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Database: UniProt
Entry: R1EFR1_BOTPV
LinkDB: R1EFR1_BOTPV
Original site: R1EFR1_BOTPV 
ID   R1EFR1_BOTPV            Unreviewed;       229 AA.
AC   R1EFR1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Dolichyldiphosphatase {ECO:0000256|RuleBase:RU367078};
DE            EC=3.6.1.43 {ECO:0000256|RuleBase:RU367078};
GN   ORFNames=UCRNP2_6935 {ECO:0000313|EMBL:EOD46352.1};
OS   Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS   (Neofusicoccum parvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Neofusicoccum.
OX   NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD46352.1, ECO:0000313|Proteomes:UP000013521};
RN   [1] {ECO:0000313|Proteomes:UP000013521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX   PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA   Blanco-Ulate B., Rolshausen P., Cantu D.;
RT   "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT   vascular pathogen associated with grapevine cankers.";
RL   Genome Announc. 1:E0033913-E0033913(2013).
CC   -!- FUNCTION: Required for efficient N-glycosylation. Necessary for
CC       maintaining optimal levels of dolichol-linked oligosaccharides.
CC       Hydrolyzes dolichyl pyrophosphate at a very high rate and dolichyl
CC       monophosphate at a much lower rate. Does not act on phosphatidate.
CC       {ECO:0000256|RuleBase:RU367078}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dolichyl diphosphate + H2O = a dolichyl phosphate + H(+) +
CC         phosphate; Xref=Rhea:RHEA:14385, Rhea:RHEA-COMP:9517, Rhea:RHEA-
CC         COMP:9529, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57497, ChEBI:CHEBI:57683; EC=3.6.1.43;
CC         Evidence={ECO:0000256|RuleBase:RU367078};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|RuleBase:RU367078}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU367078}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU367078}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the dolichyldiphosphatase family.
CC       {ECO:0000256|RuleBase:RU367078}.
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DR   EMBL; KB916466; EOD46352.1; -; Genomic_DNA.
DR   RefSeq; XP_007586192.1; XM_007586130.1.
DR   AlphaFoldDB; R1EFR1; -.
DR   STRING; 1287680.R1EFR1; -.
DR   KEGG; npa:UCRNP2_6935; -.
DR   eggNOG; KOG3146; Eukaryota.
DR   HOGENOM; CLU_074922_0_0_1; -.
DR   OMA; VYATLIW; -.
DR   OrthoDB; 989449at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000013521; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047874; F:dolichyldiphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProt.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IEA:UniProtKB-UniRule.
DR   CDD; cd03382; PAP2_dolichyldiphosphatase; 1.
DR   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR   InterPro; IPR039667; Dolichyldiphosphatase_PAP2.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   PANTHER; PTHR11247:SF1; DOLICHYLDIPHOSPHATASE 1; 1.
DR   PANTHER; PTHR11247; PALMITOYL-PROTEIN THIOESTERASE/DOLICHYLDIPHOSPHATASE 1; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|RuleBase:RU367078};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU367078};
KW   Membrane {ECO:0000256|RuleBase:RU367078};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013521};
KW   Transmembrane {ECO:0000256|RuleBase:RU367078};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU367078}.
FT   TRANSMEM        22..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367078"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367078"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367078"
FT   TRANSMEM        156..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367078"
FT   DOMAIN          52..171
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
SQ   SEQUENCE   229 AA;  25781 MW;  9D3895EB42CE62D7 CRC64;
     MDEPTLASLS LTHVHYNPND RFSYLCAWLA LVPQGLCVVY ATLIWSSREA EVGLMFAGQM
     ACEALNWGLK RLIKEERPRQ MYGKGYGMPS SHAQFVSFFS LYLALFLLFR HVPHPTQTHT
     PTTYAQRLAL SLLALASAAA VAFSRIYLSY HTAKQVLVGC AAGAAFAVVW FGLTSWVRRS
     GLLGWVLETG LARLFRIRDL VVEEDLVDAG WARWEARRTK REVGGKKRR
//
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