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Database: UniProt
Entry: A0A1S3I9H3_LINUN
LinkDB: A0A1S3I9H3_LINUN
Original site: A0A1S3I9H3_LINUN 
ID   A0A1S3I9H3_LINUN        Unreviewed;       328 AA.
AC   A0A1S3I9H3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   31-JUL-2019, entry version 11.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   Name=LOC106162205 {ECO:0000313|RefSeq:XP_013394843.1};
OS   Lingula unguis.
OC   Eukaryota; Metazoa; Lophotrochozoa; Brachiopoda; Linguliformea;
OC   Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX   NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013394843.1};
RN   [1] {ECO:0000313|RefSeq:XP_013394843.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_013394843.1};
RG   RefSeq;
RL   Submitted (APR-2018) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16;
CC         Evidence={ECO:0000256|SAAS:SAAS01116782};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-
CC         [protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-
CC         COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977;
CC         EC=3.1.3.16; Evidence={ECO:0000256|RuleBase:RU004273,
CC         ECO:0000256|SAAS:SAAS01116780};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC       {ECO:0000256|RuleBase:RU004273, ECO:0000256|SAAS:SAAS01017257}.
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DR   RefSeq; XP_013394843.1; XM_013539389.1.
DR   GeneID; 106162205; -.
DR   KEGG; lak:106162205; -.
DR   KO; K06269; -.
DR   OrthoDB; 766640at2759; -.
DR   Proteomes; UP000085678; Genome assembly.
DR   GO; GO:0000164; C:protein phosphatase type 1 complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR037981; PPP1CC.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR031675; STPPase_N.
DR   PANTHER; PTHR11668:SF204; PTHR11668:SF204; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF16891; STPPase_N; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000085678};
KW   Hydrolase {ECO:0000256|RuleBase:RU004273,
KW   ECO:0000256|SAAS:SAAS01017252};
KW   Manganese {ECO:0000256|SAAS:SAAS01017251};
KW   Metal-binding {ECO:0000256|SAAS:SAAS01017255};
KW   Protein phosphatase {ECO:0000256|SAAS:SAAS01017274};
KW   Reference proteome {ECO:0000313|Proteomes:UP000085678}.
FT   DOMAIN      121    126       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
FT   REGION      304    328       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   328 AA;  37413 MW;  519FF3084E4D35B4 CRC64;
     MADADKLNID SIIARLLEVR GSRPGKNVQL TENEIRGLCL KSREIFLSQP ILLELEAPLK
     ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL
     LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIIDEKIF CCHGGLSPDL
     QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KETMGWGEND RGVSFTFGAE VVAKFLHKHD
     LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAD
     KKKFPYGGLQ QGRPVTPPRG NGKNKGKM
//
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