ID A0A0D1BZR2_USTMA Unreviewed; 632 AA.
AC A0A0D1BZR2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Prenylcysteine lyase domain-containing protein {ECO:0000259|Pfam:PF07156};
GN ORFNames=UMAG_04318 {ECO:0000313|EMBL:KIS67212.1};
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS67212.1, ECO:0000313|Proteomes:UP000000561};
RN [1] {ECO:0000313|EMBL:KIS67212.1, ECO:0000313|Proteomes:UP000000561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2] {ECO:0000313|Proteomes:UP000000561}
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-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; CM003153; KIS67212.1; -; Genomic_DNA.
DR RefSeq; XP_011391040.1; XM_011392738.1.
DR AlphaFoldDB; A0A0D1BZR2; -.
DR STRING; 237631.A0A0D1BZR2; -.
DR EnsemblFungi; KIS67212; KIS67212; UMAG_04318.
DR GeneID; 23564539; -.
DR KEGG; uma:UMAG_04318; -.
DR VEuPathDB; FungiDB:UMAG_04318; -.
DR eggNOG; ENOG502QSHJ; Eukaryota.
DR InParanoid; A0A0D1BZR2; -.
DR OMA; QMWVESI; -.
DR OrthoDB; 1334100at2759; -.
DR Proteomes; UP000000561; Chromosome 14.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0001735; F:prenylcysteine oxidase activity; IBA:GO_Central.
DR GO; GO:0030327; P:prenylated protein catabolic process; IBA:GO_Central.
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; 2.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000561};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..632
FT /note="Prenylcysteine lyase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002227826"
FT DOMAIN 182..602
FT /note="Prenylcysteine lyase"
FT /evidence="ECO:0000259|Pfam:PF07156"
FT REGION 442..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 632 AA; 70187 MW; AB320B6721F22BE0 CRC64;
MIRASLLAYL SLLLAVLQQA NSTSADLVDD AQLYATENQN VWVPVPKKGY YIESDIPAHA
QFKEQQGRTR KIAIIGAGPS GTSAAYFLKH AQDRLASSND SSIAGDKLDL TIYERETRIG
GRAAVTYPYD DNTQDPVELG ASIFADVNLN IRRAVKDFDL ETGAKVGLSG QMGIWDGQQF
LFEGDQSSWW TSAKFFLRYG YSAITTENIV KTQLSYFAGL YRPSFLHARK GKSNTSVSGY
PWSRIEDLAD AINATSLVQT TGMQFFKDRR VSELFIEEMV EAATRVNYAQ DTDKIHGFGA
LVSLAASGAT GVKKGNYRIF EQFASRSGAR VLTGVEGQVT GIVRFNSTVP VPRRLGLQEG
AEMEEQVQWY IGTKSGEGEL YDAVIIATPW HNADITLLNT RERVKSKPFV HLHVTLLTTS
RERPRSEYFG LGEQDLVPTT ILTSSESVRR ASADRRNKPH VPETPSPPDE SAHSTTPRFG
AKDELKKPKL EFFSLNYLRS VRPPRSTSDS SSAKDYVVKI FSAQPMSDDQ LSALFGDTIS
WIKRHSWDSY PYLTPTDRYP RIQVDHNLYY SNAIESLVST METSTVASKN AVALMLRSWY
GDDFVNGNHC NSSVPIDPLD NPNWAGWGCD SG
//
