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Conserved domains on  [gi|74096433|ref|NP_795972|]
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syntabulin isoform a [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 ...
 343-634 2.28e-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: 503.11  E-value: 2.28e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433   343 NPLSPSNIHPSYAPSSPSSSN-SGSYKGSDCSPVMRRSGRYMSCGENHGVKPPNPEQYLTPLQQKEVTVRHLRTKLKESE 421
Cdd:pfam15290   1 NQGSPVNNRDAYGPSSLSSSSnSGSCKGSDSSPTRRRSGRYHSCGDNHGIKPPNPEQYLTPLQQKEVTIRHLKTKLKESE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433   422 RRLHERESEIMELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKL 501
Cdd:pfam15290  81 NRLQDRETEIEELKSQLSRMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMKSSLAEKDKGIQKYFVDINIQNKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433   502 ESLLQSMEMAHNSSLRDELCLDFSFDSPEKSLPLSSTFDKLPDGLS-------LEEQITEEGADSELLVGDSMAEGTDLL 574
Cdd:pfam15290 161 ESLLQSMELAQNGSLRDEGTLEFACDSPAKSLTRSSTYTKLSDQLAaeengleLEDQSAEEMADSGLLANDEMANRTDLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74096433   575 DEMVTATTTESSGLEFVHST-----PGPQALKALPLVSHEEGIAVMEQAVQTDVVPFSPAISELI 634
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 ...
 343-634 2.28e-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: 503.11  E-value: 2.28e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433   343 NPLSPSNIHPSYAPSSPSSSN-SGSYKGSDCSPVMRRSGRYMSCGENHGVKPPNPEQYLTPLQQKEVTVRHLRTKLKESE 421
Cdd:pfam15290   1 NQGSPVNNRDAYGPSSLSSSSnSGSCKGSDSSPTRRRSGRYHSCGDNHGIKPPNPEQYLTPLQQKEVTIRHLKTKLKESE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433   422 RRLHERESEIMELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKL 501
Cdd:pfam15290  81 NRLQDRETEIEELKSQLSRMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMKSSLAEKDKGIQKYFVDINIQNKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433   502 ESLLQSMEMAHNSSLRDELCLDFSFDSPEKSLPLSSTFDKLPDGLS-------LEEQITEEGADSELLVGDSMAEGTDLL 574
Cdd:pfam15290 161 ESLLQSMELAQNGSLRDEGTLEFACDSPAKSLTRSSTYTKLSDQLAaeengleLEDQSAEEMADSGLLANDEMANRTDLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74096433   575 DEMVTATTTESSGLEFVHST-----PGPQALKALPLVSHEEGIAVMEQAVQTDVVPFSPAISELI 634
Cdd:pfam15290 241 EEVFMSTAVEAGDLAPFSSTyeklmGSQKSVEALPSCSEEKQQMVEEQAIQTDVVPYSPDLDTLL 305
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
410-509 3.49e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.91  E-value: 3.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433  410 VRHLRTKLKESERRLHERESEIMELKSQLARMREdwIEEEchrVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQK 489
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKE--LKEK---AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE 328

                         90       100
                 ....*....|....*....|
gi 74096433  490 YFVDINIQNKKLESLLQSME 509
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLK 348
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
403-520 4.48e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.43  E-value: 4.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433 403 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDW--IEEECHRVEAQLA-----LKEARKEIKQLKQVIET 475
Cdd:COG4372  61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELesLQEEAEELQEELEelqkeRQDLEQQRKQLEAQIAE 140

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 74096433 476 MRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEMAHNSSLRDEL 520
Cdd:COG4372 141 LQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 403-520 7.26e-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: 7.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433   403 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLArmrEDWIEE--------ECHRVEAQLALKEARKEIKQLKQVIE 474
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE---QDWNKElkselknqEKKLEEIQNQISQNNKIISQLNEQIS 345

