SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog 1A) belongs to the Qb subgroup of SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptor). Vti1a interacts with syntaxin 16 (Qa), syntaxin 6 (Qc), and the lysosomal R-SNARE VAMP4 to form an endosomal SNARE core complex that mediates transport from the early endosomes to the TGN (trans-Golgi network). 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). 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 Qb SNAREs are N-terminal domains of SNAP23 and SNAP25, Vti1, Sec20 and GS27.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19923016 128 SERIERTGNRLTEGYRVALETEQLGAQVLNDLHHQRETLQGARARLRETNAELGRASRTLNT 189
Cdd:cd15891   1 TERLERSSRRLEDGYRIAVETEQIGAQILDDLHSQRETIQRSRDRLRETDSELGKSSRVLSG 62

SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog 1A) belongs to the Qb subgroup of SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptor). Vti1a interacts with syntaxin 16 (Qa), syntaxin 6 (Qc), and the lysosomal R-SNARE VAMP4 to form an endosomal SNARE core complex that mediates transport from the early endosomes to the TGN (trans-Golgi network). 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). 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 Qb SNAREs are N-terminal domains of SNAP23 and SNAP25, Vti1, Sec20 and GS27.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19923016 128 SERIERTGNRLTEGYRVALETEQLGAQVLNDLHHQRETLQGARARLRETNAELGRASRTLNT 189
Cdd:cd15891   1 TERLERSSRRLEDGYRIAVETEQIGAQILDDLHSQRETIQRSRDRLRETDSELGKSSRVLSG 62

Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein traffic between eukaryotic organelles. The v-SNAREs on transport vesicles interact with t-SNAREs on target membranes in order to facilitate this. This domain is the N-terminal half of the V-Snare proteins.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19923016    11 YATLIAEITAHIGRLQQQNNnSERHDLCSKIDSSLPEAQELLEQMGLEVRELNPGLRSSFNGKLQVAQAELKRLQAEYR 89
Cdd:pfam05008   1 FKELLAEITRKLARLSSLPG-EERKAALREIERKLDEAEELLDQMELEVRNLPSSERSKYKAKLREYKSDLKKLKKELK 78

SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog 1A) belongs to the Qb subgroup of SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptor). Vti1a interacts with syntaxin 16 (Qa), syntaxin 6 (Qc), and the lysosomal R-SNARE VAMP4 to form an endosomal SNARE core complex that mediates transport from the early endosomes to the TGN (trans-Golgi network). 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). 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 Qb SNAREs are N-terminal domains of SNAP23 and SNAP25, Vti1, Sec20 and GS27.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19923016 128 SERIERTGNRLTEGYRVALETEQLGAQVLNDLHHQRETLQGARARLRETNAELGRASRTLNT 189
Cdd:cd15891   1 TERLERSSRRLEDGYRIAVETEQIGAQILDDLHSQRETIQRSRDRLRETDSELGKSSRVLSG 62

Snare region anchored in the vesicle membrane C-terminus; Within the SNARE proteins interactions in the C-terminal half of the SNARE helix are critical to the driving of membrane fusion; whereas interactions in the N-terminal half of the SNARE domain are important for promoting priming or docking of the vesicle pfam05008.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923016   129 ERIERTGNRLTEGYRVALETEQLGAQVLNDLHHQRETLQGARARLRETNAELGRASRTLNTMMLRA 194
Cdd:pfam12352   1 ERLLREHDRLKNSHRIADETISIGQAILEDLHSQRETLKRARNKLHNTDNRLGKSNSTLRLINRRR 66

SNARE motif of Vti1b-like; Vti1b (vesicle transport through interaction with t-SNAREs homolog 1B) belongs to the Qb subgroup of SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptor). Vti1b interacts with syntaxin 7 (Qa), syntaxin 8 (Qc), and the lysosomal R-SNARE VAMP8 or VAMP7 to form the endosomal SNARE core complexes that mediate transport from the early endosomes and the MVBs (multivesicular bodies), and from the MVBs to the lysosomes, respectively. 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). 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 Qb SNAREs are N-terminal domains of SNAP23 and SNAP25, Vti1, Sec20 and GS27.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923016 129 ERIERTGNRLTEGYRVALETEQLGAQVLNDLHHQRETLQGARARLRETNAELGRASRTLN 188
Cdd:cd15890   2 ESLNRTSDSLARSQRIAAETEQIGTEIIEELGEQREQLLRTRDRLEETDANLSRARRILR 61

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 19923016      4 LEQYEQQYATLIAEITAHIGRLQQQnnnseRHDLCSKIDSSLPEAQELLEQMGLEVRELNpglrsSFNGKLQVAQAELKR 83
Cdd:TIGR02168  738 LEAEVEQLEERIAQLSKELTELEAE-----IEELEERLEEAEEELAEAEAEIEELEAQIE-----QLKEELKALREALDE 807

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923016     84 LQAEYRLTKDKQRSQANTFTTLDLGDSYEDVSIsTDQRQRLLDNSERIER-TGNRLTEGYRVALETEQLgAQVLNDLHHQ 162
Cdd:TIGR02168  808 LRAELTLLNEEAANLRERLESLERRIAATERRL-EDLEEQIEELSEDIESlAAEIEELEELIEELESEL-EALLNERASL 885

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 19923016    163 RETLQGARARLRETNAELGRASRTLNTM--MLRALREKVV 200
Cdd:TIGR02168  886 EEALALLRSELEELSEELRELESKRSELrrELEELREKLA 925