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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568950030 148 ALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVK 209
Cdd:cd15883    1 ALNEIEARHSEIQKLERSIRELHDMFTYLAMEVEAQGEMIDRIEKNILSSADYVEKAQEHVK 62

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950030    1 MAKLESKVRELEKQQV--TILATPLPEESMKQGLQNLREEIKQLGREVRAQLKAIEPQKEEADENY----NSVNTRMKKT 74
Cdd:pfam00804  13 IEKIRLLVKKLQKQNEesKLLTSARRMSVIKRRMNSIARDIKKRAESIKRRLEALDKSNAENEKKPgcgpGSAVDRIRRS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950030   75 QHGVLSQQFVELINKCN----SMQSEYREknveRIRRQLKITNAGMVSDEELEQMLDSGQSEVFVSNIL-KDTQVTRQAL 149
Cdd:pfam00804  93 QTAALRKKLKEVMAEYNelreRIREEYKE----VIQRQYETVTGKEVSEEEIEEMIETGSESVFQKAILeQGRGQARSAL 168

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 568950030  150 NEISARHSEIQQLERSIRELHEIFTFLATEVEMQG 184
Cdd:pfam00804 169 SEIEERHKELKELESSLKELHQIFLDMAVLVEAQG 203

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950030     1 MAKLESKVRELEKQQVTILATPLPEESMKQGLQNLREEIKQLGREVRAQLKAIEPQKEEADENyNSVNTRMKKTQHGVLS 80
Cdd:smart00503  17 IQKISQNVAELQKLHEELLTPPDADKELREKLERLIDDIKRLAKEIRAKLKELEKENLENRAS-GSASDRTRKAQTEKLR 95

                           90       100
                   ....*....|....*....|
gi 568950030    81 QQFVELINKCNSMQSEYREK 100
Cdd:smart00503  96 KKFKEVMNEFQRLQRKYRER 115

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".

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568950030   146 RQALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKIA 211
Cdd:smart00397   1 QQALAREEERDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKKA 66

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]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950030    29 KQGLQNLREEIKQLG---REVRAQLKAIEPQKEEADENYNSVNTRM--KKTQHGVLSQQFVELINKCNSMQSEYREKNVE 103
Cdd:TIGR02168  676 RREIEELEEKIEELEekiAELEKALAELRKELEELEEELEQLRKELeeLSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950030   104 RIRRQLKItnagmvsdEELEQMLDSGQSEvfvsniLKDTQVTRQALNEISARHS-EIQQLERSIRELHEIFTFLATEVEM 182
Cdd:TIGR02168  756 LTELEAEI--------EELEERLEEAEEE------LAEAEAEIEELEAQIEQLKeELKALREALDELRAELTLLNEEAAN 821

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 568950030   183 QGEMINRIEKNILSSADYVERGQEHVKIALENQKKARK 220
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950030    1 MAKLESKVRELEKQQV--TILATPLPEESMKQGLQNLREEIKQLGREVRAQLKAIEPQKEEADENY----NSVNTRMKKT 74
Cdd:pfam00804  13 IEKIRLLVKKLQKQNEesKLLTSARRMSVIKRRMNSIARDIKKRAESIKRRLEALDKSNAENEKKPgcgpGSAVDRIRRS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950030   75 QHGVLSQQFVELINKCN----SMQSEYREknveRIRRQLKITNAGMVSDEELEQMLDSGQSEVFVSNIL-KDTQVTRQAL 149
Cdd:pfam00804  93 QTAALRKKLKEVMAEYNelreRIREEYKE----VIQRQYETVTGKEVSEEEIEEMIETGSESVFQKAILeQGRGQARSAL 168

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 568950030  150 NEISARHSEIQQLERSIRELHEIFTFLATEVEMQG 184
Cdd:pfam00804 169 SEIEERHKELKELESSLKELHQIFLDMAVLVEAQG 203