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 74096433   475 TMRSSLADKDKGIQKYFVDINIQNKKLESLLQsmemaHNSSLRDEL 520
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKK-----ENQSYKQEI 386
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 454-509 8.16e-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: 36.39  E-value: 8.16e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 74096433 454 EAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKY---FVDINIQNKKLESLLQSME 509
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 ...
 343-634 2.28e-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: 503.11  E-value: 2.28e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433   343 NPLSPSNIHPSYAPSSPSSSN-SGSYKGSDCSPVMRRSGRYMSCGENHGVKPPNPEQYLTPLQQKEVTVRHLRTKLKESE 421
Cdd:pfam15290   1 NQGSPVNNRDAYGPSSLSSSSnSGSCKGSDSSPTRRRSGRYHSCGDNHGIKPPNPEQYLTPLQQKEVTIRHLKTKLKESE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433   422 RRLHERESEIMELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKL 501
Cdd:pfam15290  81 NRLQDRETEIEELKSQLSRMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMKSSLAEKDKGIQKYFVDINIQNKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433   502 ESLLQSMEMAHNSSLRDELCLDFSFDSPEKSLPLSSTFDKLPDGLS-------LEEQITEEGADSELLVGDSMAEGTDLL 574
Cdd:pfam15290 161 ESLLQSMELAQNGSLRDEGTLEFACDSPAKSLTRSSTYTKLSDQLAaeengleLEDQSAEEMADSGLLANDEMANRTDLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74096433   575 DEMVTATTTESSGLEFVHST-----PGPQALKALPLVSHEEGIAVMEQAVQTDVVPFSPAISELI 634
Cdd:pfam15290 241 EEVFMSTAVEAGDLAPFSSTyeklmGSQKSVEALPSCSEEKQQMVEEQAIQTDVVPYSPDLDTLL 305
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
410-509 3.49e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.91  E-value: 3.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433  410 VRHLRTKLKESERRLHERESEIMELKSQLARMREdwIEEEchrVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQK 489
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKE--LKEK---AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE 328

                         90       100
                 ....*....|....*....|
gi 74096433  490 YFVDINIQNKKLESLLQSME 509
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLK 348
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 399-509 1.85e-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: 48.58  E-value: 1.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433    399 YLTPLQQKEVTVRHLRTKLKESER----RLHERESEIMELKSQL--ARMREDWIEEECHRVEAQLA--LKEARKEIKQLK 470
Cdd:pfam15921  315 YMRQLSDLESTVSQLRSELREAKRmyedKIEELEKQLVLANSELteARTERDQFSQESGNLDDQLQklLADLHKREKELS 394

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 74096433    471 QVIETMRsSLADKDKG-------IQKYFVDINIQNKKLESLLQSME 509
Cdd:pfam15921  395 LEKEQNK-RLWDRDTGnsitidhLRRELDDRNMEVQRLEALLKAMK 439
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
403-520 4.48e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.43  E-value: 4.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433 403 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDW--IEEECHRVEAQLA-----LKEARKEIKQLKQVIET 475
Cdd:COG4372  61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELesLQEEAEELQEELEelqkeRQDLEQQRKQLEAQIAE 140

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 74096433 476 MRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEMAHNSSLRDEL 520
Cdd:COG4372 141 LQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 405-555 6.85e-05

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: 45.96  E-value: 6.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433   405 QKEVTVRH--LRTKLKESERRLHERESEIMELKSQLARMREDWIEEECHrVEAQLA-----------LKEARKEIKQLKQ 471
Cdd:pfam15905 172 MKEVMAKQegMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSE-TEKLLEyitelscvseqVEKYKLDIAQLEE 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433   472 V-------IETMRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEMAHNsslrdelcldfsfdspEKSLPLSSTFDKLPD 544
Cdd:pfam15905 251 LlkekndeIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYE----------------EKEQTLNAELEELKE 314

                         170
                  ....*....|.
gi 74096433   545 GLSLEEQITEE 555
Cdd:pfam15905 315 KLTLEEQEHQK 325
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 403-520 7.26e-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: 7.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433   403 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLArmrEDWIEE--------ECHRVEAQLALKEARKEIKQLKQVIE 474
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE---QDWNKElkselknqEKKLEEIQNQISQNNKIISQLNEQIS 345

