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Conserved domains on  [gi|966959734|ref|XP_015001376|]
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syntabulin isoform X4 [Macaca mulatta]

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 ...
 81-373 8.59e-180

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: 507.35  E-value: 8.59e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734   81 NQLSPVNIHPSYAPSSPSSSN-SGSYKGSDCSPIMRRSGRYMSCGENHGVRPPNPEQYLTPLQQKEVTVRHLKTKLKESE 159
Cdd:pfam15290   1 NQGSPVNNRDAYGPSSLSSSSnSGSCKGSDSSPTRRRSGRYHSCGDNHGIKPPNPEQYLTPLQQKEVTIRHLKTKLKESE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734  160 RRLHERESEIVELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKL 239
Cdd:pfam15290  81 NRLQDRETEIEELKSQLSRMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMKSSLAEKDKGIQKYFVDINIQNKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734  240 ESLLQSMEMAHSGSLRDELCLDFPCDSPEKSLTLNPPLDTMADGLS-------LEEQVAGEGVDRELLVGDSIADGTDLF 312
Cdd:pfam15290 161 ESLLQSMELAQNGSLRDEGTLEFACDSPAKSLTRSSTYTKLSDQLAaeengleLEDQSAEEMADSGLLANDEMANRTDLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966959734  313 DEMVTATTTESGDLELVHST-----PGANVLQLLPMvMGLEEGSVVVERAVQTDVVPYSPAISELI 373
Cdd:pfam15290 241 EEVFMSTAVEAGDLAPFSSTyeklmGSQKSVEALPS-CSEEKQQMVEEQAIQTDVVPYSPDLDTLL 305
 
Name Accession Description Interval E-value
Syntaphilin pfam15290
Golgi-localized syntaxin-1-binding clamp; Syntaphilin or Syntabulin is a family of eukaryotic ...
 81-373 8.59e-180

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: 507.35  E-value: 8.59e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734   81 NQLSPVNIHPSYAPSSPSSSN-SGSYKGSDCSPIMRRSGRYMSCGENHGVRPPNPEQYLTPLQQKEVTVRHLKTKLKESE 159
Cdd:pfam15290   1 NQGSPVNNRDAYGPSSLSSSSnSGSCKGSDSSPTRRRSGRYHSCGDNHGIKPPNPEQYLTPLQQKEVTIRHLKTKLKESE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734  160 RRLHERESEIVELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKL 239
Cdd:pfam15290  81 NRLQDRETEIEELKSQLSRMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMKSSLAEKDKGIQKYFVDINIQNKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734  240 ESLLQSMEMAHSGSLRDELCLDFPCDSPEKSLTLNPPLDTMADGLS-------LEEQVAGEGVDRELLVGDSIADGTDLF 312
Cdd:pfam15290 161 ESLLQSMELAQNGSLRDEGTLEFACDSPAKSLTRSSTYTKLSDQLAaeengleLEDQSAEEMADSGLLANDEMANRTDLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966959734  313 DEMVTATTTESGDLELVHST-----PGANVLQLLPMvMGLEEGSVVVERAVQTDVVPYSPAISELI 373
Cdd:pfam15290 241 EEVFMSTAVEAGDLAPFSSTyeklmGSQKSVEALPS-CSEEKQQMVEEQAIQTDVVPYSPDLDTLL 305
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
148-247 2.74e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.53  E-value: 2.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734 148 VRHLKTKLKESERRLHERESEIVELKSQLARMREdwIEEEchrVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQK 227
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKE--LKEK---AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE 328

                         90       100
                 ....*....|....*....|
gi 966959734 228 YFVDINIQNKKLESLLQSME 247
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLK 348
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 141-242 3.66e-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: 3.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734  141 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLArmrEDWIEE--------ECHRVEAQLALKEARKEIKQLKQVIE 212
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE---QDWNKElkselknqEKKLEEIQNQISQNNKIISQLNEQIS 345

