ID A0A0D7AYU1_9AGAR Unreviewed; 237 AA.
AC A0A0D7AYU1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Dolichyldiphosphatase {ECO:0000256|RuleBase:RU367078};
DE EC=3.6.1.43 {ECO:0000256|RuleBase:RU367078};
GN ORFNames=CYLTODRAFT_426352 {ECO:0000313|EMBL:KIY63145.1};
OS Cylindrobasidium torrendii FP15055 ss-10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae;
OC Cylindrobasidium.
OX NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY63145.1, ECO:0000313|Proteomes:UP000054007};
RN [1] {ECO:0000313|EMBL:KIY63145.1, ECO:0000313|Proteomes:UP000054007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY63145.1,
RC ECO:0000313|Proteomes:UP000054007};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
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; KN880718; KIY63145.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7AYU1; -.
DR STRING; 1314674.A0A0D7AYU1; -.
DR OrthoDB; 989449at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000054007; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047874; F:dolichyldiphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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:UP000054007};
KW Transmembrane {ECO:0000256|RuleBase:RU367078};
KW Transmembrane helix {ECO:0000256|RuleBase:RU367078}.
FT TRANSMEM 26..45
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367078"
FT TRANSMEM 52..71
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367078"
FT TRANSMEM 125..144
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367078"
FT TRANSMEM 156..174
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367078"
FT DOMAIN 54..172
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 237 AA; 27044 MW; F80EAE35EE81C641 CRC64;
MGYTAVSNGV LDLTHVVYDD SSRMSLFLAL ITLSPILLMA SYAALVVQTR EYLFIVMWAG
QFAGEGLNWV IKRMVKQSRP IESLGTGYGF PSSHSQYMGY FASFLICHLY LRHEFVPTGI
RLLDLTWRAT VYLGLLAWTG LVAYSRYDLG YHNMQQILWG LGIGIVLGVA LYIVSQHLPR
RYPGSLFGRT KRLVIASPVA TFLQIRDGWD LWKDGGRGDE WSRWRKEWAA RQHSKEQ
//
