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Conserved domains on  [gi|153090193|ref|NP_001093219|]
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syntabulin isoform d [Homo sapiens]

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 ...
 92-384 1.39e-179

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: 1.39e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193   92 NQLSPVNIHPSYAPSSPSSSN-SGSYKGSDCSPIMRRSGRYMSCGENHGVRPPNPEQYLTPLQQKEVTVRHLKTKLKESE 170
Cdd:pfam15290   1 NQGSPVNNRDAYGPSSLSSSSnSGSCKGSDSSPTRRRSGRYHSCGDNHGIKPPNPEQYLTPLQQKEVTIRHLKTKLKESE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193  171 RRLHERESEIVELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKL 250
Cdd:pfam15290  81 NRLQDRETEIEELKSQLSRMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMKSSLAEKDKGIQKYFVDINIQNKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193  251 ESLLQSMEMAHSGSLRDELCLDFPCDSPEKSLTLNPPLDTMADGLS-------LEEQVTGEGADRELLVGDSIANSTDLF 323
Cdd:pfam15290 161 ESLLQSMELAQNGSLRDEGTLEFACDSPAKSLTRSSTYTKLSDQLAaeengleLEDQSAEEMADSGLLANDEMANRTDLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153090193  324 DEIVTATTTESGDLELVHST-----PGANVLELLPiVMGQEEGSVVVERAVQTDVVPYSPAISELI 384
Cdd:pfam15290 241 EEVFMSTAVEAGDLAPFSSTyeklmGSQKSVEALP-SCSEEKQQMVEEQAIQTDVVPYSPDLDTLL 305
 
Name Accession Description Interval E-value
Syntaphilin pfam15290
Golgi-localized syntaxin-1-binding clamp; Syntaphilin or Syntabulin is a family of eukaryotic ...
 92-384 1.39e-179

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: 1.39e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193   92 NQLSPVNIHPSYAPSSPSSSN-SGSYKGSDCSPIMRRSGRYMSCGENHGVRPPNPEQYLTPLQQKEVTVRHLKTKLKESE 170
Cdd:pfam15290   1 NQGSPVNNRDAYGPSSLSSSSnSGSCKGSDSSPTRRRSGRYHSCGDNHGIKPPNPEQYLTPLQQKEVTIRHLKTKLKESE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193  171 RRLHERESEIVELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKL 250
Cdd:pfam15290  81 NRLQDRETEIEELKSQLSRMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMKSSLAEKDKGIQKYFVDINIQNKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193  251 ESLLQSMEMAHSGSLRDELCLDFPCDSPEKSLTLNPPLDTMADGLS-------LEEQVTGEGADRELLVGDSIANSTDLF 323
Cdd:pfam15290 161 ESLLQSMELAQNGSLRDEGTLEFACDSPAKSLTRSSTYTKLSDQLAaeengleLEDQSAEEMADSGLLANDEMANRTDLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153090193  324 DEIVTATTTESGDLELVHST-----PGANVLELLPiVMGQEEGSVVVERAVQTDVVPYSPAISELI 384
Cdd:pfam15290 241 EEVFMSTAVEAGDLAPFSSTyeklmGSQKSVEALP-SCSEEKQQMVEEQAIQTDVVPYSPDLDTLL 305
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
159-258 7.11e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.37  E-value: 7.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193 159 VRHLKTKLKESERRLHERESEIVELKSQLARMREdwIEEEchrVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQK 238
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKE--LKEK---AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE 328

                         90       100
                 ....*....|....*....|
gi 153090193 239 YFVDINIQNKKLESLLQSME 258
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLK 348
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 152-253 5.23e-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: 46.17  E-value: 5.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193  152 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLArmrEDWIEE--------ECHRVEAQLALKEARKEIKQLKQVIE 223
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE---QDWNKElkselknqEKKLEEIQNQISQNNKIISQLNEQIS 345

                          90       100       110
                  ....*....|....*....|....*....|
gi 153090193  224 TMRSSLADKDKGIQKYFVDINIQNKKLESL 253
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKL 375
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
144-261 6.40e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 6.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193 144 NPEQYLTPLQQKEVTVRHLKTK---LKESERRLHERESEIVELKSQLARMREDW-----------IEEECHRVEAQLA-- 207
Cdd:COG4717   65 KPELNLKELKELEEELKEAEEKeeeYAELQEELEELEEELEELEAELEELREELeklekllqllpLYQELEALEAELAel 144

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153090193 208 ------LKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKK-LESLLQSMEMAH 261
Cdd:COG4717  145 perleeLEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQ 205
DD_cGKI cd12083
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent ...
 152-187 4.57e-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: 35.24  E-value: 4.57e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 153090193 152 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQL 187
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 ...
 92-384 1.39e-179

