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Database: UniProt
Entry: A0A212EZK5_DANPL
LinkDB: A0A212EZK5_DANPL
Original site: A0A212EZK5_DANPL 
ID   A0A212EZK5_DANPL        Unreviewed;       693 AA.
AC   A0A212EZK5;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Serine/threonine-protein phosphatase with EF-hands {ECO:0000256|PIRNR:PIRNR000912};
DE            EC=3.1.3.16 {ECO:0000256|PIRNR:PIRNR000912};
GN   Name=LOC116766188 {ECO:0000313|RefSeq:XP_032511822.1};
GN   ORFNames=KGM_215997 {ECO:0000313|EMBL:OWR46920.1};
OS   Danaus plexippus plexippus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Nymphalidae; Danainae; Danaini; Danaina; Danaus; Danaus.
OX   NCBI_TaxID=278856 {ECO:0000313|EMBL:OWR46920.1, ECO:0000313|Proteomes:UP000007151};
RN   [1] {ECO:0000313|EMBL:OWR46920.1, ECO:0000313|Proteomes:UP000007151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F-2 {ECO:0000313|EMBL:OWR46920.1};
RX   PubMed=22118469; DOI=10.1016/j.cell.2011.09.052;
RA   Zhan S., Merlin C., Boore J.L., Reppert S.M.;
RT   "The monarch butterfly genome yields insights into long-distance
RT   migration.";
RL   Cell 147:1171-1185(2011).
RN   [2] {ECO:0000313|EMBL:OWR46920.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=F-2 {ECO:0000313|EMBL:OWR46920.1};
RA   Zhan S., Reppert S.M.;
RT   "MonarchBase: the monarch butterfly genome database.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:XP_032511822.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) 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, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001512};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001482,
CC         ECO:0000256|PIRNR:PIRNR000912, ECO:0000256|RuleBase:RU004273};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00008294, ECO:0000256|PIRNR:PIRNR000912,
CC       ECO:0000256|RuleBase:RU004273}.
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DR   EMBL; AGBW02011268; OWR46920.1; -; Genomic_DNA.
DR   RefSeq; XP_032511822.1; XM_032655931.1.
DR   STRING; 278856.A0A212EZK5; -.
DR   EnsemblMetazoa; XM_032655931.1; XP_032511822.1; LOC116766188.
DR   KEGG; dpl:KGM_215997; -.
DR   eggNOG; KOG0377; Eukaryota.
DR   OrthoDB; 3076469at2759; -.
DR   Proteomes; UP000007151; Unassembled WGS sequence.
DR   Proteomes; UP000596680; Chromosome 7.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050906; P:detection of stimulus involved in sensory perception; IEA:UniProtKB-UniRule.
DR   CDD; cd00051; EFh; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR012008; Ser/Thr-Pase_EF-hand_contain.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR45668; SERINE/THREONINE-PROTEIN PHOSPHATASE 5-RELATED; 1.
DR   PANTHER; PTHR45668:SF3; SERINE_THREONINE-PROTEIN PHOSPHATASE RDGC; 1.
DR   Pfam; PF13202; EF-hand_5; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   Pfam; PF00612; IQ; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF000912; PPEF; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00054; EFh; 3.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00018; EF_HAND_1; 3.
DR   PROSITE; PS50222; EF_HAND_2; 3.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR000912, ECO:0000256|RuleBase:RU004273};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRNR:PIRNR000912};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR000912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007151}.
FT   DOMAIN          520..555
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          604..639
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          644..679
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          154..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   693 AA;  79182 MW;  1BDA772BADF07803 CRC64;
     MFSFTEGCGC VSFRGGRRAR SLGDDSSSCR SSEIEQEVPK KIGKRILNGD CTMKALAPFW
     KFWKKDEASM TKAERTMKAA ILIQQWYRRY LARMEVRRRY TWTIFQSIEY AGEQDQVKLY
     NFFNALLSHM RETSGRPSSE RTSRTASVME QIFSEESDEG GGVDETAPPK NCREPDIEFP
     LQRKDIDLLI EAFRKKKVTQ ILKEASQMLK RLPNINVATT SISSQITICG DLHGKLDDLL
     VIFHKNGLPS PENPYIFNGD FVDRGKKGLE VLLLLLACML TFPGGVYLNR GNHEDLIMNT
     RYGFIREVHQ KYRHNAERLL KLIENVYRWL PLGTIINNRV FVVHGGISDT TDLDMLRSME
     RDKYASLLRP PLNEGAAPGA EAIDKVEWKQ VFDILWSDPQ STGGCVANAL RGAGTYFGPD
     VTSSFLNKNK LSFIIRSHEC KPGGYEILHN GNVITIFSAS NYYELGSNKG AYLKLCGNAL
     DRQFVQYTAA VSRTRRLTFR QRVGLVESSA MRELHSHIMT ARRTLEATFR SMDLDQSGFI
     TISDWCYAME ETTHLGLPWR MLKDKLVRTD PDTRRVRYMD TFELLANKIG RKSDAQTVVE
     TLYKNKRSLE AIFKILDKDN SGFITLEEFS EACQLLGKYM PNPMTQEQLV DICRLMDINK
     DGLVDLNEFL ESFRLAEKSL HEDEHVLAEM KAS
//
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