 5.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 247 VRHLRTKLKESERRLHERESEIMELKSQLARMREdwIEEEchrVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQK 326
Cdd:PRK03918  254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKE--LKEK---AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE 328

                          90       100
                  ....*....|....*....|
gi 1039749058 327 YFVDINIQNKKLESLLQSME 346
Cdd:PRK03918  329 RIKELEEKEERLEELKKKLK 348
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 236-346 2.22e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 47.81  E-value: 2.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058  236 YLTPLQQKEVTVRHLRTKLKESER----RLHERESEIMELKSQL--ARMREDWIEEECHRVEAQLA--LKEARKEIKQLK 307
Cdd:pfam15921  315 YMRQLSDLESTVSQLRSELREAKRmyedKIEELEKQLVLANSELteARTERDQFSQESGNLDDQLQklLADLHKREKELS 394

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1039749058  308 QVIETMRsSLADKDKG-------IQKYFVDINIQNKKLESLLQSME 346
Cdd:pfam15921  395 LEKEQNK-RLWDRDTGnsitidhLRRELDDRNMEVQRLEALLKAMK 439
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 240-357 7.53e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.78  E-value: 7.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 240 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLArmrEDWIEE--------ECHRVEAQLALKEARKEIKQLKQVIE 311
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE---QDWNKElkselknqEKKLEEIQNQISQNNKIISQLNEQIS 345

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1039749058 312 TMRSSLADKDKGIQKYFVDINIQNKKLESLLQsmemaHNSSLRDEL 357
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKK-----ENQSYKQEI 386
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
232-357 1.16e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 232 NPEQYLTPLQQKEVTVRHLRTK---LKESERRLHERESEIMELKSQLARMREDW-----------IEEECHRVEAQLA-- 295
Cdd:COG4717    65 KPELNLKELKELEEELKEAEEKeeeYAELQEELEELEEELEELEAELEELREELeklekllqllpLYQELEALEAELAel 144

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039749058 296 ------LKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKK-LESLLQSMEMAHN--SSLRDEL 357
Cdd:COG4717   145 perleeLEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQrlAELEEEL 215
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
240-357 1.18e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 240 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDW--IEEECHRVEAQLA-----LKEARKEIKQLKQVIET 312
Cdd:COG4372    61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELesLQEEAEELQEELEelqkeRQDLEQQRKQLEAQIAE 140

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1039749058 313 MRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEMAHNSSLRDEL 357
Cdd:COG4372   141 LQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 242-392 1.54e-04

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 44.42  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 242 QKEVTVRH--LRTKLKESERRLHERESEIMELKSQLARMREDWIEEECHrVEAQLA-----------LKEARKEIKQLKQ 308
Cdd:pfam15905 172 MKEVMAKQegMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSE-TEKLLEyitelscvseqVEKYKLDIAQLEE 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 309 V-------IETMRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEMAHNsslrdelcldfsfdspEKSLPLSSTFDKLPD 381
Cdd:pfam15905 251 LlkekndeIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYE----------------EKEQTLNAELEELKE 314

                         170
                  ....*....|.
gi 1039749058 382 GLSLEEQITEE 392
Cdd:pfam15905 315 KLTLEEQEHQK 325
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 240-357 1.82e-04

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: 43.37  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 240 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLarmredwieeechrVEAQLALKEARKEIKQLKQVIETMRsSLAD 319
Cdd:COG1579    12 LQELDSELDRLEHRLKELPAELAELEDELAALEARL--------------EAAKTELEDLEKEIKRLELEIEEVE-ARIK 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1039749058 320 KDKGIQKyfvdiNIQN-KKLESLLQSMEMAH--NSSLRDEL 357
Cdd:COG1579    77 KYEEQLG-----NVRNnKEYEALQKEIESLKrrISDLEDEI 112
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
240-357 2.71e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 240 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMRE--DWIEEECHRVEAQlaLKEARKEIKQLKQVIETMRSSL 317
Cdd:COG4372    54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAelAQAQEELESLQEE--AEELQEELEELQKERQDLEQQR 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1039749058 318 ADKDKGIQKYFVDINIQNKKLESLLQSMEmahnsSLRDEL 357
Cdd:COG4372   132 KQLEAQIAELQSEIAEREEELKELEEQLE-----SLQEEL 166
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
250-348 3.78e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.47  E-value: 3.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 250 LRTKLKESERRLHERESEIMELKSQLARMREDwIEEECHRV--EAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKY 327
Cdd:COG3206   275 LEAELAELSARYTPNHPDVIALRAQIAALRAQ-LQQEAQRIlaSLEAELEALQAREASLQAQLAQLEARLAELPELEAEL 353

