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Database: UniProt
Entry: E4US36_ARTGP
LinkDB: E4US36_ARTGP
Original site: E4US36_ARTGP 
ID   E4US36_ARTGP            Unreviewed;       456 AA.
AC   E4US36;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Chitobiosyldiphosphodolichol beta-mannosyltransferase {ECO:0000256|ARBA:ARBA00015841};
DE            EC=2.4.1.142 {ECO:0000256|ARBA:ARBA00012611};
GN   ORFNames=MGYG_03456 {ECO:0000313|EMBL:EFR00454.1};
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN   [1] {ECO:0000313|Proteomes:UP000002669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- FUNCTION: Participates in the formation of the lipid-linked precursor
CC       oligosaccharide for N-glycosylation. Involved in assembling the
CC       dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic
CC       surface of the ER. {ECO:0000256|ARBA:ARBA00024899}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP-alpha-D-mannose + N,N'-diacetylchitobiosyl
CC         diphosphodolichol = beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC         GlcNAc-diphosphodolichol + GDP + H(+); Xref=Rhea:RHEA:13865,
CC         Rhea:RHEA-COMP:9520, Rhea:RHEA-COMP:11044, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57269, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:58472; EC=2.4.1.142;
CC         Evidence={ECO:0000256|ARBA:ARBA00001259};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
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DR   EMBL; DS989824; EFR00454.1; -; Genomic_DNA.
DR   RefSeq; XP_003173284.1; XM_003173236.1.
DR   AlphaFoldDB; E4US36; -.
DR   STRING; 535722.E4US36; -.
DR   GeneID; 10028546; -.
DR   VEuPathDB; FungiDB:MGYG_03456; -.
DR   eggNOG; KOG2941; Eukaryota.
DR   HOGENOM; CLU_012079_1_0_1; -.
DR   InParanoid; E4US36; -.
DR   OMA; CKLIIDW; -.
DR   OrthoDB; 1219598at2759; -.
DR   Proteomes; UP000002669; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004578; F:chitobiosyldiphosphodolichol beta-mannosyltransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03816; GT33_ALG1-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR   InterPro; IPR026051; ALG1-like.
DR   InterPro; IPR028098; Glyco_trans_4-like_N.
DR   PANTHER; PTHR13036; BETA1,4 MANNOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR13036:SF0; CHITOBIOSYLDIPHOSPHODOLICHOL BETA-MANNOSYLTRANSFERASE; 1.
DR   Pfam; PF13579; Glyco_trans_4_4; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   4: Predicted;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000313|EMBL:EFR00454.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002669};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EFR00454.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          60..220
FT                   /note="Glycosyltransferase subfamily 4-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13579"
SQ   SEQUENCE   456 AA;  50340 MW;  01758E86EC65FE09 CRC64;
     MVLILVFSII AIGVSSLALF RLVPTRLARK SLEPHHVVSV QIVVLGDIGH SPRMQCHALS
     IARHGGRVSL IGYHNSTPNQ ELLDHPLISI VALPSPPALL QTKKKALFPI AAIFKVLQQT
     WHLWVALGYR AEPAHWILVQ NPPATPTLVF AILACYLRNS CLIIDWHNFG YSILALKLGS
     AHPMVRLMAW YEHVFSRYAT AHFCVSNAMA RILREQWKIK NPLMVLYDRP SSVFSPILDQ
     RQRLAVLSSI PETSQDAMEI IQGRCRLLIS STSWTPDEDF SLLLDALCQY SASAEFAVPA
     LASLLVIITG KGPLKDMYLS QIDKLKADGK LFSVSIKTAW LAFEDYARLL ACGTLGVCLH
     TSSSGVDLPM KVVDMFGAGL PVVGWDQYEA WSELVTEGAS GLGFDSADSL SRLLKNLLGH
     DESALKTLRE GAIRESKNRW DQTWDPVAGA FLGLIS
//
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