ID A0A099NYF0_PICKU Unreviewed; 784 AA.
AC A0A099NYF0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=BOH78_0201 {ECO:0000313|EMBL:ONH77869.1}, CAS74_003078
GN {ECO:0000313|EMBL:OUT22090.1}, JL09_g3785
GN {ECO:0000313|EMBL:KGK37054.1};
OS Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=4909 {ECO:0000313|EMBL:KGK37054.1, ECO:0000313|Proteomes:UP000029867};
RN [1] {ECO:0000313|Proteomes:UP000029867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SD108 {ECO:0000313|Proteomes:UP000029867};
RX PubMed=25159171; DOI=10.1186/s12934-014-0121-4;
RA Xiao H., Shao Z., Jiang Y., Dole S., Zhao H.;
RT "Exploiting Issatchenkia orientalis SD108 for succinic acid production.";
RL Microb. Cell Fact. 13:121-121(2014).
RN [2] {ECO:0000313|EMBL:KGK37054.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SD108 {ECO:0000313|EMBL:KGK37054.1};
RA Xiao H., Shao Z., Jiang Y., Dole S., Zhao H.;
RT "Exploiting Issatchenkia orientalis SD108 for Succinic Acid Production.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000189274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129 {ECO:0000313|Proteomes:UP000189274};
RX PubMed=28385833; DOI=10.1128/genomeA.00064-17;
RA van Rijswijck I.M.H., Derks M.F.L., Abee T., de Ridder D., Smid E.J.;
RT "Genome sequences of Cyberlindnera fabianii 65, Pichia kudriavzevii 129,
RT and Saccharomyces cerevisiae 131 isolated from fermented masau fruits in
RT Zimbabwe.";
RL Genome Announc. 5:E00064-E00064(2017).
RN [4] {ECO:0000313|EMBL:ONH77869.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129 {ECO:0000313|EMBL:ONH77869.1};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:OUT22090.1, ECO:0000313|Proteomes:UP000195871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ckrusei653 {ECO:0000313|EMBL:OUT22090.1,
RC ECO:0000313|Proteomes:UP000195871};
RA Cuomo C., Forche A., Young S., Abouelleil A., Cao P., Chapman S.,
RA Cusick C., Shea T., Nusbaum C., Birren B.;
RT "The Genome Sequence of Candida krusei Ckrusei653.";
RL Submitted (MAY-2017) 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}.
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:KGK37054.1}.
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DR EMBL; JQFK01000045; KGK37054.1; -; Genomic_DNA.
DR EMBL; MQVM01000001; ONH77869.1; -; Genomic_DNA.
DR EMBL; NHMM01000004; OUT22090.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099NYF0; -.
DR VEuPathDB; FungiDB:C5L36_0E01790; -.
DR eggNOG; KOG3359; Eukaryota.
DR HOGENOM; CLU_008438_2_1_1; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000029867; Unassembled WGS sequence.
DR Proteomes; UP000189274; Unassembled WGS sequence.
DR Proteomes; UP000195871; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU367007};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367007};
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 57..74
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 142..160
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 167..185
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 247..269
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 281..302
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 593..618
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 630..651
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 663..680
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 687..705
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT DOMAIN 330..384
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 393..452
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 462..518
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
SQ SEQUENCE 784 AA; 89085 MW; 45840297973FF852 CRC64;
MAPKKSGKGT KLQSVGEVEP QTTELILETG ELRRFPKSEL SETVAMNRIV SSTKERVLVA
ILVAFALLIR VSNLNNPNSV VFDEVHFGGF AKKYIKGDFF MDVHPPLAKL LFAAVGALGG
FKGDFSFEKI GDVFPPNVPY VLMRQLSAFM GVGTVLFMYF TLRATGCNPL VSFFTAALLI
IENGLVTISR YILLDSPLIF FIAGTAYFYT RSELEKPLSF NWFKYLAICG SFLGFALSSK
WVGLFTFAWL GLANVLRLWF VIGDLTVPVK SIVKNTLARG VILVGIPTII YLISFYIHFI
VLDKEGEGAA FMSSAFRTDF KDTTVPRVTT ADVGVSSIIT LKHLNTHGGY LHSHDHLYEG
GSNQQQVTLY PHLDENNKWA IELYNETSEP FEFIPITDGT KIRLNHIVTN RRLHSHDIRP
AVSEIEWQNE ASCYGFEGFE GDPNDDFIVE IVKDLSVPGE AQKRLRAIDT VFRLRHAMTG
CYLWSHETKL PKWGFEQQEV TCATQGIKPL SYWYIEDNVN IYLPPDAEKV GYRPLSFFQK
FIELHKKMWH VNNGLTATHY YESRPLDWLL LNRGISYWSA APHHIYLLGN PVVWWPASFL
FLGFATYLLV LIFQYQLGYE IKVSDTTFNF TYNVFSFLLG WGLHLAPFFL MDRQLFLHHY
FPALYFAILA LGHCFQLLYV SLKNKKVLVY VLFGLMFSAS LYSYFARFPI TNGSDWTVEK
CEQSKWLKSW DYDCSNFPSS KADTNAPVKA GQGNIDFNSA MKPEEVEPIV EKVVANETPV
KDEL
//
