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Conserved domains on  [gi|74096435|ref|NP_001027899|]
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syntabulin isoform b [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 ...
 143-434 4.36e-177

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: 503.11  E-value: 4.36e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435   143 NPLSPSNIHPSYAPSSPSSSN-SGSYKGSDCSPVMRRSGRYMSCGENHGVKPPNPEQYLTPLQQKEVTVRHLRTKLKESE 221
Cdd:pfam15290   1 NQGSPVNNRDAYGPSSLSSSSnSGSCKGSDSSPTRRRSGRYHSCGDNHGIKPPNPEQYLTPLQQKEVTIRHLKTKLKESE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435   222 RRLHERESEIMELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKL 301
Cdd:pfam15290  81 NRLQDRETEIEELKSQLSRMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMKSSLAEKDKGIQKYFVDINIQNKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435   302 ESLLQSMEMAHNSSLRDELCLDFSFDSPEKSLPLSSTFDKLPDGLS-------LEEQITEEGADSELLVGDSMAEGTDLL 374
Cdd:pfam15290 161 ESLLQSMELAQNGSLRDEGTLEFACDSPAKSLTRSSTYTKLSDQLAaeengleLEDQSAEEMADSGLLANDEMANRTDLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74096435   375 DEMVTATTTESSGLEFVHST-----PGPQALKALPLVSHEEGIAVMEQAVQTDVVPFSPAISELI 434
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 ...
 143-434 4.36e-177

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: 503.11  E-value: 4.36e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435   143 NPLSPSNIHPSYAPSSPSSSN-SGSYKGSDCSPVMRRSGRYMSCGENHGVKPPNPEQYLTPLQQKEVTVRHLRTKLKESE 221
Cdd:pfam15290   1 NQGSPVNNRDAYGPSSLSSSSnSGSCKGSDSSPTRRRSGRYHSCGDNHGIKPPNPEQYLTPLQQKEVTIRHLKTKLKESE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435   222 RRLHERESEIMELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKL 301
Cdd:pfam15290  81 NRLQDRETEIEELKSQLSRMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMKSSLAEKDKGIQKYFVDINIQNKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435   302 ESLLQSMEMAHNSSLRDELCLDFSFDSPEKSLPLSSTFDKLPDGLS-------LEEQITEEGADSELLVGDSMAEGTDLL 374
Cdd:pfam15290 161 ESLLQSMELAQNGSLRDEGTLEFACDSPAKSLTRSSTYTKLSDQLAaeengleLEDQSAEEMADSGLLANDEMANRTDLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74096435   375 DEMVTATTTESSGLEFVHST-----PGPQALKALPLVSHEEGIAVMEQAVQTDVVPFSPAISELI 434
Cdd:pfam15290 241 EEVFMSTAVEAGDLAPFSSTyeklmGSQKSVEALPSCSEEKQQMVEEQAIQTDVVPYSPDLDTLL 305
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
210-309 5.58e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.76  E-value: 5.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435  210 VRHLRTKLKESERRLHERESEIMELKSQLARMREdwIEEEchrVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQK 289
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKE--LKEK---AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE 328

                         90       100
                 ....*....|....*....|
gi 74096435  290 YFVDINIQNKKLESLLQSME 309
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLK 348
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 203-320 7.03e-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: 7.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435   203 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLArmrEDWIEE--------ECHRVEAQLALKEARKEIKQLKQVIE 274
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE---QDWNKElkselknqEKKLEEIQNQISQNNKIISQLNEQIS 345

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 74096435   275 TMRSSLADKDKGIQKYFVDINIQNKKLESLLQsmemaHNSSLRDEL 320
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKK-----ENQSYKQEI 386
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
203-320 7.89e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 7.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435 203 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDW--IEEECHRVEAQLA-----LKEARKEIKQLKQVIET 275
Cdd:COG4372  61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELesLQEEAEELQEELEelqkeRQDLEQQRKQLEAQIAE 140