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 74096433   475 TMRSSLADKDKGIQKYFVDINIQNKKLESLLQsmemaHNSSLRDEL 520
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKK-----ENQSYKQEI 386
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
403-520 9.25e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 9.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433 403 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMRE--DWIEEECHRVEAQlaLKEARKEIKQLKQVIETMRSSL 480
Cdd:COG4372  54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAelAQAQEELESLQEE--AEELQEELEELQKERQDLEQQR 131

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 74096433 481 ADKDKGIQKYFVDINIQNKKLESLLQSMEmahnsSLRDEL 520
Cdd:COG4372 132 KQLEAQIAELQSEIAEREEELKELEEQLE-----SLQEEL 166
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
395-520 9.65e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 9.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433 395 NPEQYLTPLQQKEVTVRHLRTK---LKESERRLHERESEIMELKSQLARMREDW-----------IEEECHRVEAQLA-- 458
Cdd:COG4717  65 KPELNLKELKELEEELKEAEEKeeeYAELQEELEELEEELEELEAELEELREELeklekllqllpLYQELEALEAELAel 144

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74096433 459 ------LKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKK-LESLLQSMEMAHN--SSLRDEL 520
Cdd:COG4717 145 perleeLEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQrlAELEEEL 215
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 403-520 1.21e-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: 1.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433 403 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLarmredwieeechrVEAQLALKEARKEIKQLKQVIETMRsSLAD 482
Cdd:COG1579  12 LQELDSELDRLEHRLKELPAELAELEDELAALEARL--------------EAAKTELEDLEKEIKRLELEIEEVE-ARIK 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 74096433 483 KDKGIQKyfvdiNIQN-KKLESLLQSMEMAH--NSSLRDEL 520
Cdd:COG1579  77 KYEEQLG-----NVRNnKEYEALQKEIESLKrrISDLEDEI 112
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
405-520 1.96e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 1.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433 405 QKEVtvRHLRTKLKESERRLHERESEIMELKSQLARMRE--DWIEEECHRVEAQLA-----LKEARKEIKQLKQVIETMR 477
Cdd:COG4372  44 QEEL--EQLREELEQAREELEQLEEELEQARSELEQLEEelEELNEQLQAAQAELAqaqeeLESLQEEAEELQEELEELQ 121

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 74096433 478 SSLADkdkgIQKYFVDINIQNKKLESLLQSMEMAHNsSLRDEL 520
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 ...
 413-490 2.23e-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: 41.40  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433   413 LRTKLKESERRLHERESEIMELKSQLARMREDWIE-----EECH--RVEAQLALKEARK-------EIKQLKQVIETMRS 478
Cdd:pfam13863  15 LDAKREEIERLEELLKQREEELEKKEQELKEDLIKfdkflKENDakRRRALKKAEEETKlkkekekEIKKLTAQIEELKS 94

                          90
                  ....*....|..
gi 74096433   479 SLADKDKGIQKY 490
Cdd:pfam13863  95 EISKLEEKLEEY 106
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 395-510 4.48e-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: 4.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433   395 NPEQYLTPLQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIE 474
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 74096433   475 TMRSSLADKDKGIQKyfvdINIQNKKLESLLQSMEM 510
Cdd:TIGR04523 264 KIKKQLSEKQKELEQ----NNKKIKELEKQLNQLKS 295
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
413-511 5.55e-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: 5.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433 413 LRTKLKESERRLHERESEIMELKSQLARMREDwIEEECHRV--EAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKY 490
Cdd:COG3206 275 LEAELAELSARYTPNHPDVIALRAQIAALRAQ-LQQEAQRIlaSLEAELEALQAREASLQAQLAQLEARLAELPELEAEL 353

                        90       100
                ....*....|....*....|....
gi 74096433 491 FV---DINIQNKKLESLLQSMEMA 511
Cdd:COG3206 354 RRlerEVEVARELYESLLQRLEEA 377
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 416-533 6.94e-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: 6.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433 416 KLKESERRLHERESEIMELKSQLARMREDwieeechRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDIN 495
Cdd:COG4942  21 AAAEAEAELEQLQQEIAELEKELAALKKE-------EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 74096433 496 IQNKKLESLLQSME----MAHNSSLRDELCLDFSFDSPEKSL 533
Cdd:COG4942  94 ELRAELEAQKEELAellrALYRLGRQPPLALLLSPEDFLDAV 135
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 403-517 9.93e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 9.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433    403 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDwIEEECHRV--------EAQLALKEARKEIKQLKQVIE 474
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED-IESLAAEIeeleelieELESELEALLNERASLEEALA 890

