NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|564331154|ref|XP_006230407|]
View 

syntaxin-4 isoform X1 [Rattus norvegicus]

Protein Classification

SNARE domain-containing protein; syntaxin family protein( domain architecture ID 10075370)

SNARE domain-containing protein such as SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which interact to form a SNARE complex that mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation| syntaxin family protein similar to syntaxin 5 (Syn5) that regulates the transport from the ER to the Golgi, as well as the early/recycling endosomes to the trans-Golgi network and participates in the assembly of transitional ER and the Golgi, lipid droplet fusion, and cytokinesis

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SynN cd00179
Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the ...
 39-189 4.17e-52

Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane; they are a family of receptors for intracellular transport vesicles; each target membrane may be identified by a specific member of the syntaxin family; syntaxins contain a moderately well conserved amino-terminal domain, called Habc, whose structure is an antiparallel three-helix bundle; a linker of about 30 amino acids connects this to the carboxy-terminal region, designated H3 (t_SNARE), of the syntaxin cytoplasmic domain; the highly conserved H3 region forms a single, long alpha-helix when it is part of the core SNARE complex and anchors the protein on the cytoplasmic surface of cellular membranes; H3 is not included in defining this domain


:

Pssm-ID: 238105 [Multi-domain]  Cd Length: 151  Bit Score: 172.47  E-value: 4.17e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  39 DEFFQKVQTIRQTMAKLESKVRELEKQQVTILATPLPEESMKQGLQNLREEIKQLGREVRAQLKAIEPQKEEADENYNSV 118
Cdd:cd00179    2 EEFFEEVEEIRGNIDKISEDVEELQKLHSQLLTAPDADPELKQELESLVQEIKKLAKEIKGKLKELEESNEQNEALNGSS 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564331154 119 NTRMKKTQHGVLSQQFVELINKCNSMQSEYREKNVERIRRQLKITNaGMVSDEELEQMLDSGQSEVFVSNI 189
Cdd:cd00179   82 VDRIRKTQHSGLSKKFVEVMTEFNKAQRKYRERYKERIQRQLEITG-GEATDEELEDMLESGNSEIFTSQI 151
SNARE_syntaxin4 cd15883
SNARE motif of syntaxin 4; Syntaxin-4 forms a complex with SNAP-23 (Qb/Qc) and R-SNAREs VAMP8, ...
 199-260 1.85e-31

SNARE motif of syntaxin 4; Syntaxin-4 forms a complex with SNAP-23 (Qb/Qc) and R-SNAREs VAMP8, VAMP2 and VAMP7 which plays a role in exocytosis of secetory granule. Syntaxin 4 is member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle.


:

Pssm-ID: 277236  Cd Length: 63  Bit Score: 115.04  E-value: 1.85e-31
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564331154 199 ALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVK 260
Cdd:cd15883    1 ALNEIEARHSEIQKLERSIRELHDMFTYLAMEVEAQGEMIDRIEKNILSSADYVEKAQEHVK 62
 
Name Accession Description Interval E-value
SynN cd00179
Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the ...
 39-189 4.17e-52

Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane; they are a family of receptors for intracellular transport vesicles; each target membrane may be identified by a specific member of the syntaxin family; syntaxins contain a moderately well conserved amino-terminal domain, called Habc, whose structure is an antiparallel three-helix bundle; a linker of about 30 amino acids connects this to the carboxy-terminal region, designated H3 (t_SNARE), of the syntaxin cytoplasmic domain; the highly conserved H3 region forms a single, long alpha-helix when it is part of the core SNARE complex and anchors the protein on the cytoplasmic surface of cellular membranes; H3 is not included in defining this domain


Pssm-ID: 238105 [Multi-domain]  Cd Length: 151  Bit Score: 172.47  E-value: 4.17e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  39 DEFFQKVQTIRQTMAKLESKVRELEKQQVTILATPLPEESMKQGLQNLREEIKQLGREVRAQLKAIEPQKEEADENYNSV 118
Cdd:cd00179    2 EEFFEEVEEIRGNIDKISEDVEELQKLHSQLLTAPDADPELKQELESLVQEIKKLAKEIKGKLKELEESNEQNEALNGSS 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564331154 119 NTRMKKTQHGVLSQQFVELINKCNSMQSEYREKNVERIRRQLKITNaGMVSDEELEQMLDSGQSEVFVSNI 189
Cdd:cd00179   82 VDRIRKTQHSGLSKKFVEVMTEFNKAQRKYRERYKERIQRQLEITG-GEATDEELEDMLESGNSEIFTSQI 151
Syntaxin pfam00804
Syntaxin; Syntaxins are the prototype family of SNARE proteins. They usually consist of three ...
 40-235 4.49e-40

Syntaxin; Syntaxins are the prototype family of SNARE proteins. They usually consist of three main regions - a C-terminal transmembrane region, a central SNARE domain which is characteriztic of and conserved in all syntaxins (pfam05739), and an N-terminal domain that is featured in this entry. This domain varies between syntaxin isoforms; in syntaxin 1A it is found as three alpha-helices with a left-handed twist. It may fold back on the SNARE domain to allow the molecule to adopt a 'closed' configuration that prevents formation of the core fusion complex - it thus has an auto-inhibitory role. The function of syntaxins is determined by their localization. They are involved in neuronal exocytosis, ER-Golgi transport and Golgi-endosome transport, for example. They also interact with other proteins as well as those involved in SNARE complexes. These include vesicle coat proteins, Rab GTPases, and tethering factors.


Pssm-ID: 459942 [Multi-domain]  Cd Length: 203  Bit Score: 142.71  E-value: 4.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154   40 EFFQKVQTIRQTMAKLESKVRELEKQQV--TILATPLPEESMKQGLQNLREEIKQLGREVRAQLKAIEPQKEEADENY-- 115
Cdd:pfam00804   1 DFFKEVQEIKEEIEKIRLLVKKLQKQNEesKLLTSARRMSVIKRRMNSIARDIKKRAESIKRRLEALDKSNAENEKKPgc 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  116 --NSVNTRMKKTQHGVLSQQFVELINKCN----SMQSEYREknveRIRRQLKITNAGMVSDEELEQMLDSGQSEVFVSNI 189
Cdd:pfam00804  81 gpGSAVDRIRRSQTAALRKKLKEVMAEYNelreRIREEYKE----VIQRQYETVTGKEVSEEEIEEMIETGSESVFQKAI 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 564331154  190 L-KDTQVTRQALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQG 235
Cdd:pfam00804 157 LeQGRGQARSALSEIEERHKELKELESSLKELHQIFLDMAVLVEAQG 203
SNARE_syntaxin4 cd15883
SNARE motif of syntaxin 4; Syntaxin-4 forms a complex with SNAP-23 (Qb/Qc) and R-SNAREs VAMP8, ...
 199-260 1.85e-31

SNARE motif of syntaxin 4; Syntaxin-4 forms a complex with SNAP-23 (Qb/Qc) and R-SNAREs VAMP8, VAMP2 and VAMP7 which plays a role in exocytosis of secetory granule. Syntaxin 4 is member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle.