                          90       100       110
                  ....*....|....*....|....*....|
gi 966959734  213 TMRSSLADKDKGIQKYFVDINIQNKKLESL 242
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKL 375
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
141-258 4.21e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 4.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734 141 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMREDW--IEEECHRVEAQLA-----LKEARKEIKQLKQVIET 213
Cdd:COG4372   61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELesLQEEAEELQEELEelqkeRQDLEQQRKQLEAQIAE 140

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 966959734 214 MRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEMAHSGSLRDEL 258
Cdd:COG4372  141 LQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
DD_cGKI cd12083
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent ...
 141-176 3.40e-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: 35.62  E-value: 3.40e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 966959734 141 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQL 176
Cdd:cd12083    4 LEEKTEELRKKDERIRELEQELQEKDEEIQELRSQL 39
 
Name Accession Description Interval E-value
Syntaphilin pfam15290
Golgi-localized syntaxin-1-binding clamp; Syntaphilin or Syntabulin is a family of eukaryotic ...
 81-373 8.59e-180

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: 507.35  E-value: 8.59e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734   81 NQLSPVNIHPSYAPSSPSSSN-SGSYKGSDCSPIMRRSGRYMSCGENHGVRPPNPEQYLTPLQQKEVTVRHLKTKLKESE 159
Cdd:pfam15290   1 NQGSPVNNRDAYGPSSLSSSSnSGSCKGSDSSPTRRRSGRYHSCGDNHGIKPPNPEQYLTPLQQKEVTIRHLKTKLKESE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734  160 RRLHERESEIVELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKL 239
Cdd:pfam15290  81 NRLQDRETEIEELKSQLSRMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMKSSLAEKDKGIQKYFVDINIQNKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734  240 ESLLQSMEMAHSGSLRDELCLDFPCDSPEKSLTLNPPLDTMADGLS-------LEEQVAGEGVDRELLVGDSIADGTDLF 312
Cdd:pfam15290 161 ESLLQSMELAQNGSLRDEGTLEFACDSPAKSLTRSSTYTKLSDQLAaeengleLEDQSAEEMADSGLLANDEMANRTDLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966959734  313 DEMVTATTTESGDLELVHST-----PGANVLQLLPMvMGLEEGSVVVERAVQTDVVPYSPAISELI 373
Cdd:pfam15290 241 EEVFMSTAVEAGDLAPFSSTyeklmGSQKSVEALPS-CSEEKQQMVEEQAIQTDVVPYSPDLDTLL 305
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
148-247 2.74e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.53  E-value: 2.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734 148 VRHLKTKLKESERRLHERESEIVELKSQLARMREdwIEEEchrVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQK 227
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKE--LKEK---AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE 328

                         90       100
                 ....*....|....*....|
gi 966959734 228 YFVDINIQNKKLESLLQSME 247
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLK 348
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 143-289 4.16e-07

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: 52.12  E-value: 4.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734  143 QKEVTVRHLKT--KLKESERRLHERESEIVELKSQLARMREDWIEEECHrVEAQLA-----------LKEARKEIKQLKQ 209
Cdd:pfam15905 172 MKEVMAKQEGMegKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSE-TEKLLEyitelscvseqVEKYKLDIAQLEE 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734  210 V-------IETMRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEMAHSgslrdelcldfpcdspEKSLTLNPPLDTMAD 282
Cdd:pfam15905 251 LlkekndeIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYE----------------EKEQTLNAELEELKE 314


                  ....*..
gi 966959734  283 GLSLEEQ 289
Cdd:pfam15905 315 KLTLEEQ 321
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 141-242 3.66e-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: 3.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734  141 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLArmrEDWIEE--------ECHRVEAQLALKEARKEIKQLKQVIE 212
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE---QDWNKElkselknqEKKLEEIQNQISQNNKIISQLNEQIS 345

                          90       100       110
                  ....*....|....*....|....*....|
gi 966959734  213 TMRSSLADKDKGIQKYFVDINIQNKKLESL 242
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKL 375
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 133-248 1.54e-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: 44.63  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734  133 NPEQYLTPLQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIE 212
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 966959734  213 TMRSSLADKDKGIQKyfvdINIQNKKLESLLQSMEM 248
Cdd:TIGR04523 264 KIKKQLSEKQKELEQ----NNKKIKELEKQLNQLKS 295
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 151-228 3.11e-04

