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Conserved domains on  [gi|213512890|ref|NP_001134781|]
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vesicle-associated membrane protein 5-like [Salmo salar]

Protein Classification

SNARE domain-containing protein; synaptobrevin family protein( domain architecture ID 10205236)

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| synaptobrevin family protein with similarity to the C-terminal domain of vesicle-associated membrane proteins (VAMPs) which are involved in the targeting and/or fusion of transport vesicles to their target membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
R-SNARE_VAMP5 cd15872
SNARE motif of VAMP5; The VAMP-5 (vesicle-associated membrane protein 5) protein belongs to ...
 5-72 1.34e-27

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.


:

Pssm-ID: 277225 [Multi-domain]  Cd Length: 68  Bit Score: 96.32  E-value: 1.34e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 213512890   5 NSRLRQAQEEAEEVKVIMMDNMEKTEERKEKLQDLDERAEELKLKSKSFYKTSRKLNEQKKCDNIKAK 72
Cdd:cd15872    1 KNRLERCQREAEEVKVIMLDNLNKALEREGKLSDLEDRADELLNMSKAFEKTTQTVAQKKRWENIKYK 68
 
Name Accession Description Interval E-value
R-SNARE_VAMP5 cd15872
SNARE motif of VAMP5; The VAMP-5 (vesicle-associated membrane protein 5) protein belongs to ...
 5-72 1.34e-27

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.


Pssm-ID: 277225 [Multi-domain]  Cd Length: 68  Bit Score: 96.32  E-value: 1.34e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 213512890   5 NSRLRQAQEEAEEVKVIMMDNMEKTEERKEKLQDLDERAEELKLKSKSFYKTSRKLNEQKKCDNIKAK 72
Cdd:cd15872    1 KNRLERCQREAEEVKVIMLDNLNKALEREGKLSDLEDRADELLNMSKAFEKTTQTVAQKKRWENIKYK 68
Synaptobrevin pfam00957
Synaptobrevin;
5-90 1.30e-18

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 74.11  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213512890    5 NSRLRQAQEEAEEVKVIMMDNMEKTEERKEKLQDLDERAEELKLKSKSFYKTSRKLNEQKKCDNIKAKWKLIAVVAASAI 84
Cdd:pfam00957   2 NDKLAKIQAEVDEVKDIMTENIDKVLERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMWWKNMKLYIILGLVVLILIL 81


                  ....*.
gi 213512890   85 IVILVA 90
Cdd:pfam00957  82 IIIIFI 87
SNC1 COG5143
Synaptobrevin/VAMP-like protein [Intracellular trafficking and secretion];
10-62 3.20e-05

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


Pssm-ID: 227472 [Multi-domain]  Cd Length: 190  Bit Score: 41.26  E-value: 3.20e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 213512890  10 QAQEEAEEVKVIMMDNMEKTEERKEKLQDLDERAEELKLKSKSFYKTSRKLNE 62
Cdd:COG5143  133 QLQQELEETKRVLNKNIEKVLYRDEKLDLLVDLSSILLLSSKMFPKSAKKSNL 185
 
Name Accession Description Interval E-value
R-SNARE_VAMP5 cd15872
SNARE motif of VAMP5; The VAMP-5 (vesicle-associated membrane protein 5) protein belongs to ...
 5-72 1.34e-27

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.


Pssm-ID: 277225 [Multi-domain]  Cd Length: 68  Bit Score: 96.32  E-value: 1.34e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 213512890   5 NSRLRQAQEEAEEVKVIMMDNMEKTEERKEKLQDLDERAEELKLKSKSFYKTSRKLNEQKKCDNIKAK 72
Cdd:cd15872    1 KNRLERCQREAEEVKVIMLDNLNKALEREGKLSDLEDRADELLNMSKAFEKTTQTVAQKKRWENIKYK 68
Synaptobrevin pfam00957
Synaptobrevin;
5-90 1.30e-18

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 74.11  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213512890    5 NSRLRQAQEEAEEVKVIMMDNMEKTEERKEKLQDLDERAEELKLKSKSFYKTSRKLNEQKKCDNIKAKWKLIAVVAASAI 84
Cdd:pfam00957   2 NDKLAKIQAEVDEVKDIMTENIDKVLERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMWWKNMKLYIILGLVVLILIL 81


                  ....*.
gi 213512890   85 IVILVA 90
Cdd:pfam00957  82 IIIIFI 87
R-SNARE cd15843
SNARE motif, subgroup R-SNARE; SNARE (soluble N-ethylmaleimide-sensitive factor attachment ...
 7-63 1.46e-11

SNARE motif, subgroup R-SNARE; 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). In contrast to Qa-, Qb- and Qc-SNAREs that are localized to target organelle membranes, R-SNAREs are 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: 277196 [Multi-domain]  Cd Length: 60  Bit Score: 55.20  E-value: 1.46e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 213512890   7 RLRQAQEEAEEVKVIMMDNMEKTEERKEKLQDLDERAEELKLKSKSFYKTSRKLNEQ 63
Cdd:cd15843    2 KLSKVQEQVDEVKDVMQENIDKVLERGEKLEDLVDKTENLNESANAFKKQARKLKRK 58
R-SNARE_VAMP2 cd15870
SNARE motif of VAMP2; The VAMP-2 (vesicle-associated membrane protein 2, also called ...
 6-60 6.10e-11

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.


Pssm-ID: 277223 [Multi-domain]  Cd Length: 63  Bit Score: 53.93  E-value: 6.10e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 213512890   6 SRLRQAQEEAEEVKVIMMDNMEKTEERKEKLQDLDERAEELKLKSKSFYKTSRKL 60
Cdd:cd15870    1 KRLQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFETSAGKL 55
R-SNARE_YKT6 cd15867
SNARE motif of YKT6; Ykt6 forms complexes with syntaxin-5 (Qa), GS28 (Qb) and either Bet1 (Qc) ...
 10-61 1.93e-10

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.


Pssm-ID: 277220  Cd Length: 61  Bit Score: 52.76  E-value: 1.93e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 213512890  10 QAQEEAEEVKVIMMDNMEKTEERKEKLQDLDERAEELKLKSKSFYKTSRKLN 61
Cdd:cd15867    6 KVQSELDETKIILHKTIESVLERGEKLDDLVEKSEDLSDQSKMFYKTAKKQN 57
R-SNARE_VAMP8 cd15868
SNARE motif of VAMP8; The lysosomal VAMP8 (vesicle-associated membrane protein 8, also called ...
 5-60 1.22e-09

SNARE motif of VAMP8; The lysosomal VAMP8 (vesicle-associated membrane protein 8, also called endobrevin) protein belongs to the R-SNARE subgroup of SNAREs and interacts with STX17 (Qa) and SNAP29 (Qb/Qc). The complex plays a role in autophagosome-lysosome fusion via regulating the transport from early endosomes to multivesicular bodies. 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 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.


Pssm-ID: 277221 [Multi-domain]  Cd Length: 68  Bit Score: 50.78  E-value: 1.22e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 213512890   5 NSRLRQAQEEAEEVKVIMMDNMEKTEERKEKLQDLDERAEELKLKSKSFYKTSRKL 60
Cdd:cd15868    1 NDKVSALQSQVDEVKNIMTQNIDKILARGERLDDLMDKTEDLEATSKTFQKTSQKV 56
R-SNARE_VAMP4 cd15869
SNARE motif of VAMP4; The VAMP-4 (vesicle-associated membrane protein 4) protein belongs to ...
 5-63 3.34e-08

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.


Pssm-ID: 277222 [Multi-domain]  Cd Length: 67  Bit Score: 47.00  E-value: 3.34e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 213512890   5 NSRLRQAQEEAEEVKVIMMDNMEKTEERKEKLQDLDERAEELKLKSKSFYKTSRKLNEQ 63
Cdd:cd15869    1 DDKIRRVQNQVDEVVDVMQDNITKVIDRGEKLEDLQDKSESLSDNASAFRSRSKQLRRK 59
R-SNARE_VAMP7 cd15871
SNARE motif of VAMP7; The VAMP-7 (vesicle-associated membrane protein 7, also called ...
 6-70 5.18e-08

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.


Pssm-ID: 277224 [Multi-domain]  Cd Length: 65  Bit Score: 46.25  E-value: 5.18e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 213512890   6 SRLRQAQEEAEEVKVIMMDNMEKTEERKEKLQDLDERAEELKLKSKSFYKTSRKLNEQKKCDNIK 70
Cdd:cd15871    1 DKVSKVQGQLDELKGIMVKNIDSIAQRGEKLELLVDKTEDLSSSSVTFKKTSRNLARAMCMKNIK 65
R-SNARE_STXBP5_6 cd15873
SNARE domain of STXBP5, STXBP6 and related proteins; Syntaxin binding protein 5 (STXBP5, also ...
 5-65 1.61e-06

SNARE domain of STXBP5, STXBP6 and related proteins; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as its relative Syntaxin binding protein 6 (STXBP6, also called Amisyn) contains a C-terminal R-SNARE-like domain, which allows it to assemble into SNARE complexes, which in turn makes the complexes inactive and inhibits exocytosis. In general, 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). 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.


Pssm-ID: 277226  Cd Length: 61  Bit Score: 42.24  E-value: 1.61e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 213512890   5 NSRLRQAQEEAEEVKVIMMDNMEKTEERKEKLQDLDERAEELKLKSKSFYKTSRKLNEQKK 65
Cdd:cd15873    1 GGGMKALRAKAGSAASAAARARQALNERGEKLSELEDRTAEMEDNAESFASTAKELAKKYK 61
SNC1 COG5143
Synaptobrevin/VAMP-like protein [Intracellular trafficking and secretion];
10-62 3.20e-05

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


Pssm-ID: 227472 [Multi-domain]  Cd Length: 190  Bit Score: 41.26  E-value: 3.20e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 213512890  10 QAQEEAEEVKVIMMDNMEKTEERKEKLQDLDERAEELKLKSKSFYKTSRKLNE 62
Cdd:COG5143  133 QLQQELEETKRVLNKNIEKVLYRDEKLDLLVDLSSILLLSSKMFPKSAKKSNL 185
R-SNARE_SEC22 cd15866
SNARE motif of SEC22; SEC22 forms complexes with syntaxin 18 (Qa), Sec20 (Qb) and USE1 (Qc), ...
 5-63 1.55e-04

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.


Pssm-ID: 277219 [Multi-domain]  Cd Length: 64  Bit Score: 37.11  E-value: 1.55e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 213512890   5 NSRLRQAQEEAEEVKVIMMDNMEKTEERKEKLQDLDERAEELKLKSKSFYKTSRKLNEQ 63
Cdd:cd15866    1 RRNLSKLNDELQDVQRIMTKNIDDVLGRGEKLDDLSDKSSNLSSESKKYKKDAKKLNLQ 59
SNARE cd00193
SNARE motif; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) ...
 6-59 3.79e-03

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: 33.51  E-value: 3.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 213512890   6 SRLRQAQEEAEEVKVIMMDNMEKTEERKEKLQDLDERAEELKLKSKSFYKTSRK 59
Cdd:cd00193    1 ESLEQLEASIGELKDIGRDMAMELEEQGEQLDRIEERAESTQARVSRAEKSLAK 54
 
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.
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