Pssm-ID: 277236  Cd Length: 63  Bit Score: 115.04  E-value: 1.85e-31
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564331154 199 ALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVK 260
Cdd:cd15883    1 ALNEIEARHSEIQKLERSIRELHDMFTYLAMEVEAQGEMIDRIEKNILSSADYVEKAQEHVK 62
SynN smart00503
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction ...
 36-151 1.88e-30

Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction with the SNAP-25 homologue Sec9p


Pssm-ID: 214699 [Multi-domain]  Cd Length: 117  Bit Score: 113.98  E-value: 1.88e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154    36 SPDDEFFQKVQTIRQTMAKLESKVRELEKQQVTILATPLPEESMKQGLQNLREEIKQLGREVRAQLKAIEPQKEEADENy 115
Cdd:smart00503   1 SNLDEFFEKVEEIRANIQKISQNVAELQKLHEELLTPPDADKELREKLERLIDDIKRLAKEIRAKLKELEKENLENRAS- 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 564331154   116 NSVNTRMKKTQHGVLSQQFVELINKCNSMQSEYREK 151
Cdd:smart00503  80 GSASDRTRKAQTEKLRKKFKEVMNEFQRLQRKYRER 115
COG5074 COG5074
t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular ...
 41-271 3.35e-25

t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 227406 [Multi-domain]  Cd Length: 280  Bit Score: 104.58  E-value: 3.35e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  41 FFQKVQTIRQTMAKLESKVRELEKQQVTILATPLPEESM--KQGLQNLREEIKQLGREVRAQLKAIEPQKeeadenynsV 118
Cdd:COG5074   23 FMNKILSINKNLSVYEKEINQIDNLHKDLLTEVFEEQSRklRRSLDNFSSQTTDLQRNLKKDIKSAERDG---------I 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154 119 NTRMKKTQHGVLSQQFVELINKCNSMQSEYREKNVERIRRQLKITNAGMVSDEELEQMLDSGQSEVFVSNILKDTQV--T 196
Cdd:COG5074   94 HLANKQAQAENVRQKFLKLIQDYRIIDSNYREEEKEQARRQYIIAQPEATEDEVEAAINDVNGQQVFSQALLNANRRgeA 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564331154 197 RQALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKIALENQKKARK 271
Cdd:COG5074  174 KTALAEVQARHQEIKKIEKTMAELTQLFNDMEELVIEQQENVDVIDKNVEDAQENVEQGVGHTDKAVKSARAARK 248
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
 197-262 2.41e-16

Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel four-helix bundles in target soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptor proteins. This motif found in "Q-SNAREs".


Pssm-ID: 197699 [Multi-domain]  Cd Length: 66  Bit Score: 73.00  E-value: 2.41e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564331154   197 RQALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKIA 262
Cdd:smart00397   1 QQALAREEERDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKKA 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 40-271 9.25e-07

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: 51.60  E-value: 9.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154    40 EFFQKVQTIRQTMAKLESKVRELEKQ------------------------QVTILATPLpeESMKQGLQNLREEIKQLGR 95
Cdd:TIGR02168  176 ETERKLERTRENLDRLEDILNELERQlkslerqaekaerykelkaelrelELALLVLRL--EELREELEELQEELKEAEE 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154    96 EVR---AQLKAIEPQKEEADENYNSVNTRMKKTQHGVlsQQFVELINKCNSMQSEYREKnVERIRRQLKITNAgmvSDEE 172
Cdd:TIGR02168  254 ELEeltAELQELEEKLEELRLEVSELEEEIEELQKEL--YALANEISRLEQQKQILRER-LANLERQLEELEA---QLEE 327

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154   173 LEQMLDSGQSEV-FVSNILKDTQVTRQAL-NEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSAD 250
Cdd:TIGR02168  328 LESKLDELAEELaELEEKLEELKEELESLeAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407

                          250       260
                   ....*....|....*....|.
gi 564331154   251 YVERGQEHVKIALENQKKARK 271
Cdd:TIGR02168  408 RLERLEDRRERLQQEIEELLK 428
SNARE pfam05739
SNARE domain; Most if not all vesicular membrane fusion events in eukaryotic cells are ...
 236-271 1.06e-06

SNARE domain; Most if not all vesicular membrane fusion events in eukaryotic cells are believed to be mediated by a conserved fusion machinery, the SNARE [soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptors] machinery. The SNARE domain is thought to act as a protein-protein interaction module in the assembly of a SNARE protein complex.


Pssm-ID: 461727 [Multi-domain]  Cd Length: 52  Bit Score: 45.49  E-value: 1.06e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 564331154  236 EMINRIEKNILSSADYVERGQEHVKIALENQKKARK 271
Cdd:pfam05739   1 EMLDRIDTNVENAQSNVERAQKELKKAVKYQKSNRK 36
mukB PRK04863
chromosome partition protein MukB;
43-221 6.95e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.17  E-value: 6.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154   43 QKVQTIRQTMAKLEskvRELEKQQVTILAtpLPEESMKQGLQ-NLREEIKQLGREVRAQLKAIEPQKEEADENynsvntR 121
Cdd:PRK04863  513 EQLQQLRMRLSELE---QRLRQQQRAERL--LAEFCKRLGKNlDDEDELEQLQEELEARLESLSESVSEARER------R 581

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  122 MKKTQHGvlsQQFVELINKCNSMQSEYREKN--VERIRRQlkitnagmvSDEELEqmlDSGQSEVFVSNILKDTQVTRQA 199
Cdd:PRK04863  582 MALRQQL---EQLQARIQRLAARAPAWLAAQdaLARLREQ---------SGEEFE---DSQDVTEYMQQLLERERELTVE 646

                         170       180
                  ....*....|....*....|..
gi 564331154  200 LNEISARhseIQQLERSIRELH 221
Cdd:PRK04863  647 RDELAAR---KQALDEEIERLS 665
 
Name Accession Description Interval E-value
SynN cd00179
Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the ...
 39-189 4.17e-52

Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane; they are a family of receptors for intracellular transport vesicles; each target membrane may be identified by a specific member of the syntaxin family; syntaxins contain a moderately well conserved amino-terminal domain, called Habc, whose structure is an antiparallel three-helix bundle; a linker of about 30 amino acids connects this to the carboxy-terminal region, designated H3 (t_SNARE), of the syntaxin cytoplasmic domain; the highly conserved H3 region forms a single, long alpha-helix when it is part of the core SNARE complex and anchors the protein on the cytoplasmic surface of cellular membranes; H3 is not included in defining this domain


