ID A0A409XME3_PSICY Unreviewed; 773 AA.
AC A0A409XME3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JUN-2023, entry version 14.
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=CVT25_000755 {ECO:0000313|EMBL:PPQ91880.1};
OS Psilocybe cyanescens.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Psilocybe.
OX NCBI_TaxID=93625 {ECO:0000313|EMBL:PPQ91880.1, ECO:0000313|Proteomes:UP000283269};
RN [1] {ECO:0000313|EMBL:PPQ91880.1, ECO:0000313|Proteomes:UP000283269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2631 {ECO:0000313|EMBL:PPQ91880.1,
RC ECO:0000313|Proteomes:UP000283269};
RX PubMed=30283667; DOI=10.1002/evl3.42;
RA Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA Matheny P.B., Slot J.C.;
RT "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT diversity.";
RL Evol. Lett. 2:88-101(2018).
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:PPQ91880.1}.
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DR EMBL; NHYD01001227; PPQ91880.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A409XME3; -.
DR STRING; 93625.A0A409XME3; -.
DR InParanoid; A0A409XME3; -.
DR OrthoDB; 5489060at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000283269; 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 Reference proteome {ECO:0000313|Proteomes:UP000283269};
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 100..120
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 140..161
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 226..243
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 249..266
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 286..308
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 603..625
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 646..663
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 675..698
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 719..742
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT DOMAIN 335..395
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 404..461
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 466..522
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 773 AA; 87972 MW; 9ACD0A0DBEE9CEF4 CRC64;
MAGKGKSTLR QRQTAHAGPS DLEHEHTQDD EHADVIYQNP KNRNQLELLL ETHQGSAIVV
AVLTALAFAL RFYKINHPDQ VVFDEVHFGK FASHYIMRQY YFDVHPPFAK LLFGLAGWFV
GFDGQFTFDN IGDSYTTNHV PFVGMRALPA ILGSLTVPVV YAIMKTSGYP TIVAAFSAAI
ILFDNAHIAQ SRLILLDATL IFFMSLTIYA YIRFRKLRYR EFTTEWWTWL ILTGVFMACT
WGSKVNGILT VFAIGLAVLV DLWDILDYKK EGHTMEYFWR HFSARATGLI VVPFVIYLSF
FYIHFAVLTQ SGPGDNFMSP AFQETLAGNE MLLNSKEIHY YDTVVMRHKE TRVYLHSHVE
RYPLTYADGR ISSQGQQVTG YGHNDTNNHW KIIPTKALPE TGRGRIVRNE DVVQLLHVNT
QTHLLTHDVA SPLMPTNQEF TTWSKDDHSR HNDTLFQLVL ASGNPGEAWK TKSGHFRLIH
VPTKVSMWTH AEQLPDWAFK QQEVNGNKNP TEKTATWYVD EIITEALEDD REEEKVPVKV
PKSMNFFRKF GELQLLMMQH NAGLTASHPY ASSPINWPFL LSGISFWTDN DAKKQIYLIG
NIIGWWTCTV ALSIYVGILG ADLLARRRGM DPIPDSVRNR LWNNTGFFLL VWAVHYVPFF
LMNRQLFIHH YLPSHLASAL IAGAVLNFVL SETINYPISV FGNKTRARPS QYADIGLKGP
IIFVGFSLIM FLMFVFIAPL TYGTPGLTGE QVNSKRLLST WTLHFAAKVT GET
//
