longin domain; Longin-domain is N-terminal domain of a subgroup of R-SNARE proteins, including VAMP7, Ykt6, and Sec22. Longin is one of the approximately 26 components required for transporting proteins from the ER to the plasma membrane, via the Golgi apparatus. It is necessary for the steps of the transfer from the ER to the Golgi complex. Longins are the only R-SNAREs that are common to all eukaryotes, and they are characterized by a conserved N-terminal domain with a profilin-like fold called a longin domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449437158   4 IYALVARGS--VVLAE------FSATPTNASSISRQILDKIPGNDdSHVSYSQDRYIFHVKRTDGLTVLCMADDTAGRRI 75
Cdd:cd14824    1 LYALIARGSdgLILAEytdlssFSSVKENFKFVAKTILERTPPSG-QRQSVEEGDYVFHYLVEDGLCYLCITDKEYPKRV 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 449437158  76 PFAFLEDIHQRFVRTYGRAVHSANAYGMNDEFSRVLSQQLEYY 118
Cdd:cd14824   80 AFAFLEEVLDEFLSKYGSSAWTAARPYLFSEFDPELKKLMKKY 122

longin domain; Longin-domain is N-terminal domain of a subgroup of R-SNARE proteins, including VAMP7, Ykt6, and Sec22. Longin is one of the approximately 26 components required for transporting proteins from the ER to the plasma membrane, via the Golgi apparatus. It is necessary for the steps of the transfer from the ER to the Golgi complex. Longins are the only R-SNAREs that are common to all eukaryotes, and they are characterized by a conserved N-terminal domain with a profilin-like fold called a longin domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449437158   4 IYALVARGS--VVLAE------FSATPTNASSISRQILDKIPGNDdSHVSYSQDRYIFHVKRTDGLTVLCMADDTAGRRI 75
Cdd:cd14824    1 LYALIARGSdgLILAEytdlssFSSVKENFKFVAKTILERTPPSG-QRQSVEEGDYVFHYLVEDGLCYLCITDKEYPKRV 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 449437158  76 PFAFLEDIHQRFVRTYGRAVHSANAYGMNDEFSRVLSQQLEYY 118
Cdd:cd14824   80 AFAFLEEVLDEFLSKYGSSAWTAARPYLFSEFDPELKKLMKKY 122

Regulated-SNARE-like domain; Longin is one of the approximately 26 components required for transporting proteins from the ER to the plasma membrane, via the Golgi apparatus. It is necessary for the steps of the transfer from the ER to the Golgi complex. Longins are the only R-SNAREs that are common to all eukaryotes, and they are characterized by a conserved N-terminal domain with a profilin-like fold called a longin domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449437158   29 SRQILDKIPgNDDSHVSYSQDRYIFHVKRTDGLTVLCMADDTAGRRIPFAFLEDIHQRFVRTYGRAVHSAN-AYGMNDEF 107
Cdd:pfam13774   1 AKTILEKIP-QNPQRQTYEGDNYTFHYLIEDGLTYLVIADKSYPRRLAFAFLEEIKDEFLSTYGPWTASALrPYAFNKEF 79

                  ..
gi 449437158  108 SR 109
Cdd:pfam13774  80 DT 81

Synaptobrevin/VAMP-like protein [Intracellular trafficking and secretion];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449437158   1 MAIIYALVARGSVVLAEFSATPTNASSIS-----RQILDKIPGNDDSHVSYSQDRYIFHV-KRTDGLTVLCMADDTAGRR 74
Cdd:COG5143    1 IASISLFRVKGEPLRTLSDAESLSSFSFFhrskvKEVLRFLSKTSASRASIESGDYFFHYlKMSSGIVYVPISDKEYPNK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449437158  75 IPFAFLEDIHQRFVRTYGRAVHSANAYG-MNDEFSRVLSqqlEYYSNDPNADRINRLKGEMSQVRNVMIENIDKVLERGD 153
Cdd:COG5143   81 LAYGYLNSIATEFLKSSALEQLIDDTVGiMRVNIDKVIE---KGYRDPSIQDKLDQLQQELEETKRVLNKNIEKVLYRDE 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 449437158 154 RLELLVDKTTNMQGNTMRFRKQARRFRNTIWW 185
Cdd:COG5143  158 KLDLLVDLSSILLLSSKMFPKSAKKSNLCCLI 189

longin domain; Longin-domain is N-terminal domain of a subgroup of R-SNARE proteins, including VAMP7, Ykt6, and Sec22. Longin is one of the approximately 26 components required for transporting proteins from the ER to the plasma membrane, via the Golgi apparatus. It is necessary for the steps of the transfer from the ER to the Golgi complex. Longins are the only R-SNAREs that are common to all eukaryotes, and they are characterized by a conserved N-terminal domain with a profilin-like fold called a longin domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449437158   4 IYALVARGS--VVLAE------FSATPTNASSISRQILDKIPGNDdSHVSYSQDRYIFHVKRTDGLTVLCMADDTAGRRI 75
Cdd:cd14824    1 LYALIARGSdgLILAEytdlssFSSVKENFKFVAKTILERTPPSG-QRQSVEEGDYVFHYLVEDGLCYLCITDKEYPKRV 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 449437158  76 PFAFLEDIHQRFVRTYGRAVHSANAYGMNDEFSRVLSQQLEYY 118
Cdd:cd14824   80 AFAFLEEVLDEFLSKYGSSAWTAARPYLFSEFDPELKKLMKKY 122