Pssm-ID: 238105 [Multi-domain]  Cd Length: 151  Bit Score: 172.47  E-value: 4.17e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  39 DEFFQKVQTIRQTMAKLESKVRELEKQQVTILATPLPEESMKQGLQNLREEIKQLGREVRAQLKAIEPQKEEADENYNSV 118
Cdd:cd00179    2 EEFFEEVEEIRGNIDKISEDVEELQKLHSQLLTAPDADPELKQELESLVQEIKKLAKEIKGKLKELEESNEQNEALNGSS 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564331154 119 NTRMKKTQHGVLSQQFVELINKCNSMQSEYREKNVERIRRQLKITNaGMVSDEELEQMLDSGQSEVFVSNI 189
Cdd:cd00179   82 VDRIRKTQHSGLSKKFVEVMTEFNKAQRKYRERYKERIQRQLEITG-GEATDEELEDMLESGNSEIFTSQI 151
Syntaxin pfam00804
Syntaxin; Syntaxins are the prototype family of SNARE proteins. They usually consist of three ...
 40-235 4.49e-40

Syntaxin; Syntaxins are the prototype family of SNARE proteins. They usually consist of three main regions - a C-terminal transmembrane region, a central SNARE domain which is characteriztic of and conserved in all syntaxins (pfam05739), and an N-terminal domain that is featured in this entry. This domain varies between syntaxin isoforms; in syntaxin 1A it is found as three alpha-helices with a left-handed twist. It may fold back on the SNARE domain to allow the molecule to adopt a 'closed' configuration that prevents formation of the core fusion complex - it thus has an auto-inhibitory role. The function of syntaxins is determined by their localization. They are involved in neuronal exocytosis, ER-Golgi transport and Golgi-endosome transport, for example. They also interact with other proteins as well as those involved in SNARE complexes. These include vesicle coat proteins, Rab GTPases, and tethering factors.


Pssm-ID: 459942 [Multi-domain]  Cd Length: 203  Bit Score: 142.71  E-value: 4.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154   40 EFFQKVQTIRQTMAKLESKVRELEKQQV--TILATPLPEESMKQGLQNLREEIKQLGREVRAQLKAIEPQKEEADENY-- 115
Cdd:pfam00804   1 DFFKEVQEIKEEIEKIRLLVKKLQKQNEesKLLTSARRMSVIKRRMNSIARDIKKRAESIKRRLEALDKSNAENEKKPgc 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  116 --NSVNTRMKKTQHGVLSQQFVELINKCN----SMQSEYREknveRIRRQLKITNAGMVSDEELEQMLDSGQSEVFVSNI 189
Cdd:pfam00804  81 gpGSAVDRIRRSQTAALRKKLKEVMAEYNelreRIREEYKE----VIQRQYETVTGKEVSEEEIEEMIETGSESVFQKAI 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 564331154  190 L-KDTQVTRQALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQG 235
Cdd:pfam00804 157 LeQGRGQARSALSEIEERHKELKELESSLKELHQIFLDMAVLVEAQG 203
SNARE_syntaxin4 cd15883
SNARE motif of syntaxin 4; Syntaxin-4 forms a complex with SNAP-23 (Qb/Qc) and R-SNAREs VAMP8, ...
 199-260 1.85e-31

SNARE motif of syntaxin 4; Syntaxin-4 forms a complex with SNAP-23 (Qb/Qc) and R-SNAREs VAMP8, VAMP2 and VAMP7 which plays a role in exocytosis of secetory granule. Syntaxin 4 is member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle.


Pssm-ID: 277236  Cd Length: 63  Bit Score: 115.04  E-value: 1.85e-31
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564331154 199 ALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVK 260
Cdd:cd15883    1 ALNEIEARHSEIQKLERSIRELHDMFTYLAMEVEAQGEMIDRIEKNILSSADYVEKAQEHVK 62
SynN smart00503
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction ...
 36-151 1.88e-30

Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction with the SNAP-25 homologue Sec9p


Pssm-ID: 214699 [Multi-domain]  Cd Length: 117  Bit Score: 113.98  E-value: 1.88e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154    36 SPDDEFFQKVQTIRQTMAKLESKVRELEKQQVTILATPLPEESMKQGLQNLREEIKQLGREVRAQLKAIEPQKEEADENy 115
Cdd:smart00503   1 SNLDEFFEKVEEIRANIQKISQNVAELQKLHEELLTPPDADKELREKLERLIDDIKRLAKEIRAKLKELEKENLENRAS- 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 564331154   116 NSVNTRMKKTQHGVLSQQFVELINKCNSMQSEYREK 151
Cdd:smart00503  80 GSASDRTRKAQTEKLRKKFKEVMNEFQRLQRKYRER 115
COG5074 COG5074
t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular ...
 41-271 3.35e-25

t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 227406 [Multi-domain]  Cd Length: 280  Bit Score: 104.58  E-value: 3.35e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  41 FFQKVQTIRQTMAKLESKVRELEKQQVTILATPLPEESM--KQGLQNLREEIKQLGREVRAQLKAIEPQKeeadenynsV 118
Cdd:COG5074   23 FMNKILSINKNLSVYEKEINQIDNLHKDLLTEVFEEQSRklRRSLDNFSSQTTDLQRNLKKDIKSAERDG---------I 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154 119 NTRMKKTQHGVLSQQFVELINKCNSMQSEYREKNVERIRRQLKITNAGMVSDEELEQMLDSGQSEVFVSNILKDTQV--T 196
Cdd:COG5074   94 HLANKQAQAENVRQKFLKLIQDYRIIDSNYREEEKEQARRQYIIAQPEATEDEVEAAINDVNGQQVFSQALLNANRRgeA 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564331154 197 RQALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKIALENQKKARK 271
Cdd:COG5074  174 KTALAEVQARHQEIKKIEKTMAELTQLFNDMEELVIEQQENVDVIDKNVEDAQENVEQGVGHTDKAVKSARAARK 248
SNARE_syntaxin1-like cd15848
SNARE motif of syntaxin 1 and related proteins; SNARE (soluble N-ethylmaleimide-sensitive ...
 199-260 7.31e-25

SNARE motif of syntaxin 1 and related proteins; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. This subgroup of the Qa SNAREs includes syntaxin 1, syntaxin 11, syntaxin 19, syntaxin 2, syntaxin 3, syntaxin 4 and related proteins.


Pssm-ID: 277201  Cd Length: 63  Bit Score: 96.84  E-value: 7.31e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564331154 199 ALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVK 260
Cdd:cd15848    1 ALADIEERHQDILKLEKSIRELHQMFLDMAVLVESQGELIDNIEYNVEKAKDYVEKGNEELK 62
SNARE_syntaxin2 cd15882
SNARE motif of syntaxin 2; Syntaxin 2 (STX2), also known as epimorphin (EPM or EPIM), may ...
 199-266 1.51e-21

SNARE motif of syntaxin 2; Syntaxin 2 (STX2), also known as epimorphin (EPM or EPIM), may interact with SNAP-23 (Qb/c) and genetic varioations are associated with type 1 von Willebrand disease (VWD). Syntaxin 2 is a member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle.


