ID C5E478_ZYGRC Unreviewed; 514 AA.
AC C5E478;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=ZYRO0E03564p {ECO:0000313|EMBL:CAR30839.1};
GN OrderedLocusNames=ZYRO0E03564g {ECO:0000313|EMBL:CAR30839.1};
OS Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS / NRRL Y-229) (Candida mogii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX NCBI_TaxID=559307 {ECO:0000313|EMBL:CAR30839.1, ECO:0000313|Proteomes:UP000008536};
RN [1] {ECO:0000313|Proteomes:UP000008536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC Y-229 {ECO:0000313|Proteomes:UP000008536};
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
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DR EMBL; CU928181; CAR30839.1; -; Genomic_DNA.
DR RefSeq; XP_002499094.1; XM_002499049.1.
DR AlphaFoldDB; C5E478; -.
DR STRING; 559307.C5E478; -.
DR GeneID; 8204636; -.
DR KEGG; zro:ZYRO0E03564g; -.
DR HOGENOM; CLU_017594_3_0_1; -.
DR InParanoid; C5E478; -.
DR Proteomes; UP000008536; Chromosome E.
DR GO; GO:0019637; P:organophosphate metabolic process; IEA:UniProt.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IEA:UniProt.
DR CDD; cd16018; Enpp; 1.
DR Gene3D; 3.30.1360.180; -; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR PANTHER; PTHR10151:SF120; BIS(5'-ADENOSYL)-TRIPHOSPHATASE; 1.
DR PANTHER; PTHR10151; ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008536};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..514
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002950766"
SQ SEQUENCE 514 AA; 57916 MW; 4345EA5AAF05EEF1 CRC64;
MFLLPLSLVL SILLVVILTG LRDSYNNRYK PHGFDPSAKY SNGTHEFYPI TLVLSLDGFH
PSLISKEATP FLHELYTLQQ PNTSVAPFIV PSFPSQTFPN HWSIVTGKYP SENGIVANWF
WDHSLEKQFG PGNIDPELWE TASEPIWSTL ENAFFADTFK SAAHMWPGCE VQGRTPHFFT
AFNDSETLEE KSESIFRNYV DGKRDASERP QLILAYAPQP DAYGHEYGYP APHTPSFREL
LNKIDSYVSR VFAALDQRHM RHFTNVVILS DHGMATVPSH NVLLEKEILP DDLRTQHVSH
SYLEGPALAI YTPNASHVER QLIKRLERLK IGKNFHVTRN LQQEFGYKLS GERTADIWVL
PDVHYAVAHQ RRLLGTHGYN NSSPEMRALF IANGPAFTEG YVEPFENVAI HGLLLELAGW
KSEPHVGRPS HKIATADTKP QGLLVPLRSP PQDDLALLSR IFGNGSSYNA VFHNETTKLD
AVVPEKQQQD FSSLLGEIVG ELQAELAEWG SNDK
//