ID A0A0D1DVD8_USTMA Unreviewed; 787 AA.
AC A0A0D1DVD8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, 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=UMAG_10749 {ECO:0000313|EMBL:KIS66480.1};
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS66480.1, ECO:0000313|Proteomes:UP000000561};
RN [1] {ECO:0000313|EMBL:KIS66480.1, ECO:0000313|Proteomes:UP000000561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2] {ECO:0000313|Proteomes:UP000000561}
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) 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; CM003157; KIS66480.1; -; Genomic_DNA.
DR RefSeq; XP_011391930.1; XM_011393628.1.
DR AlphaFoldDB; A0A0D1DVD8; -.
DR STRING; 237631.A0A0D1DVD8; -.
DR EnsemblFungi; KIS66480; KIS66480; UMAG_10749.
DR GeneID; 23566735; -.
DR KEGG; uma:UMAG_10749; -.
DR VEuPathDB; FungiDB:UMAG_10749; -.
DR eggNOG; KOG3359; Eukaryota.
DR InParanoid; A0A0D1DVD8; -.
DR OrthoDB; 5489060at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000561; Chromosome 18.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0035269; P:protein O-linked mannosylation; IBA:GO_Central.
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; 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:UP000000561};
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 85..103
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 168..189
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 201..231
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 251..284
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 305..324
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 632..651
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 672..694
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 700..720
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 741..761
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT DOMAIN 358..412
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 429..485
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 496..554
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 787 AA; 90052 MW; 3725AAA8D5D337EF CRC64;
MSSPAANSRR FAAGFDPYSP ATTVDSDHAD LSSDSAALKA KEAGFQPPSS NTPKVNKYAH
LIPVHQQRKP PNFEIVLWTL RQEEVIGLIY TLFSLITRLW GIGNSNVVVW DEAHFGKFGS
HYLQQEFYFD VHPPLGKMLV GLAGLISGYR GQFEFKSGET YPADVNYIGM RVILAMFGVA
MVPLAWFTSG GLNWNWRARH LLTLMVLLDN GWLVISRFIL LDSMLLCFTF TTVHGLVKFL
QYKSAPFTKA WWFWLAFTGA SIGCVSSVKW VGLFVTALVG VFTVEDLWEK FGDLRMPVRA
YVRHWCARIL CLIFLPLTIY MLSFKAHFLI LSRSGPGDAQ MSSLFQSHLR GNDFALSPPE
AAFGSKITLK NMGYGGGLLH SHVQTYPVGS QQQQVTCYHY RDNNNEFIIT PPWNERALPA
NYSSSTEPVR MLKNNDVIRL VHDQTKRNIH SHHVAAPVTK ENLEVSGYGD DQTGDDNDHW
VVEVVDDMVH GKVARDAPVR SLTSRLRLRH KNLGCYMRAA NAVLPQWGWK QVEVSCDKEN
NPKDQHTWWN IENHWNERLA PGDSQLYKSP FLRDFIHLNV AMMTSNNALI PDADKEDILA
SKPFDWPWLW NGLRMNSWDD NSIKFYLLGN PVIWWASSSS LLAFGATWLW YMMRRQRRIH
DLSPADWAHF LYVAKLAAFG WLLHYLPFLV MARVCYLHHY LPILYFAVLM LVHLIDHFVW
RPSTAVYAFG ASRRKQPLSE ALKNAVFVVS VVAITAAFWW FRGNSYGFKG DIKSHKGLKW
RKSWNIY
//