Pssm-ID: 277235  Cd Length: 69  Bit Score: 88.18  E-value: 1.51e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564331154 199 ALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKIALENQ 266
Cdd:cd15882    1 ALNEIESRHKDIMKLESSIRELHDMFVDMAMLVETQGEMINNIEKNVHNAVEYVEHAKEETKKAVKYQ 68
SNARE_syntaxin1 cd15880
SNARE motif of syntaxin 1; Syntaxin-1 belongs to the Qa subgroup of SNAREs and interacts with ...
 199-266 9.47e-18

SNARE motif of syntaxin 1; Syntaxin-1 belongs to the Qa subgroup of SNAREs and interacts with SNAP-25 (Qb/Qc) and the R-SNARE VAMP2 (also called synaptobrevin-2). The complex plays a role in exocytosis of synaptic vesicles. SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle.


Pssm-ID: 277233  Cd Length: 69  Bit Score: 77.17  E-value: 9.47e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564331154 199 ALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKIALENQ 266
Cdd:cd15880    1 ALSEIEARHNDIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQ 68
SNARE_syntaxin3 cd15881
SNARE motif of syntaxin 3; Syntaxin 3 (STX3) has been shown to form a complex with VAMP8 ...
 199-267 2.03e-16

SNARE motif of syntaxin 3; Syntaxin 3 (STX3) has been shown to form a complex with VAMP8 (R-SNARE) and SNAP-23 (Qb/c) in mast cells. Mutations have been implicated in human microvillus inclusion disease (MVID), a disorder of the differentiation of intestinal epithelium. Syntaxin 3 is a member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle.


Pssm-ID: 277234  Cd Length: 69  Bit Score: 73.52  E-value: 2.03e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564331154 199 ALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKIALENQK 267
Cdd:cd15881    1 ALSEIEGRHKDIVRLESSIKELHDMFVDIAMLVENQGEMLDNIELNVMKTVDHVEKARDETKKAVKYQS 69
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
 197-262 2.41e-16

Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel four-helix bundles in target soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptor proteins. This motif found in "Q-SNAREs".


Pssm-ID: 197699 [Multi-domain]  Cd Length: 66  Bit Score: 73.00  E-value: 2.41e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564331154   197 RQALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKIA 262
Cdd:smart00397   1 QQALAREEERDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKKA 66
SNARE_Qa cd15840
SNARE motif, subgroup Qa; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein ...
 203-260 8.15e-15

SNARE motif, subgroup Qa; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Examples for members of the Qa SNAREs are syntaxin 18, syntaxin 5, syntaxin 16, and syntaxin 1.


Pssm-ID: 277193 [Multi-domain]  Cd Length: 59  Bit Score: 68.69  E-value: 8.15e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564331154 203 ISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVK 260
Cdd:cd15840    1 IEEREEEIREIESSIGEVNEIFKDLATLVTEQGEQIDNIENNIEEAAANTEEANKELR 58
SNARE_syntaxin11 cd15878
SNARE motif of syntaxin 11; Syntaxin 11 (also known as STX11, FHL4, HLH4, HPLH4) is present on ...
 199-260 5.06e-13

SNARE motif of syntaxin 11; Syntaxin 11 (also known as STX11, FHL4, HLH4, HPLH4) is present on endosomal membranes, including late endosomes and lysosomes in macrophages, and has been shown to bind Vti1b and regulate the availability of Vti1b to form other SNARE-complexes. Mutations in human STX11 has been linked to familial hemophagocytic lymphohistiocytosis type-4 (FHL-4), an autosomal recessive disorder of immune dysregulation. Syntaxin 11 is a member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle.


Pssm-ID: 277231  Cd Length: 63  Bit Score: 63.71  E-value: 5.06e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564331154 199 ALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVK 260
Cdd:cd15878    1 ALNEIETRHKELLELESRIREVHELFLQMALLVEEQADTLNNIELNVEKTQDYVGKAKAQVK 62
COG5325 COG5325
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
46-271 9.20e-13

t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];


Pssm-ID: 227635 [Multi-domain]  Cd Length: 283  Bit Score: 68.33  E-value: 9.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  46 QTIRQTMAKLESKVRELEKQQVtILATPLPEESMKQglqnlREEIKQLGREVRAQLKAIEPQKEEADENYNSVNTRMKkt 125
Cdd:COG5325   41 ASVDQELTAVRRSISRLGKVYA-KHTEPSFSDKSEK-----EDEIDELSKKVNQDLQRCEKILKTKYKNLQSSFLQSK-- 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154 126 qhgvLSQQFVELINKCNSMQSEYREKNVERIRRQ----LKITNAGMVSDEELEQMLDSGQSEVFV--SNILKDTQVTRQA 199
Cdd:COG5325  113 ----LLRDLNTECMEGQRIQQKSAQFRKYQVLQAkflrNKNNDQHPLEEEEDEESLSSLGSQQTLqqQGLSNEELEYQQI 188

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564331154 200 LNEisARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKIALENQKKARK 271
Cdd:COG5325  189 LIT--ERDEEIKNLARGIYELNEIFRDLGSLVGEQGELVDRIDFNIENTSDNLKNANKELEKAPAHQRRTKK 258
SNARE_Sso1 cd15849
SNARE motif of Sso1; Saccharomyces cerevisiae SNARE protein Sso1p forms a complex with ...
 200-262 2.84e-12

SNARE motif of Sso1; Saccharomyces cerevisiae SNARE protein Sso1p forms a complex with synaptobrevin homolog Snc1p (R-SNARE) and the SNAP-25 homolog Sec9p (Qb/c) which is involved in exocytosis. Sso1 is member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle.


Pssm-ID: 277202  Cd Length: 64  Bit Score: 61.39  E-value: 2.84e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564331154 200 LNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKIA 262
Cdd:cd15849    1 LGEVQARHNEIQRIEQTLTELAQLFNDMATLVEQQDEVIQQIEQNAEEVETDLEKGNVHLEKA 63
SNARE_syntaxin12 cd15876
SNARE motif of syntaxin 12; Syntaxin 12 (STX12, also known as STX13 and STX14) forms a complex ...
 203-269 6.83e-12

SNARE motif of syntaxin 12; Syntaxin 12 (STX12, also known as STX13 and STX14) forms a complex with SNAP25 (Qb/Qc) or SNAP29 (Qb/Qc) and VAMP2 or VAMP3 (R-SNARE) and plays a role in plasma membrane to early endosome transport. Syntaxin 12 is a member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle.