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568950030 148 ALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVK 209
Cdd:cd15848    1 ALADIEERHQDILKLEKSIRELHQMFLDMAVLVESQGELIDNIEYNVEKAKDYVEKGNEELK 62

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950030   3 KLESKVRELEKQQVTILATPLPEESM--KQGLQNLREEIKQLGREVRAQLKAIEPQKeeadenynsVNTRMKKTQHGVLS 80
Cdd:COG5074   36 VYEKEINQIDNLHKDLLTEVFEEQSRklRRSLDNFSSQTTDLQRNLKKDIKSAERDG---------IHLANKQAQAENVR 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950030  81 QQFVELINKCNSMQSEYREKNVERIRRQLKITNAGMVSDEELEQMLDSGQSEVFVSNILKDTQV--TRQALNEISARHSE 158
Cdd:COG5074  107 QKFLKLIQDYRIIDSNYREEEKEQARRQYIIAQPEATEDEVEAAINDVNGQQVFSQALLNANRRgeAKTALAEVQARHQE 186

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568950030 159 IQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKIALENQKKARK 220
Cdd:COG5074  187 IKKIEKTMAELTQLFNDMEELVIEQQENVDVIDKNVEDAQENVEQGVGHTDKAVKSARAARK 248

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568950030 148 ALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKIALENQ 215
Cdd:cd15880    1 ALSEIEARHNDIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQ 68

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568950030 148 ALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKIALENQK 216
Cdd:cd15881    1 ALSEIEGRHKDIVRLESSIKELHDMFVDIAMLVENQGEMLDNIELNVMKTVDHVEKARDETKKAVKYQS 69

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568950030 148 ALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVK 209
Cdd:cd15878    1 ALNEIETRHKELLELESRIREVHELFLQMALLVEEQADTLNNIELNVEKTQDYVGKAKAQVK 62

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568950030 152 ISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKIALENQKKA 218
Cdd:cd15876    1 IKERETAIQQLEADILDVNQIFKDLAMMIHDQGDMIDSIEANVESAEVHVERASEQLQRAAYYQKKS 67

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568950030 152 ISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEH 207
Cdd:cd15844    1 LQSRADAVQNIESTIVELGQIFQQLATMVAEQGEMVQRIDENVEDALANVEAAHSE 56

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568950030 149 LNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKI 210
Cdd:cd15879    2 LSEIEQRHKELVSLENQIKDLKDLFIQISLLVEEQGEMINNIEISVNNTQEYVQASKEKFGL 63

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 568950030 157 SEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVER 203
Cdd:cd00193    1 ESLEQLEASIGELKDIGRDMAMELEEQGEQLDRIEERAESTQARVSR 47

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.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 568950030  185 EMINRIEKNILSSADYVERGQEHVKIALENQKKARK 220
Cdd:pfam05739   1 EMLDRIDTNVENAQSNVERAQKELKKAVKYQKSNRK 36

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950030    8 VRELEKQQVTILATPLPEESMKQGLQNL--------------REEIKQLGREVRAQLkaiepqkEEADENYNSVNTRMKK 73
Cdd:pfam05483 512 TLELKKHQEDIINCKKQEERMLKQIENLeekemnlrdelesvREEFIQKGDEVKCKL-------DKSEENARSIEYEVLK 584

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950030   74 TQhgvlsQQFVELINKCNSM--QSEYREKNVERIRRQLK-ITNAGMVSDEELEQMldsgqsEVFVSNILKDTQVTRQALN 150
Cdd:pfam05483 585 KE-----KQMKILENKCNNLkkQIENKNKNIEELHQENKaLKKKGSAENKQLNAY------EIKVNKLELELASAKQKFE 653

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568950030  151 EISARHS---EIQQL--ERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVER 203
Cdd:pfam05483 654 EIIDNYQkeiEDKKIseEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEK 711

