ID A0A1S3H6S1_LINUN Unreviewed; 842 AA.
AC A0A1S3H6S1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=LOC106152588 {ECO:0000313|RefSeq:XP_013381677.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013381677.1};
RN [1] {ECO:0000313|RefSeq:XP_013381677.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013381677.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|RuleBase:RU363067};
CC Note=Binds 2 divalent metal cations per subunit. Site 1 may
CC preferentially bind zinc ions, while site 2 has a preference for
CC magnesium and/or manganese ions. {ECO:0000256|RuleBase:RU363067};
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000256|RuleBase:RU363067}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_013381677.1; XM_013526223.2.
DR AlphaFoldDB; A0A1S3H6S1; -.
DR EnsemblMetazoa; XM_013526223.2; XP_013381677.1; LOC106152588.
DR GeneID; 106152588; -.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000085678; Unplaced.
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:SF179; 3',5'-CYCLIC PHOSPHODIESTERASE PDE-3-RELATED; 1.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU363067};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678}.
FT DOMAIN 354..790
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 111..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..749
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 842 AA; 94309 MW; BA22BF6B06F12C13 CRC64;
MVVCEVNIPC AGGIVVGRRH SFPLVGCQRW AEAGSTTLQE RVLTRSSVPS YESELIREAH
GLITDMLADT SLPPHVISGL KAVGSLLKPP ENHMPINRPR VSPLVSLAES TNYGSDSEDL
PYTGERPSSL PRRLRRSLPP SLLRRMSTST WTTTTSATGM PTLEPEPCRT RSSSFRHSRE
STPASSPSGS RSNSPSPNTA TTISLTIPKS RSFSLASAGP VSSVNQKRFP RDRKNVFMPS
APEEAGTHLK PLSPLVKSSE ESMTIRNTPT KEAHALLTKR LQRTSDYESS DSPNNSDHSD
NIVNTEEMID SKTTSKIGTT SQVEHLANRT AHHTVESLIQ NNNASQLDKQ EDTNTLPYEL
SVFENLELLQ ISNINKWEYP IFDLSKAVGN YILSLVAYRL FSETGLFETF RIPLPQFMHY
FHALEEGYRD KPYHNRIHAT DVLHGVYYFT TQPVPGFQQI NPDDVLNKQG SSSESDSDPG
ERPTLKHHQS FTAEDSYGIM GGNLPPLELM ALYTAAAMHD YDHPGRTNAF LVTTNAPQAV
LYNDRSVLEN HHAAAAWSLF LSHPKYNFLC HIDKAEFKRF RFLVIEAILA TDLKRHFEIL
AEFNAKVNEE DSPGVDWTSE TDRLLVSQIV IKLADINGPC KPRDLHVSWT MSITEEFYEQ
GDEEKRLGLP ISPYMDRRHP QLSKLQETFI NHLVAPLCNA YGQAGLLPGT WLDEESDEEG
SSESQDEEDE EERDSSACKD TEDEGDEEEK VSVSVAPAPK HKQKTRKILC QLTKNLKENH
DMWVAKIKAE QEEKERLESE IENQKNLENN SSISDNKPEM EPIQEEDTNG NKPPSPPQSG
EK
//