Pssm-ID: 277229 [Multi-domain]  Cd Length: 67  Bit Score: 60.83  E-value: 6.83e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564331154 203 ISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKIALENQKKA 269
Cdd:cd15876    1 IKERETAIQQLEADILDVNQIFKDLAMMIHDQGDMIDSIEANVESAEVHVERASEQLQRAAYYQKKS 67
SNARE_syntaxin5 cd15844
SNARE motif of syntaxin 5; Syntaxin 5 (Syn5) regulates the transport from the ER to the Golgi, ...
 203-258 2.74e-10

SNARE motif of syntaxin 5; Syntaxin 5 (Syn5) regulates the transport from the ER to the Golgi, as well as the early/recycling endosomes to the trans-Golgi network and participates in the assembly of transitional ER and the Golgi, lipid droplet fusion, and cytokinesis. Syn5 exists in 2 isoforms, long (42 kDa) and short (35 kDa). The short form is localized in the Golgi complex, whereas the long form is additionally found in the endoplasmic reticulum (ER). The syntaxin-5 SNARE complexes, which also contain Bet1 (Qc) and either GS27 (Qb) and Sec22B (R-SNARE) or GS28 (Qb) and Ykt6 (R-SNARE), regulate the early secretory pathway of eukaryotic cells at the level of endoplasmic reticulum (ER) to Golgi transport. The syntaxin-5 SNARE complex, which also contains GS15 (Qc), GS28 (Qb) and Ykt6 (R-SNAREs) is involved in the transport from the trans-Golgi network to the cis-Golgi. Syn5 is member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle.


Pssm-ID: 277197  Cd Length: 86  Bit Score: 56.75  E-value: 2.74e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564331154 203 ISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEH 258
Cdd:cd15844    1 LQSRADAVQNIESTIVELGQIFQQLATMVAEQGEMVQRIDENVEDALANVEAAHSE 56
SNARE_syntaxin7_like cd15847
SNARE motif of syntaxin 7, 12 and related sequences; SNARE (soluble N-ethylmaleimide-sensitive ...
 206-262 2.84e-09

SNARE motif of syntaxin 7, 12 and related sequences; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. This subgroup of the Qa SNAREs includes syntaxin 7, syntaxin 12, TSNARE1 and related proteins.


Pssm-ID: 277200 [Multi-domain]  Cd Length: 60  Bit Score: 52.96  E-value: 2.84e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564331154 206 RHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKIA 262
Cdd:cd15847    4 REERIRQIESDILDVNQIFKDLATLVHEQGETIDSIEANIESAYVNVESGNSQLAKA 60
SNARE_syntaxin19 cd15879
SNARE motif of syntaxin 19; Syntaxin 19 has been shown to have the potential to form SNARE ...
 200-261 4.15e-09

SNARE motif of syntaxin 19; Syntaxin 19 has been shown to have the potential to form SNARE complexes with SNAP-23, 25 and 29 (Qb/Qc) and VAMP3 and VAMP8 (R-SNARE), indicating a role in post-Golgi trafficking or plasma membrane fusion. Syntaxin 19 is member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle.


Pssm-ID: 277232  Cd Length: 63  Bit Score: 52.53  E-value: 4.15e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564331154 200 LNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKI 261
Cdd:cd15879    2 LSEIEQRHKELVSLENQIKDLKDLFIQISLLVEEQGEMINNIEISVNNTQEYVQASKEKFGL 63
SNARE_syntaxin16 cd15845
SNARE motif of syntaxin 16; Syntaxin 16 is located in trans-Golgi network (TGN) and regulated ...
 203-260 7.17e-08

SNARE motif of syntaxin 16; Syntaxin 16 is located in trans-Golgi network (TGN) and regulated by the SM protein Vps45p. It forms a complex with syntaxin 6 (Qc), Vti1a (Qb) and VAMP4 (R-SNARE) and is involved in the regulation of recycling of early endosomes to the trans-Golgi network (TGN). Syntaxin 16 is a member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle.


Pssm-ID: 277198  Cd Length: 59  Bit Score: 48.99  E-value: 7.17e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564331154 203 ISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVK 260
Cdd:cd15845    1 IQERDREIAKIVESINELAEIFKDLATLVIEQGTILDRIDYNIEQTATRVEKGVKELK 58
SNARE cd00193
SNARE motif; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) ...
 208-254 1.61e-07

SNARE motif; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, Qb- and Qc-SNAREs are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles.


Pssm-ID: 277192  Cd Length: 54  Bit Score: 47.77  E-value: 1.61e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 564331154 208 SEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVER 254
Cdd:cd00193    1 ESLEQLEASIGELKDIGRDMAMELEEQGEQLDRIEERAESTQARVSR 47
SNARE_syntaxin7 cd15875
SNARE motif of syntaxin 7; Syntaxin 7 forms a complex with syntaxin 8 (Qc), Vti1b (Qb) and ...
 203-262 2.71e-07

SNARE motif of syntaxin 7; Syntaxin 7 forms a complex with syntaxin 8 (Qc), Vti1b (Qb) and either VAMP7 or VAMP8 (R-SNARE) and is involved in the transport from early endosomes to the lysosome. Syntaxin 7 is member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle.


Pssm-ID: 277228 [Multi-domain]  Cd Length: 60  Bit Score: 47.43  E-value: 2.71e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154 203 ISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKIA 262
Cdd:cd15875    1 LEERERSIRQLESDIMDVNQIFKDLGMLVHEQGEVIDSIEANVETAAVHVEEANQQLSQA 60
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 40-271 9.25e-07

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: 51.60  E-value: 9.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154    40 EFFQKVQTIRQTMAKLESKVRELEKQ------------------------QVTILATPLpeESMKQGLQNLREEIKQLGR 95
Cdd:TIGR02168  176 ETERKLERTRENLDRLEDILNELERQlkslerqaekaerykelkaelrelELALLVLRL--EELREELEELQEELKEAEE 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154    96 EVR---AQLKAIEPQKEEADENYNSVNTRMKKTQHGVlsQQFVELINKCNSMQSEYREKnVERIRRQLKITNAgmvSDEE 172
Cdd:TIGR02168  254 ELEeltAELQELEEKLEELRLEVSELEEEIEELQKEL--YALANEISRLEQQKQILRER-LANLERQLEELEA---QLEE 327

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154   173 LEQMLDSGQSEV-FVSNILKDTQVTRQAL-NEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSAD 250
Cdd:TIGR02168  328 LESKLDELAEELaELEEKLEELKEELESLeAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407

                          250       260
                   ....*....|....*....|.
gi 564331154   251 YVERGQEHVKIALENQKKARK 271
Cdd:TIGR02168  408 RLERLEDRRERLQQEIEELLK 428
SNARE pfam05739
SNARE domain; Most if not all vesicular membrane fusion events in eukaryotic cells are ...
 236-271 1.06e-06

SNARE domain; Most if not all vesicular membrane fusion events in eukaryotic cells are believed to be mediated by a conserved fusion machinery, the SNARE [soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptors] machinery. The SNARE domain is thought to act as a protein-protein interaction module in the assembly of a SNARE protein complex.