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: 1.39e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193   92 NQLSPVNIHPSYAPSSPSSSN-SGSYKGSDCSPIMRRSGRYMSCGENHGVRPPNPEQYLTPLQQKEVTVRHLKTKLKESE 170
Cdd:pfam15290   1 NQGSPVNNRDAYGPSSLSSSSnSGSCKGSDSSPTRRRSGRYHSCGDNHGIKPPNPEQYLTPLQQKEVTIRHLKTKLKESE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193  171 RRLHERESEIVELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKL 250
Cdd:pfam15290  81 NRLQDRETEIEELKSQLSRMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMKSSLAEKDKGIQKYFVDINIQNKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193  251 ESLLQSMEMAHSGSLRDELCLDFPCDSPEKSLTLNPPLDTMADGLS-------LEEQVTGEGADRELLVGDSIANSTDLF 323
Cdd:pfam15290 161 ESLLQSMELAQNGSLRDEGTLEFACDSPAKSLTRSSTYTKLSDQLAaeengleLEDQSAEEMADSGLLANDEMANRTDLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153090193  324 DEIVTATTTESGDLELVHST-----PGANVLELLPiVMGQEEGSVVVERAVQTDVVPYSPAISELI 384
Cdd:pfam15290 241 EEVFMSTAVEAGDLAPFSSTyeklmGSQKSVEALP-SCSEEKQQMVEEQAIQTDVVPYSPDLDTLL 305
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
159-258 7.11e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.37  E-value: 7.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193 159 VRHLKTKLKESERRLHERESEIVELKSQLARMREdwIEEEchrVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQK 238
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKE--LKEK---AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE 328

                         90       100
                 ....*....|....*....|
gi 153090193 239 YFVDINIQNKKLESLLQSME 258
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLK 348
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 154-300 1.34e-06

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: 50.58  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193  154 QKEVTVRHLKT--KLKESERRLHERESEIVELKSQLARMREDWIEEECHrVEAQLA-----------LKEARKEIKQLKQ 220
Cdd:pfam15905 172 MKEVMAKQEGMegKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSE-TEKLLEyitelscvseqVEKYKLDIAQLEE 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193  221 V-------IETMRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEMAHSgslrdelcldfpcdspEKSLTLNPPLDTMAD 293
Cdd:pfam15905 251 LlkekndeIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYE----------------EKEQTLNAELEELKE 314


                  ....*..
gi 153090193  294 GLSLEEQ 300
Cdd:pfam15905 315 KLTLEEQ 321
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 152-253 5.23e-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: 46.17  E-value: 5.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193  152 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLArmrEDWIEE--------ECHRVEAQLALKEARKEIKQLKQVIE 223
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE---QDWNKElkselknqEKKLEEIQNQISQNNKIISQLNEQIS 345

                          90       100       110
                  ....*....|....*....|....*....|
gi 153090193  224 TMRSSLADKDKGIQKYFVDINIQNKKLESL 253
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKL 375
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 144-259 2.09e-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: 44.24  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193  144 NPEQYLTPLQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIE 223
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 153090193  224 TMRSSLADKDKGIQKyfvdINIQNKKLESLLQSMEM 259
Cdd:TIGR04523 264 KIKKQLSEKQKELEQ----NNKKIKELEKQLNQLKS 295
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 162-239 5.53e-04

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


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 39.86  E-value: 5.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193  162 LKTKLKESERRLHERESEIVELKSQLARMREDWIE-----EECH--RVEAQLALKEARK-------EIKQLKQVIETMRS 227
Cdd:pfam13863  15 LDAKREEIERLEELLKQREEELEKKEQELKEDLIKfdkflKENDakRRRALKKAEEETKlkkekekEIKKLTAQIEELKS 94

                          90
                  ....*....|..
gi 153090193  228 SLADKDKGIQKY 239
Cdd:pfam13863  95 EISKLEEKLEEY 106
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 152-252 5.96e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.89  E-value: 5.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193 152 LQQKEvtvRHLKTKLKESERRLHERESEIVELKSQLARM--REDWIEEECHRvEAQLALKEARKE----IKQLKQVIETM 225
Cdd:PRK00409 525 LEELE---RELEQKAEEAEALLKEAEKLKEELEEKKEKLqeEEDKLLEEAEK-EAQQAIKEAKKEadeiIKELRQLQKGG 600

                         90       100
                 ....*....|....*....|....*...
gi 153090193 226 RSSLADKD-KGIQKyfvDINIQNKKLES 252
Cdd:PRK00409 601 YASVKAHElIEARK---RLNKANEKKEK 625
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
144-261 6.40e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 6.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193 144 NPEQYLTPLQQKEVTVRHLKTK---LKESERRLHERESEIVELKSQLARMREDW-----------IEEECHRVEAQLA-- 207
Cdd:COG4717   65 KPELNLKELKELEEELKEAEEKeeeYAELQEELEELEEELEELEAELEELREELeklekllqllpLYQELEALEAELAel 144