                          90       100
                  ....*....|....*....|....
gi 1039749058 328 FV---DINIQNKKLESLLQSMEMA 348
Cdd:COG3206   354 RRlerEVEVARELYESLLQRLEEA 377
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 232-347 4.40e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 4.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 232 NPEQYLTPLQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIE 311
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039749058 312 TMRSSLADKDKGIQKyfvdINIQNKKLESLLQSMEM 347
Cdd:TIGR04523 264 KIKKQLSEKQKELEQ----NNKKIKELEKQLNQLKS 295
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 253-370 5.18e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 5.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 253 KLKESERRLHERESEIMELKSQLARMREDwieeechRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDIN 332
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKE-------EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1039749058 333 IQNKKLESLLQSME----MAHNSSLRDELCLDFSFDSPEKSL 370
Cdd:COG4942    94 ELRAELEAQKEELAellrALYRLGRQPPLALLLSPEDFLDAV 135
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 250-327 6.20e-04

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 39.86  E-value: 6.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 250 LRTKLKESERRLHERESEIMELKSQLARMREDWIE-----EECH--RVEAQLALKEARK-------EIKQLKQVIETMRS 315
Cdd:pfam13863  15 LDAKREEIERLEELLKQREEELEKKEQELKEDLIKfdkflKENDakRRRALKKAEEETKlkkekekEIKKLTAQIEELKS 94

                          90
                  ....*....|..
gi 1039749058 316 SLADKDKGIQKY 327
Cdd:pfam13863  95 EISKLEEKLEEY 106
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
242-357 7.03e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 7.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 242 QKEVtvRHLRTKLKESERRLHERESEIMELKSQLARMRE--DWIEEECHRVEAQLA-----LKEARKEIKQLKQVIETMR 314
Cdd:COG4372    44 QEEL--EQLREELEQAREELEQLEEELEQARSELEQLEEelEELNEQLQAAQAELAqaqeeLESLQEEAEELQEELEELQ 121

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1039749058 315 SSLADkdkgIQKYFVDINIQNKKLESLLQSMEMAHNsSLRDEL 357
Cdd:COG4372   122 KERQD----LEQQRKQLEAQIAELQSEIAEREEELK-ELEEQL 159
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 240-354 1.24e-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: 41.97  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058  240 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDwIEEECHRV--------EAQLALKEARKEIKQLKQVIE 311
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED-IESLAAEIeeleelieELESELEALLNERASLEEALA 890

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1039749058  312 TMRSSLADKDKGIQkyfvDINIQNKKLESLLQS-MEMAHNSSLR 354
Cdd:TIGR02168  891 LLRSELEELSEELR----ELESKRSELRRELEElREKLAQLELR 930
RNase_Y_N pfam12072
RNase Y N-terminal region;
240-318 1.55e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 40.25  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 240 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMRED---WIEEECHRVE--AQLALKEARKEIkqLKQVIETMR 314
Cdd:pfam12072  87 LLQKEETLDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEEleeLIEEQRQELEriSGLTSEEAKEIL--LDEVEEELR 164


                  ....
gi 1039749058 315 SSLA 318
Cdd:pfam12072 165 HEAA 168
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 234-327 1.57e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 234 EQYLTPLQQKEVTVRHLRTKLKESERRLHER----ESEIMELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQV 309
Cdd:pfam13868 158 LEYLKEKAEREEEREAEREEIEEEKEREIARlraqQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQEL 237

                          90
                  ....*....|....*...
gi 1039749058 310 IETMRSSLADKDKGIQKY 327
Cdd:pfam13868 238 QQAREEQIELKERRLAEE 255
RNase_Y_N pfam12072
RNase Y N-terminal region;
243-341 1.72e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 40.25  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 243 KEVTVRhlRTKLKESERRLHEREsEIMELKSQLARMREDwieeechrveaqlALKEARKEIKQLKQVIETMRSSLADKdk 322
Cdd:pfam12072  71 RELKER--RNELQRQERRLLQKE-ETLDRKDESLEKKEE-------------SLEKKEKELEAQQQQLEEKEEELEEL-- 132

                          90
                  ....*....|....*....
gi 1039749058 323 giqkyfvdINIQNKKLESL 341
Cdd:pfam12072 133 --------IEEQRQELERI 143
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 235-357 1.84e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 235 QYLTPlQQKE--VTVRHLRTKLKESERRLHERESEIMELKSQLARmreDWIEEEchrveaqlaLKEARKEIKQLKQVIET 312
Cdd:TIGR04523 513 KDLTK-KISSlkEKIEKLESEKKEKESKISDLEDELNKDDFELKK---ENLEKE---------IDEKNKEIEELKQTQKS 579

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1039749058 313 MRSSLADKDKGIQKYFVDINIQNKKLESLLQSMemahnSSLRDEL 357
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI-----SSLEKEL 619
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
250-344 2.26e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 250 LRTKLKESERRLHERESEIMELKSQLARM---REDWIEEECHRVEA----QLALKEARKEIKQLKQVIETMRSSLADKDK 322
Cdd:PRK03918  554 LKKKLAELEKKLDELEEELAELLKELEELgfeSVEELEERLKELEPfyneYLELKDAEKELEREEKELKKLEEELDKAFE 633

