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Database: UniProt
Entry: G3B7F7_CANTC
LinkDB: G3B7F7_CANTC
Original site: G3B7F7_CANTC 
ID   G3B7F7_CANTC            Unreviewed;       355 AA.
AC   G3B7F7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=HD-domain/PDEase-like protein {ECO:0000313|EMBL:EGV62265.1};
GN   ORFNames=CANTEDRAFT_131639 {ECO:0000313|EMBL:EGV62265.1};
OS   Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS   10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX   NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN   [1] {ECO:0000313|EMBL:EGV62265.1, ECO:0000313|Proteomes:UP000000707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC   NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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DR   EMBL; GL996527; EGV62265.1; -; Genomic_DNA.
DR   RefSeq; XP_006688435.1; XM_006688372.1.
DR   AlphaFoldDB; G3B7F7; -.
DR   GeneID; 18249544; -.
DR   HOGENOM; CLU_028903_0_0_1; -.
DR   OrthoDB; 5479253at2759; -.
DR   Proteomes; UP000000707; Unassembled WGS sequence.
DR   GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd00077; HDc; 1.
DR   Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR   InterPro; IPR023174; PDEase_CS.
DR   PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR   PANTHER; PTHR11347:SF230; HIGH AFFINITY CGMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE 9A; 1.
DR   Pfam; PF00233; PDEase_I; 1.
DR   SMART; SM00471; HDc; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS00126; PDEASE_I_1; 1.
DR   PROSITE; PS51845; PDEASE_I_2; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000707}.
FT   DOMAIN          1..353
FT                   /note="PDEase"
FT                   /evidence="ECO:0000259|PROSITE:PS51845"
SQ   SEQUENCE   355 AA;  40204 MW;  F448D693FE916E5D CRC64;
     MVRDSYKNGN PFHNFRHAVD VLQACFHYVI RLGYLSPFTQ FQSDPKADEL ICLKAEKFGN
     AVELISMKAA TRVPPTSSAA ETPDTEDTSL NLVSTLALLV AALGHDVGHP GVTNQFLVKH
     SSPTSLVFNE RSVLESFHTS VFLNKILVVN WPQFLQLKID TNLKLIVKEL IITCILATDM
     AEHFDYIDKL NKFNDIHHHH HHHQGTYSTT DSTSSASSRT IANSFDIQNR TNQVKLISSL
     LIKCADISNV TRPLRVSAQW ASVLSREFDE VSKVEEKITD SGKQFSIKYD KVPMFLVDIL
     QANPTIHKGQ MFFINTFAEN LFNNISELLP PLKFTGEIVQ ENKDYWLKRD SNRNK
//
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