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BMT2_KOMPC
ID   BMT2_KOMPC              Reviewed;         635 AA.
AC   F2QZ66;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Beta-mannosyltransferase 2;
DE            EC=2.4.1.-;
GN   Name=BMT2; OrderedLocusNames=PP7435_Chr4-0530;
OS   Komagataella phaffii (strain ATCC 76273 / CBS 7435 / CECT 11047 / NRRL
OS   Y-11430 / Wegner 21-1) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=981350;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 76273 / CBS 7435 / CECT 11047 / NRRL Y-11430 / Wegner 21-1;
RX   PubMed=21575661; DOI=10.1016/j.jbiotec.2011.04.014;
RA   Kueberl A., Schneider J., Thallinger G.G., Anderl I., Wibberg D., Hajek T.,
RA   Jaenicke S., Brinkrolf K., Goesmann A., Szczepanowski R., Puehler A.,
RA   Schwab H., Glieder A., Pichler H.;
RT   "High-quality genome sequence of Pichia pastoris CBS7435.";
RL   J. Biotechnol. 154:312-320(2011).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 76273 / CBS 7435 / CECT 11047 / NRRL Y-11430 / Wegner 21-1;
RX   PubMed=27388471; DOI=10.1093/femsyr/fow051;
RA   Valli M., Tatto N.E., Peymann A., Gruber C., Landes N., Ekker H.,
RA   Thallinger G.G., Mattanovich D., Gasser B., Graf A.B.;
RT   "Curation of the genome annotation of Pichia pastoris (Komagataella
RT   phaffii) CBS7435 from gene level to protein function.";
RL   FEMS Yeast Res. 16:0-0(2016).
CC   -!- FUNCTION: Beta-mannosyltransferase involved in cell wall biosynthesis.
CC       Initiates the beta-mannosylation of core N-linked glycans (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the BMT family. {ECO:0000305}.
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DR   EMBL; FR839631; CCA40694.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2QZ66; -.
DR   SMR; F2QZ66; -.
DR   CAZy; GT91; Glycosyltransferase Family 91.
DR   EnsemblFungi; CCA40694; CCA40694; PP7435_CHR4-0530.
DR   HOGENOM; CLU_013841_2_1_1; -.
DR   Proteomes; UP000006853; Chromosome 4.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000030; F:mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   InterPro; IPR021988; BMT1.
DR   PANTHER; PTHR37989; PTHR37989; 2.
DR   Pfam; PF12141; DUF3589; 2.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Coiled coil; Glycoprotein;
KW   Glycosyltransferase; Membrane; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..635
FT                   /note="Beta-mannosyltransferase 2"
FT                   /id="PRO_0000426101"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..635
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          517..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          512..635
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        484
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   635 AA;  73436 MW;  DB5480C45B9F7E61 CRC64;
     MRTRLNFLLL CIASVLSVIW IGVLLTWNDN NLGGISLNGG KDSAYDDLLS LGSFNDMEVD
     SYVTNIYDNA PVLGCTDLSY HGLLKVTPKH DLACDLEFIR AQILDIDVYS AIKDLEDKAL
     TVKQKVEKHW FTFYGSSVFL PEHDVHYLVR RVIFSAEGKA NSPVTSIIVA QIYDKNWNEL
     NGHFLDILNP NTGKVQHNTF PQVLPIATNF VKGKKFRGAE DPRVVLRKGR FGPDPLVMFN
     SLTQDNKRRR IFTISPFDQF KTVMYDIKDY EMPRYEKNWV PFFLKDNQEA VHFVYSFNPL
     RVLKCSLDDG SCDIVFEIPK VDSMSSELRG ATPMINLPQA IPMAKDKEIW VSFPRTRIAN
     CGCSRTTYRP MLMLFVREGS NFFVELLSTS LDFGLEVLPY SGNGLPCSAD HSVLIPNSID
     NWEVVDSNGD DILTLSFSEA DKSTSVIHIR GLYNYLSELD GYQGPEAEDE HNFQRILSDL
     HFDNKTTVNN FIKVQSCALD AAKGYCKEYG LTRGEAERRR RVAEERKKKE KEEEEKKKKK
     EKEEEEKKRI EEEKKKIEEK ERKEKEKEEA ERKKLQEMKK KLEEITEKLE KGQRNKEIDP
     KEKQREEEER KERVRKIAEK QRKEAEKKEA EKKGK
 
 
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