                          90       100
                  ....*....|....*....|..
gi 1039749058 323 GIQKYFVDINIQNKKLESLLQS 344
Cdd:PRK03918  634 ELAETEKRLEELRKELEELEKK 655
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
240-346 3.10e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 240 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDWIEEECHRVEAQL-----ALKEARKEIKQLKQVIETMR 314
Cdd:PRK03918  614 LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYlelsrELAGLRAELEELEKRREEIK 693

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039749058 315 SSL----ADKDKgIQKYFVDIniqnKKLESLLQSME 346
Cdd:PRK03918  694 KTLeklkEELEE-REKAKKEL----EKLEKALERVE 724
PRK12704 PRK12704
phosphodiesterase; Provisional
 242-341 3.60e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 242 QKEVTVRhlRTKLKESERRLHEREsEIMELKSQLARMREDWIEEECHRVEAQLalkearKEIKQLKQVIETMRSSladkd 321
Cdd:PRK12704   74 EKELRER--RNELQKLEKRLLQKE-ENLDRKLELLEKREEELEKKEKELEQKQ------QELEKKEEELEELIEE----- 139

                          90       100
                  ....*....|....*....|
gi 1039749058 322 kgiqkyfvdiniQNKKLESL 341
Cdd:PRK12704  140 ------------QLQELERI 147
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 243-358 3.68e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 40.26  E-value: 3.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 243 KEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDK 322
Cdd:pfam07888 127 HEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDT 206

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1039749058 323 GIQKYFVDINIQNKKLESLLQ---SMEMAHN--SSLRDELC 358
Cdd:pfam07888 207 QVLQLQDTITTLTQKLTTAHRkeaENEALLEelRSLQERLN 247
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
249-357 4.53e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 4.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058  249 HLRTKLKESERRLHERESEIMELKSQLARMRE----------------DW--IEEECHRVEAQLA--------LKEARKE 302
Cdd:COG4913    614 ALEAELAELEEELAEAEERLEALEAELDALQErrealqrlaeyswdeiDVasAEREIAELEAELErldassddLAALEEQ 693

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039749058  303 IKQLKQVIETMRSSLADKDK---GIQKYFVDINIQNKKLESLLQSMEMAHNSSLRDEL 357
Cdd:COG4913    694 LEELEAELEELEEELDELKGeigRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 240-327 7.08e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 7.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 240 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDwieeechrveaqlaLKEARKEIKQLKQVIETMRSSLAD 319
Cdd:COG4942    43 LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE--------------LAELEKEIAELRAELEAQKEELAE 108


                  ....*...
gi 1039749058 320 KDKGIQKY 327
Cdd:COG4942   109 LLRALYRL 116
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
 250-344 8.62e-03

SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.


Pssm-ID: 293683 [Multi-domain]  Cd Length: 228  Bit Score: 38.18  E-value: 8.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 250 LRTKLKESERRLHERESEIMELKSQL-------ARMREDW---------IEEECHRVEAQL-ALKEARKEIKQ-LKQVIE 311
Cdd:pfam17078  57 LSSMLNRKERRLKDLEDQLSELKNSYeeltesnKQLKKRLenssasettLEAELERLQIQYdALVDSQNEYKDhYQQEIN 136

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1039749058 312 TMRSSL----ADKDKGIQKYFVDINIQNKKLESLLQS 344
Cdd:pfam17078 137 TLQESLedlkLENEKQLENYQQRISSNDKDIDTKLDS 173
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
232-316 8.87e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 8.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058 232 NPEQYLTPLQQKEvTVRHLRTKLKESERRLHERESEIMELksqLARMREDWIEEECHRVEAQLA-----LKEARKEIKQL 306
Cdd:COG4717   383 DEEELRAALEQAE-EYQELKEELEELEEQLEELLGELEEL---LEALDEEELEEELEELEEELEeleeeLEELREELAEL 458

                          90
                  ....*....|
gi 1039749058 307 KQVIETMRSS 316
Cdd:COG4717   459 EAELEQLEED 468
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 263-357 9.57e-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: 9.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058  263 ERESEIMELKSQLARMredwiEEECHrvEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKLESLL 342
Cdd:TIGR02168  674 ERRREIEELEEKIEEL-----EEKIA--ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746

                           90
                   ....*....|....*
gi 1039749058  343 QsmEMAHNSSLRDEL 357
Cdd:TIGR02168  747 E--RIAQLSKELTEL 759
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 244-371 9.90e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.28  E-value: 9.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749058  244 EVTVRHLRTKLKESERRLHERESEIMELKSQLARMrEDWIEEECHRVE---------------AQLALKEARKEIKQLKQ 308
Cdd:TIGR02169  811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL-KEQIKSIEKEIEnlngkkeeleeeleeLEAALRDLESRLGDLKK 889

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039749058  309 VIETMRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEMA--HNSSLRDELCLDFSFDSPEKSLP 371
Cdd:TIGR02169  890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALeeELSEIEDPKGEDEEIPEEELSLE 954
 
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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