ID A0A1B7MY66_9AGAM Unreviewed; 939 AA.
AC A0A1B7MY66;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 28-JUN-2023, 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=K503DRAFT_866782 {ECO:0000313|EMBL:OAX37558.1};
OS Rhizopogon vinicolor AM-OR11-026.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX NCBI_TaxID=1314800 {ECO:0000313|EMBL:OAX37558.1, ECO:0000313|Proteomes:UP000092154};
RN [1] {ECO:0000313|EMBL:OAX37558.1, ECO:0000313|Proteomes:UP000092154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM-OR11-026 {ECO:0000313|EMBL:OAX37558.1,
RC ECO:0000313|Proteomes:UP000092154};
RG DOE Joint Genome Institute;
RA Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA Barry K., Grigoriev I.V., Spatafora J.W.;
RT "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT divergence of the mating type B locus.";
RL Submitted (JUN-2016) 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}.
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DR EMBL; KV448344; OAX37558.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7MY66; -.
DR STRING; 1314800.A0A1B7MY66; -.
DR InParanoid; A0A1B7MY66; -.
DR OrthoDB; 5489060at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000092154; 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:SF50; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE 1-RELATED; 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:UP000092154};
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 109..131
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 201..222
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 288..307
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 609..632
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 644..665
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 677..695
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 707..727
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT DOMAIN 340..394
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 409..468
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 478..534
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..923
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 939 AA; 105616 MW; A11EA91C27A0EB65 CRC64;
MATKRVGRPA TPPPGLPHVA PSSHKYPPIR HDQLSADERR EAASKGYGPG RRSHSPGGLS
ITPGEWKLLA VVLLVAAGVR MFRISKPNSV VFDEVHFGKF ASRYIKTRYF VDVHPPLAKL
LITAAAFVFG FDGDFDFKDI GKVFENVPYV AMRMVPATFG VATVPLAYLT LRALDCRATT
ALFASIFLTF ENGLVTQSRH ILLDSPLVFF TALTTFLFVG FSNEDKKEPF TEQWWTWLVL
TGLSLGAVVS CKWVGLFTIA TVGACTVLQL WLLLGDLHVT PRTWARHFFA RAVCLILIPI
LFYMIMFQLH FAILGSSGEG DAFMSSEFRQ TLGHGMEDTY ADVALGSDIT IRHLNTQGGY
LHSHAHNYPG GSGQQQITLY PHRDENNIWR VLNATVDGYE QYDYEHKPIV YIEDHSRIKL
RHIVTDKALH SHEVRPPVSD VDFQNEVSAY GMTGFVGDIN DDWIVEIEKG DGSDKQSSKR
LRTLRTHFKL RHLHSGCYLF SHKVKLPEWG FEQQEVTCNK NAVKANSLWY VETAAKHPQL
PADAPRVNYK IPGFLSKFWE LQRVMWTTNA GLTDRHAYDS RPSTWPGLRR GINFWVKDHR
QIYLIGNPFV WWSSTASVII YMLVRGFLIL CAKRGYRDFD NTKVVKYDSL CGFLFVGYCL
HYFPFFLMGR QLFLHHYFPA LYFAVLLNGA VFDLVTSTLR PKIRLQIAAV LMIIAIMTFS
KFSPLAYGDP WTKKKCESAR WVKTWDIACN EFLDEYSQYS GVTVPTLNRS TPMATIGGEP
GGRAPIVVED KLGQDEVAPP QDDHTTAAPV GAAEPGRDVF AKDEQKEIKS QIIAQDVPVD
IDEKEISVVK FEPTNEAAQE PSSTREEDKV YDGDVGSGTR TGEPEDQGHP GAVVENLEEV
VEVGEDNDKP RVPHGPLDHE EAIADQVAYE LYPDARDVE
//