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153090193 208 ------LKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKK-LESLLQSMEMAH 261
Cdd:COG4717  145 perleeLEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQ 205
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
162-260 1.03e-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: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193 162 LKTKLKESERRLHERESEIVELKSQLARMREDwIEEECHRV--EAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKY 239
Cdd:COG3206  275 LEAELAELSARYTPNHPDVIALRAQIAALRAQ-LQQEAQRIlaSLEAELEALQAREASLQAQLAQLEARLAELPELEAEL 353

                         90       100
                 ....*....|....*....|....
gi 153090193 240 FV---DINIQNKKLESLLQSMEMA 260
Cdd:COG3206  354 RRlerEVEVARELYESLLQRLEEA 377
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 147-269 1.03e-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: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193  147 QYLTPlQQKE--VTVRHLKTKLKESERRLHERESEIVELKSQLARmreDWIEEEchrveaqlaLKEARKEIKQLKQVIET 224
Cdd:TIGR04523 513 KDLTK-KISSlkEKIEKLESEKKEKESKISDLEDELNKDDFELKK---ENLEKE---------IDEKNKEIEELKQTQKS 579

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 153090193  225 MRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEmahsgSLRDEL 269
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS-----SLEKEL 619
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
162-256 1.14e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193 162 LKTKLKESERRLHERESEIVELKSQLARM---REDWIEEECHRVEA----QLALKEARKEIKQLKQVIETMRSSLADKDK 234
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELEELgfeSVEELEERLKELEPfyneYLELKDAEKELEREEKELKKLEEELDKAFE 633

                         90       100
                 ....*....|....*....|..
gi 153090193 235 GIQKYFVDINIQNKKLESLLQS 256
Cdd:PRK03918 634 ELAETEKRLEELRKELEELEKK 655
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
152-258 1.61e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193 152 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLAD 231
Cdd:COG4372   54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133

                         90       100
                 ....*....|....*....|....*..
gi 153090193 232 KDKGIQKYFVDINIQNKKLESLLQSME 258
Cdd:COG4372  134 LEAQIAELQSEIAEREEELKELEEQLE 160
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 152-269 1.72e-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: 40.29  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193 152 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLarmredwieeechrVEAQLALKEARKEIKQLKQVIETMRsSLAD 231
Cdd:COG1579   12 LQELDSELDRLEHRLKELPAELAELEDELAALEARL--------------EAAKTELEDLEKEIKRLELEIEEVE-ARIK 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 153090193 232 KDKGIQKyfvdiNIQN-KKLESLLQSMEMAHS--GSLRDEL 269
Cdd:COG1579   77 KYEEQLG-----NVRNnKEYEALQKEIESLKRriSDLEDEI 112
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 165-253 2.07e-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: 40.52  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193 165 KLKESERRLHERESEIVELKSQLARMREDwieeechRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDIN 244
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKE-------EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93


                 ....*....
gi 153090193 245 IQNKKLESL 253
Cdd:COG4942   94 ELRAELEAQ 102
RNase_Y_N pfam12072
RNase Y N-terminal region;
152-230 2.30e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 39.48  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193  152 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMRED---WIEEECHRVE--AQLALKEARKEIkqLKQVIETMR 226
Cdd:pfam12072  87 LLQKEETLDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEEleeLIEEQRQELEriSGLTSEEAKEIL--LDEVEEELR 164


                  ....
gi 153090193  227 SSLA 230
Cdd:pfam12072 165 HEAA 168
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 153-258 2.50e-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: 40.77  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193  153 QQKEVTVRHLKTKLKESERRLHERESEIV-------ELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLK------ 219
Cdd:TIGR04523 303 QKEQDWNKELKSELKNQEKKLEEIQNQISqnnkiisQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKkenqsy 382

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 153090193  220 -QVIETMRSSLADKDKGIQKY-----FVDINIQNKKLESLLQSME 258
Cdd:TIGR04523 383 kQEIKNLESQINDLESKIQNQeklnqQKDEQIKKLQQEKELLEKE 427
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
 162-256 2.52e-03

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


Pssm-ID: 293683 [Multi-domain]  Cd Length: 228  Bit Score: 39.72  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193  162 LKTKLKESERRLHERESEIVELKSQL-------ARMREDW---------IEEECHRVEAQL-ALKEARKEIKQ-LKQVIE 223
Cdd:pfam17078  57 LSSMLNRKERRLKDLEDQLSELKNSYeeltesnKQLKKRLenssasettLEAELERLQIQYdALVDSQNEYKDhYQQEIN 136

