SNARE motif of Bet1; Bet1 forms a complexes with GS27 (Qb), syntaxin-5 (Qa) and Sec22B (R-SNARE) or GS28 (Qb), syntaxin-5 (Qa) and Ykt6 (R-SNARE). These complexes regulates the early secretory pathway of eukaryotic cells at the level of the transport from endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC) and from ERGIC to the cis-Golgi, respectively. Bet1 is a member of the Qc 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
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1759282204  93 ESQNDEQLNGMSAKVKMLKDITLAIGDEIRDSTALAEKMNDSFDSTRVRLRGTMNRMLR 151
Cdd:cd15853     1 ESQNDRRLDELSSKVSALKSLTIDIGDEVRDQNKLLDGMGDDFDSTGGLLGGTMKRLKR 59

SNARE motif of Bet1; Bet1 forms a complexes with GS27 (Qb), syntaxin-5 (Qa) and Sec22B (R-SNARE) or GS28 (Qb), syntaxin-5 (Qa) and Ykt6 (R-SNARE). These complexes regulates the early secretory pathway of eukaryotic cells at the level of the transport from endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC) and from ERGIC to the cis-Golgi, respectively. Bet1 is a member of the Qc 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
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1759282204  93 ESQNDEQLNGMSAKVKMLKDITLAIGDEIRDSTALAEKMNDSFDSTRVRLRGTMNRMLR 151
Cdd:cd15853     1 ESQNDRRLDELSSKVSALKSLTIDIGDEVRDQNKLLDGMGDDFDSTGGLLGGTMKRLKR 59

chromosomal replication initiator protein DnaA;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759282204  10 HQRDARSQLFSPYEQ----RKASPS--PHSRPASRPASGAGY-------GFPGAANPGPAFSAYPGASNPPPSQSSYRSA 76
Cdd:PRK14086  124 PRADDRPPGLPRQDQlptaRPAYPAyqQRPEPGAWPRAADDYgwqqqrlGFPPRAPYASPASYAPEQERDREPYDAGRPE 203

                  ....*....
gi 1759282204  77 TPNTRGQYS 85
Cdd:PRK14086  204 YDQRRRDYD 212

SNARE motif of Bet1; Bet1 forms a complexes with GS27 (Qb), syntaxin-5 (Qa) and Sec22B (R-SNARE) or GS28 (Qb), syntaxin-5 (Qa) and Ykt6 (R-SNARE). These complexes regulates the early secretory pathway of eukaryotic cells at the level of the transport from endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC) and from ERGIC to the cis-Golgi, respectively. Bet1 is a member of the Qc 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
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1759282204  93 ESQNDEQLNGMSAKVKMLKDITLAIGDEIRDSTALAEKMNDSFDSTRVRLRGTMNRMLR 151
Cdd:cd15853     1 ESQNDRRLDELSSKVSALKSLTIDIGDEVRDQNKLLDGMGDDFDSTGGLLGGTMKRLKR 59

SNARE motif of syntaxin 6; Syntaxin 6 forms a complex with syntaxin 16 (Qa), Vti1a (Qb) and VAMP4 (R-SNARE) and is involved in the regulation of recycling of early endosomes to the trans-Golgi network (TGN). Syntaxin 6 and its yeast homolog TLG1 are members of the Qc 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 1759282204  95 QNDEQLNGMSAKVKMLKDITLAIGDEIRDSTALAEKMNDSFDSTRVRLRGTMNRM---LRMAE 154
Cdd:cd15851     3 EQDEQLDGVGGTVGNLREQAQLIGDELEEQAELLDDLDHEVDRTESRLDRGMKKMakvIRKNE 65

SNARE motif of VAM7; Fungal VAM7 (vacuolar morphogenesis protein 7) is a member of the Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein family involved in vacuolar protein transport and membrane fusion. SNARE 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). Qc-, as well as Qa- and Qb-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        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1759282204  92 LESQnDEQLNGMSAKVKMLKDITLAIGDEIRDSTALAEKMNDSFDSTRVRLRGTMNRM 149
Cdd:cd15858     1 MQEQ-DQQLEQLRKIVQRQKELGLAINQELEEQNELLDELDEDVDRTGGKLRVANKRA 57

C-terminal SNARE motif of SNAP29; C-terminal SNARE motif of SNAP29, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP29 interacts with STX17 (Qa) 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. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, 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. Other members of the Qb/Qc SNAREs are SNAP23, SNAP25, SNAP47 and SEC9.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1759282204  93 ESQNDEQLNGMSAKVKMLKDITLAIGDEIRDSTALAEKMNDSFDSTRVRLRGT---MNR 148
Cdd:cd15856     1 DQQLDENLDEMSSGLSRLKGLALGLGTEIDSQNDLLDRITDKADKADIKIKKQnkqMNK 59

SNARE motif of syntaxin 8; Syntaxin 8 forms a complex with syntaxin 7 (Qa), Vti1b (Qb) and either VAMP7 or VAMP8 (R-SNARE) and is involved in the transport from early endosomes to the lysosome. Syntaxin 8 is a member of the Qc 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
                  ....*....|....*....|....*....|....*....|....*....|
gi 1759282204  94 SQNDEQLNGMSAKVKMLKDITLAIGDEIRDSTALAEKMNDSFDSTRVRLR 143
Cdd:cd15852     2 QEQDQGLDALSSIISRQKQIGQAIGDEVDDQNEIIDDLADGMDRTDARLR 51