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 74096433    475 TMRSSLADKDKGIQkyfvDINIQNKKLESLLQS-MEMAHNSSLR 517
Cdd:TIGR02168  891 LLRSELEELSEELR----ELESKRSELRRELEElREKLAQLELR 930
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 397-490 1.23e-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: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433   397 EQYLTPLQQKEVTVRHLRTKLKESERRLHER----ESEIMELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQV 472
Cdd:pfam13868 158 LEYLKEKAEREEEREAEREEIEEEKEREIARlraqQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQEL 237

                          90
                  ....*....|....*...
gi 74096433   473 IETMRSSLADKDKGIQKY 490
Cdd:pfam13868 238 QQAREEQIELKERRLAEE 255
RNase_Y_N pfam12072
RNase Y N-terminal region;
403-481 1.31e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 40.64  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433   403 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMRED---WIEEECHRVE--AQLALKEARKEIkqLKQVIETMR 477
Cdd:pfam12072  87 LLQKEETLDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEEleeLIEEQRQELEriSGLTSEEAKEIL--LDEVEEELR 164


                  ....
gi 74096433   478 SSLA 481
Cdd:pfam12072 165 HEAA 168
RNase_Y_N pfam12072
RNase Y N-terminal region;
406-504 1.32e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 40.64  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433   406 KEVTVRhlRTKLKESERRLHEREsEIMELKSQLARMREDwieeechrveaqlALKEARKEIKQLKQVIETMRSSLADKdk 485
Cdd:pfam12072  71 RELKER--RNELQRQERRLLQKE-ETLDRKDESLEKKEE-------------SLEKKEKELEAQQQQLEEKEEELEEL-- 132

                          90
                  ....*....|....*....
gi 74096433   486 giqkyfvdINIQNKKLESL 504
Cdd:pfam12072 133 --------IEEQRQELERI 143
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
413-507 1.59e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433  413 LRTKLKESERRLHERESEIMELKSQLARM---REDWIEEECHRVEA----QLALKEARKEIKQLKQVIETMRSSLADKDK 485
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELEELgfeSVEELEERLKELEPfyneYLELKDAEKELEREEKELKKLEEELDKAFE 633

                         90       100
                 ....*....|....*....|..
gi 74096433  486 GIQKYFVDINIQNKKLESLLQS 507
Cdd:PRK03918 634 ELAETEKRLEELRKELEELEKK 655
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 398-520 1.67e-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: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433   398 QYLTPlQQKE--VTVRHLRTKLKESERRLHERESEIMELKSQLARmreDWIEEEchrveaqlaLKEARKEIKQLKQVIET 475
Cdd:TIGR04523 513 KDLTK-KISSlkEKIEKLESEKKEKESKISDLEDELNKDDFELKK---ENLEKE---------IDEKNKEIEELKQTQKS 579

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 74096433   476 MRSSLADKDKGIQKYFVDINIQNKKLESLLQSMemahnSSLRDEL 520
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI-----SSLEKEL 619
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
 413-507 1.81e-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: 40.49  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433   413 LRTKLKESERRLHERESEIMELKSQL-------ARMREDW---------IEEECHRVEAQL-ALKEARKEIKQ-LKQVIE 474
Cdd:pfam17078  57 LSSMLNRKERRLKDLEDQLSELKNSYeeltesnKQLKKRLenssasettLEAELERLQIQYdALVDSQNEYKDhYQQEIN 136

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 74096433   475 TMRSSL----ADKDKGIQKYFVDINIQNKKLESLLQS 507
Cdd:pfam17078 137 TLQESLedlkLENEKQLENYQQRISSNDKDIDTKLDS 173
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
403-509 1.82e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433  403 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDWIEEECHRVEAQL-----ALKEARKEIKQLKQVIETMR 477
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYlelsrELAGLRAELEELEKRREEIK 693

