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Database: UniProt
Entry: A0A367XUP5_9ASCO
LinkDB: A0A367XUP5_9ASCO
Original site: A0A367XUP5_9ASCO 
ID   A0A367XUP5_9ASCO        Unreviewed;       764 AA.
AC   A0A367XUP5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   03-MAY-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   Name=PMT2_1 {ECO:0000313|EMBL:RCK57338.1};
GN   ORFNames=Cantr_06118 {ECO:0000313|EMBL:RCK57338.1};
OS   Candida viswanathii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5486 {ECO:0000313|EMBL:RCK57338.1, ECO:0000313|Proteomes:UP000253472};
RN   [1] {ECO:0000313|EMBL:RCK57338.1, ECO:0000313|Proteomes:UP000253472}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20962 {ECO:0000313|EMBL:RCK57338.1,
RC   ECO:0000313|Proteomes:UP000253472};
RA   Ahn J.;
RT   "Whole genome sequencing of Candida tropicalis (genome annotated by CSBL at
RT   Korea University).";
RL   Submitted (JUN-2018) 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:RCK57338.1}.
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DR   EMBL; QLNQ01000028; RCK57338.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367XUP5; -.
DR   STRING; 5486.A0A367XUP5; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000253472; 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: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; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000253472};
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        61..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        147..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        171..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        195..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        233..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        284..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        609..630
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        650..670
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        676..693
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        713..733
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   DOMAIN          407..463
FT                   /note="MIR"
FT                   /evidence="ECO:0000259|PROSITE:PS50919"
FT   DOMAIN          469..529
FT                   /note="MIR"
FT                   /evidence="ECO:0000259|PROSITE:PS50919"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   764 AA;  87826 MW;  117B380520BD1F69 CRC64;
     MSTSVEPNET EALKRKVDEF SSSTTASIEE KYDDETTDAS KRTQYDETKE TIESLKKAES
     ILAPLLFTIL SFFVRFYRIS VNNNVVWDEA HFGKFGSYYL RHEFYHDVHP PLGKMLVGLS
     GYLAGYNGSW DFPSGEKYPD YIDYTKMRLF NATFSALCVP LAYYTMKEIG LSVATTWLFT
     LMVTVESSYV TLGKFILLDS MLLFFTVATV FCFSRFNNFN TKEHEFSRKW WKWILLTGVS
     IGCTCSVKMV GLFVTTLVGI YTVVDLWNKL AHKSISWGRY FNHWFARILA LIVVPIVIFM
     LSFKVHFDLL YKSGTGDANM SSLFQANLIG SGVGGGPREV SMFHSIVTLK NQGLSGGLLH
     SHVQTFPEGS KQQQVTTYGH KDSNNNWIFQ RARGQPPYDP ANNNTAIEYI IDGMHVRLMH
     PQSGRNLHTH DIQAPVTKTE YEVACYGNLT IGDAKDNWIV EIVDQAGDED KMRLHPLTTS
     FRLKNEVMGC YLGASGSTLP QWGFRQGEVV CYKNPFKKDK RTWWNLEDNR NAILPPAPES
     FKLPKTRFIR DFIQLNLAMM ATNNALLPDP DKQDDLASSF WQWPTLNVGI RMCGWGAEKP
     KYFMIGSPAT TWTSTAGVIF FAFLVIYYLV RWQRQYIDFP STDPNKLKRF LMGGIYPMFG
     WGLHFMPFVI MGRVTYVHHY VPALYFAMMV FCYEIDSFTT GLRRPNATQG QKIAYAGIYL
     ALYVFVGYTF WYFRYLSWGM EGPKENWKHL KLLDSWRVSD DRYV
//
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