ID   W0TH42_KLUMD            Unreviewed;       763 AA.
AC   W0TH42;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Alpha-1,3-mannosyltransferase {ECO:0000313|EMBL:BAO42373.1};
GN   Name=MNN1 {ECO:0000313|EMBL:BAO42373.1};
GN   ORFNames=KLMA_80062 {ECO:0000313|EMBL:BAO42373.1};
OS   Kluyveromyces marxianus (strain DMKU3-1042 / BCC 29191 / NBRC 104275)
OS   (Yeast) (Candida kefyr).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=1003335 {ECO:0000313|EMBL:BAO42373.1, ECO:0000313|Proteomes:UP000065495};
RN   [1] {ECO:0000313|EMBL:BAO42373.1, ECO:0000313|Proteomes:UP000065495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DMKU3-1042 / BCC 29191 / NBRC 104275
RC   {ECO:0000313|Proteomes:UP000065495};
RX   PubMed=25834639; DOI=10.1186/s13068-015-0227-x;
RA   Lertwattanasakul N., Kosaka T., Hosoyama A., Suzuki Y., Rodrussamee N.,
RA   Matsutani M., Murata M., Fujimoto N., Suprayogi, Tsuchikane K., Limtong S.,
RA   Fujita N., Yamada M.;
RT   "Genetic basis of the highly efficient yeast Kluyveromyces marxianus:
RT   complete genome sequence and transcriptome analyses.";
RL   Biotechnol. Biofuels 8:47-47(2015).
CC   -!- SIMILARITY: Belongs to the MNN1/MNT family.
CC       {ECO:0000256|ARBA:ARBA00009105}.
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DR   EMBL; AP012220; BAO42373.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0TH42; -.
DR   VEuPathDB; FungiDB:KLMA_80062; -.
DR   OrthoDB; 2005743at2759; -.
DR   Proteomes; UP000065495; Chromosome 8.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000030; F:mannosyltransferase activity; IEA:UniProt.
DR   GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR   InterPro; IPR022751; Alpha_mannosyltransferase.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR31392; ALPHA-1,3-MANNOSYLTRANSFERASE MNN1-RELATED; 1.
DR   PANTHER; PTHR31392:SF1; ALPHA-1,3-MANNOSYLTRANSFERASE MNN1-RELATED; 1.
DR   Pfam; PF11051; Mannosyl_trans3; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000313|EMBL:BAO42373.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000313|EMBL:BAO42373.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        30..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   763 AA;  89041 MW;  77D322BE76AE9977 CRC64;
     MTIRRLISSG SRTRTRTRTR THLGWVRYRY VMYGFVITCI GTLVYLLVDR TGMDVEKWHR
     AARMADKMLE SYSWDLISDA KIKAIEEIPV SPLELIPDIE LNTKKRYDAS WDLLFRGRKY
     KSFSEYDLST KCEFYFQNLY NLDEEWTNEI GMFTFDIKDI KSDSRMSELK DDDGVKLIDE
     KALRYYKRKH NIALGMERFR IYDRCFVGNN NNKHDSLKMN ELFEQGGSEG STSTASKLDK
     TVIGNKDSLR PTRKASFLSE LDSGKFSKFN QWDFEHRMFP FIPYFEQHNF TQVMPIFTGP
     GSHQPLPQGK FPVFNRDTGE LSTVESFNYD ETKSLWDNWN DLSARCSHKG IVMSAGNGQV
     DQTMRLIAVL REQHNRMPIQ IIHNDQLSDN SVALLSEAAQ STDFSNGPKQ SVWFLNVKPT
     LSESEKGRFD RYKNKWLSVI FNTFEEFIFI DSDAISYIGL EEYFKFDEYS ATGTLMFKDR
     SLKFGAEQKC PVLFETLQPK ILERYYFDTV PQINAEFVEQ ACMKELTPEE RVYKRFFELG
     QQHHLESGLL AINKRQHIMS MIISTVLNIS PKIGGCAWGD KEFFWLGLLV SGHRYSIYDV
     AASAVGIPSM KERERGDELK EAQEICSTQV GHTSYDKHLL WLNGGSQLCK FEGTFDSDWE
     QFENIRKEFH DNKDKARQAY KDVMPIEAAI IPDINVGRWA HKDRRCSGYV WCGEYFEKIK
     PYTYSKKIVK GELIHFDQKE IEHIRHLNTI WNKASLLPID KKE
//