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


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 40.63  E-value: 3.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734  151 LKTKLKESERRLHERESEIVELKSQLARMREDWIE-----EECH--RVEAQLALKEARK-------EIKQLKQVIETMRS 216
Cdd:pfam13863  15 LDAKREEIERLEELLKQREEELEKKEQELKEDLIKfdkflKENDakRRRALKKAEEETKlkkekekEIKKLTAQIEELKS 94

                          90
                  ....*....|..
gi 966959734  217 SLADKDKGIQKY 228
Cdd:pfam13863  95 EISKLEEKLEEY 106
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 141-241 4.18e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 4.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734 141 LQQKEvtvRHLKTKLKESERRLHERESEIVELKSQLARM--REDWIEEECHRvEAQLALKEARKE----IKQLKQVIETM 214
Cdd:PRK00409 525 LEELE---RELEQKAEEAEALLKEAEKLKEELEEKKEKLqeEEDKLLEEAEK-EAQQAIKEAKKEadeiIKELRQLQKGG 600

                         90       100
                 ....*....|....*....|....*...
gi 966959734 215 RSSLADKD-KGIQKyfvDINIQNKKLES 241
Cdd:PRK00409 601 YASVKAHElIEARK---RLNKANEKKEK 625
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
141-258 4.21e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 4.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734 141 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMREDW--IEEECHRVEAQLA-----LKEARKEIKQLKQVIET 213
Cdd:COG4372   61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELesLQEEAEELQEELEelqkeRQDLEQQRKQLEAQIAE 140

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 966959734 214 MRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEMAHSGSLRDEL 258
Cdd:COG4372  141 LQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
151-245 5.05e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 5.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734 151 LKTKLKESERRLHERESEIVELKSQLARM---REDWIEEECHRVEA----QLALKEARKEIKQLKQVIETMRSSLADKDK 223
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELEELgfeSVEELEERLKELEPfyneYLELKDAEKELEREEKELKKLEEELDKAFE 633

                         90       100
                 ....*....|....*....|..
gi 966959734 224 GIQKYFVDINIQNKKLESLLQS 245
Cdd:PRK03918 634 ELAETEKRLEELRKELEELEKK 655
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
133-250 5.19e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 5.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734 133 NPEQYLTPLQQKEVTVRHLKTK---LKESERRLHERESEIVELKSQLARMREDW-----------IEEECHRVEAQLA-- 196
Cdd:COG4717   65 KPELNLKELKELEEELKEAEEKeeeYAELQEELEELEEELEELEAELEELREELeklekllqllpLYQELEALEAELAel 144

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966959734 197 ------LKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKK-LESLLQSMEMAH 250
Cdd:COG4717  145 perleeLEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQ 205
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 136-258 6.70e-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: 42.31  E-value: 6.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734  136 QYLTPlQQKE--VTVRHLKTKLKESERRLHERESEIVELKSQLARmreDWIEEEchrveaqlaLKEARKEIKQLKQVIET 213
Cdd:TIGR04523 513 KDLTK-KISSlkEKIEKLESEKKEKESKISDLEDELNKDDFELKK---ENLEKE---------IDEKNKEIEELKQTQKS 579

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 966959734  214 MRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEmahsgSLRDEL 258
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS-----SLEKEL 619
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
151-249 1.00e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734 151 LKTKLKESERRLHERESEIVELKSQLARMREDwIEEECHRV--EAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKY 228
Cdd:COG3206  275 LEAELAELSARYTPNHPDVIALRAQIAALRAQ-LQQEAQRIlaSLEAELEALQAREASLQAQLAQLEARLAELPELEAEL 353