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 74096435 276 MRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEMAHNSSLRDEL 320
Cdd:COG4372 141 LQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
 
Name Accession Description Interval E-value
Syntaphilin pfam15290
Golgi-localized syntaxin-1-binding clamp; Syntaphilin or Syntabulin is a family of eukaryotic ...
 143-434 4.36e-177

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: 503.11  E-value: 4.36e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435   143 NPLSPSNIHPSYAPSSPSSSN-SGSYKGSDCSPVMRRSGRYMSCGENHGVKPPNPEQYLTPLQQKEVTVRHLRTKLKESE 221
Cdd:pfam15290   1 NQGSPVNNRDAYGPSSLSSSSnSGSCKGSDSSPTRRRSGRYHSCGDNHGIKPPNPEQYLTPLQQKEVTIRHLKTKLKESE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435   222 RRLHERESEIMELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKL 301
Cdd:pfam15290  81 NRLQDRETEIEELKSQLSRMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMKSSLAEKDKGIQKYFVDINIQNKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435   302 ESLLQSMEMAHNSSLRDELCLDFSFDSPEKSLPLSSTFDKLPDGLS-------LEEQITEEGADSELLVGDSMAEGTDLL 374
Cdd:pfam15290 161 ESLLQSMELAQNGSLRDEGTLEFACDSPAKSLTRSSTYTKLSDQLAaeengleLEDQSAEEMADSGLLANDEMANRTDLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74096435   375 DEMVTATTTESSGLEFVHST-----PGPQALKALPLVSHEEGIAVMEQAVQTDVVPFSPAISELI 434
Cdd:pfam15290 241 EEVFMSTAVEAGDLAPFSSTyeklmGSQKSVEALPSCSEEKQQMVEEQAIQTDVVPYSPDLDTLL 305
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
210-309 5.58e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.76  E-value: 5.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435  210 VRHLRTKLKESERRLHERESEIMELKSQLARMREdwIEEEchrVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQK 289
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKE--LKEK---AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE 328

                         90       100
                 ....*....|....*....|
gi 74096435  290 YFVDINIQNKKLESLLQSME 309
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLK 348
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 199-309 1.93e-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: 1.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435    199 YLTPLQQKEVTVRHLRTKLKESER----RLHERESEIMELKSQL--ARMREDWIEEECHRVEAQLA--LKEARKEIKQLK 270
Cdd:pfam15921  315 YMRQLSDLESTVSQLRSELREAKRmyedKIEELEKQLVLANSELteARTERDQFSQESGNLDDQLQklLADLHKREKELS 394

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 74096435    271 QVIETMRsSLADKDKG-------IQKYFVDINIQNKKLESLLQSME 309
Cdd:pfam15921  395 LEKEQNK-RLWDRDTGnsitidhLRRELDDRNMEVQRLEALLKAMK 439
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 203-320 7.03e-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: 7.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435   203 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLArmrEDWIEE--------ECHRVEAQLALKEARKEIKQLKQVIE 274
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE---QDWNKElkselknqEKKLEEIQNQISQNNKIISQLNEQIS 345

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 74096435   275 TMRSSLADKDKGIQKYFVDINIQNKKLESLLQsmemaHNSSLRDEL 320
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKK-----ENQSYKQEI 386
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
203-320 7.89e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 7.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435 203 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDW--IEEECHRVEAQLA-----LKEARKEIKQLKQVIET 275
Cdd:COG4372  61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELesLQEEAEELQEELEelqkeRQDLEQQRKQLEAQIAE 140

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 74096435 276 MRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEMAHNSSLRDEL 320
Cdd:COG4372 141 LQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
195-320 9.31e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 9.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435 195 NPEQYLTPLQQKEVTVRHLRTK---LKESERRLHERESEIMELKSQLARMREDW-----------IEEECHRVEAQLA-- 258
Cdd:COG4717  65 KPELNLKELKELEEELKEAEEKeeeYAELQEELEELEEELEELEAELEELREELeklekllqllpLYQELEALEAELAel 144

