ID A0A319CYS7_9EURO Unreviewed; 942 AA.
AC A0A319CYS7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 28-JUN-2023, entry version 18.
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=BO82DRAFT_355233 {ECO:0000313|EMBL:PYH80758.1};
OS Aspergillus uvarum CBS 121591.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH80758.1, ECO:0000313|Proteomes:UP000248340};
RN [1] {ECO:0000313|EMBL:PYH80758.1, ECO:0000313|Proteomes:UP000248340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH80758.1,
RC ECO:0000313|Proteomes:UP000248340};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-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; KZ821707; PYH80758.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319CYS7; -.
DR STRING; 1448315.A0A319CYS7; -.
DR VEuPathDB; FungiDB:BO82DRAFT_355233; -.
DR OrthoDB; 5489060at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000248340; 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:UP000248340};
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 145..166
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 173..190
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 202..220
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 232..251
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 257..276
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 288..311
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 614..635
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 656..673
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 718..739
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT DOMAIN 340..394
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 415..474
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 484..540
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 942 AA; 106127 MW; 6BB91E893E6112EA CRC64;
MASQSKNTLE VNPPPKSQLR SSSRSPGPKS RKNVTVRAPS YASEGVTDNN IFKLPASDYK
TLVVVTIVAA VVRLFRIYQP SSVVFDEVHF GGFASKYIKG RFFMDVHPPL AKLLLTLAGW
LAGFDGEFDF KDIGKDYLEP GVPYVAMRML PAILGVLTVP LMFLTLKASG CRTISAILGA
GVVIFENGLI TQSRLILLDS PLVFFTALTA LSFTCFTNQH EMGPSHAFRG PWWFWLVASG
LALGATLSVK WVGLFTVAWV GSLTVLQLWV LLGDTVNVTP RLWFKHFFAR FFCLIVIPLT
FYCGMFAIHF LCLVNPGDGD GFMSSEFQAT LNSKSMQDVP ADVVFGSRVS LRHLNTQGGY
LHSHNHMYPT GSKQQQITLY PHKDENNVFI LENQTQPLGP YGTLEGPLAW DNITAEYIED
GATIKLNHFV TRRRVHSHDE RPPVTDVDWQ FEVSAYGYDG FPGDANDLFR VEIVKSMSDG
EEAKKRLRTI QTKFRLVHVM TNCVLFSHKV KLPEWGFDQQ EVTCARGATL PNSVWYIESN
NHPMLAEDAE KVNYKNPGFF GKFFELQKVM WVTNAGLTES HAWDSRPPSW PTLLRGINFW
GKDHRQVYLL GNPFIWWSST VAIAVYFLFK GVSVLRWQRS CGDYRNVNFK RFDYEIGTTV
LGWAFHYFPF YLMARQLFLH HYFPALYFAI MALCQEFDFI ANRVRSLGLP SKPVIGKILA
GLFLTLSIFT FVIYSPLVYG NPWTQEACRQ VKLLDTWDFD CNTFYTDLSH YVTQYVDSNA
NVAIPPTETS VPQAPPAVAP PQDAPQQHAQ EVLQEEPQEP AITPRARHST KARVEYRDQD
GNILDEELVA SLRKEGKVSF ETRHETSTRL DKGHLVDMVD GEIEFAPPHP DVEGQNPETI
QRYQPQDVEE GPASVVGHGS SEERKGSADP KPASEVNEAT KS
//
