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Conserved domains on  [gi|767953277|ref|XP_011515456|]
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syntabulin isoform X3 [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 ...
 44-336 0e+00

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: 509.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277   44 NQLSPVNIHPSYAPSSPSSSN-SGSYKGSDCSPIMRRSGRYMSCGENHGVRPPNPEQYLTPLQQKEVTVRHLKTKLKESE 122
Cdd:pfam15290   1 NQGSPVNNRDAYGPSSLSSSSnSGSCKGSDSSPTRRRSGRYHSCGDNHGIKPPNPEQYLTPLQQKEVTIRHLKTKLKESE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277  123 RRLHERESEIVELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKL 202
Cdd:pfam15290  81 NRLQDRETEIEELKSQLSRMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMKSSLAEKDKGIQKYFVDINIQNKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277  203 ESLLQSMEMAHSGSLRDELCLDFPCDSPEKSLTLNPPLDTMADGLS-------LEEQVTGEGADRELLVGDSIANSTDLF 275
Cdd:pfam15290 161 ESLLQSMELAQNGSLRDEGTLEFACDSPAKSLTRSSTYTKLSDQLAaeengleLEDQSAEEMADSGLLANDEMANRTDLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767953277  276 DEIVTATTTESGDLELVHST-----PGANVLELLPiVMGQEEGSVVVERAVQTDVVPYSPAISELI 336
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 ...
 44-336 0e+00

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: 509.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277   44 NQLSPVNIHPSYAPSSPSSSN-SGSYKGSDCSPIMRRSGRYMSCGENHGVRPPNPEQYLTPLQQKEVTVRHLKTKLKESE 122
Cdd:pfam15290   1 NQGSPVNNRDAYGPSSLSSSSnSGSCKGSDSSPTRRRSGRYHSCGDNHGIKPPNPEQYLTPLQQKEVTIRHLKTKLKESE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277  123 RRLHERESEIVELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKL 202
Cdd:pfam15290  81 NRLQDRETEIEELKSQLSRMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMKSSLAEKDKGIQKYFVDINIQNKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277  203 ESLLQSMEMAHSGSLRDELCLDFPCDSPEKSLTLNPPLDTMADGLS-------LEEQVTGEGADRELLVGDSIANSTDLF 275
Cdd:pfam15290 161 ESLLQSMELAQNGSLRDEGTLEFACDSPAKSLTRSSTYTKLSDQLAaeengleLEDQSAEEMADSGLLANDEMANRTDLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767953277  276 DEIVTATTTESGDLELVHST-----PGANVLELLPiVMGQEEGSVVVERAVQTDVVPYSPAISELI 336
Cdd:pfam15290 241 EEVFMSTAVEAGDLAPFSSTyeklmGSQKSVEALP-SCSEEKQQMVEEQAIQTDVVPYSPDLDTLL 305
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
111-210 6.15e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.99  E-value: 6.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277 111 VRHLKTKLKESERRLHERESEIVELKSQLARMREdwIEEEchrVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQK 190
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKE--LKEK---AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE 328

                         90       100
                 ....*....|....*....|
gi 767953277 191 YFVDINIQNKKLESLLQSME 210
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLK 348
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 104-205 4.55e-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: 4.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277  104 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLArmrEDWIEE--------ECHRVEAQLALKEARKEIKQLKQVIE 175
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE---QDWNKElkselknqEKKLEEIQNQISQNNKIISQLNEQIS 345

                          90       100       110
                  ....*....|....*....|....*....|
gi 767953277  176 TMRSSLADKDKGIQKYFVDINIQNKKLESL 205
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKL 375
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
96-213 7.92e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 7.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277  96 NPEQYLTPLQQKEVTVRHLKTK---LKESERRLHERESEIVELKSQLARMREDW-----------IEEECHRVEAQLA-- 159
Cdd:COG4717   65 KPELNLKELKELEEELKEAEEKeeeYAELQEELEELEEELEELEAELEELREELeklekllqllpLYQELEALEAELAel 144

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767953277 160 ------LKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKK-LESLLQSMEMAH 213
Cdd:COG4717  145 perleeLEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQ 205
DD_cGKI cd12083
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent ...
 104-139 5.33e-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: 5.33e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 767953277 104 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQL 139
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 ...
 44-336 0e+00

