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Conserved domains on  [gi|1907113054|ref|XP_036015351|]
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syntabulin isoform X4 [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 ...
 274-565 1.53e-174

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: 501.19  E-value: 1.53e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 274 NPLSPSNIHPSYAPSSPSSSN-SGSYKGSDCSPVMRRSGRYMSCGENHGVKPPNPEQYLTPLQQKEVTVRHLRTKLKESE 352
Cdd:pfam15290   1 NQGSPVNNRDAYGPSSLSSSSnSGSCKGSDSSPTRRRSGRYHSCGDNHGIKPPNPEQYLTPLQQKEVTIRHLKTKLKESE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 353 RRLHERESEIMELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKL 432
Cdd:pfam15290  81 NRLQDRETEIEELKSQLSRMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMKSSLAEKDKGIQKYFVDINIQNKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 433 ESLLQSMEMAHNSSLRDELCLDFSFDSPEKSLPLSSTFDKLPDGLS-------LEEQITEEGADSELLVGDSMAEGTDLL 505
Cdd:pfam15290 161 ESLLQSMELAQNGSLRDEGTLEFACDSPAKSLTRSSTYTKLSDQLAaeengleLEDQSAEEMADSGLLANDEMANRTDLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907113054 506 DEMVTATTTESSGLEFVHST-----PGPQALKALPLVSHEEGIAVMEQAVQTDVVPFSPAISELI 565
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 ...
 274-565 1.53e-174

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: 501.19  E-value: 1.53e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 274 NPLSPSNIHPSYAPSSPSSSN-SGSYKGSDCSPVMRRSGRYMSCGENHGVKPPNPEQYLTPLQQKEVTVRHLRTKLKESE 352
Cdd:pfam15290   1 NQGSPVNNRDAYGPSSLSSSSnSGSCKGSDSSPTRRRSGRYHSCGDNHGIKPPNPEQYLTPLQQKEVTIRHLKTKLKESE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 353 RRLHERESEIMELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKL 432
Cdd:pfam15290  81 NRLQDRETEIEELKSQLSRMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMKSSLAEKDKGIQKYFVDINIQNKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 433 ESLLQSMEMAHNSSLRDELCLDFSFDSPEKSLPLSSTFDKLPDGLS-------LEEQITEEGADSELLVGDSMAEGTDLL 505
Cdd:pfam15290 161 ESLLQSMELAQNGSLRDEGTLEFACDSPAKSLTRSSTYTKLSDQLAaeengleLEDQSAEEMADSGLLANDEMANRTDLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907113054 506 DEMVTATTTESSGLEFVHST-----PGPQALKALPLVSHEEGIAVMEQAVQTDVVPFSPAISELI 565
Cdd:pfam15290 241 EEVFMSTAVEAGDLAPFSSTyeklmGSQKSVEALPSCSEEKQQMVEEQAIQTDVVPYSPDLDTLL 305
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
341-440 5.18e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.14  E-value: 5.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 341 VRHLRTKLKESERRLHERESEIMELKSQLARMREdwIEEEchrVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQK 420
Cdd:PRK03918  254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKE--LKEK---AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE 328

                          90       100
                  ....*....|....*....|
gi 1907113054 421 YFVDINIQNKKLESLLQSME 440
Cdd:PRK03918  329 RIKELEEKEERLEELKKKLK 348
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 334-451 6.45e-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: 46.55  E-value: 6.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 334 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLArmrEDWIEE--------ECHRVEAQLALKEARKEIKQLKQVIE 405
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE---QDWNKElkselknqEKKLEEIQNQISQNNKIISQLNEQIS 345

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907113054 406 TMRSSLADKDKGIQKYFVDINIQNKKLESLLQsmemaHNSSLRDEL 451
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKK-----ENQSYKQEI 386
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
334-451 7.49e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 7.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 334 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDW--IEEECHRVEAQLA-----LKEARKEIKQLKQVIET 406
Cdd:COG4372    61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELesLQEEAEELQEELEelqkeRQDLEQQRKQLEAQIAE 140

