ID A0A2W1EK61_9PLEO Unreviewed; 807 AA.
AC A0A2W1EK61;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000256|ARBA:ARBA00012839, ECO:0000256|RuleBase:RU367007};
DE EC=2.4.1.109 {ECO:0000256|ARBA:ARBA00012839, ECO:0000256|RuleBase:RU367007};
GN ORFNames=Ptr86124_005837 {ECO:0000313|EMBL:KAI1515836.1}, PtrM4_09507
GN {ECO:0000313|EMBL:PWO10626.1}, PtrM4_135080
GN {ECO:0000313|EMBL:KAF7566917.1};
OS Pyrenophora tritici-repentis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=45151 {ECO:0000313|EMBL:PWO10626.1};
RN [1] {ECO:0000313|EMBL:PWO10626.1, ECO:0000313|Proteomes:UP000245464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M4 {ECO:0000313|EMBL:PWO10626.1,
RC ECO:0000313|Proteomes:UP000245464};
RX PubMed=29685100; DOI=10.1186/s12864-018-4680-3;
RA Moolhuijzen P., See P.T., Hane J.K., Shi G., Liu Z., Oliver R.P.,
RA Moffat C.S.;
RT "Comparative genomics of the wheat fungal pathogen Pyrenophora tritici-
RT repentis reveals chromosomal variations and genome plasticity.";
RL BMC Genomics 19:279-279(2018).
RN [2] {ECO:0000313|EMBL:KAI1515836.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=86-124 {ECO:0000313|EMBL:KAI1515836.1};
RA Moolhuijzen P.M., Moffat C.S.;
RL Submitted (MAY-2021) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAI1515836.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=86-124 {ECO:0000313|EMBL:KAI1515836.1};
RA Moolhuijzen P., See P.T., Shi G., Powell H.R., Cockram J., Jorgensen L.N.,
RA Benslimane H., Strelkov S.E., Turner J., Liu Z., Moffat C.S.;
RT "A global pangenome for the wheat fungal pathogen Pyrenophora tritici-
RT repentis and prediction of effector protein structural homology.";
RL bioRxiv 0:0-0(2022).
CC -!- FUNCTION: Transfers mannose from Dol-P-mannose to Ser or Thr residues
CC on proteins. {ECO:0000256|RuleBase:RU367007}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-
CC O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+);
CC Xref=Rhea:RHEA:17377, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137321; EC=2.4.1.109;
CC Evidence={ECO:0000256|ARBA:ARBA00034032,
CC ECO:0000256|RuleBase:RU367007};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] =
CC 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a dolichyl phosphate +
CC H(+); Xref=Rhea:RHEA:53396, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137323; EC=2.4.1.109;
CC Evidence={ECO:0000256|ARBA:ARBA00033990,
CC ECO:0000256|RuleBase:RU367007};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU367007}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367007}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU367007}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000256|ARBA:ARBA00007222, ECO:0000256|RuleBase:RU367007}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWO10626.1}.
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DR EMBL; NQIK02000008; KAF7566917.1; -; Genomic_DNA.
DR EMBL; NRDI02000006; KAI1515836.1; -; Genomic_DNA.
DR EMBL; NQIK01000007; PWO10626.1; -; Genomic_DNA.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000245464; Unassembled WGS sequence.
DR Proteomes; UP000249757; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 2.80.10.50; -; 1.
DR InterPro; IPR027005; GlyclTrfase_39-like.
DR InterPro; IPR003342; Glyco_trans_39/83.
DR InterPro; IPR036300; MIR_dom_sf.
DR InterPro; IPR016093; MIR_motif.
DR InterPro; IPR032421; PMT_4TMC.
DR PANTHER; PTHR10050; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE; 1.
DR PANTHER; PTHR10050:SF51; PROTEIN O-MANNOSYL-TRANSFERASE 1; 1.
DR Pfam; PF02815; MIR; 1.
DR Pfam; PF02366; PMT; 1.
DR Pfam; PF16192; PMT_4TMC; 1.
DR SMART; SM00472; MIR; 3.
DR SUPFAM; SSF82109; MIR domain; 1.
DR PROSITE; PS50919; MIR; 3.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU367007};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU367007};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367007};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367007};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367007};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367007}.
FT TRANSMEM 59..78
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 107..125
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 196..218
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 238..266
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 287..306
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 605..628
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 649..667
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 679..697
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 752..779
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT DOMAIN 340..400
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 408..467
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 471..526
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 807 AA; 91939 MW; 0ED62D42378E8FE0 CRC64;
MSSPPGTLRQ RTGKDKKRPV SPNPDALSEK VANVVEKVKP AMDKVKPYKA AQQSGEWDYK
LAIAVMTVLA FITRFWGIRH PDQVVFDEVH FGKFASYYLQ RTYFFDVHPP FGKLLFAFAG
WLVGYKGDFL FESIGDSYIT NKVPYVAYRA MPASLGALTV PIVFMIMWES GYSLPACITA
AGLMLFDNAH IGQTRLILLD ASLIFFMALS VLSYIRFYKE RHASFGAKWW KWLLLTGISL
SCVISIKYVG VFTFFSIGVP VMIDLWDLMD VNRRQGALTL AEFGKHFAAR AVGLVIVPFF
LYLFWFQVHF TILTRSGPGD DFMTPEFQET LSDNVMSLQS VGINYYDSIT IRHKETKVYL
HSHPDRYPLR YDDGRVSSQG QQVTGYPHND TNNHWQVLPH KALPSEEGQR VKVGDVIRLR
HLITDTILLT HDVASPHYPT NQEFTTVTKD EASGARYNDT LFEIKVDKGK GDFTTMSTHF
KLVHVATKVA MWTHTKPLPD WAYKQAEING NKAVQASSNI WYVDDIPSLP VEDVRNKKEP
KKVKHLGFLR KWVELQRAMF YHNNALTSSH PYASQPISWP FLLRGVSFWT HNDTREQIYF
LGNPLGWWLA SSLLAVFAGI IGADQLALRR GMDALDDRKS QFSYQTKPGF FNLFMALAFE
NKVLTFFKTG TRSRLYNSTG FFFLTWAAHY IPFYIMGRQL FLHHYLPAHL ASCLVTGALV
EFVFCIEPQD PETPGAVKGH RRTRSRPVRE RVASSSLMGS WIACGVILAA VLWCFLFFAP
LTYGSPGLSI SQVQMRKWLG YDLHFAK
//