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]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950030    25 EESMKQgLQNLREEIKQLG---REVRAQLKAIEPQKEEAdENYNSVNTRMKKTQHGVLSQQFVELINKCNSMQSEYREKN 101
Cdd:TIGR02168  175 KETERK-LERTRENLDRLEdilNELERQLKSLERQAEKA-ERYKELKAELRELELALLVLRLEELREELEELQEELKEAE 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950030   102 VERIRRQLKITNAG------MVSDEELEQMLDSGQSEVFVSNILKDT-----QVTRQAL----NEISARHSEIQQLERSI 166
Cdd:TIGR02168  253 EELEELTAELQELEekleelRLEVSELEEEIEELQKELYALANEISRleqqkQILRERLanleRQLEELEAQLEELESKL 332

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568950030   167 RELHEIFTFLATEVEMQGEMINRIEKNILSSADYV---ERGQEHVKIALENQKKAR 219
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELeelESRLEELEEQLETLRSKV 388

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]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950030     2 AKLESKVRELEKQQVTILATPLPEESMKQGLQNLREEIKQLgrevRAQLKAIEPQKEEADENYNSVNtrmkktqhgvlsq 81
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL----RLEVSELEEEIEELQKELYALA------------- 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950030    82 qfvELINKCNSMQSEYREKnVERIRRQLKITNAgmvSDEELEQMLDSGQSEV-FVSNILKDTQVTRQAL-NEISARHSEI 159
Cdd:TIGR02168  295 ---NEISRLEQQKQILRER-LANLERQLEELEA---QLEELESKLDELAEELaELEEKLEELKEELESLeAELEELEAEL 367

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568950030   160 QQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKIALENQKKARK 220
Cdd:TIGR02168  368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950030  26 ESMKQGLQNLREEIKQLgrevRAQLKAIEPQKEEADENYNSVNTrmkKTQHGVLSQQFVELINKCNSMQSEYREKN--VE 103
Cdd:COG3206  171 EEARKALEFLEEQLPEL----RKELEEAEAALEEFRQKNGLVDL---SEEAKLLLQQLSELESQLAEARAELAEAEarLA 243

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950030 104 RIRRQLKItnagmvSDEELEQMLDSGQsevfVSNILKDTQVTRQALNEISAR----HSEIQQLERSIREL 169
Cdd:COG3206  244 ALRAQLGS------GPDALPELLQSPV----IQQLRAQLAELEAELAELSARytpnHPDVIALRAQIAAL 303

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950030   26 ESMKQGLQNLREEIKQLGREVRAQLKAIEPQKEEADENYNSVNTRMKKTQHGVLSQQFV------ELINKCNSMQSEY-- 97
Cdd:pfam09787  64 QKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEElryleeELRRSKATLQSRIkd 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950030   98 REKNVERIRRQLKITNAGMVSDEELEQMLdsgqSEVFVSNILKDTQVtrQALNeiSARHSEIQQLERSIRELHEIftfla 177
Cdd:pfam09787 144 REAEIEKLRNQLTSKSQSSSSQSELENRL----HQLTETLIQKQTML--EALS--TEKNSLVLQLERMEQQIKEL----- 210

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568950030  178 tevemQGEMINrieknilssadyvergqeHVKIALENQKKARKVSLAPSPGLG 230
Cdd:pfam09787 211 -----QGEGSN------------------GTSINMEGISDGEGTRLRNVPGLF 240

Uncharacterized protein, contains DUF3084 domain [Function unknown];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568950030  26 ESMKQGLQNLREEIKQLgrevRAQLKAIEPQKEEADENYNSVNTRMKKTQhgvlsQQFVELINKCNSMQSEY--REKNVE 103
Cdd:COG4372   41 DKLQEELEQLREELEQA----REELEQLEEELEQARSELEQLEEELEELN-----EQLQAAQAELAQAQEELesLQEEAE 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568950030 104 RIRRQLKITNAGMVSDEELEQMLDSGQSEVFVSNILKDTQVtRQALNEISARHSEIQQLERSIREL 169
Cdd:COG4372  112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL-KELEEQLESLQEELAALEQELQAL 176