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 153090193  224 TMRSSL----ADKDKGIQKYFVDINIQNKKLESLLQS 256
Cdd:pfam17078 137 TLQESLedlkLENEKQLENYQQRISSNDKDIDTKLDS 173
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 152-255 2.55e-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: 40.81  E-value: 2.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193   152 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMREDwIEEECHRV--------EAQLALKEARKEIKQLKQVIE 223
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED-IESLAAEIeeleelieELESELEALLNERASLEEALA 890

                           90       100       110
                   ....*....|....*....|....*....|..
gi 153090193   224 TMRSSLADKDKGIQkyfvDINIQNKKLESLLQ 255
Cdd:TIGR02168  891 LLRSELEELSEELR----ELESKRSELRRELE 918
PRK01156 PRK01156
chromosome segregation protein; Provisional
 163-260 4.56e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.88  E-value: 4.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193 163 KTKLKESERRLHERESEIVELKSQLAR-MREdwIEEECHRVEAQLALKEARK-EIKQLKQVIETMRSSLADKDkGIQKYF 240
Cdd:PRK01156 593 KKQLNDLESRLQEIEIGFPDDKSYIDKsIRE--IENEANNLNNKYNEIQENKiLIEKLRGKIDNYKKQIAEID-SIIPDL 669

                         90       100
                 ....*....|....*....|
gi 153090193 241 VDINIQNKKLESLLQSMEMA 260
Cdd:PRK01156 670 KEITSRINDIEDNLKKSRKA 689
DD_cGKI cd12083
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent ...
 152-187 4.57e-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: 35.24  E-value: 4.57e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 153090193 152 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQL 187
Cdd:cd12083    4 LEEKTEELRKKDERIRELEQELQEKDEEIQELRSQL 39
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
152-258 5.40e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 5.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193 152 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMREDWIEEECHRVEAQL-----ALKEARKEIKQLKQVIETMR 226
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYlelsrELAGLRAELEELEKRREEIK 693

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 153090193 227 SSL----ADKDKgIQKYFVDIniqnKKLESLLQSME 258
Cdd:PRK03918 694 KTLeklkEELEE-REKAKKEL----EKLEKALERVE 724
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
152-255 5.91e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 5.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193 152 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLAD 231
Cdd:COG4372   89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168

                         90       100
                 ....*....|....*....|....
gi 153090193 232 KDKGIQKYfvDINIQNKKLESLLQ 255
Cdd:COG4372  169 LEQELQAL--SEAEAEQALDELLK 190
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 154-259 7.09e-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: 39.27  E-value: 7.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193  154 QKEVTVRHLKTKLKESER---RLHERESEIVELKSQLA------RMREDWIeeECHRV-----EAQlaLKEARKEIKQLK 219
Cdd:pfam05911 696 EKENLEVELASCTENLEStksQLQESEQLIAELRSELAslkesnSLAETQL--KCMAEsyedlETR--LTELEAELNELR 771

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 153090193  220 QVIETMRSSLADKDKGIQkyfvDINIQNKKLESLLQSMEM 259
Cdd:pfam05911 772 QKFEALEVELEEEKNCHE----ELEAKCLELQEQLERNEK 807
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
154-258 8.60e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 8.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193 154 QKEVtvRHLKTKLKESERRLHERESEIVELKSQLARMRE--DWIEEECHRVEAQLA-----LKEARKEIKQLKQVIETMR 226
Cdd:COG4372   44 QEEL--EQLREELEQAREELEQLEEELEQARSELEQLEEelEELNEQLQAAQAELAqaqeeLESLQEEAEELQEELEELQ 121

                         90       100       110
                 ....*....|....*....|....*....|..
gi 153090193 227 SSLADkdkgIQKYFVDINIQNKKLESLLQSME 258
Cdd:COG4372  122 KERQD----LEQQRKQLEAQIAELQSEIAERE 149
PRK12704 PRK12704
phosphodiesterase; Provisional
 154-232 8.71e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.61  E-value: 8.71e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153090193 154 QKEVTVRhlKTKLKESERRLHEREsEIVELKSQLARMREDWIEEECHRVEAQLalkearKEIKQLKQVIETMRSSLADK 232
Cdd:PRK12704  74 EKELRER--RNELQKLEKRLLQKE-ENLDRKLELLEKREEELEKKEKELEQKQ------QELEKKEEELEELIEEQLQE 143
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 152-239 9.45e-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: 38.59  E-value: 9.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153090193 152 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMREDwieeechrveaqlaLKEARKEIKQLKQVIETMRSSLAD 231
Cdd:COG4942   43 LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE--------------LAELEKEIAELRAELEAQKEELAE 108


                 ....*...
gi 153090193 232 KDKGIQKY 239
Cdd:COG4942  109 LLRALYRL 116
 
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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