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907113054 407 MRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEMAHNSSLRDEL 451
Cdd:COG4372   141 LQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 385-440 9.84e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 36.00  E-value: 9.84e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907113054 385 EAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKY---FVDINIQNKKLESLLQSME 440
Cdd:cd22887     8 ELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILndeLIALQIENNLLEEKLRKLQ 66
 
Name Accession Description Interval E-value
Syntaphilin pfam15290
Golgi-localized syntaxin-1-binding clamp; Syntaphilin or Syntabulin is a family of eukaryotic ...
 274-565 1.53e-174

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: 501.19  E-value: 1.53e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 274 NPLSPSNIHPSYAPSSPSSSN-SGSYKGSDCSPVMRRSGRYMSCGENHGVKPPNPEQYLTPLQQKEVTVRHLRTKLKESE 352
Cdd:pfam15290   1 NQGSPVNNRDAYGPSSLSSSSnSGSCKGSDSSPTRRRSGRYHSCGDNHGIKPPNPEQYLTPLQQKEVTIRHLKTKLKESE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 353 RRLHERESEIMELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKL 432
Cdd:pfam15290  81 NRLQDRETEIEELKSQLSRMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMKSSLAEKDKGIQKYFVDINIQNKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 433 ESLLQSMEMAHNSSLRDELCLDFSFDSPEKSLPLSSTFDKLPDGLS-------LEEQITEEGADSELLVGDSMAEGTDLL 505
Cdd:pfam15290 161 ESLLQSMELAQNGSLRDEGTLEFACDSPAKSLTRSSTYTKLSDQLAaeengleLEDQSAEEMADSGLLANDEMANRTDLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907113054 506 DEMVTATTTESSGLEFVHST-----PGPQALKALPLVSHEEGIAVMEQAVQTDVVPFSPAISELI 565
Cdd:pfam15290 241 EEVFMSTAVEAGDLAPFSSTyeklmGSQKSVEALPSCSEEKQQMVEEQAIQTDVVPYSPDLDTLL 305
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
341-440 5.18e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.14  E-value: 5.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 341 VRHLRTKLKESERRLHERESEIMELKSQLARMREdwIEEEchrVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQK 420
Cdd:PRK03918  254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKE--LKEK---AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE 328

                          90       100
                  ....*....|....*....|
gi 1907113054 421 YFVDINIQNKKLESLLQSME 440
Cdd:PRK03918  329 RIKELEEKEERLEELKKKLK 348
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 330-440 2.55e-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: 2.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054  330 YLTPLQQKEVTVRHLRTKLKESER----RLHERESEIMELKSQL--ARMREDWIEEECHRVEAQLA--LKEARKEIKQLK 401
Cdd:pfam15921  315 YMRQLSDLESTVSQLRSELREAKRmyedKIEELEKQLVLANSELteARTERDQFSQESGNLDDQLQklLADLHKREKELS 394

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1907113054  402 QVIETMRsSLADKDKG-------IQKYFVDINIQNKKLESLLQSME 440
Cdd:pfam15921  395 LEKEQNK-RLWDRDTGnsitidhLRRELDDRNMEVQRLEALLKAMK 439
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 334-451 6.45e-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: 46.55  E-value: 6.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 334 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLArmrEDWIEE--------ECHRVEAQLALKEARKEIKQLKQVIE 405
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE---QDWNKElkselknqEKKLEEIQNQISQNNKIISQLNEQIS 345

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907113054 406 TMRSSLADKDKGIQKYFVDINIQNKKLESLLQsmemaHNSSLRDEL 451
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKK-----ENQSYKQEI 386
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
334-451 7.49e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 7.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 334 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDW--IEEECHRVEAQLA-----LKEARKEIKQLKQVIET 406
Cdd:COG4372    61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELesLQEEAEELQEELEelqkeRQDLEQQRKQLEAQIAE 140

