ID A0A063BPL9_USTVR Unreviewed; 915 AA.
AC A0A063BPL9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 03-MAY-2023, entry version 38.
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=UV8b_05916 {ECO:0000313|EMBL:QUC21673.1}, UVI_02015040
GN {ECO:0000313|EMBL:GAO18804.1};
OS Ustilaginoidea virens (Rice false smut fungus) (Villosiclava virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Ustilaginoidea.
OX NCBI_TaxID=1159556 {ECO:0000313|EMBL:GAO18804.1, ECO:0000313|Proteomes:UP000054053};
RN [1] {ECO:0000313|EMBL:GAO18804.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IPU010 {ECO:0000313|EMBL:GAO18804.1};
RA Kumagai T., Ishii T., Terai G., Umemura M., Machida M., Asai K.;
RT "Genome Sequence of Ustilaginoidea virens IPU010, a Rice Pathogenic Fungus
RT Causing False Smut.";
RL Genome Announc. 4:e00306-16(2016).
RN [2] {ECO:0000313|Proteomes:UP000054053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IPU010 {ECO:0000313|Proteomes:UP000054053};
RX PubMed=27151791; DOI=10.1128/genomea.00306-16;
RA Kumagai T., Ishii T., Terai G., Umemura M., Machida M., Asai K.;
RT "Genome sequence of Ustilaginoidea virens IPU010, a rice pathogenic fungus
RT causing false smut.";
RL Genome Announc. 4:0-0(2016).
RN [3] {ECO:0000313|EMBL:QUC21673.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UV-8b {ECO:0000313|EMBL:QUC21673.1};
RA Zhang K., Zhao Z., Zhang Z., Li Y., Hsiang T., Sun W.;
RT "A mixture of massive structural variations and highly conserved coding
RT sequences in Ustilaginoidea virens genome.";
RL Submitted (MAR-2020) 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; BBTG02000006; GAO18804.1; -; Genomic_DNA.
DR EMBL; CP072756; QUC21673.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A063BPL9; -.
DR STRING; 1159556.A0A063BPL9; -.
DR HOGENOM; CLU_008438_2_2_1; -.
DR OrthoDB; 5489060at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000027002; Chromosome 4.
DR Proteomes; UP000054053; 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:UP000027002};
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 130..151
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 158..175
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 213..230
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 236..257
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 277..296
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 602..623
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 673..694
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 706..727
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT DOMAIN 325..379
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 403..462
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 472..528
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 915 AA; 102579 MW; 08C8C598C10478AC CRC64;
MARSSYARNK SPRPQGNNGK AKITSYKSDG VEDHDIFQLP SSDYVVGLGL TLLGALVRIF
RIYQPSSVVF DEVHFGGFAS KYIKGKFFMD VHPPLAKMLI ALTGWLAGFD GNFDFKDIGK
DYLEPKVPYV AMRLFPALCG ILLVPFMFFT LKAAGCRTVT AAMGASLIVF ENGLLTQARL
ILLDSPLVAA TAFTALAFSC FTNQHEQGPA KAFRPVWWFW LAMTGLGLGI TVSIKWVGLF
TIAWVGALTL LQLWVLLGDN NNVTMRLWTK HFMARAFCLI VIPLTFYMAM FAIHFVCLVN
PGDGDGFMTS EFQATLNSKG MQDVAADVVF GSRVSIRHVN TQGGYLHSHS LMYPTGSKQQ
QITLYPHKDE NNIWFLENQT QPLDSQGNPI NGTMAWDNLP DGPIFIENGA VLRLFHYPTH
RRLHSHDVRP PVTEADWQNE VSAYGYEGFD GDANDFFRVE IVTSKSKGSV AKKRVRTIET
KFRLVHVMTG CVLFSHKVKL PDWASEQQEV TCARGGSLPN SLWYVEHNEH PQFGPGTEKV
NYRNPGFFGK FWELQKVMWT TNAGLTDSHA WDSRPQSWPL LRRGINFWSK NHTQIYLIGN
PVIWWSSTLS IAVWFLFKAV AVLRWQRSYD DYASTTFKRF DYELGTSVLG WALHYFPFFL
MGRQLFLHHY FPALYFAIVA LCQLFDFLTV RIPGVGAKDN AVVNKAATML FLVLSIAAFS
LYSPLAYGNS WTKNDCKRVK LFDKWDWDCN TFFDRYDQYT PGYEADSNVP SSSSPAPPVL
ESQLPGGAGV SADAGPAGAR VVNQEQRVEY RDQNGNLLNE EQVKALQGKV KFETRYETRT
RVVDEGGNEV AAGHAAVAPP HPDVQGVNPE TVQDNQQQAE ADSNVAASRD GEKEAEQMKA
KPASEGQEAT HRDEL
//