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 74096433  478 SSL----ADKDKgIQKYFVDIniqnKKLESLLQSME 509
Cdd:PRK03918 694 KTLeklkEELEE-REKAKKEL----EKLEKALERVE 724
PRK12704 PRK12704
phosphodiesterase; Provisional
 405-504 3.21e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 3.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433  405 QKEVTVRhlRTKLKESERRLHEREsEIMELKSQLARMREDWIEEECHRVEAQLalkearKEIKQLKQVIETMRSSladkd 484
Cdd:PRK12704  74 EKELRER--RNELQKLEKRLLQKE-ENLDRKLELLEKREEELEKKEKELEQKQ------QELEKKEEELEELIEE----- 139

                         90       100
                 ....*....|....*....|
gi 74096433  485 kgiqkyfvdiniQNKKLESL 504
Cdd:PRK12704 140 ------------QLQELERI 147
PRK01156 PRK01156
chromosome segregation protein; Provisional
 416-518 4.16e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.66  E-value: 4.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433  416 KLKESERRLHERESEIMELKSQLAR-MREdwIEEECHRVEAQLALKEARK-EIKQLKQVIETMRSSLADKDkGIQKYFVD 493
Cdd:PRK01156 595 QLNDLESRLQEIEIGFPDDKSYIDKsIRE--IENEANNLNNKYNEIQENKiLIEKLRGKIDNYKKQIAEID-SIIPDLKE 671

                         90       100
                 ....*....|....*....|....*
gi 74096433  494 INIQNKKLESLLQSMEMAHNSSLRD 518
Cdd:PRK01156 672 ITSRINDIEDNLKKSRKALDDAKAN 696
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 406-521 5.30e-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: 5.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433   406 KEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDK 485
Cdd:pfam07888 127 HEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDT 206

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 74096433   486 GIQKYFVDINIQNKKLESLLQ---SMEMAHN--SSLRDELC 521
Cdd:pfam07888 207 QVLQLQDTITTLTQKLTTAHRkeaENEALLEelRSLQERLN 247
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
412-520 6.07e-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: 6.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433  412 HLRTKLKESERRLHERESEIMELKSQLARMRE----------------DW--IEEECHRVEAQLA--------LKEARKE 465
Cdd:COG4913  614 ALEAELAELEEELAEAEERLEALEAELDALQErrealqrlaeyswdeiDVasAEREIAELEAELErldassddLAALEEQ 693

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 74096433  466 IKQLKQVIETMRSSLADKDK---GIQKYFVDINIQNKKLESLLQSMEMAHNSSLRDEL 520
Cdd:COG4913  694 LEELEAELEELEEELDELKGeigRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
403-577 6.51e-03

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 39.04  E-value: 6.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433 403 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQ----LARMRED----WIEEechRVEAQLALKEARKEIKQLKQVIE 474
Cdd:COG1842  39 LVEARQALAQVIANQKRLERQLEELEAEAEKWEEKarlaLEKGREDlareALER---KAELEAQAEALEAQLAQLEEQVE 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433 475 TMRSSLAD-KDKgIQKYfvdiniQNKKlESLLQSMEMAH-----NSSLRdelclDFSFDSPEkslplsSTFDKlpdglsL 548
Cdd:COG1842 116 KLKEALRQlESK-LEEL------KAKK-DTLKARAKAAKaqekvNEALS-----GIDSDDAT------SALER------M 170

                       170       180
                ....*....|....*....|....*....
gi 74096433 549 EEQITEEGADSELLvgDSMAEGTDLLDEM 577
Cdd:COG1842 171 EEKIEEMEARAEAA--AELAAGDSLDDEL 197
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
 419-551 7.09e-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: 39.45  E-value: 7.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433   419 ESERRLHERESEIM----ELKSQLARMRE----------------DWIEEECHRVEAQLALKEARKEI--------KQLK 470
Cdd:pfam03148  43 DSNRRLGERIQDITfwksELEKELEELDEeiellleekrrlekalEALEEPLHIAQECLTLREKRQGIdlvhdeveKELL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433   471 QVIETMrssladkdKGIQKYFV----DINIQNKKLESLLQSMEMAH---NSSLR-DELCLDFSFDSPEKSLPLSSTfdKL 542
Cdd:pfam03148 123 KEVELI--------EGIQELLQrtleQAWEQLRLLRAARHKLEKDLsdkKEALEiDEKCLSLNNTSPNISYKPGPT--RI 192