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907113054 407 MRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEMAHNSSLRDEL 451
Cdd:COG4372   141 LQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
326-451 1.08e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 326 NPEQYLTPLQQKEVTVRHLRTK---LKESERRLHERESEIMELKSQLARMREDW-----------IEEECHRVEAQLA-- 389
Cdd:COG4717    65 KPELNLKELKELEEELKEAEEKeeeYAELQEELEELEEELEELEAELEELREELeklekllqllpLYQELEALEAELAel 144

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907113054 390 ------LKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKK-LESLLQSMEMAHN--SSLRDEL 451
Cdd:COG4717   145 perleeLEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQrlAELEEEL 215
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 336-486 1.19e-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: 44.80  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 336 QKEVTVRH--LRTKLKESERRLHERESEIMELKSQLARMREDWIEEECHrVEAQLA-----------LKEARKEIKQLKQ 402
Cdd:pfam15905 172 MKEVMAKQegMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSE-TEKLLEyitelscvseqVEKYKLDIAQLEE 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 403 V-------IETMRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEMAHNsslrdelcldfsfdspEKSLPLSSTFDKLPD 475
Cdd:pfam15905 251 LlkekndeIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYE----------------EKEQTLNAELEELKE 314

                         170
                  ....*....|.
gi 1907113054 476 GLSLEEQITEE 486
Cdd:pfam15905 315 KLTLEEQEHQK 325
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 334-451 1.38e-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: 44.15  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 334 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLarmredwieeechrVEAQLALKEARKEIKQLKQVIETMRsSLAD 413
Cdd:COG1579    12 LQELDSELDRLEHRLKELPAELAELEDELAALEARL--------------EAAKTELEDLEKEIKRLELEIEEVE-ARIK 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907113054 414 KDKGIQKyfvdiNIQN-KKLESLLQSMEMAH--NSSLRDEL 451
Cdd:COG1579    77 KYEEQLG-----NVRNnKEYEALQKEIESLKrrISDLEDEI 112
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
334-451 1.56e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 334 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMRE--DWIEEECHRVEAQlaLKEARKEIKQLKQVIETMRSSL 411
Cdd:COG4372    54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAelAQAQEELESLQEE--AEELQEELEELQKERQDLEQQR 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907113054 412 ADKDKGIQKYFVDINIQNKKLESLLQSMEmahnsSLRDEL 451
Cdd:COG4372   132 KQLEAQIAELQSEIAEREEELKELEEQLE-----SLQEEL 166
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 344-421 3.43e-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: 41.01  E-value: 3.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 344 LRTKLKESERRLHERESEIMELKSQLARMREDWIE-----EECH--RVEAQLALKEARK-------EIKQLKQVIETMRS 409
Cdd:pfam13863  15 LDAKREEIERLEELLKQREEELEKKEQELKEDLIKfdkflKENDakRRRALKKAEEETKlkkekekEIKKLTAQIEELKS 94

                          90
                  ....*....|..
gi 1907113054 410 SLADKDKGIQKY 421
Cdd:pfam13863  95 EISKLEEKLEEY 106
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
336-451 3.57e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 336 QKEVtvRHLRTKLKESERRLHERESEIMELKSQLARMRE--DWIEEECHRVEAQLA-----LKEARKEIKQLKQVIETMR 408
Cdd:COG4372    44 QEEL--EQLREELEQAREELEQLEEELEQARSELEQLEEelEELNEQLQAAQAELAqaqeeLESLQEEAEELQEELEELQ 121

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1907113054 409 SSLADkdkgIQKYFVDINIQNKKLESLLQSMEMAHNsSLRDEL 451
Cdd:COG4372   122 KERQD----LEQQRKQLEAQIAELQSEIAEREEELK-ELEEQL 159
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 326-441 3.98e-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: 43.86  E-value: 3.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 326 NPEQYLTPLQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIE 405
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907113054 406 TMRSSLADKDKGIQKyfvdINIQNKKLESLLQSMEM 441
Cdd:TIGR04523 264 KIKKQLSEKQKELEQ----NNKKIKELEKQLNQLKS 295
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 347-464 6.20e-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: 6.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 347 KLKESERRLHERESEIMELKSQLARMREDwieeechRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDIN 426
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKE-------EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907113054 427 IQNKKLESLLQSME----MAHNSSLRDELCLDFSFDSPEKSL 464
Cdd:COG4942    94 ELRAELEAQKEELAellrALYRLGRQPPLALLLSPEDFLDAV 135
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
344-442 6.39e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.08  E-value: 6.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 344 LRTKLKESERRLHERESEIMELKSQLARMREDwIEEECHRV--EAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKY 421
Cdd:COG3206   275 LEAELAELSARYTPNHPDVIALRAQIAALRAQ-LQQEAQRIlaSLEAELEALQAREASLQAQLAQLEARLAELPELEAEL 353

                          90       100
                  ....*....|....*....|....
gi 1907113054 422 FV---DINIQNKKLESLLQSMEMA 442
Cdd:COG3206   354 RRlerEVEVARELYESLLQRLEEA 377
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 334-448 1.10e-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: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054  334 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDwIEEECHRV--------EAQLALKEARKEIKQLKQVIE 405
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED-IESLAAEIeeleelieELESELEALLNERASLEEALA 890

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907113054  406 TMRSSLADKDKGIQkyfvDINIQNKKLESLLQS-MEMAHNSSLR 448
Cdd:TIGR02168  891 LLRSELEELSEELR----ELESKRSELRRELEElREKLAQLELR 930
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 328-421 1.14e-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: 41.83  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 328 EQYLTPLQQKEVTVRHLRTKLKESERRLHER----ESEIMELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQV 403
Cdd:pfam13868 158 LEYLKEKAEREEEREAEREEIEEEKEREIARlraqQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQEL 237

                          90
                  ....*....|....*...
gi 1907113054 404 IETMRSSLADKDKGIQKY 421
Cdd:pfam13868 238 QQAREEQIELKERRLAEE 255
RNase_Y_N pfam12072
RNase Y N-terminal region;
334-412 1.33e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 40.64  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 334 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMRED---WIEEECHRVE--AQLALKEARKEIkqLKQVIETMR 408
Cdd:pfam12072  87 LLQKEETLDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEEleeLIEEQRQELEriSGLTSEEAKEIL--LDEVEEELR 164


                  ....
gi 1907113054 409 SSLA 412
Cdd:pfam12072 165 HEAA 168
RNase_Y_N pfam12072
RNase Y N-terminal region;
337-435 1.38e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 40.64  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 337 KEVTVRhlRTKLKESERRLHEREsEIMELKSQLARMREDwieeechrveaqlALKEARKEIKQLKQVIETMRSSLADKdk 416
Cdd:pfam12072  71 RELKER--RNELQRQERRLLQKE-ETLDRKDESLEKKEE-------------SLEKKEKELEAQQQQLEEKEEELEEL-- 132

                          90
                  ....*....|....*....
gi 1907113054 417 giqkyfvdINIQNKKLESL 435
Cdd:pfam12072 133 --------IEEQRQELERI 143
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 329-451 1.49e-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: 41.93  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 329 QYLTPlQQKE--VTVRHLRTKLKESERRLHERESEIMELKSQLARmreDWIEEEchrveaqlaLKEARKEIKQLKQVIET 406
Cdd:TIGR04523 513 KDLTK-KISSlkEKIEKLESEKKEKESKISDLEDELNKDDFELKK---ENLEKE---------IDEKNKEIEELKQTQKS 579

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907113054 407 MRSSLADKDKGIQKYFVDINIQNKKLESLLQSMemahnSSLRDEL 451
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI-----SSLEKEL 619
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
344-438 1.99e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 344 LRTKLKESERRLHERESEIMELKSQLARM---REDWIEEECHRVEA----QLALKEARKEIKQLKQVIETMRSSLADKDK 416
Cdd:PRK03918  554 LKKKLAELEKKLDELEEELAELLKELEELgfeSVEELEERLKELEPfyneYLELKDAEKELEREEKELKKLEEELDKAFE 633

