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Conserved domains on  [gi|1958649369|ref|XP_038946009|]
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vesicle transport through interaction with t-SNAREs homolog 1A isoform X4 [Rattus norvegicus]

Protein Classification

vesicle transport through interaction with t-SNAREs homolog 1A( domain architecture ID 10523358)

vesicle transport through interaction with t-SNAREs homolog 1A is a v-SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane

CATH:  1.20.58.400
Gene Ontology:  GO:0005484|GO:0006906|GO:0015031
SCOP:  4000986
TCDB:  1.F.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SNARE_Vti1a cd15891
SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog ...
 129-195 4.96e-25

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.


:

Pssm-ID: 277244  Cd Length: 62  Bit Score: 92.75  E-value: 4.96e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649369 129 TERLERSSRRLEAGYQIAVETgknseKQIGQEMLENLSHDRERIQRARERLRETDANLGKSSRILTG 195
Cdd:cd15891     1 TERLERSSRRLEDGYRIAVET-----EQIGAQILDDLHSQRETIQRSRDRLRETDSELGKSSRVLSG 62
V-SNARE pfam05008
Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein ...
 12-90 7.09e-23

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.


:

Pssm-ID: 461516  Cd Length: 79  Bit Score: 87.66  E-value: 7.09e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958649369  12 FAVLTAEITSKISRVPRLPPDEKKQMVANVEKQLEEARELLEQMDLEVREIPPQSRGMYSNRMRSYKQEMGKLETDFKR 90
Cdd:pfam05008   1 FKELLAEITRKLARLSSLPGEERKAALREIERKLDEAEELLDQMELEVRNLPSSERSKYKAKLREYKSDLKKLKKELKR 79
 
Name Accession Description Interval E-value
SNARE_Vti1a cd15891
SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog ...
 129-195 4.96e-25

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.


Pssm-ID: 277244  Cd Length: 62  Bit Score: 92.75  E-value: 4.96e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649369 129 TERLERSSRRLEAGYQIAVETgknseKQIGQEMLENLSHDRERIQRARERLRETDANLGKSSRILTG 195
Cdd:cd15891     1 TERLERSSRRLEDGYRIAVET-----EQIGAQILDDLHSQRETIQRSRDRLRETDSELGKSSRVLSG 62
V-SNARE pfam05008
Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein ...
 12-90 7.09e-23

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.


Pssm-ID: 461516  Cd Length: 79  Bit Score: 87.66  E-value: 7.09e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958649369  12 FAVLTAEITSKISRVPRLPPDEKKQMVANVEKQLEEARELLEQMDLEVREIPPQSRGMYSNRMRSYKQEMGKLETDFKR 90
Cdd:pfam05008   1 FKELLAEITRKLARLSSLPGEERKAALREIERKLDEAEELLDQMELEVRNLPSSERSKYKAKLREYKSDLKKLKKELKR 79
V-SNARE_C pfam12352
Snare region anchored in the vesicle membrane C-terminus; Within the SNARE proteins ...
 130-199 6.57e-15

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.


Pssm-ID: 289148  Cd Length: 66  Bit Score: 66.48  E-value: 6.57e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649369 130 ERLERSSRRLEAGYQIAVETgknseKQIGQEMLENLSHDRERIQRARERLRETDANLGKSSRILTGMLRR 199
Cdd:pfam12352   1 ERLLREHDRLKNSHRIADET-----ISIGQAILEDLHSQRETLKRARNKLHNTDNRLGKSNSTLRLINRR 65
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
 127-196 4.63e-04

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".


Pssm-ID: 197699 [Multi-domain]  Cd Length: 66  Bit Score: 37.18  E-value: 4.63e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649369  127 DNTERLERSSRRLEAGYQIAVETgknseKQIGQEMLENLSHDRERIQRARERLRETDANLGKSSRILTGM 196
Cdd:smart00397   2 QALAREEERDEELEQLEKSIQEL-----KQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKKA 66
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
46-186 9.58e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 9.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649369  46 EEARELLEQMDLEvREIPPQSRGMYSNRMRSYKQEMGKLETDFKRSRIAYSDEVRNELLGDAGNSSENQLIKLREERAHL 125
Cdd:COG4717   319 EELEELLAALGLP-PDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY 397

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958649369 126 LDNTERLERSSRRLEAGYQIAVETGKNSEKQIGQEMLENLSHDRERIQRARERLRETDANL 186
Cdd:COG4717   398 QELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAEL 458
 
Name Accession Description Interval E-value
SNARE_Vti1a cd15891
SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog ...
 129-195 4.96e-25

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.