Pssm-ID: 461727 [Multi-domain]  Cd Length: 52  Bit Score: 45.49  E-value: 1.06e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 564331154  236 EMINRIEKNILSSADYVERGQEHVKIALENQKKARK 271
Cdd:pfam05739   1 EMLDRIDTNVENAQSNVERAQKELKKAVKYQKSNRK 36
SNARE_syntaxin17 cd15846
SNARE motif of syntaxin 17; Synthaxin 17 (STX17) belongs to the Qa subgroup of SNAREs and ...
 209-258 1.71e-06

SNARE motif of syntaxin 17; Synthaxin 17 (STX17) belongs to the Qa subgroup of SNAREs and interacts with SNAP29 (Qb/Qc) and the lysosomal R-SNARE VAMP8. The complex plays a role in autophagosome-lysosome fusion. Autophagosome transports cytoplasmic materials, including cytoplasmic proteins, glycogen, lipids, organelles, and invading bacteria to the lysosome for degradation. SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle.


Pssm-ID: 277199 [Multi-domain]  Cd Length: 62  Bit Score: 44.97  E-value: 1.71e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 564331154 209 EIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEH 258
Cdd:cd15846   10 SWETLQQDLEDLHGLFTDFHQLVHDQGEQVDTIEDNVEEALENVQEGTKN 59
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 59-254 6.40e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 48.56  E-value: 6.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154   59 VRELEKQQVTILATPLPEESMKQGLQNL--------------REEIKQLGREVRAQLkaiepqkEEADENYNSVNTRMKK 124
Cdd:pfam05483 512 TLELKKHQEDIINCKKQEERMLKQIENLeekemnlrdelesvREEFIQKGDEVKCKL-------DKSEENARSIEYEVLK 584

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  125 TQhgvlsQQFVELINKCNSM--QSEYREKNVERIRRQLK-ITNAGMVSDEELEQMldsgqsEVFVSNILKDTQVTRQALN 201
Cdd:pfam05483 585 KE-----KQMKILENKCNNLkkQIENKNKNIEELHQENKaLKKKGSAENKQLNAY------EIKVNKLELELASAKQKFE 653

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 564331154  202 EISARHS---EIQQL--ERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVER 254
Cdd:pfam05483 654 EIIDNYQkeiEDKKIseEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEK 711
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 23-249 5.87e-05

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: 45.14  E-value: 5.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  23 VALVVHSGAARLSSPDDEFFQKVQTIRQTMAKLESKVRELEKQqvtilatplpEESMKQGLQNLREEIKQLGREVRA--- 99
Cdd:COG4942    7 LALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKE----------EKALLKQLAALERRIAALARRIRAleq 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154 100 QLKAIEPQKEEADENYNSVNTRMKKtQHGVLSQQFVE------------LINKCNSMQSEYREKNVERIRRQLKITNAGM 167
Cdd:COG4942   77 ELAALEAELAELEKEIAELRAELEA-QKEELAELLRAlyrlgrqpplalLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154 168 VSD----EELEQMLDSGQSEvfVSNILKDTQVTRQALN-EISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIE 242
Cdd:COG4942  156 RADlaelAALRAELEAERAE--LEALLAELEEERAALEaLKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233


                 ....*..
gi 564331154 243 KNILSSA 249
Cdd:COG4942  234 AEAAAAA 240
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 67-279 7.12e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.82  E-value: 7.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  67 VTILATPLPEESMKQGLQNLREEIKQLGREVRAQLKAIEPQKEEADENYNSVNTRMKKTQHGVlsQQFVELINKCNSMQS 146
Cdd:COG3883    5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI--DKLQAEIAEAEAEIE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154 147 EYREKNVERIRRQLKitNAGMVSDeeLEQMLDSGQSEVFVSNILKDTQVT---RQALNEISARHSEIQQLERSIRELHEI 223
Cdd:COG3883   83 ERREELGERARALYR--SGGSVSY--LDVLLGSESFSDFLDRLSALSKIAdadADLLEELKADKAELEAKKAELEAKLAE 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564331154 224 FTFLATEVE-MQGEMINRIE--KNILSSADYVERGQEHVKIALENQKKARKVSLASDPS 279
Cdd:COG3883  159 LEALKAELEaAKAELEAQQAeqEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 80-271 9.37e-05

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: 45.05  E-value: 9.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154    80 KQGLQNLREEIKQLG---REVRAQLKAIEPQKEEADENYNSVNTRM--KKTQHGVLSQQFVELINKCNSMQSEYREKNVE 154
Cdd:TIGR02168  676 RREIEELEEKIEELEekiAELEKALAELRKELEELEEELEQLRKELeeLSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154   155 RIRRQLKItnagmvsdEELEQMLDSGQSEvfvsniLKDTQVTRQALNEISARHS-EIQQLERSIRELHEIFTFLATEVEM 233
Cdd:TIGR02168  756 LTELEAEI--------EELEERLEEAEEE------LAEAEAEIEELEAQIEQLKeELKALREALDELRAELTLLNEEAAN 821

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 564331154   234 QGEMINRIEKNILSSADYVERGQEHVKIALENQKKARK 271
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 39-289 2.68e-04

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 43.41  E-value: 2.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  39 DEFFQKVQTIRQTMAKLESKVRELEKQQVTILATPLP--EESMKQ---GLQNLREEIKQLGREVRAQLKAIEPQKEEADE 113
Cdd:COG5185  289 KQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQelEESKREtetGIQNLTAEIEQGQESLTENLEAIKEEIENIVG 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154 114 NYNsvntrmkktqhgvlSQQFVELINKCNSMQSEYREKNVERIRRQLKITNAGMVSDEELEQMLDSgQSEVFVSNILKDT 193
Cdd:COG5185  369 EVE--------------LSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADR-QIEELQRQIEQAT 433

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154 194 QVTRQALNEISARHSEIQQLERSIREL---------HEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKIALE 264
Cdd:COG5185  434 SSNEEVSKLLNELISELNKVMREADEEsqsrleeayDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLE 513

                        250       260
                 ....*....|....*....|....*
gi 564331154 265 NQKKARKVSLASDPSLGHARVTFHD 289
Cdd:COG5185  514 GVRSKLDQVAESLKDFMRARGYAHI 538
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
77-220 5.91e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.31  E-value: 5.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  77 ESMKQGLQNLREEIKQLgrevRAQLKAIEPQKEEADENYNSVNTRmkkTQHGVLSQQFVELINKCNSMQSEYREKN--VE 154
Cdd:COG3206  171 EEARKALEFLEEQLPEL----RKELEEAEAALEEFRQKNGLVDLS---EEAKLLLQQLSELESQLAEARAELAEAEarLA 243

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154 155 RIRRQLKItnagmvSDEELEQMLDSGQsevfVSNILKDTQVTRQALNEISAR----HSEIQQLERSIREL 220
Cdd:COG3206  244 ALRAQLGS------GPDALPELLQSPV----IQQLRAQLAELEAELAELSARytpnHPDVIALRAQIAAL 303
SNARE_TSNARE1 cd15877
SNARE motif of TSNARE1; TSNARE1 is member of the Qa subgroup of SNARE (soluble ...
 200-257 5.94e-04

SNARE motif of TSNARE1; TSNARE1 is member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. Its function is unknown, but polymorphisms in human TSNARE1 have been associated with schizophrenia susceptibility. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. TSNARE1 is part of a subgroup of the Qa SNAREs that also includes syntaxin 7, syntaxin 12 and related proteins.