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: 509.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277   44 NQLSPVNIHPSYAPSSPSSSN-SGSYKGSDCSPIMRRSGRYMSCGENHGVRPPNPEQYLTPLQQKEVTVRHLKTKLKESE 122
Cdd:pfam15290   1 NQGSPVNNRDAYGPSSLSSSSnSGSCKGSDSSPTRRRSGRYHSCGDNHGIKPPNPEQYLTPLQQKEVTIRHLKTKLKESE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277  123 RRLHERESEIVELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKL 202
Cdd:pfam15290  81 NRLQDRETEIEELKSQLSRMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMKSSLAEKDKGIQKYFVDINIQNKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277  203 ESLLQSMEMAHSGSLRDELCLDFPCDSPEKSLTLNPPLDTMADGLS-------LEEQVTGEGADRELLVGDSIANSTDLF 275
Cdd:pfam15290 161 ESLLQSMELAQNGSLRDEGTLEFACDSPAKSLTRSSTYTKLSDQLAaeengleLEDQSAEEMADSGLLANDEMANRTDLL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767953277  276 DEIVTATTTESGDLELVHST-----PGANVLELLPiVMGQEEGSVVVERAVQTDVVPYSPAISELI 336
Cdd:pfam15290 241 EEVFMSTAVEAGDLAPFSSTyeklmGSQKSVEALP-SCSEEKQQMVEEQAIQTDVVPYSPDLDTLL 305
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
111-210 6.15e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.99  E-value: 6.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277 111 VRHLKTKLKESERRLHERESEIVELKSQLARMREdwIEEEchrVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQK 190
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKE--LKEK---AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE 328

                         90       100
                 ....*....|....*....|
gi 767953277 191 YFVDINIQNKKLESLLQSME 210
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLK 348
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 106-252 1.00e-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: 1.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277  106 QKEVTVRHLKT--KLKESERRLHERESEIVELKSQLARMREDWIEEECHrVEAQLA-----------LKEARKEIKQLKQ 172
Cdd:pfam15905 172 MKEVMAKQEGMegKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSE-TEKLLEyitelscvseqVEKYKLDIAQLEE 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277  173 V-------IETMRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEMAHSgslrdelcldfpcdspEKSLTLNPPLDTMAD 245
Cdd:pfam15905 251 LlkekndeIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYE----------------EKEQTLNAELEELKE 314


                  ....*..
gi 767953277  246 GLSLEEQ 252
Cdd:pfam15905 315 KLTLEEQ 321
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 104-205 4.55e-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: 4.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277  104 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLArmrEDWIEE--------ECHRVEAQLALKEARKEIKQLKQVIE 175
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE---QDWNKElkselknqEKKLEEIQNQISQNNKIISQLNEQIS 345

                          90       100       110
                  ....*....|....*....|....*....|
gi 767953277  176 TMRSSLADKDKGIQKYFVDINIQNKKLESL 205
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKL 375
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 96-211 1.81e-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: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277   96 NPEQYLTPLQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIE 175
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767953277  176 TMRSSLADKDKGIQKyfvdINIQNKKLESLLQSMEM 211
Cdd:TIGR04523 264 KIKKQLSEKQKELEQ----NNKKIKELEKQLNQLKS 295
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 104-204 5.26e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.51  E-value: 5.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277 104 LQQKEvtvRHLKTKLKESERRLHERESEIVELKSQLARM--REDWIEEECHRvEAQLALKEARKE----IKQLKQVIETM 177
Cdd:PRK00409 525 LEELE---RELEQKAEEAEALLKEAEKLKEELEEKKEKLqeEEDKLLEEAEK-EAQQAIKEAKKEadeiIKELRQLQKGG 600

                         90       100
                 ....*....|....*....|....*...
gi 767953277 178 RSSLADKD-KGIQKyfvDINIQNKKLES 204
Cdd:PRK00409 601 YASVKAHElIEARK---RLNKANEKKEK 625
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 114-191 6.59e-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: 39.47  E-value: 6.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277  114 LKTKLKESERRLHERESEIVELKSQLARMREDWIE-----EECH--RVEAQLALKEARK-------EIKQLKQVIETMRS 179
Cdd:pfam13863  15 LDAKREEIERLEELLKQREEELEKKEQELKEDLIKfdkflKENDakRRRALKKAEEETKlkkekekEIKKLTAQIEELKS 94

                          90
                  ....*....|..
gi 767953277  180 SLADKDKGIQKY 191
Cdd:pfam13863  95 EISKLEEKLEEY 106
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
96-213 7.92e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 7.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277  96 NPEQYLTPLQQKEVTVRHLKTK---LKESERRLHERESEIVELKSQLARMREDW-----------IEEECHRVEAQLA-- 159
Cdd:COG4717   65 KPELNLKELKELEEELKEAEEKeeeYAELQEELEELEEELEELEAELEELREELeklekllqllpLYQELEALEAELAel 144