Pssm-ID: 277244  Cd Length: 62  Bit Score: 92.75  E-value: 4.96e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649369 129 TERLERSSRRLEAGYQIAVETgknseKQIGQEMLENLSHDRERIQRARERLRETDANLGKSSRILTG 195
Cdd:cd15891     1 TERLERSSRRLEDGYRIAVET-----EQIGAQILDDLHSQRETIQRSRDRLRETDSELGKSSRVLSG 62
V-SNARE pfam05008
Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein ...
 12-90 7.09e-23

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.


Pssm-ID: 461516  Cd Length: 79  Bit Score: 87.66  E-value: 7.09e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958649369  12 FAVLTAEITSKISRVPRLPPDEKKQMVANVEKQLEEARELLEQMDLEVREIPPQSRGMYSNRMRSYKQEMGKLETDFKR 90
Cdd:pfam05008   1 FKELLAEITRKLARLSSLPGEERKAALREIERKLDEAEELLDQMELEVRNLPSSERSKYKAKLREYKSDLKKLKKELKR 79
V-SNARE_C pfam12352
Snare region anchored in the vesicle membrane C-terminus; Within the SNARE proteins ...
 130-199 6.57e-15

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.


Pssm-ID: 289148  Cd Length: 66  Bit Score: 66.48  E-value: 6.57e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649369 130 ERLERSSRRLEAGYQIAVETgknseKQIGQEMLENLSHDRERIQRARERLRETDANLGKSSRILTGMLRR 199
Cdd:pfam12352   1 ERLLREHDRLKNSHRIADET-----ISIGQAILEDLHSQRETLKRARNKLHNTDNRLGKSNSTLRLINRR 65
SNARE_Vti1 cd15862
SNARE motif of Vti1; Vti1 (vesicle transport through interaction with t-SNAREs homolog 1) ...
 129-195 5.00e-14

SNARE motif of Vti1; Vti1 (vesicle transport through interaction with t-SNAREs homolog 1) 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 complex that mediates transport from the early endosomes and the MVBs (multivesicular bodies), and from the MVBs to the lysosomes, respectively. 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.


Pssm-ID: 277215  Cd Length: 62  Bit Score: 64.09  E-value: 5.00e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649369 129 TERLERSSRRLEAGYQIAVETgknseKQIGQEMLENLSHDRERIQRARERLRETDANLGKSSRILTG 195
Cdd:cd15862     1 TDRLDRSSDRLEDSRRIAAET-----EEVGANILEDLGRQRETLLRARDRLRETDGNLDRSRRILKS 62
SNARE_Vti1b cd15890
SNARE motif of Vti1b-like; Vti1b (vesicle transport through interaction with t-SNAREs homolog ...
 129-195 5.61e-11

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.


Pssm-ID: 277243  Cd Length: 62  Bit Score: 56.04  E-value: 5.61e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649369 129 TERLERSSRRLEAGYQIAVETgknseKQIGQEMLENLSHDRERIQRARERLRETDANLGKSSRILTG 195
Cdd:cd15890     1 TESLNRTSDSLARSQRIAAET-----EQIGTEIIEELGEQREQLLRTRDRLEETDANLSRARRILRS 62
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
 127-196 4.63e-04

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".


Pssm-ID: 197699 [Multi-domain]  Cd Length: 66  Bit Score: 37.18  E-value: 4.63e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649369  127 DNTERLERSSRRLEAGYQIAVETgknseKQIGQEMLENLSHDRERIQRARERLRETDANLGKSSRILTGM 196
Cdd:smart00397   2 QALAREEERDEELEQLEKSIQEL-----KQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKKA 66
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
46-186 9.58e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 9.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649369  46 EEARELLEQMDLEvREIPPQSRGMYSNRMRSYKQEMGKLETDFKRSRIAYSDEVRNELLGDAGNSSENQLIKLREERAHL 125
Cdd:COG4717   319 EELEELLAALGLP-PDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY 397

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958649369 126 LDNTERLERSSRRLEAGYQIAVETGKNSEKQIGQEMLENLSHDRERIQRARERLRETDANL 186
Cdd:COG4717   398 QELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAEL 458
 
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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