                         90       100
                 ....*....|....*....|....
gi 966959734 229 FV---DINIQNKKLESLLQSMEMA 249
Cdd:COG3206  354 RRlerEVEVARELYESLLQRLEEA 377
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 141-258 1.05e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734 141 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLarmredwieeechrVEAQLALKEARKEIKQLKQVIETMRsSLAD 220
Cdd:COG1579   12 LQELDSELDRLEHRLKELPAELAELEDELAALEARL--------------EAAKTELEDLEKEIKRLELEIEEVE-ARIK 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 966959734 221 KDKGIQKyfvdiNIQN-KKLESLLQSMEMAHS--GSLRDEL 258
Cdd:COG1579   77 KYEEQLG-----NVRNnKEYEALQKEIESLKRriSDLEDEI 112
RNase_Y_N pfam12072
RNase Y N-terminal region;
141-219 1.25e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 40.25  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734  141 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMRED---WIEEECHRVE--AQLALKEARKEIkqLKQVIETMR 215
Cdd:pfam12072  87 LLQKEETLDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEEleeLIEEQRQELEriSGLTSEEAKEIL--LDEVEEELR 164


                  ....
gi 966959734  216 SSLA 219
Cdd:pfam12072 165 HEAA 168
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 141-244 1.59e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734   141 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMREDwIEEECHRV--------EAQLALKEARKEIKQLKQVIE 212
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED-IESLAAEIeeleelieELESELEALLNERASLEEALA 890

                           90       100       110
                   ....*....|....*....|....*....|..
gi 966959734   213 TMRSSLADKDKGIQkyfvDINIQNKKLESLLQ 244
Cdd:TIGR02168  891 LLRSELEELSEELR----ELESKRSELRRELE 918
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 154-242 1.59e-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: 40.90  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734 154 KLKESERRLHERESEIVELKSQLARMREDwieeechRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDIN 233
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKE-------EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93


                 ....*....
gi 966959734 234 IQNKKLESL 242
Cdd:COG4942   94 ELRAELEAQ 102
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
 151-245 1.62e-03

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


Pssm-ID: 293683 [Multi-domain]  Cd Length: 228  Bit Score: 40.11  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734  151 LKTKLKESERRLHERESEIVELKSQL-------ARMREDW---------IEEECHRVEAQL-ALKEARKEIKQ-LKQVIE 212
Cdd:pfam17078  57 LSSMLNRKERRLKDLEDQLSELKNSYeeltesnKQLKKRLenssasettLEAELERLQIQYdALVDSQNEYKDhYQQEIN 136

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 966959734  213 TMRSSL----ADKDKGIQKYFVDINIQNKKLESLLQS 245
Cdd:pfam17078 137 TLQESLedlkLENEKQLENYQQRISSNDKDIDTKLDS 173
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 142-247 1.72e-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: 41.16  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734  142 QQKEVTVRHLKTKLKESERRLHERESEIV-------ELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLK------ 208
Cdd:TIGR04523 303 QKEQDWNKELKSELKNQEKKLEEIQNQISqnnkiisQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKkenqsy 382

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 966959734  209 -QVIETMRSSLADKDKGIQKY-----FVDINIQNKKLESLLQSME 247
Cdd:TIGR04523 383 kQEIKNLESQINDLESKIQNQeklnqQKDEQIKKLQQEKELLEKE 427
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
141-247 1.86e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734 141 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMREDWIEEECHRVEAQL-----ALKEARKEIKQLKQVIETMR 215
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYlelsrELAGLRAELEELEKRREEIK 693

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 966959734 216 SSL----ADKDKgIQKYFVDIniqnKKLESLLQSME 247
Cdd:PRK03918 694 KTLeklkEELEE-REKAKKEL----EKLEKALERVE 724
PRK01156 PRK01156
chromosome segregation protein; Provisional
 152-249 2.33e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.66  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734 152 KTKLKESERRLHERESEIVELKSQLAR-MREdwIEEECHRVEAQLALKEARK-EIKQLKQVIETMRSSLADKDkGIQKYF 229
Cdd:PRK01156 593 KKQLNDLESRLQEIEIGFPDDKSYIDKsIRE--IENEANNLNNKYNEIQENKiLIEKLRGKIDNYKKQIAEID-SIIPDL 669