Regulated-SNARE-like domain; Longin is one of the approximately 26 components required for transporting proteins from the ER to the plasma membrane, via the Golgi apparatus. It is necessary for the steps of the transfer from the ER to the Golgi complex. Longins are the only R-SNAREs that are common to all eukaryotes, and they are characterized by a conserved N-terminal domain with a profilin-like fold called a longin domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449437158   29 SRQILDKIPgNDDSHVSYSQDRYIFHVKRTDGLTVLCMADDTAGRRIPFAFLEDIHQRFVRTYGRAVHSAN-AYGMNDEF 107
Cdd:pfam13774   1 AKTILEKIP-QNPQRQTYEGDNYTFHYLIEDGLTYLVIADKSYPRRLAFAFLEEIKDEFLSTYGPWTASALrPYAFNKEF 79

                  ..
gi 449437158  108 SR 109
Cdd:pfam13774  80 DT 81

SNARE motif of VAMP7; The VAMP-7 (vesicle-associated membrane protein 7, also called synaptobrevin-like protein 1) protein belongs to the R-SNARE subgroup of SNAREs and interacts with syntaxin 7(Qa), syntaxin 8 (Qc) and Vti1b (Qb). The complex is involved in the transport from early endosomes to the lysosome via regulating the transport from multivesicular bodies to the lysosomes. SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins contain 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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449437158 125 DRINRLKGEMSQVRNVMIENIDKVLERGDRLELLVDKTTNMQGNTMRFRKQARRFRNTIWWKNVK 189
Cdd:cd15871    1 DKVSKVQGQLDELKGIMVKNIDSIAQRGEKLELLVDKTEDLSSSSVTFKKTSRNLARAMCMKNIK 65

SNARE motif of VAMP4; The VAMP-4 (vesicle-associated membrane protein 4) protein belongs to the R-SNARE subgroup of SNAREs and interacts with syntaxin 16 (Qa), Vti1a (Qb) and syntaxin 6 (Qc). This complex plays a role in maintenance of Golgi ribbon structure and normal retrograde trafficking from the early endosome to the trans-Golgi network (TGN). SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins contain 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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449437158 125 DRINRLKGEMSQVRNVMIENIDKVLERGDRLELLVDKTTNMQGNTMRFRKQARRFRNTIWWKNVK 189
Cdd:cd15869    2 DKIRRVQNQVDEVVDVMQDNITKVIDRGEKLEDLQDKSESLSDNASAFRSRSKQLRRKMWWQNCK 66

SNARE motif of VAMP2; The VAMP-2 (vesicle-associated membrane protein 2, also called synaptobrevin-2) protein belongs to the R-SNARE subgroup of SNAREs and interacts with Syntaxin-1 (Qa) and SNAP-25(Qb/Qc), as well as syntaxin 12 (Qa) and SNAP23 (Qb/Qc). The complexes play a role in transport of secretory granule from trans-Golgi network to the plasma membrane, and in the transport from early endosomes to and from the plasma membrane, respectively. SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins contain 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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 449437158 125 DRINRLKGEMSQVRNVMIENIDKVLERGDRLELLVDKTTNMQGNTMRFRKQARRFRNTIWWKN 187
Cdd:cd15870    1 KRLQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFETSAGKLKRKYWWKN 63

SNARE motif of SEC22; SEC22 forms complexes with syntaxin 18 (Qa), Sec20 (Qb) and USE1 (Qc), and with syntaxin 5 (Qa), GS27 (Qb) and Bet1 (Qc). These complexes are involved in the transport from cis-Golgi to the endoplasmic reticulum (ER) and in the transport from endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC), respectively. SEC22 is a member of the R-SNARE subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins which contain 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. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 449437158 127 INRLKGEMSQVRNVMIENIDKVLERGDRLELLVDKTTNMQGNTMRFRKQARRFR 180
Cdd:cd15866    4 LSKLNDELQDVQRIMTKNIDDVLGRGEKLDDLSDKSSNLSSESKKYKKDAKKLN 57

SNARE motif of YKT6; Ykt6 forms complexes with syntaxin-5 (Qa), GS28 (Qb) and either Bet1 (Qc) or GS15 (Qc). This complex regulates the early secretory pathway of eukaryotic cells at the level of the transport from the ER-Golgi intermediate compartment (ERGIC) to the cis-Golgi and transport from the trans-Golgi network to the cis-Golgi, respectively. Ykt6 is a member of the R-SNARE subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins which contain 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. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 449437158 124 ADRINRLKGEMSQVRNVMIENIDKVLERGDRLELLVDKTTNMQGNTMRFRKQARRFRNT 182
Cdd:cd15867    1 ADKIMKVQSELDETKIILHKTIESVLERGEKLDDLVEKSEDLSDQSKMFYKTAKKQNAV 59

SNARE motif of VAMP5; The VAMP-5 (vesicle-associated membrane protein 5) protein belongs to the R-SNARE subgroup of SNAREs. Its function is unknown. SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins contain 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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 449437158 126 RINRLKGEMSQVRNVMIENIDKVLERGDRLELLVDKTTNMQGNTMRFRKQARRFRNTIWWKNVK 189
Cdd:cd15872    3 RLERCQREAEEVKVIMLDNLNKALEREGKLSDLEDRADELLNMSKAFEKTTQTVAQKKRWENIK 66