                          90       100
                  ....*....|....*....|..
gi 1907113054 417 GIQKYFVDINIQNKKLESLLQS 438
Cdd:PRK03918  634 ELAETEKRLEELRKELEELEKK 655
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
334-440 2.61e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 334 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDWIEEECHRVEAQL-----ALKEARKEIKQLKQVIETMR 408
Cdd:PRK03918  614 LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYlelsrELAGLRAELEELEKRREEIK 693

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907113054 409 SSL----ADKDKgIQKYFVDIniqnKKLESLLQSME 440
Cdd:PRK03918  694 KTLeklkEELEE-REKAKKEL----EKLEKALERVE 724
PRK12704 PRK12704
phosphodiesterase; Provisional
 336-435 3.21e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 336 QKEVTVRhlRTKLKESERRLHEREsEIMELKSQLARMREDWIEEECHRVEAQLalkearKEIKQLKQVIETMRSSladkd 415
Cdd:PRK12704   74 EKELRER--RNELQKLEKRLLQKE-ENLDRKLELLEKREEELEKKEKELEQKQ------QELEKKEEELEELIEE----- 139

                          90       100
                  ....*....|....*....|
gi 1907113054 416 kgiqkyfvdiniQNKKLESL 435
Cdd:PRK12704  140 ------------QLQELERI 147
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
 344-438 4.47e-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: 39.34  E-value: 4.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 344 LRTKLKESERRLHERESEIMELKSQL-------ARMREDW---------IEEECHRVEAQL-ALKEARKEIKQ-LKQVIE 405
Cdd:pfam17078  57 LSSMLNRKERRLKDLEDQLSELKNSYeeltesnKQLKKRLenssasettLEAELERLQIQYdALVDSQNEYKDhYQQEIN 136

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907113054 406 TMRSSL----ADKDKGIQKYFVDINIQNKKLESLLQS 438
Cdd:pfam17078 137 TLQESLedlkLENEKQLENYQQRISSNDKDIDTKLDS 173
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 337-452 4.74e-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: 4.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 337 KEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDK 416
Cdd:pfam07888 127 HEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDT 206

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907113054 417 GIQKYFVDINIQNKKLESLLQ---SMEMAHN--SSLRDELC 452
Cdd:pfam07888 207 QVLQLQDTITTLTQKLTTAHRkeaENEALLEelRSLQERLN 247
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
343-451 5.41e-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: 5.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054  343 HLRTKLKESERRLHERESEIMELKSQLARMRE----------------DW--IEEECHRVEAQLA--------LKEARKE 396
Cdd:COG4913    614 ALEAELAELEEELAEAEERLEALEAELDALQErrealqrlaeyswdeiDVasAEREIAELEAELErldassddLAALEEQ 693

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907113054  397 IKQLKQVIETMRSSLADKDK---GIQKYFVDINIQNKKLESLLQSMEMAHNSSLRDEL 451
Cdd:COG4913    694 LEELEAELEELEEELDELKGeigRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
PRK01156 PRK01156
chromosome segregation protein; Provisional
 347-449 6.97e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.88  E-value: 6.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 347 KLKESERRLHERESEIMELKSQLAR-MREdwIEEECHRVEAQLALKEARK-EIKQLKQVIETMRSSLADKDkGIQKYFVD 424
Cdd:PRK01156  595 QLNDLESRLQEIEIGFPDDKSYIDKsIRE--IENEANNLNNKYNEIQENKiLIEKLRGKIDNYKKQIAEID-SIIPDLKE 671

                          90       100
                  ....*....|....*....|....*
gi 1907113054 425 INIQNKKLESLLQSMEMAHNSSLRD 449
Cdd:PRK01156  672 ITSRINDIEDNLKKSRKALDDAKAN 696
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
334-508 7.35e-03