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767953277 160 ------LKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKK-LESLLQSMEMAH 213
Cdd:COG4717  145 perleeLEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQ 205
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 99-221 9.05e-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: 41.93  E-value: 9.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277   99 QYLTPlQQKE--VTVRHLKTKLKESERRLHERESEIVELKSQLARmreDWIEEEchrveaqlaLKEARKEIKQLKQVIET 176
Cdd:TIGR04523 513 KDLTK-KISSlkEKIEKLESEKKEKESKISDLEDELNKDDFELKK---ENLEKE---------IDEKNKEIEELKQTQKS 579

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 767953277  177 MRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEmahsgSLRDEL 221
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS-----SLEKEL 619
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
114-208 1.02e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277 114 LKTKLKESERRLHERESEIVELKSQLARM---REDWIEEECHRVEA----QLALKEARKEIKQLKQVIETMRSSLADKDK 186
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELEELgfeSVEELEERLKELEPfyneYLELKDAEKELEREEKELKKLEEELDKAFE 633

                         90       100
                 ....*....|....*....|..
gi 767953277 187 GIQKYFVDINIQNKKLESLLQS 208
Cdd:PRK03918 634 ELAETEKRLEELRKELEELEKK 655
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
114-212 1.16e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277 114 LKTKLKESERRLHERESEIVELKSQLARMREDwIEEECHRV--EAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKY 191
Cdd:COG3206  275 LEAELAELSARYTPNHPDVIALRAQIAALRAQ-LQQEAQRIlaSLEAELEALQAREASLQAQLAQLEARLAELPELEAEL 353

                         90       100
                 ....*....|....*....|....
gi 767953277 192 FV---DINIQNKKLESLLQSMEMA 212
Cdd:COG3206  354 RRlerEVEVARELYESLLQRLEEA 377
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
104-210 1.55e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277 104 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLAD 183
Cdd:COG4372   54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133

                         90       100
                 ....*....|....*....|....*..
gi 767953277 184 KDKGIQKYFVDINIQNKKLESLLQSME 210
Cdd:COG4372  134 LEAQIAELQSEIAEREEELKELEEQLE 160
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 117-205 2.01e-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: 2.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277 117 KLKESERRLHERESEIVELKSQLARMREDwieeechRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDIN 196
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKE-------EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93


                 ....*....
gi 767953277 197 IQNKKLESL 205
Cdd:COG4942   94 ELRAELEAQ 102
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 104-221 2.02e-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: 39.91  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277 104 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLarmredwieeechrVEAQLALKEARKEIKQLKQVIETMRsSLAD 183
Cdd:COG1579   12 LQELDSELDRLEHRLKELPAELAELEDELAALEARL--------------EAAKTELEDLEKEIKRLELEIEEVE-ARIK 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767953277 184 KDKGIQKyfvdiNIQN-KKLESLLQSMEMAHS--GSLRDEL 221
Cdd:COG1579   77 KYEEQLG-----NVRNnKEYEALQKEIESLKRriSDLEDEI 112
RNase_Y_N pfam12072
RNase Y N-terminal region;
104-182 2.03e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 39.48  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277  104 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMRED---WIEEECHRVE--AQLALKEARKEIkqLKQVIETMR 178
Cdd:pfam12072  87 LLQKEETLDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEEleeLIEEQRQELEriSGLTSEEAKEIL--LDEVEEELR 164


                  ....
gi 767953277  179 SSLA 182
Cdd:pfam12072 165 HEAA 168
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 105-210 2.20e-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: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277  105 QQKEVTVRHLKTKLKESERRLHERESEIV-------ELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLK------ 171
Cdd:TIGR04523 303 QKEQDWNKELKSELKNQEKKLEEIQNQISqnnkiisQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKkenqsy 382

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 767953277  172 -QVIETMRSSLADKDKGIQKY-----FVDINIQNKKLESLLQSME 210
Cdd:TIGR04523 383 kQEIKNLESQINDLESKIQNQeklnqQKDEQIKKLQQEKELLEKE 427
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 104-207 2.42e-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: 2.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277   104 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMREDwIEEECHRV--------EAQLALKEARKEIKQLKQVIE 175
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED-IESLAAEIeeleelieELESELEALLNERASLEEALA 890

                           90       100       110
                   ....*....|....*....|....*....|..
gi 767953277   176 TMRSSLADKDKGIQkyfvDINIQNKKLESLLQ 207
Cdd:TIGR02168  891 LLRSELEELSEELR----ELESKRSELRRELE 918
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
 114-208 2.47e-03

