ID F9X237_ZYMTI Unreviewed; 240 AA.
AC F9X237;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Dolichol-phosphate mannosyltransferase subunit 1 {ECO:0000256|RuleBase:RU365083};
DE EC=2.4.1.83 {ECO:0000256|RuleBase:RU365083};
GN Name=Mg68111 {ECO:0000313|EMBL:EGP89788.1};
GN ORFNames=MYCGRDRAFT_67965 {ECO:0000313|EMBL:EGP89788.1};
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP89788.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP89788.1, ECO:0000313|Proteomes:UP000008062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(2011).
CC -!- FUNCTION: Transfers mannose from GDP-mannose to dolichol monophosphate
CC to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl
CC donor in pathways leading to N-glycosylation, glycosyl
CC phosphatidylinositol membrane anchoring, and O-mannosylation of
CC proteins. {ECO:0000256|RuleBase:RU365083}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl phosphate + GDP-alpha-D-mannose = a dolichyl beta-
CC D-mannosyl phosphate + GDP; Xref=Rhea:RHEA:21184, Rhea:RHEA-
CC COMP:9517, Rhea:RHEA-COMP:9527, ChEBI:CHEBI:57527, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:58211;
CC Evidence={ECO:0000256|RuleBase:RU365083};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU365083}.
CC -!- SUBUNIT: Component of the dolichol-phosphate mannose (DPM) synthase
CC complex. {ECO:0000256|RuleBase:RU365083}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|RuleBase:RU365083}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC {ECO:0000256|ARBA:ARBA00006739, ECO:0000256|RuleBase:RU365083}.
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DR EMBL; CM001197; EGP89788.1; -; Genomic_DNA.
DR RefSeq; XP_003854812.1; XM_003854764.1.
DR AlphaFoldDB; F9X237; -.
DR STRING; 336722.F9X237; -.
DR EnsemblFungi; Mycgr3T67965; Mycgr3P67965; Mycgr3G67965.
DR GeneID; 13395997; -.
DR KEGG; ztr:MYCGRDRAFT_67965; -.
DR VEuPathDB; FungiDB:ZTRI_2.262; -.
DR eggNOG; KOG2978; Eukaryota.
DR HOGENOM; CLU_033536_13_3_1; -.
DR InParanoid; F9X237; -.
DR OMA; VNVINWP; -.
DR OrthoDB; 604at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008062; Chromosome 2.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0004582; F:dolichyl-phosphate beta-D-mannosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR CDD; cd06442; DPM1_like; 1.
DR InterPro; IPR039528; DPM1-like.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43398; DOLICHOL-PHOSPHATE MANNOSYLTRANSFERASE SUBUNIT 1; 1.
DR PANTHER; PTHR43398:SF1; DOLICHOL-PHOSPHATE MANNOSYLTRANSFERASE SUBUNIT 1; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU365083};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU365083};
KW Reference proteome {ECO:0000313|Proteomes:UP000008062};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365083}.
FT DOMAIN 8..177
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
SQ SEQUENCE 240 AA; 26843 MW; D75824EA00A79A3A CRC64;
MAVKNKYSVL LPTYNERRNL PIIVWLLNKT FTEHTLDYEI IIVDDGSPDG TQDIAKQLIK
AYGASRILLK PRAGKLGLGT AYVHGLQFAT GNFVIIMDAD FSHHPKFLPR MIATQKEGNY
DIVTGTRYAG DGGVYGWDLK RKMVSRGANL FADTVLRPGV SDLTGSFRLY KKEVLAQVME
KTESKGYSFQ MEMMVRAKAM GFKVAECPIS FVDRVYGESK LGGEEIVEYL KGVLGLWVKV
//