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 38.65  E-value: 7.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 334 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQ----LARMRED----WIEEechRVEAQLALKEARKEIKQLKQVIE 405
Cdd:COG1842    39 LVEARQALAQVIANQKRLERQLEELEAEAEKWEEKarlaLEKGREDlareALER---KAELEAQAEALEAQLAQLEEQVE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 406 TMRSSLAD-KDKgIQKYfvdiniQNKKlESLLQSMEMAH-----NSSLRdelclDFSFDSPEkslplsSTFDKlpdglsL 479
Cdd:COG1842   116 KLKEALRQlESK-LEEL------KAKK-DTLKARAKAAKaqekvNEALS-----GIDSDDAT------SALER------M 170

                         170       180
                  ....*....|....*....|....*....
gi 1907113054 480 EEQITEEGADSELLvgDSMAEGTDLLDEM 508
Cdd:COG1842   171 EEKIEEMEARAEAA--AELAAGDSLDDEL 197
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
 350-482 8.03e-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: 39.07  E-value: 8.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 350 ESERRLHERESEIM----ELKSQLARMRE----------------DWIEEECHRVEAQLALKEARKEI--------KQLK 401
Cdd:pfam03148  43 DSNRRLGERIQDITfwksELEKELEELDEeiellleekrrlekalEALEEPLHIAQECLTLREKRQGIdlvhdeveKELL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 402 QVIETMrssladkdKGIQKYFV----DINIQNKKLESLLQSMEMAH---NSSLR-DELCLDFSFDSPEKSLPLSSTfdKL 473
Cdd:pfam03148 123 KEVELI--------EGIQELLQrtleQAWEQLRLLRAARHKLEKDLsdkKEALEiDEKCLSLNNTSPNISYKPGPT--RI 192


                  ....*....
gi 1907113054 474 PDGLSLEEQ 482
Cdd:pfam03148 193 PPNSSTPEE 201
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
326-410 8.32e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 8.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 326 NPEQYLTPLQQKEvTVRHLRTKLKESERRLHERESEIMELksqLARMREDWIEEECHRVEAQLA-----LKEARKEIKQL 400
Cdd:COG4717   383 DEEELRAALEQAE-EYQELKEELEELEEQLEELLGELEEL---LEALDEEELEEELEELEEELEeleeeLEELREELAEL 458

                          90
                  ....*....|
gi 1907113054 401 KQVIETMRSS 410
Cdd:COG4717   459 EAELEQLEED 468
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 334-421 8.42e-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: 8.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054 334 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDwieeechrveaqlaLKEARKEIKQLKQVIETMRSSLAD 413
Cdd:COG4942    43 LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE--------------LAELEKEIAELRAELEAQKEELAE 108


                  ....*...
gi 1907113054 414 KDKGIQKY 421
Cdd:COG4942   109 LLRALYRL 116
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 357-451 8.71e-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: 8.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054  357 ERESEIMELKSQLARMredwiEEECHrvEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKLESLL 436
Cdd:TIGR02168  674 ERRREIEELEEKIEEL-----EEKIA--ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746

                           90
                   ....*....|....*
gi 1907113054  437 QsmEMAHNSSLRDEL 451
Cdd:TIGR02168  747 E--RIAQLSKELTEL 759
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 338-465 8.92e-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: 39.67  E-value: 8.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113054  338 EVTVRHLRTKLKESERRLHERESEIMELKSQLARMrEDWIEEECHRVE---------------AQLALKEARKEIKQLKQ 402
Cdd:TIGR02169  811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL-KEQIKSIEKEIEnlngkkeeleeeleeLEAALRDLESRLGDLKK 889

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907113054  403 VIETMRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEMA--HNSSLRDELCLDFSFDSPEKSLP 465
Cdd:TIGR02169  890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALeeELSEIEDPKGEDEEIPEEELSLE 954
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 385-440 9.84e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 36.00  E-value: 9.84e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907113054 385 EAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKY---FVDINIQNKKLESLLQSME 440
Cdd:cd22887     8 ELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILndeLIALQIENNLLEEKLRKLQ 66
 
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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