Pssm-ID: 277230  Cd Length: 64  Bit Score: 38.08  E-value: 5.94e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564331154 200 LNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQE 257
Cdd:cd15877    1 LEAIRQREEAIQQIESDMLDVNQIIKDLASMVSEQGDTIDSIEANIEAASSHVESANQ 58
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 40-223 1.27e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 40.90  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154   40 EFFQKVQTIRQTMAKLESKVRELEK----QQVTILATPLpeESMKQGLQNLREEIKQLGREV---RAQLKAIEPQKEEAD 112
Cdd:pfam09787  11 DYKQKAARILQSKEKLIASLKEGSGveglDSSTALTLEL--EELRQERDLLREEIQKLRGQIqqlRTELQELEAQQQEEA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  113 ENYNSVNTRMKKTQHGV-------------LSQQFV----ELINKCNSMQSEY--REKNVERIRRQLKITNAGMVSDEEL 173
Cdd:pfam09787  89 ESSREQLQELEEQLATErsarreaeaelerLQEELRyleeELRRSKATLQSRIkdREAEIEKLRNQLTSKSQSSSSQSEL 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 564331154  174 EQMLdsgqSEVFVSNILKDTQVtrQALNeiSARHSEIQQLERSIRELHEI 223
Cdd:pfam09787 169 ENRL----HQLTETLIQKQTML--EALS--TEKNSLVLQLERMEQQIKEL 210
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
 38-206 2.33e-03

FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440310 [Multi-domain]  Cd Length: 424  Bit Score: 40.11  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  38 DDEFFQKVQTIrQTMAKLESKVRE-LE-----------KQQVT--ILAT---PLPeESMkqglqnLREEIKQLGREVRAQ 100
Cdd:COG0544  249 DDEFAKKLGEF-ETLEELKADIREnLErekkqraraklKDQVLdaLVENnefDLP-EAL------VEREIDRLLEQAEQQ 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154 101 LKAIEPQKEEADEnynsvntrmkktqhgvlsQQFVElinkcnsmqsEYREKNVERIRRQL---------KITnagmVSDE 171
Cdd:COG0544  321 LQQQGLQDTGKTE------------------EELRE----------EFREQAERRVKLGLildeiakkeNIE----VTDE 368

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 564331154 172 ELEQMLDS-----GQSEVFVSNILKDtqvtRQALNEISAR 206
Cdd:COG0544  369 EVEAEIEEmaqqyGMPPEEVKEYLQN----PGQLEQLRAD 404
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 76-272 2.54e-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: 40.43  E-value: 2.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154    76 EESMKQgLQNLREEIKQLG---REVRAQLKAIEPQKEEAdENYNSVNTRMKKTQHGVLSQQFVELINKCNSMQSEYREKN 152
Cdd:TIGR02168  175 KETERK-LERTRENLDRLEdilNELERQLKSLERQAEKA-ERYKELKAELRELELALLVLRLEELREELEELQEELKEAE 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154   153 VERIRRQLKITNagmvSDEELEQmLDSGQSEVfvSNILKDTQVTRQAL-NEISARHSEIQQLERSIRELHEIFTFLATEV 231
Cdd:TIGR02168  253 EELEELTAELQE----LEEKLEE-LRLEVSEL--EEEIEELQKELYALaNEISRLEQQKQILRERLANLERQLEELEAQL 325

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 564331154   232 EMQGEMINRIEKNILSSADYVERGQEHVKIALENQKKARKV 272
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 39-245 3.56e-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: 40.00  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154   39 DEFFQKVQTIRQTMAKLES----KVRELEKQQVTILATPLPEESMKQGLQNLREEIKQLGREVRAQlKAIEPQKEEaden 114
Cdd:TIGR04523 338 SQLNEQISQLKKELTNSESenseKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ-EKLNQQKDE---- 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  115 ynsvNTRMKKTQHGVLSQQFVELINKCNSMQSEYREKNVERIRRQLKITNAGMvSDEELEQMLD--SGQSEVFVSNILKD 192
Cdd:TIGR04523 413 ----QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDN-TRESLETQLKvlSRSINKIKQNLEQK 487

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564331154  193 TQVTRQALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNI 245
Cdd:TIGR04523 488 QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI 540
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 43-256 3.58e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 3.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154    43 QKVQTIRQTMAKLESKVRELEKQqvtilatplpEESMKQGLQNLREEIKQLGR---EVRAQLKAIEPQKEEADENYNSVN 119
Cdd:TIGR02168  288 KELYALANEISRLEQQKQILRER----------LANLERQLEELEAQLEELESkldELAEELAELEEKLEELKEELESLE 357

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154   120 TRMKKTQHgvLSQQFVELINKCNSmQSEYREKNVERIRRQLKITNAGMVSDEELEQMLDSGQsEVFVSNILkdTQVTRQA 199
Cdd:TIGR02168  358 AELEELEA--ELEELESRLEELEE-QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR-ERLQQEIE--ELLKKLE 431

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 564331154   200 LNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQ 256
Cdd:TIGR02168  432 EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 40-274 3.95e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.03  E-value: 3.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154    40 EFFQKVQTIRQTMAKLESKVRELEKQQVTILATplpEESMKQGL------QNLREEIKQLGREVRAQlkAIEPQKEEADE 113
Cdd:TIGR00606  748 ELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPE---EESAKVCLtdvtimERFQMELKDVERKIAQQ--AAKLQGSDLDR 822

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154   114 NYNSVNTRMKKTQHGVLS-QQFVELINKCNSMQSEyREKNVERIRRQLKITNAGMVSDEELEQMLDSgQSEVFVSNILKD 192
Cdd:TIGR00606  823 TVQQVNQEKQEKQHELDTvVSKIELNRKLIQDQQE-QIQHLKSKTNELKSEKLQIGTNLQRRQQFEE-QLVELSTEVQSL 900