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74096435 259 ------LKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKK-LESLLQSMEMAHN--SSLRDEL 320
Cdd:COG4717 145 perleeLEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQrlAELEEEL 215
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 205-355 1.30e-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: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435   205 QKEVTVRH--LRTKLKESERRLHERESEIMELKSQLARMREDWIEEECHrVEAQLA-----------LKEARKEIKQLKQ 271
Cdd:pfam15905 172 MKEVMAKQegMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSE-TEKLLEyitelscvseqVEKYKLDIAQLEE 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435   272 V-------IETMRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEMAHNsslrdelcldfsfdspEKSLPLSSTFDKLPD 344
Cdd:pfam15905 251 LlkekndeIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYE----------------EKEQTLNAELEELKE 314

                         170
                  ....*....|.
gi 74096435   345 GLSLEEQITEE 355
Cdd:pfam15905 315 KLTLEEQEHQK 325
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 203-320 1.60e-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: 1.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435 203 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLarmredwieeechrVEAQLALKEARKEIKQLKQVIETMRsSLAD 282
Cdd:COG1579  12 LQELDSELDRLEHRLKELPAELAELEDELAALEARL--------------EAAKTELEDLEKEIKRLELEIEEVE-ARIK 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 74096435 283 KDKGIQKyfvdiNIQN-KKLESLLQSMEMAH--NSSLRDEL 320
Cdd:COG1579  77 KYEEQLG-----NVRNnKEYEALQKEIESLKrrISDLEDEI 112
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
203-320 1.66e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 1.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435 203 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMRE--DWIEEECHRVEAQlaLKEARKEIKQLKQVIETMRSSL 280
Cdd:COG4372  54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAelAQAQEELESLQEE--AEELQEELEELQKERQDLEQQR 131

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 74096435 281 ADKDKGIQKYFVDINIQNKKLESLLQSMEmahnsSLRDEL 320
Cdd:COG4372 132 KQLEAQIAELQSEIAEREEELKELEEQLE-----SLQEEL 166
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
213-311 3.37e-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: 3.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435 213 LRTKLKESERRLHERESEIMELKSQLARMREDwIEEECHRV--EAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKY 290
Cdd:COG3206 275 LEAELAELSARYTPNHPDVIALRAQIAALRAQ-LQQEAQRIlaSLEAELEALQAREASLQAQLAQLEARLAELPELEAEL 353

                        90       100
                ....*....|....*....|....
gi 74096435 291 FV---DINIQNKKLESLLQSMEMA 311
Cdd:COG3206 354 RRlerEVEVARELYESLLQRLEEA 377
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 195-310 3.88e-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: 3.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435   195 NPEQYLTPLQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIE 274
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 74096435   275 TMRSSLADKDKGIQKyfvdINIQNKKLESLLQSMEM 310
Cdd:TIGR04523 264 KIKKQLSEKQKELEQ----NNKKIKELEKQLNQLKS 295
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
205-320 4.05e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 4.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435 205 QKEVtvRHLRTKLKESERRLHERESEIMELKSQLARMRE--DWIEEECHRVEAQLA-----LKEARKEIKQLKQVIETMR 277
Cdd:COG4372  44 QEEL--EQLREELEQAREELEQLEEELEQARSELEQLEEelEELNEQLQAAQAELAqaqeeLESLQEEAEELQEELEELQ 121

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 74096435 278 SSLADkdkgIQKYFVDINIQNKKLESLLQSMEMAHNsSLRDEL 320
Cdd:COG4372 122 KERQD----LEQQRKQLEAQIAELQSEIAEREEELK-ELEEQL 159
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 213-290 4.64e-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: 40.24  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435   213 LRTKLKESERRLHERESEIMELKSQLARMREDWIE-----EECH--RVEAQLALKEARK-------EIKQLKQVIETMRS 278
Cdd:pfam13863  15 LDAKREEIERLEELLKQREEELEKKEQELKEDLIKfdkflKENDakRRRALKKAEEETKlkkekekEIKKLTAQIEELKS 94

