ID W0TBS1_KLUMD Unreviewed; 701 AA.
AC W0TBS1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Protein VHS3 {ECO:0000313|EMBL:BAO39549.1};
GN Name=VHS3 {ECO:0000313|EMBL:BAO39549.1};
GN ORFNames=KLMA_30254 {ECO:0000313|EMBL:BAO39549.1};
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:BAO39549.1, ECO:0000313|Proteomes:UP000065495};
RN [1] {ECO:0000313|EMBL:BAO39549.1, 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 HFCD (homooligomeric flavin containing Cys
CC decarboxylase) superfamily. {ECO:0000256|ARBA:ARBA00038350}.
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DR EMBL; AP012215; BAO39549.1; -; Genomic_DNA.
DR AlphaFoldDB; W0TBS1; -.
DR VEuPathDB; FungiDB:KLMA_30254; -.
DR OrthoDB; 168599at2759; -.
DR Proteomes; UP000065495; Chromosome 3.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR Gene3D; 3.40.50.1950; Flavin prenyltransferase-like; 1.
DR InterPro; IPR036551; Flavin_trans-like.
DR InterPro; IPR003382; Flavoprotein.
DR PANTHER; PTHR14359; HOMO-OLIGOMERIC FLAVIN CONTAINING CYS DECARBOXYLASE FAMILY; 1.
DR PANTHER; PTHR14359:SF17; PHOSPHOPANTOTHENOYLCYSTEINE DECARBOXYLASE SUBUNIT SIS2-RELATED; 1.
DR Pfam; PF02441; Flavoprotein; 1.
DR SUPFAM; SSF52507; Homo-oligomeric flavin-containing Cys decarboxylases, HFCD; 2.
PE 3: Inferred from homology;
FT DOMAIN 332..618
FT /note="Flavoprotein"
FT /evidence="ECO:0000259|Pfam:PF02441"
FT REGION 34..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..685
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 701 AA; 74254 MW; DE7C6AA3FFAE3BA9 CRC64;
MSPVTPHPTE EQQPSLVSPR FTNLGERRNT EMLNTGGSPQ SVAIGSQATS PVNKPASPPV
SITKSIMNAS GTSGAVISNT PASGLKRVPT VTFTDAKHAI LKQQATAEQT SALLNSLNNQ
GSKKAAHSPP GSDKASSPPP MELYANSNKH SQQHMAAAAF AAATAAADAA RQKGQSGVST
GGLGDARLPE DARARKNIVS NGERGPAAEG ETVVTPVEAS DVREGVEKMN IGTPKHDSEQ
HPHFVVNDEL HSPKFKARSR SNSVSPMPTV AAQGNQAPQF KLNETSIPEN EQLDSGGEPP
IEIAQIVAPN IPKREAAKNV DPRLPQDDGK LHILFGATGS LSVLKIKSMI KKLEEIYGRD
RVSIQVILTH AAAQFFANRT LSKKKGSLSG HPHSYAAAAA GVASTPSPAA GAAGTSGAGT
GAGDGVGPTS GQLLSQPLGQ TSSNPATSSP LSHDAHLTSN DTLAGQDAKA ATDGNAISTA
AKIELPSHIQ VWTDQDEWDA WKQRTDPVLH IELRRWADIL VVAPLTANTL SKIALGLCDN
LLTSVIRAWN PLFPIFLAPS MVSNSFNSSI TKRHLNMIKE EMPWITVFKP SEKVVGIYGD
IGLGGMMDGN EIVDKVVMKL GGYPEDENQE EEGEDEDEDE DEEDDEDPSD KKNNEEDDDD
DDDDDDDDDD DDDDDDDDDD DDLIDIDDVK SLHETGPSAS A
//
