ID A0A1S3H971_LINUN Unreviewed; 1087 AA.
AC A0A1S3H971;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=LOC106152588 {ECO:0000313|RefSeq:XP_013381674.1};
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_013381674.1};
RN [1] {ECO:0000313|RefSeq:XP_013381674.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013381674.1};
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}.
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DR RefSeq; XP_013381674.1; XM_013526220.1.
DR AlphaFoldDB; A0A1S3H971; -.
DR STRING; 7574.A0A1S3H971; -.
DR EnsemblMetazoa; XM_013526220.1; XP_013381674.1; LOC106152588.
DR GeneID; 106152588; -.
DR KEGG; lak:106152588; -.
DR InParanoid; A0A1S3H971; -.
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 599..1035
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..220
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..994
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1087
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1087 AA; 122730 MW; AAFEDBFF6488C3F8 CRC64;
MKKWKALIES RKRGKYEKRR QTAYQNIENS EPLLTDSHYD NGGSEHKQRK TYATAEAGDS
AQGKTVEKRK TYMVNKDDRM ANQYSCCTSK HTDEQPEPEH RHTDLCVEES KERKRTKGIS
LLKRISKSSE RPSKSKKSVE VDLQCQTLVD SSEAQSATST LWMGLRKKKT PKVKVKAEGA
TKAAESSPLG RKDERGAHSE QKQHHHHHHH QCQHHTHHSH YQSANKVDKW DHPACRSPPS
YTRKGVQYFP NTPSTSELKY RPSRSGSRKH HEGLHCKLQD HDGKVAVGYR SSVPSYESEL
IREAHGLITD MLADTSLPPH VISGLKAVGS LLKPPENHMP INRPRVSPLV SLAESTNYGS
DSEDLPYTGE RPSSLPRRLR RSLPPSLLRR MSTSTWTTTT SATGMPTLEP EPCRTRSSSF
RHSRESTPAS SPSGSRSNSP SPNTATTISL TIPKSRSFSL ASAGPVSSVN QKRFPRDRKN
VFMPSAPEEA GTHLKPLSPL VKSSEESMTI RNTPTKEAHA LLTKRLQRTS DYESSDSPNN
SDHSDNIVNT EEMIDSKTTS KIGTTSQVEH LANRTAHHTV ESLIQNNNAS QLDKQEDTNT
LPYELSVFEN LELLQISNIN KWEYPIFDLS KAVGNYILSL VAYRLFSETG LFETFRIPLP
QFMHYFHALE EGYRDKPYHN RIHATDVLHG VYYFTTQPVP GFQQINPDDV LNKQGSSSES
DSDPGERPTL KHHQSFTAED SYGIMGGNLP PLELMALYTA AAMHDYDHPG RTNAFLVTTN
APQAVLYNDR SVLENHHAAA AWSLFLSHPK YNFLCHIDKA EFKRFRFLVI EAILATDLKR
HFEILAEFNA KVNEEDSPGV DWTSETDRLL VSQIVIKLAD INGPCKPRDL HVSWTMSITE
EFYEQGDEEK RLGLPISPYM DRRHPQLSKL QETFINHLVA PLCNAYGQAG LLPGTWLDEE
SDEEGSSESQ DEEDEEERDS SACKDTEDEG DEEEKVSVSV APAPKHKQKT RKILCQLTKN
LKENHDMWVA KIKAEQEEKE RLESEIENQK NLENNSSISD NKPEMEPIQE EDTNGNKPPS
PPQSGEK
//
