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Database: UniProt
Entry: A0A0P1BDF6_9BASI
LinkDB: A0A0P1BDF6_9BASI
Original site: A0A0P1BDF6_9BASI 
ID   A0A0P1BDF6_9BASI        Unreviewed;      1165 AA.
AC   A0A0P1BDF6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Cyclic nucleotide phosphodiesterase {ECO:0000313|EMBL:CEH13795.1};
OS   Ceraceosorus bombacis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX   NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH13795.1, ECO:0000313|Proteomes:UP000054845};
RN   [1] {ECO:0000313|EMBL:CEH13795.1, ECO:0000313|Proteomes:UP000054845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA   Brescovit A.D., Santos A.J.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CCYA01000230; CEH13795.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P1BDF6; -.
DR   STRING; 401625.A0A0P1BDF6; -.
DR   OrthoDB; 5479253at2759; -.
DR   Proteomes; UP000054845; 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   PANTHER; PTHR11347:SF198; CAMP-SPECIFIC 3',5'-CAMP PHOSPHODIESTERASE 4; 1.
DR   PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR   Pfam; PF00233; PDEase_I; 2.
DR   SMART; SM00471; HDc; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 2.
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:UP000054845}.
FT   DOMAIN          463..912
FT                   /note="PDEase"
FT                   /evidence="ECO:0000259|PROSITE:PS51845"
FT   REGION          1..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          154..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          266..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          409..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          800..822
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1116..1165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..387
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..432
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        630..646
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1165 AA;  122320 MW;  CEFA2E02C0EF1E9E CRC64;
     MTPGSSTSNA DLLSAPARSS HTSSHTDGSP GLSASSGSNS SSDGTTTPAK NRARQTSKTS
     RSRSVDVGEA ITPGRVSESA RTAPSSPASG TPSVGRTLQN TYKALQLRAR RSLLDLRVGG
     SGSARRHEGL HGATRHLHPH ARDASLHPLS ARTASQGFGT SESKLGRRAG DIDGSLGSLV
     TPTAARPSVA EERRGSGGTV KGSRWGIRPS SRPSSSGSGA ASSTQGSSPW SNRRRRERDE
     SSRQSAALHT SSLAGYGASP DVGDYADALA MGPSPSTQSR LLPPLDVDGR DARALQGFPA
     GPSNGLGSLA SFSFPHDAAF LRTRAQPLQG MDGGMRHPGP TDTKSASVKW LSNSPTTPLA
     SHFTHCRPSV IGHAHQSSGT NAERRRASEN PPCTCPAVLP RRHSELPVLV PSHLSPSPSR
     SILEQPSAAS PALSRRRSVR PSAARNRLVT QMASWDFCSL DLSDEDMRSA CEIVFEAVLC
     APIPRNVLDQ PPVLHDATTS AQTSTSTSES PLTTLGEHLG VTMDAVRRVL DSIMDLYHSS
     NAYHNFNHAA DVLQALYALL VDLKAVPSLS PNSTAAWDPA SSPLSPQDAL ALLFAAIGHD
     AGHPGLSNAY LSNASAPIAI AFRCGAPEHG NAEKGKSKDE VGSDDSLVKP AKGSPLESYH
     AILFEGLMER CGLAHLLWAE PGARSEFGEV IRSCILATDM AIHSSFVSAL STFEARLYDE
     PVVSDRRDRA QKIRAQPRSE RTLLCAALLK CADISNPVRA RSVGRRWSVA LRKEWERQSA
     LEEECGLPVT AGAANKCKHK RRSAAPVSMP PLPGSPSANE DGLRRTSAAQ MVAQIGGGGG
     AAAEIVEVSL NDLAAAGELE EERALARGQV AFVNAFVAPL MVAIAKLLPS LDTYLQLAID
     NKALWEKHLE AVEARILAEG PSKPSSPPGN PSMTALSIAD EQLAQLHGRP AISLSMLDSE
     RLRLPSIFLP PVDKVPLDAQ SCREQVQRAI DDALIGAVRA WKVPVPEGVT ADHPFIAIDV
     ADANKSSTAA MPDAADDRQR CASSASLASS IRSAASSTPA TAHSTSTAAT SSASGVLGLG
     KVDLHWSALK SQLTAPSSRH EDLSVGLAPA LPPITASTSS LERPTSSLYD VQVPSSAPSP
     GHASQSRRKT PISVMRRLSA WSTSK
//
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