                          90
                  ....*....|..
gi 74096435   279 SLADKDKGIQKY 290
Cdd:pfam13863  95 EISKLEEKLEEY 106
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 216-333 4.79e-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: 4.79e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435 216 KLKESERRLHERESEIMELKSQLARMREDwieeechRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDIN 295
Cdd:COG4942  21 AAAEAEAELEQLQQEIAELEKELAALKKE-------EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 74096435 296 IQNKKLESLLQSME----MAHNSSLRDELCLDFSFDSPEKSL 333
Cdd:COG4942  94 ELRAELEAQKEELAellrALYRLGRQPPLALLLSPEDFLDAV 135
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 197-290 9.60e-04

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: 41.83  E-value: 9.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435   197 EQYLTPLQQKEVTVRHLRTKLKESERRLHER----ESEIMELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQV 272
Cdd:pfam13868 158 LEYLKEKAEREEEREAEREEIEEEKEREIARlraqQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQEL 237

                          90
                  ....*....|....*...
gi 74096435   273 IETMRSSLADKDKGIQKY 290
Cdd:pfam13868 238 QQAREEQIELKERRLAEE 255
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 203-317 1.07e-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: 42.35  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435    203 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDwIEEECHRV--------EAQLALKEARKEIKQLKQVIE 274
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED-IESLAAEIeeleelieELESELEALLNERASLEEALA 890

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 74096435    275 TMRSSLADKDKGIQkyfvDINIQNKKLESLLQS-MEMAHNSSLR 317
Cdd:TIGR02168  891 LLRSELEELSEELR----ELESKRSELRRELEElREKLAQLELR 930
RNase_Y_N pfam12072
RNase Y N-terminal region;
203-281 1.33e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 40.25  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435   203 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMRED---WIEEECHRVE--AQLALKEARKEIkqLKQVIETMR 277
Cdd:pfam12072  87 LLQKEETLDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEEleeLIEEQRQELEriSGLTSEEAKEIL--LDEVEEELR 164


                  ....
gi 74096435   278 SSLA 281
Cdd:pfam12072 165 HEAA 168
RNase_Y_N pfam12072
RNase Y N-terminal region;
206-304 1.47e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 40.25  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435   206 KEVTVRhlRTKLKESERRLHEREsEIMELKSQLARMREDwieeechrveaqlALKEARKEIKQLKQVIETMRSSLADKdk 285
Cdd:pfam12072  71 RELKER--RNELQRQERRLLQKE-ETLDRKDESLEKKEE-------------SLEKKEKELEAQQQQLEEKEEELEEL-- 132

                          90
                  ....*....|....*....
gi 74096435   286 giqkyfvdINIQNKKLESL 304
Cdd:pfam12072 133 --------IEEQRQELERI 143
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 198-320 1.70e-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: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435   198 QYLTPlQQKE--VTVRHLRTKLKESERRLHERESEIMELKSQLARmreDWIEEEchrveaqlaLKEARKEIKQLKQVIET 275
Cdd:TIGR04523 513 KDLTK-KISSlkEKIEKLESEKKEKESKISDLEDELNKDDFELKK---ENLEKE---------IDEKNKEIEELKQTQKS 579

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 74096435   276 MRSSLADKDKGIQKYFVDINIQNKKLESLLQSMemahnSSLRDEL 320
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI-----SSLEKEL 619
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
213-307 2.19e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435  213 LRTKLKESERRLHERESEIMELKSQLARM---REDWIEEECHRVEA----QLALKEARKEIKQLKQVIETMRSSLADKDK 285
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELEELgfeSVEELEERLKELEPfyneYLELKDAEKELEREEKELKKLEEELDKAFE 633