                         90       100
                 ....*....|....*....|
gi 966959734 230 VDINIQNKKLESLLQSMEMA 249
Cdd:PRK01156 670 KEITSRINDIEDNLKKSRKA 689
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
143-247 2.47e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734 143 QKEVtvRHLKTKLKESERRLHERESEIVELKSQLARMRE--DWIEEECHRVEAQLA-----LKEARKEIKQLKQVIETMR 215
Cdd:COG4372   44 QEEL--EQLREELEQAREELEQLEEELEQARSELEQLEEelEELNEQLQAAQAELAqaqeeLESLQEEAEELQEELEELQ 121

                         90       100       110
                 ....*....|....*....|....*....|..
gi 966959734 216 SSLADkdkgIQKYFVDINIQNKKLESLLQSME 247
Cdd:COG4372  122 KERQD----LEQQRKQLEAQIAELQSEIAERE 149
DD_cGKI cd12083
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent ...
 141-176 3.40e-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: 35.62  E-value: 3.40e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 966959734 141 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQL 176
Cdd:cd12083    4 LEEKTEELRKKDERIRELEQELQEKDEEIQELRSQL 39
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 143-248 4.41e-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: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734  143 QKEVTVRHLKTKLKESER---RLHERESEIVELKSQLA------RMREDWIeeECHRV-----EAQlaLKEARKEIKQLK 208
Cdd:pfam05911 696 EKENLEVELASCTENLEStksQLQESEQLIAELRSELAslkesnSLAETQL--KCMAEsyedlETR--LTELEAELNELR 771

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 966959734  209 QVIETMRSSLADKDKGIQkyfvDINIQNKKLESLLQSMEM 248
Cdd:pfam05911 772 QKFEALEVELEEEKNCHE----ELEAKCLELQEQLERNEK 807
PRK12704 PRK12704
phosphodiesterase; Provisional
 143-221 6.65e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.99  E-value: 6.65e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966959734 143 QKEVTVRhlKTKLKESERRLHEREsEIVELKSQLARMREDWIEEECHRVEAQLalkearKEIKQLKQVIETMRSSLADK 221
Cdd:PRK12704  74 EKELRER--RNELQKLEKRLLQKE-ENLDRKLELLEKREEELEKKEKELEQKQ------QELEKKEEELEELIEEQLQE 143
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 141-228 7.02e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 7.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734 141 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMREDwieeechrveaqlaLKEARKEIKQLKQVIETMRSSLAD 220
Cdd:COG4942   43 LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE--------------LAELEKEIAELRAELEAQKEELAE 108


                 ....*...
gi 966959734 221 KDKGIQKY 228
Cdd:COG4942  109 LLRALYRL 116
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 144-281 7.19e-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: 39.11  E-value: 7.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734  144 KEVTVRHLKTKLKESERRLHERESEIVELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDK 223
Cdd:pfam07888 127 HEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDT 206

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966959734  224 GIQKYFVDINIQNKKL----------ESLLQSMEmahsgSLRDELCLdfpcdSPEKSLTLNPPLDTMA 281
Cdd:pfam07888 207 QVLQLQDTITTLTQKLttahrkeaenEALLEELR-----SLQERLNA-----SERKVEGLGEELSSMA 264
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 135-228 8.15e-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: 38.36  E-value: 8.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734  135 EQYLTPLQQKEVTVRHLKTKLKESERRLHER----ESEIVELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQV 210
Cdd:pfam13868 158 LEYLKEKAEREEEREAEREEIEEEKEREIARlraqQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQEL 237

                          90
                  ....*....|....*...
gi 966959734  211 IETMRSSLADKDKGIQKY 228
Cdd:pfam13868 238 QQAREEQIELKERRLAEE 255
PRK12704 PRK12704
phosphodiesterase; Provisional
 141-215 8.48e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.61  E-value: 8.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734 141 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMR---EDWIEEECHRVE--AQLALKEARKEIkqLKQVIETMR 215
Cdd:PRK12704  91 LLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEeelEELIEEQLQELEriSGLTAEEAKEIL--LEKVEEEAR 168
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 135-221 9.95e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 9.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966959734 135 EQYLTPLQ-QKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIET 213
Cdd:COG1196  199 ERQLEPLErQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278


                 ....*...
gi 966959734 214 MRSSLADK 221
Cdd:COG1196  279 LELELEEA 286
 
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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