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Database: UniProt
Entry: W6MKM8_9ASCO
LinkDB: W6MKM8_9ASCO
Original site: W6MKM8_9ASCO 
ID   W6MKM8_9ASCO            Unreviewed;       497 AA.
AC   W6MKM8;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   22-FEB-2023, entry version 26.
DE   RecName: Full=Prenylcysteine lyase domain-containing protein {ECO:0000259|Pfam:PF07156};
GN   ORFNames=KUCA_T00002530001 {ECO:0000313|EMBL:CDK26558.1};
OS   Kuraishia capsulata CBS 1993.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX   NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK26558.1};
RN   [1] {ECO:0000313|EMBL:CDK26558.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK26558.1};
RA   Genoscope - CEA;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDK26558.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK26558.1};
RA   Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA   Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA   Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA   Gabaldon T., Wincker P., Dujon B.;
RT   "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT   features among budding yeasts (/Saccharomycotina/).";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the prenylcysteine oxidase family.
CC       {ECO:0000256|ARBA:ARBA00009967}.
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DR   EMBL; HG793127; CDK26558.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6MKM8; -.
DR   STRING; 1382522.W6MKM8; -.
DR   HOGENOM; CLU_021176_0_0_1; -.
DR   OrthoDB; 1334100at2759; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0001735; F:prenylcysteine oxidase activity; IEA:InterPro.
DR   GO; GO:0030328; P:prenylcysteine catabolic process; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR010795; Prenylcys_lyase.
DR   InterPro; IPR017046; Prenylcysteine_Oxase.
DR   PANTHER; PTHR15944; FARNESYLCYSTEINE LYASE; 1.
DR   PANTHER; PTHR15944:SF0; PRENYLCYS_LYASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   Pfam; PF07156; Prenylcys_lyase; 1.
DR   PIRSF; PIRSF036292; Prenylcysteine_oxidase; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          152..487
FT                   /note="Prenylcysteine lyase"
FT                   /evidence="ECO:0000259|Pfam:PF07156"
SQ   SEQUENCE   497 AA;  54807 MW;  F2AA5FB43114C7FC CRC64;
     MSSLGQKANR YILIFGVMTL VPLVFLAYSL SLVWGNSCGA SPPSSDSIGA ERIAIIGAGA
     GGSSCAYYLQ KFTSFGYNIT VFERSNYVGG RSTTVRAKNS STLVELGASI FIGDNEIMMN
     AVETFGLDHH DFSTSDEFLI WNGEEALYTY QDSSIPYYSQ TKLLLRYGLS YFSAKTLVSG
     IVDKFLTYYY SDYFPFPSLT KLSLTTGFSE LTGETSETFF TSNNIGSLYL HEIIEAVTRV
     NYAQNVNQIH ALGASVCMAA GSAYSVTGGN WQVFDSFIKV SEANLLLQHG VASIKKNAQS
     NFEVTAVDSS GYEFTEEYDQ VVIAAPYYQT NINLPTGYSS EVENRQYVEL HVTLLTTFGT
     LSKSYFNADY VPTTVITSSE GAQKNTPFFS ISKVGNISET TESIYKIFSP AELSDKFITT
     LFEKGSTISW VHRKTWKPYP YLKPTTQFTD FQLDQDGLWY LNGMEEFIST METSALAGAN
     VAALISKGKN TTFLTVP
//
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