                         90       100
                 ....*....|....*....|..
gi 74096435  286 GIQKYFVDINIQNKKLESLLQS 307
Cdd:PRK03918 634 ELAETEKRLEELRKELEELEKK 655
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
203-309 2.88e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 2.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435  203 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDWIEEECHRVEAQL-----ALKEARKEIKQLKQVIETMR 277
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYlelsrELAGLRAELEELEKRREEIK 693

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 74096435  278 SSL----ADKDKgIQKYFVDIniqnKKLESLLQSME 309
Cdd:PRK03918 694 KTLeklkEELEE-REKAKKEL----EKLEKALERVE 724
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 206-321 2.91e-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: 2.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435   206 KEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDK 285
Cdd:pfam07888 127 HEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDT 206

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 74096435   286 GIQKYFVDINIQNKKLESLLQ---SMEMAHN--SSLRDELC 321
Cdd:pfam07888 207 QVLQLQDTITTLTQKLTTAHRkeaENEALLEelRSLQERLN 247
PRK12704 PRK12704
phosphodiesterase; Provisional
 205-304 3.27e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 3.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435  205 QKEVTVRhlRTKLKESERRLHEREsEIMELKSQLARMREDWIEEECHRVEAQLalkearKEIKQLKQVIETMRSSladkd 284
Cdd:PRK12704  74 EKELRER--RNELQKLEKRLLQKE-ENLDRKLELLEKREEELEKKEKELEQKQ------QELEKKEEELEELIEE----- 139

                         90       100
                 ....*....|....*....|
gi 74096435  285 kgiqkyfvdiniQNKKLESL 304
Cdd:PRK12704 140 ------------QLQELERI 147
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
212-320 4.18e-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: 4.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435  212 HLRTKLKESERRLHERESEIMELKSQLARMRE----------------DW--IEEECHRVEAQLA--------LKEARKE 265
Cdd:COG4913  614 ALEAELAELEEELAEAEERLEALEAELDALQErrealqrlaeyswdeiDVasAEREIAELEAELErldassddLAALEEQ 693

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 74096435  266 IKQLKQVIETMRSSLADKDK---GIQKYFVDINIQNKKLESLLQSMEMAHNSSLRDEL 320
Cdd:COG4913  694 LEELEAELEELEEELDELKGeigRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 203-290 6.55e-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: 6.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435 203 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDwieeechrveaqlaLKEARKEIKQLKQVIETMRSSLAD 282
Cdd:COG4942  43 LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE--------------LAELEKEIAELRAELEAQKEELAE 108


                ....*...
gi 74096435 283 KDKGIQKY 290
Cdd:COG4942 109 LLRALYRL 116
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
195-279 7.14e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 7.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435 195 NPEQYLTPLQQKEvTVRHLRTKLKESERRLHERESEIMELksqLARMREDWIEEECHRVEAQLA-----LKEARKEIKQL 269
Cdd:COG4717 383 DEEELRAALEQAE-EYQELKEELEELEEQLEELLGELEEL---LEALDEEELEEELEELEEELEeleeeLEELREELAEL 458

                        90
                ....*....|
gi 74096435 270 KQVIETMRSS 279
Cdd:COG4717 459 EAELEQLEED 468
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
203-377 8.10e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 38.27  E-value: 8.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435 203 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQ----LARMRED----WIEEechRVEAQLALKEARKEIKQLKQVIE 274
Cdd:COG1842  39 LVEARQALAQVIANQKRLERQLEELEAEAEKWEEKarlaLEKGREDlareALER---KAELEAQAEALEAQLAQLEEQVE 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435 275 TMRSSLAD-KDKgIQKYfvdiniQNKKlESLLQSMEMAH-----NSSLRdelclDFSFDSPEkslplsSTFDKlpdglsL 348
Cdd:COG1842 116 KLKEALRQlESK-LEEL------KAKK-DTLKARAKAAKaqekvNEALS-----GIDSDDAT------SALER------M 170