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


Pssm-ID: 293683 [Multi-domain]  Cd Length: 228  Bit Score: 39.34  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277  114 LKTKLKESERRLHERESEIVELKSQL-------ARMREDW---------IEEECHRVEAQL-ALKEARKEIKQ-LKQVIE 175
Cdd:pfam17078  57 LSSMLNRKERRLKDLEDQLSELKNSYeeltesnKQLKKRLenssasettLEAELERLQIQYdALVDSQNEYKDhYQQEIN 136

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767953277  176 TMRSSL----ADKDKGIQKYFVDINIQNKKLESLLQS 208
Cdd:pfam17078 137 TLQESLedlkLENEKQLENYQQRISSNDKDIDTKLDS 173
PRK01156 PRK01156
chromosome segregation protein; Provisional
 115-212 3.81e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.88  E-value: 3.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277 115 KTKLKESERRLHERESEIVELKSQLAR-MREdwIEEECHRVEAQLALKEARK-EIKQLKQVIETMRSSLADKDkGIQKYF 192
Cdd:PRK01156 593 KKQLNDLESRLQEIEIGFPDDKSYIDKsIRE--IENEANNLNNKYNEIQENKiLIEKLRGKIDNYKKQIAEID-SIIPDL 669

                         90       100
                 ....*....|....*....|
gi 767953277 193 VDINIQNKKLESLLQSMEMA 212
Cdd:PRK01156 670 KEITSRINDIEDNLKKSRKA 689
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-210 4.71e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 4.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277 104 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMREDWIEEECHRVEAQL-----ALKEARKEIKQLKQVIETMR 178
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYlelsrELAGLRAELEELEKRREEIK 693

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767953277 179 SSL----ADKDKgIQKYFVDIniqnKKLESLLQSME 210
Cdd:PRK03918 694 KTLeklkEELEE-REKAKKEL----EKLEKALERVE 724
DD_cGKI cd12083
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent ...
 104-139 5.33e-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: 5.33e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 767953277 104 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQL 139
Cdd:cd12083    4 LEEKTEELRKKDERIRELEQELQEKDEEIQELRSQL 39
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
104-207 5.50e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 5.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277 104 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLAD 183
Cdd:COG4372   89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168

                         90       100
                 ....*....|....*....|....
gi 767953277 184 KDKGIQKYfvDINIQNKKLESLLQ 207
Cdd:COG4372  169 LEQELQAL--SEAEAEQALDELLK 190
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 106-211 5.72e-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: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277  106 QKEVTVRHLKTKLKESER---RLHERESEIVELKSQLA------RMREDWIeeECHRV-----EAQlaLKEARKEIKQLK 171
Cdd:pfam05911 696 EKENLEVELASCTENLEStksQLQESEQLIAELRSELAslkesnSLAETQL--KCMAEsyedlETR--LTELEAELNELR 771

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767953277  172 QVIETMRSSLADKDKGIQkyfvDINIQNKKLESLLQSMEM 211
Cdd:pfam05911 772 QKFEALEVELEEEKNCHE----ELEAKCLELQEQLERNEK 807
PRK12704 PRK12704
phosphodiesterase; Provisional
 106-184 7.68e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.61  E-value: 7.68e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767953277 106 QKEVTVRhlKTKLKESERRLHEREsEIVELKSQLARMREDWIEEECHRVEAQLalkearKEIKQLKQVIETMRSSLADK 184
Cdd:PRK12704  74 EKELRER--RNELQKLEKRLLQKE-ENLDRKLELLEKREEELEKKEKELEQKQ------QELEKKEEELEELIEEQLQE 143
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
106-210 8.23e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.34  E-value: 8.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277 106 QKEVtvRHLKTKLKESERRLHERESEIVELKSQLARMRE--DWIEEECHRVEAQLA-----LKEARKEIKQLKQVIETMR 178
Cdd:COG4372   44 QEEL--EQLREELEQAREELEQLEEELEQARSELEQLEEelEELNEQLQAAQAELAqaqeeLESLQEEAEELQEELEELQ 121

                         90       100       110
                 ....*....|....*....|....*....|..
gi 767953277 179 SSLADkdkgIQKYFVDINIQNKKLESLLQSME 210
Cdd:COG4372  122 KERQD----LEQQRKQLEAQIAELQSEIAERE 149
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 104-191 8.80e-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: 8.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953277 104 LQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMREDwieeechrveaqlaLKEARKEIKQLKQVIETMRSSLAD 183
Cdd:COG4942   43 LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE--------------LAELEKEIAELRAELEAQKEELAE 108


                 ....*...
gi 767953277 184 KDKGIQKY 191
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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