ID A0A1R1XV55_9FUNG Unreviewed; 835 AA.
AC A0A1R1XV55;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=AYI70_g5326 {ECO:0000313|EMBL:OMJ18496.1};
OS Smittium culicis.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133412 {ECO:0000313|EMBL:OMJ18496.1, ECO:0000313|Proteomes:UP000187283};
RN [1] {ECO:0000313|EMBL:OMJ18496.1, ECO:0000313|Proteomes:UP000187283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSMNP {ECO:0000313|EMBL:OMJ18496.1,
RC ECO:0000313|Proteomes:UP000187283};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:OMJ18496.1}.
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DR EMBL; LSSN01001733; OMJ18496.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R1XV55; -.
DR STRING; 133412.A0A1R1XV55; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000187283; 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:SF46; PROTEIN O-MANNOSYL-TRANSFERASE 2; 1.
DR Pfam; PF02815; MIR; 1.
DR Pfam; PF02366; PMT; 1.
DR Pfam; PF16192; PMT_4TMC; 2.
DR SMART; SM00472; MIR; 3.
DR SUPFAM; SSF82109; MIR domain; 1.
DR PROSITE; PS50919; MIR; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000187283};
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 92..110
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 180..199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 211..229
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 235..250
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 262..295
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 315..341
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 638..661
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 725..745
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 752..768
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 788..810
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT DOMAIN 434..492
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
SQ SEQUENCE 835 AA; 95893 MW; 07410950E2E46AA8 CRC64;
MFEDNLSAKR RNKSFSPAQI ILPQNQSIEL ESIDINSDKK KKYLPNNSSF SSLSDSFPKG
SSFSVDNLIK RSSHLFSSSV YSSKKFIHDN KIDVIIVVLL TIAGLFTRIY KIGISNKVTW
DEAHFGKFGA FYINRTFYHD VHPPLAKMLV ALAEVIAGHN GTFDFPSGNE YPSYVNYVSM
RIQLALYGIL LIPLAYVTCK SLHMSRNTST LAALFILFDN ALCVMSKFIL LDQPLLFFTA
LSIMCFAKFG QYRRQAFTNK WFLWLALTGV SLGFVLSSKW IGLFCVATVG LSTVMHLWEM
YGQLKMPLEY YLNHWAARIV CLIFIPLVIY LLTFVVHFGI LNRAGSGDER LSTKFQAGQI
GHRLNTQPID VADNSTARLR SYYSRSGLLH SHNHTYPTNS IQYQATTFQG KDFNNEWLLY
LDAESQLKKT DPTSKIFEDG DFMRLVHKNS SRVLRTISQE APITPSDLMV STYDNSKETD
LDKSDLWKIE IFKQTGPLKD NKIHPIITKF VLRNVKYDCL LRTKPRHLPS WGWNQREVSC
TKIKKSDYSD EVFWNVEEHT NTALKNGNMG KYVSSFLLFD IVQLNIEMAN SNNALVPDQD
KYNQLESTPE MWPFLYRPMR MVGWGDTEIK YYEIGNPILW WLSSFAILLF PFQILVCSIL
YSRFLSAKKH GKTTIPLPQP NMSNIIDSPM TGLPAGYSTI SNSSNSFSIE IGGSALYKLV
NDKNYWIGAY LLWSGWAFHY LPFFLMGRVT YLHHYLPALY FALLFLAYQI DYLTKFSFRS
NKVALNRIVV VLALASMIVF IYFFPFTVGY NKPAKDLKGR VWRSSWNVYE DPFEI
//