                       170       180
                ....*....|....*....|....*....
gi 74096435 349 EEQITEEGADSELLvgDSMAEGTDLLDEM 377
Cdd:COG1842 171 EEKIEEMEARAEAA--AELAAGDSLDDEL 197
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 226-320 8.33e-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: 8.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435    226 ERESEIMELKSQLARMredwiEEECHrvEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKLESLL 305
Cdd:TIGR02168  674 ERRREIEELEEKIEEL-----EEKIA--ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746

                           90
                   ....*....|....*
gi 74096435    306 QsmEMAHNSSLRDEL 320
Cdd:TIGR02168  747 E--RIAQLSKELTEL 759
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 207-334 8.69e-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: 8.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435    207 EVTVRHLRTKLKESERRLHERESEIMELKSQLARMrEDWIEEECHRVE---------------AQLALKEARKEIKQLKQ 271
Cdd:TIGR02169  811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL-KEQIKSIEKEIEnlngkkeeleeeleeLEAALRDLESRLGDLKK 889

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74096435    272 VIETMRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEMA--HNSSLRDELCLDFSFDSPEKSLP 334
Cdd:TIGR02169  890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALeeELSEIEDPKGEDEEIPEEELSLE 954
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
 213-307 8.69e-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: 8.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435   213 LRTKLKESERRLHERESEIMELKSQL-------ARMREDW---------IEEECHRVEAQL-ALKEARKEIKQ-LKQVIE 274
Cdd:pfam17078  57 LSSMLNRKERRLKDLEDQLSELKNSYeeltesnKQLKKRLenssasettLEAELERLQIQYdALVDSQNEYKDhYQQEIN 136

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 74096435   275 TMRSSL----ADKDKGIQKYFVDINIQNKKLESLLQS 307
Cdd:pfam17078 137 TLQESLedlkLENEKQLENYQQRISSNDKDIDTKLDS 173
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
 219-351 9.15e-03

Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.


Pssm-ID: 460827 [Multi-domain]  Cd Length: 383  Bit Score: 38.68  E-value: 9.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435   219 ESERRLHERESEIM----ELKSQLARMRE----------------DWIEEECHRVEAQLALKEARKEI--------KQLK 270
Cdd:pfam03148  43 DSNRRLGERIQDITfwksELEKELEELDEeiellleekrrlekalEALEEPLHIAQECLTLREKRQGIdlvhdeveKELL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435   271 QVIETMrssladkdKGIQKYFV----DINIQNKKLESLLQSMEMAH---NSSLR-DELCLDFSFDSPEKSLPLSSTfdKL 342
Cdd:pfam03148 123 KEVELI--------EGIQELLQrtleQAWEQLRLLRAARHKLEKDLsdkKEALEiDEKCLSLNNTSPNISYKPGPT--RI 192


                  ....*....
gi 74096435   343 PDGLSLEEQ 351
Cdd:pfam03148 193 PPNSSTPEE 201
PRK01156 PRK01156
chromosome segregation protein; Provisional
 216-318 9.49e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.11  E-value: 9.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096435  216 KLKESERRLHERESEIMELKSQLAR-MREdwIEEECHRVEAQLALKEARK-EIKQLKQVIETMRSSLADKDkGIQKYFVD 293
Cdd:PRK01156 595 QLNDLESRLQEIEIGFPDDKSYIDKsIRE--IENEANNLNNKYNEIQENKiLIEKLRGKIDNYKKQIAEID-SIIPDLKE 671

                         90       100
                 ....*....|....*....|....*
gi 74096435  294 INIQNKKLESLLQSMEMAHNSSLRD 318
Cdd:PRK01156 672 ITSRINDIEDNLKKSRKALDDAKAN 696
 
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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