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154   193 TQVTRQALNEIS----ARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKIALENQKK 268
Cdd:TIGR00606  901 IREIKDAKEQDSpletFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELN 980


                   ....*.
gi 564331154   269 ARKVSL 274
Cdd:TIGR00606  981 TVNAQL 986
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
39-220 4.99e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 4.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  39 DEFFQKVQTIRQTMAKLESKVRELEKQQVTILATPLPE-ESMKQGLQNLREEIKQLgrevRAQLKAIEPQKEEADENYNS 117
Cdd:COG4372    2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFElDKLQEELEQLREELEQA----REELEQLEEELEQARSELEQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154 118 VNTRMKKTQhgvlsQQFVELINKCNSMQSEY--REKNVERIRRQLKITNAGMVSDEELEQMLDSGQSEVFVSNILKDTQV 195
Cdd:COG4372   78 LEEELEELN-----EQLQAAQAELAQAQEELesLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL 152

                        170       180
                 ....*....|....*....|....*
gi 564331154 196 tRQALNEISARHSEIQQLERSIREL 220
Cdd:COG4372  153 -KELEEQLESLQEELAALEQELQAL 176
PilO COG3167
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
43-123 5.11e-03

Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];


Pssm-ID: 442400 [Multi-domain]  Cd Length: 202  Bit Score: 38.00  E-value: 5.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  43 QKVQTIRQTMAKLESKVRELEKQqvtilatpLPEesmKQGLQNLREEIKQLGREVRAQLKAIEPQKEEADENYNSVNTRM 122
Cdd:COG3167   70 ANLPALKAQLEELEQQLGELLKQ--------LPS---KAEVPALLDDISQAALGSGLEFELFKPGPEVPKEFYAELPISI 138


                 .
gi 564331154 123 K 123
Cdd:COG3167  139 R 139
mukB PRK04863
chromosome partition protein MukB;
43-221 6.95e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.17  E-value: 6.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154   43 QKVQTIRQTMAKLEskvRELEKQQVTILAtpLPEESMKQGLQ-NLREEIKQLGREVRAQLKAIEPQKEEADENynsvntR 121
Cdd:PRK04863  513 EQLQQLRMRLSELE---QRLRQQQRAERL--LAEFCKRLGKNlDDEDELEQLQEELEARLESLSESVSEARER------R 581

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  122 MKKTQHGvlsQQFVELINKCNSMQSEYREKN--VERIRRQlkitnagmvSDEELEqmlDSGQSEVFVSNILKDTQVTRQA 199
Cdd:PRK04863  582 MALRQQL---EQLQARIQRLAARAPAWLAAQdaLARLREQ---------SGEEFE---DSQDVTEYMQQLLERERELTVE 646

                         170       180
                  ....*....|....*....|..
gi 564331154  200 LNEISARhseIQQLERSIRELH 221
Cdd:PRK04863  647 RDELAAR---KQALDEEIERLS 665
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 53-220 8.01e-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: 38.85  E-value: 8.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154   53 AKLESKVRELEKQQVTILATPLPEESMKQGLQNLREEIKQLGREVRAQLKAIEPQKEEADENYNSVNTRM---------- 122
Cdd:TIGR04523 127 NKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLlklelllsnl 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  123 -KKTQ-HGVLSQQFVELINKCNSMQSEYREKNVERIRRQLKITNAgmvsDEELEQMLDSGQSEVfvsNILKD-TQVTRQA 199
Cdd:TIGR04523 207 kKKIQkNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNT----QTQLNQLKDEQNKIK---KQLSEkQKELEQN 279

                         170       180
                  ....*....|....*....|.
gi 564331154  200 LNEISARHSEIQQLERSIREL 220
Cdd:TIGR04523 280 NKKIKELEKQLNQLKSEISDL 300
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
36-269 8.02e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 38.35  E-value: 8.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  36 SPDDEFFQKVQTIRQTMAKLESKVRELEKQQVTIlatplpEESMKQGLQNLREEIKQLgREVRAQLKAIepqKEEADENY 115
Cdd:COG1340    1 SKTDELSSSLEELEEKIEELREEIEELKEKRDEL------NEELKELAEKRDELNAQV-KELREEAQEL---REKRDELN 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154 116 NSVntRMKKTQHGVLSQQFVELINKCNSMQSEYREKNVERI-RRQLKitnagmvsdEELEQMLDSGQSEVFvsnilkDTQ 194
Cdd:COG1340   71 EKV--KELKEERDELNEKLNELREELDELRKELAELNKAGGsIDKLR---------KEIERLEWRQQTEVL------SPE 133

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564331154 195 VTRQALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMiNRIEKNIlssADYVERGQEHVKIALENQKKA 269
Cdd:COG1340  134 EEKELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEA-EEIHKKI---KELAEEAQELHEEMIELYKEA 204
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
44-126 8.09e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.84  E-value: 8.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  44 KVQTIRQTMAKLESKVRELEKQQVTILATPLpeESMKQGLQNLREEIKQLGREVR------AQLKAIEPQKEEADENYNS 117
Cdd:COG3206  292 DVIALRAQIAALRAQLQQEAQRILASLEAEL--EALQAREASLQAQLAQLEARLAelpeleAELRRLEREVEVARELYES 369


                 ....*....
gi 564331154 118 VNTRMKKTQ 126
Cdd:COG3206  370 LLQRLEEAR 378
Filament pfam00038
Intermediate filament protein;
41-270 9.99e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 37.98  E-value: 9.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154   41 FFQKVQTIRQTMAKLESKVRELEkQQVTILATPLpEESMKQGLQNLREEIKQLGREvRAQLKA-IEPQKEEADE--NYNS 117
Cdd:pfam00038  16 YIDKVRFLEQQNKLLETKISELR-QKKGAEPSRL-YSLYEKEIEDLRRQLDTLTVE-RARLQLeLDNLRLAAEDfrQKYE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  118 VNTRMKKTQHG---VLSQQF-------VELINKCNSMQSE--YREKNVErirrqlkitnagmvsdEELEQMldsgQSEVF 185
Cdd:pfam00038  93 DELNLRTSAENdlvGLRKDLdeatlarVDLEAKIESLKEElaFLKKNHE----------------EEVREL----QAQVS 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331154  186 VSNILKDTQVTRQ-----ALNEISARHSEIqqLERSIRELHEIF----TFLATEVEMQGEMINRIEKNILSSadyvERGQ 256
Cdd:pfam00038 153 DTQVNVEMDAARKldltsALAEIRAQYEEI--AAKNREEAEEWYqsklEELQQAAARNGDALRSAKEEITEL----RRTI 226

                         250
                  ....*....|....
gi 564331154  257 EHVKIALENQKKAR 270
Cdd:pfam00038 227 QSLEIELQSLKKQK 240
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH