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Database: UniProt
Entry: M7BMI8_CHEMY
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Original site: M7BMI8_CHEMY 
ID   M7BMI8_CHEMY            Unreviewed;       570 AA.
AC   M7BMI8;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Serine/threonine-protein kinase PLK1 {ECO:0000256|ARBA:ARBA00020241};
DE            EC=2.7.11.21 {ECO:0000256|ARBA:ARBA00012424};
DE   AltName: Full=Polo-like kinase 1 {ECO:0000256|ARBA:ARBA00030335};
GN   ORFNames=UY3_05910 {ECO:0000313|EMBL:EMP36930.1};
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP36930.1, ECO:0000313|Proteomes:UP000031443};
RN   [1] {ECO:0000313|Proteomes:UP000031443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
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};
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DR   EMBL; KB523472; EMP36930.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7BMI8; -.
DR   STRING; 8469.M7BMI8; -.
DR   eggNOG; KOG0575; Eukaryota.
DR   Proteomes; UP000031443; Unassembled WGS sequence.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EMP36930.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..270
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          383..446
FT                   /note="POLO box"
FT                   /evidence="ECO:0000259|PROSITE:PS50078"
FT   DOMAIN          481..550
FT                   /note="POLO box"
FT                   /evidence="ECO:0000259|PROSITE:PS50078"
FT   REGION          21..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   570 AA;  64360 MW;  B7342E679DE2B290 CRC64;
     MKELLGLLRF VYTPTWCGKP GAAGRGSSLA QTTRCSGRAP GGRRPRREEG PRRRVVLRRS
     SPGALRETQG RNDPPRPLAP LTAGSSQSRL ESSQLRGECE KSLLELHKRR KALTEPEARY
     YLRQTILGCQ YLHGNRVIHR DLKLGNLFLN DDMEVKIGDF GLATKVEYDG ERKKTLCGTP
     NYIAPEVLGK KGHSFEVDIW SIGCIMYTLL VGKPPFETSC LKETYIRIKK NEYNIPKHIN
     PVAANLIQKM LRSDPATRPT IDELLNDEFF TSGYIPTRLP TTCLTIPPRF SIAPSGFDPS
     GRKPLTALNK GLDSPALDKT HEKEDEAALR ELGEPVDCHL ADMLQQLSVA NAAKPSERAV
     VRQEEAEDPA CIPIFWVSKW VDYSDKYGLG YQLCDNSVGV LFNDSTRLIM YNDGDSLQYI
     EQNSTESYFT VRSYPSTLTK KITLLKYFRN YMSEHLLKAG ANITPREGDE LARLPYLRTW
     FRTRSAIILH LSNGTVQINF FQDHTKIILC PLMAAVTYID EKRDFRTYKL SLIEEHGCCK
     ELASRLRYAR TMVEKLLSSK SGSARVKPSA
//
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