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Conserved domains on  [gi|281182635|ref|NP_001162571|]
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vesicle transport protein USE1 [Rattus norvegicus]

Protein Classification

SNARE_USE1 domain-containing protein( domain architecture ID 11184514)

SNARE_USE1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Use1 pfam09753
Membrane fusion protein Use1; This entry is of a family of proteins all approximately 300 ...
 16-266 7.09e-106

Membrane fusion protein Use1; This entry is of a family of proteins all approximately 300 residues in length. The proteins have a single C-terminal trans-membrane domain and a SNARE [soluble NSF (N-ethylmaleimide-sensitive fusion protein) attachment protein receptor] domain of approximately 60 residues. The SNARE domains are essential for membrane fusion and are conserved from yeasts to humans. Use1 is one of the three protein subunits that make up the SNARE complex and it is specifically required for Golgi-endoplasmic reticulum retrograde transport.


:

Pssm-ID: 462882 [Multi-domain]  Cd Length: 245  Bit Score: 306.94  E-value: 7.09e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182635   16 RLELNLVRLLCRCESMAAEKREPDEWRLEKYVGALEDMLQALKVQASKPASEVISEYSRKVDFLKGMLQAEKLTSSSEKA 95
Cdd:pfam09753   1 KLEINFRRLLSRCERLAKEDRSDNQWRLEKYVKALEEMLEELQKERDKPSKDVLNEYSERVEFLKGLLEAEKLSSPEEKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182635   96 LANQFLAPG-----RVPTTAKERVPATKTVHLQSRARYTSEMRSELLGTESSgeleadmrkrvVKGPRPADEKQSASELD 170
Cdd:pfam09753  81 LANQFLAPGfaespRSPEESSERESASKELRQKTKAKYQSELRKELLGTGDS-----------SSSPRGRAELKLDEDLD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182635  171 LVLQRHQGLQEKLAEEMLGLARSLKTNTLAAQSVIKKDNQTLSHSLKMADQNLEKLKLESERLEQHAQKSVNWLLWAMLI 250
Cdd:pfam09753 150 AVLKKHRNLQEKLAEEMLSLARNLKENSLAASNIIKKDTEILSKSEKAADQNLASLKRESERLEEHYKSKTNCWLWLMLF 229

                         250
                  ....*....|....*.
gi 281182635  251 VVCFVFISMILFIRIM 266
Cdd:pfam09753 230 VVCCVFIMMVLFIRVF 245
 
Name Accession Description Interval E-value
Use1 pfam09753
Membrane fusion protein Use1; This entry is of a family of proteins all approximately 300 ...
 16-266 7.09e-106

Membrane fusion protein Use1; This entry is of a family of proteins all approximately 300 residues in length. The proteins have a single C-terminal trans-membrane domain and a SNARE [soluble NSF (N-ethylmaleimide-sensitive fusion protein) attachment protein receptor] domain of approximately 60 residues. The SNARE domains are essential for membrane fusion and are conserved from yeasts to humans. Use1 is one of the three protein subunits that make up the SNARE complex and it is specifically required for Golgi-endoplasmic reticulum retrograde transport.


Pssm-ID: 462882 [Multi-domain]  Cd Length: 245  Bit Score: 306.94  E-value: 7.09e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182635   16 RLELNLVRLLCRCESMAAEKREPDEWRLEKYVGALEDMLQALKVQASKPASEVISEYSRKVDFLKGMLQAEKLTSSSEKA 95
Cdd:pfam09753   1 KLEINFRRLLSRCERLAKEDRSDNQWRLEKYVKALEEMLEELQKERDKPSKDVLNEYSERVEFLKGLLEAEKLSSPEEKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182635   96 LANQFLAPG-----RVPTTAKERVPATKTVHLQSRARYTSEMRSELLGTESSgeleadmrkrvVKGPRPADEKQSASELD 170
Cdd:pfam09753  81 LANQFLAPGfaespRSPEESSERESASKELRQKTKAKYQSELRKELLGTGDS-----------SSSPRGRAELKLDEDLD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182635  171 LVLQRHQGLQEKLAEEMLGLARSLKTNTLAAQSVIKKDNQTLSHSLKMADQNLEKLKLESERLEQHAQKSVNWLLWAMLI 250
Cdd:pfam09753 150 AVLKKHRNLQEKLAEEMLSLARNLKENSLAASNIIKKDTEILSKSEKAADQNLASLKRESERLEEHYKSKTNCWLWLMLF 229

