ID F2SCY6_TRIRC Unreviewed; 456 AA.
AC F2SCY6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Chitobiosyldiphosphodolichol beta-mannosyltransferase {ECO:0000256|ARBA:ARBA00015841};
DE EC=2.4.1.142 {ECO:0000256|ARBA:ARBA00012611};
GN ORFNames=TERG_01514 {ECO:0000313|EMBL:EGD85238.1};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD85238.1, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
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; GG700648; EGD85238.1; -; Genomic_DNA.
DR RefSeq; XP_003239529.1; XM_003239481.1.
DR AlphaFoldDB; F2SCY6; -.
DR STRING; 559305.F2SCY6; -.
DR GeneID; 10375087; -.
DR VEuPathDB; FungiDB:TERG_01514; -.
DR eggNOG; KOG2941; Eukaryota.
DR HOGENOM; CLU_012079_1_0_1; -.
DR InParanoid; F2SCY6; -.
DR OMA; CKLIIDW; -.
DR OrthoDB; 1219598at2759; -.
DR Proteomes; UP000008864; 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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000008864};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 60..217
FT /note="Glycosyltransferase subfamily 4-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13579"
SQ SEQUENCE 456 AA; 49937 MW; 03F7033AD505FD22 CRC64;
MTLVLLLSIL AIGFSSVAFI QLLPTRREKK SSETHDAVSV QIVVLGDIGH SPRMQCHALS
IARHGGRVTV IGYHNSTPNQ ELLDHPLISI VALPSPPALL QTKKKFLFPV AAILKVLQQA
WHLWTALGYR TGPAHWILVQ NPPAAPTLAL ALLACHLRHS RLIIDWHNFG YSILALKLGS
AHPMVKLMAL YEKAFSCYAT AHFCVSNAMA RILREQFEIK KPLMVLHDRP SSAFSPIFDE
KRRLAILSSI PETSQSATDI IEGRCRLLVS STSWTPDEDF SLLLDALCRY STSAKSSVLP
SVPLLVIITG KGPLKDMYLS QIDKLKAEGK LFNVFIKTAW LSFENYAQLL ACATLGVCLH
TSSSGVDLPM KVVDMFGAGL PVVGWDQYEA WPELVTEGVT GLGFDSADKL SGLLKSVLGG
DGSALKVLRE GAVKESRNRW DQTWDPIAGT FLGLVT
//
