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Database: UniProt
Entry: A0A087Y0D6_POEFO
LinkDB: A0A087Y0D6_POEFO
Original site: A0A087Y0D6_POEFO 
ID   A0A087Y0D6_POEFO        Unreviewed;       591 AA.
AC   A0A087Y0D6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 2.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Serine/threonine-protein kinase PLK {ECO:0000256|RuleBase:RU361162};
DE            EC=2.7.11.21 {ECO:0000256|RuleBase:RU361162};
DE   AltName: Full=Polo-like kinase {ECO:0000256|RuleBase:RU361162};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000011489.2, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000011489.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00000540};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.21; Evidence={ECO:0000256|ARBA:ARBA00000856,
CC         ECO:0000256|RuleBase:RU361162};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. CDC5/Polo subfamily. {ECO:0000256|RuleBase:RU361162}.
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DR   EMBL; AYCK01019436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A087Y0D6; -.
DR   STRING; 48698.ENSPFOP00000011489; -.
DR   Ensembl; ENSPFOT00000011505.2; ENSPFOP00000011489.2; ENSPFOG00000011431.2.
DR   eggNOG; KOG0575; Eukaryota.
DR   GeneTree; ENSGT00940000166918; -.
DR   OMA; IQIHKSM; -.
DR   Proteomes; UP000028760; Unassembled WGS sequence.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR   CDD; cd13118; POLO_box_1; 1.
DR   CDD; cd13117; POLO_box_2; 1.
DR   Gene3D; 3.30.1120.30; POLO box domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR033701; POLO_box_1.
DR   InterPro; IPR033695; POLO_box_2.
DR   InterPro; IPR000959; POLO_box_dom.
DR   InterPro; IPR036947; POLO_box_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR   PANTHER; PTHR24345:SF0; SERINE_THREONINE-PROTEIN KINASE PLK1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00659; POLO_box; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF82615; Polo-box domain; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50078; POLO_BOX; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361162};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU361162};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361162}.
FT   DOMAIN          38..290
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          408..471
FT                   /note="POLO box"
FT                   /evidence="ECO:0000259|PROSITE:PS50078"
FT   DOMAIN          506..575
FT                   /note="POLO box"
FT                   /evidence="ECO:0000259|PROSITE:PS50078"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         76
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   591 AA;  67485 MW;  98A668F345968850 CRC64;
     MSAGVAKPAP TSALSDPKSA PLKEIPDILV DPRTTKRYTR GRFLGKGGFA KCYEITDVET
     KQVFAGKIVP KSLILKQHQR EKMTSEIAIH KSLNHPNIVG FHGFFEDDDF VFVVLEICRR
     RSLLELHKRR KAVTEPEARY YMTQLLKGVH YLHNNRVIHR DLKLGNIFLN DEMEVKIGDF
     GLATKIEFDG ERKKTLCGTP NYIAPEVLCK KGHSYEVDVW SLGCILYTLL VGKPPFETSC
     LKETYSRIKK NSYVIPWHIN PAAASLIKRM LHADPAQRPT ITQLQEDEFL TSGYIPLRLP
     TTCLTVPPRF SIAPSTAAEL GQRRPLSALN NKGNESRLSR WDREDGGERR CCAKVREIEP
     SENHLKDMLQ QLNSIMASKP AEKAFIRQEE AEDPACIPIF WISKWVDYSD KYGLGYQLCD
     NSVGVLFNDY TRLIMYADGD SLQYIDKMAA ESYMSVRSFP TTLNKKITLL KYFRNYMSEH
     LLKAGANVAR REGDELARLP YLSLWFRTKS AIVLHLSNGT VQINFFQDHT KLILCPLMAA
     VTYIDEKRDF RTYKLSLLEE FGCCRELASR MRYAKLMVEK LLDSKSSSAA H
//
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