                  ....*....
gi 74096433   543 PDGLSLEEQ 551
Cdd:pfam03148 193 PPNSSTPEE 201
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 405-514 7.38e-03

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 40.04  E-value: 7.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433   405 QKEVTVRHLRTKLKESER---RLHERESEIMELKSQLA------RMREDWIeeECHRV-----EAQlaLKEARKEIKQLK 470
Cdd:pfam05911 696 EKENLEVELASCTENLEStksQLQESEQLIAELRSELAslkesnSLAETQL--KCMAEsyedlETR--LTELEAELNELR 771

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 74096433   471 QVIETMRSSLADKDKGIQkyfvDINIQNKKLESLLQSMEMAHNS 514
Cdd:pfam05911 772 QKFEALEVELEEEKNCHE----ELEAKCLELQEQLERNEKKESS 811
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 426-520 7.68e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 7.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433    426 ERESEIMELKSQLARMredwiEEECHrvEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKLESLL 505
Cdd:TIGR02168  674 ERRREIEELEEKIEEL-----EEKIA--ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746

                           90
                   ....*....|....*
gi 74096433    506 QsmEMAHNSSLRDEL 520
Cdd:TIGR02168  747 E--RIAQLSKELTEL 759
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 407-534 7.74e-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: 40.05  E-value: 7.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433    407 EVTVRHLRTKLKESERRLHERESEIMELKSQLARMrEDWIEEECHRVE---------------AQLALKEARKEIKQLKQ 471
Cdd:TIGR02169  811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL-KEQIKSIEKEIEnlngkkeeleeeleeLEAALRDLESRLGDLKK 889

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74096433    472 VIETMRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEMA--HNSSLRDELCLDFSFDSPEKSLP 534
Cdd:TIGR02169  890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALeeELSEIEDPKGEDEEIPEEELSLE 954
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
395-479 7.84e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 7.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433 395 NPEQYLTPLQQKEvTVRHLRTKLKESERRLHERESEIMELksqLARMREDWIEEECHRVEAQLA-----LKEARKEIKQL 469
Cdd:COG4717 383 DEEELRAALEQAE-EYQELKEELEELEEQLEELLGELEEL---LEALDEEELEEELEELEEELEeleeeLEELREELAEL 458

                        90
                ....*....|
gi 74096433 470 KQVIETMRSS 479
Cdd:COG4717 459 EAELEQLEED 468
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 454-509 8.16e-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: 36.39  E-value: 8.16e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 74096433 454 EAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKY---FVDINIQNKKLESLLQSME 509
Cdd:cd22887   8 ELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILndeLIALQIENNLLEEKLRKLQ 66
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 403-490 9.40e-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: 9.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74096433 403 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQLARMREDwieeechrveaqlaLKEARKEIKQLKQVIETMRSSLAD 482
Cdd:COG4942  43 LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE--------------LAELEKEIAELRAELEAQKEELAE 108


                ....*...
gi 74096433 483 KDKGIQKY 490
Cdd:COG4942 109 LLRALYRL 116
DD_cGKI cd12083
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent ...
 403-438 9.83e-03

Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent Protein Kinase I (PKG1 or cGKI) is a Serine/Threonine Kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. They contain an N-terminal regulatory domain containing a dimerization/docking region and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. It is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. The dimerization/docking (D/D) domain is a leucine/isoleucine zipper that mediates both homodimerization and interaction with isotype-specific G-kinase-anchoring proteins (GKAPs). The D/D domain of the two variants (alpha and beta) differ, allowing their targeting to different subcellular compartments and intracellular substrates.


Pssm-ID: 213373 [Multi-domain]  Cd Length: 48  Bit Score: 34.85  E-value: 9.83e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 74096433 403 LQQKEVTVRHLRTKLKESERRLHERESEIMELKSQL 438
Cdd:cd12083   4 LEEKTEELRKKDERIRELEQELQEKDEEIQELRSQL 39
 
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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