ID W0TDK0_KLUMD Unreviewed; 616 AA.
AC W0TDK0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Protein TTP1 {ECO:0000313|EMBL:BAO41425.1};
GN Name=MNN2 {ECO:0000313|EMBL:BAO41425.1};
GN ORFNames=KLMA_60134 {ECO:0000313|EMBL:BAO41425.1};
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:BAO41425.1, ECO:0000313|Proteomes:UP000065495};
RN [1] {ECO:0000313|EMBL:BAO41425.1, 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 -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SIMILARITY: Belongs to the MNN1/MNT family.
CC {ECO:0000256|ARBA:ARBA00009105}.
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DR EMBL; AP012218; BAO41425.1; -; Genomic_DNA.
DR AlphaFoldDB; W0TDK0; -.
DR VEuPathDB; FungiDB:KLMA_60134; -.
DR OrthoDB; 1985716at2759; -.
DR Proteomes; UP000065495; Chromosome 6.
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; PTHR31646; ALPHA-1,2-MANNOSYLTRANSFERASE MNN2; 1.
DR PANTHER; PTHR31646:SF1; ALPHA-1,2-MANNOSYLTRANSFERASE MNN2-RELATED; 1.
DR Pfam; PF11051; Mannosyl_trans3; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
FT REGION 70..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 616 AA; 69991 MW; 0ED7142A5E6AA68A CRC64;
MVVSRKRMQK LVKIVAIAGL LVFLLTHAGS YLSPDMSVDQ YAGALKEYVD KYKEDHEKAV
VDDKTVGSGE EVGAGIGSKP VSNGKTEGSG SSGKNSKVSS SSGERELLKS FFGRAFQYVK
EYGPEGVNTP NYDPNCNLKG DIGYRKDNVN EWWKLTGKEL SNCLKLTKKQ IAMLKDGHTN
YVRAINEMKL PANAYSGDGI VTVGGGKFSI MAFLIIKTVR NFGTTLPVEV FIPPNDEGDD
EFCNVLLPKY NAKCIYLSDV LPDDVIQKTE FKGYQFKSLA MIASSFRNLL LLDADNFPIK
PLDNIFDEKV YKENGLVLWP DFWRRTTHPV YYDIANIPLS YQRVRNTMDD VTPPSVYTQD
LSDLSKVPLH DLEGTIPDAS TESGQMMINK VQHIRTVLLS LYYNAYGPSW YYSIFSQRSS
GEGDKETFIA AANHYGLPFY QVRSEPTVDG YHKANGEGFR GVCMLQHDFA QDYDRYLLAQ
KEIKQKYANK PASYDPDYKY QESYLEKYFS VDSADVMFVH SHLPKFDPVG LALTKDLIEN
GKHIRSYRNL QRMHGYDLEL EAFKTFKEYV CKTRVHFKYF EKAVKSESEW TTICNYVDER
LQYLKQSHAD ALEGKF
//