                         250
                  ....*....|....*.
gi 281182635  251 VVCFVFISMILFIRIM 266
Cdd:pfam09753 230 VVCCVFIMMVLFIRVF 245
SNARE_USE1 cd15860
SNARE motif of USE1; USE1 (unconventional SNARE in the ER 1 homolog, also known as SNARE-like ...
 176-235 2.05e-19

SNARE motif of USE1; USE1 (unconventional SNARE in the ER 1 homolog, also known as SNARE-like tail-anchored protein 1 or SLT1) is involved in retrograde transport of CopI coatomer coated vesicles from the Golgi to the ER. It forms a complex with syntaxin18 (Ufe1p, Qa), Bnip1 (Sec20p, Qb) and Sec22b (R-SNARE). USE1 is a member of the Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein family. 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.


Pssm-ID: 277213  Cd Length: 60  Bit Score: 79.53  E-value: 2.05e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182635 176 HQGLQEKLAEEMLGLARSLKTNTLAAQSVIKKDNQTLSHSLKMADQNLEKLKLESERLEQ 235
Cdd:cd15860    1 HRNLQEELAEELLSLARQLKENALAFSNILKEDNKVLEATEKLADRNLDKLKRESGRLEE 60
 
Name Accession Description Interval E-value
Use1 pfam09753
Membrane fusion protein Use1; This entry is of a family of proteins all approximately 300 ...
 16-266 7.09e-106

Membrane fusion protein Use1; This entry is of a family of proteins all approximately 300 residues in length. The proteins have a single C-terminal trans-membrane domain and a SNARE [soluble NSF (N-ethylmaleimide-sensitive fusion protein) attachment protein receptor] domain of approximately 60 residues. The SNARE domains are essential for membrane fusion and are conserved from yeasts to humans. Use1 is one of the three protein subunits that make up the SNARE complex and it is specifically required for Golgi-endoplasmic reticulum retrograde transport.


Pssm-ID: 462882 [Multi-domain]  Cd Length: 245  Bit Score: 306.94  E-value: 7.09e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182635   16 RLELNLVRLLCRCESMAAEKREPDEWRLEKYVGALEDMLQALKVQASKPASEVISEYSRKVDFLKGMLQAEKLTSSSEKA 95
Cdd:pfam09753   1 KLEINFRRLLSRCERLAKEDRSDNQWRLEKYVKALEEMLEELQKERDKPSKDVLNEYSERVEFLKGLLEAEKLSSPEEKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182635   96 LANQFLAPG-----RVPTTAKERVPATKTVHLQSRARYTSEMRSELLGTESSgeleadmrkrvVKGPRPADEKQSASELD 170
Cdd:pfam09753  81 LANQFLAPGfaespRSPEESSERESASKELRQKTKAKYQSELRKELLGTGDS-----------SSSPRGRAELKLDEDLD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182635  171 LVLQRHQGLQEKLAEEMLGLARSLKTNTLAAQSVIKKDNQTLSHSLKMADQNLEKLKLESERLEQHAQKSVNWLLWAMLI 250
Cdd:pfam09753 150 AVLKKHRNLQEKLAEEMLSLARNLKENSLAASNIIKKDTEILSKSEKAADQNLASLKRESERLEEHYKSKTNCWLWLMLF 229

                         250
                  ....*....|....*.
gi 281182635  251 VVCFVFISMILFIRIM 266
Cdd:pfam09753 230 VVCCVFIMMVLFIRVF 245
SNARE_USE1 cd15860
SNARE motif of USE1; USE1 (unconventional SNARE in the ER 1 homolog, also known as SNARE-like ...
 176-235 2.05e-19

SNARE motif of USE1; USE1 (unconventional SNARE in the ER 1 homolog, also known as SNARE-like tail-anchored protein 1 or SLT1) is involved in retrograde transport of CopI coatomer coated vesicles from the Golgi to the ER. It forms a complex with syntaxin18 (Ufe1p, Qa), Bnip1 (Sec20p, Qb) and Sec22b (R-SNARE). USE1 is a member of the Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein family. 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.


Pssm-ID: 277213  Cd Length: 60  Bit Score: 79.53  E-value: 2.05e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182635 176 HQGLQEKLAEEMLGLARSLKTNTLAAQSVIKKDNQTLSHSLKMADQNLEKLKLESERLEQ 235
Cdd:cd15860    1 HRNLQEELAEELLSLARQLKENALAFSNILKEDNKVLEATEKLADRNLDKLKRESGRLEE 60
 
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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