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Database: UniProt
Entry: A0A210QQL5_MIZYE
LinkDB: A0A210QQL5_MIZYE
Original site: A0A210QQL5_MIZYE 
ID   A0A210QQL5_MIZYE        Unreviewed;       757 AA.
AC   A0A210QQL5;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Serine/threonine-protein kinase tousled-like 2 {ECO:0000313|EMBL:OWF51025.1};
GN   ORFNames=KP79_PYT19593 {ECO:0000313|EMBL:OWF51025.1};
OS   Mizuhopecten yessoensis (Japanese scallop) (Patinopecten yessoensis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pectinida; Pectinoidea; Pectinidae;
OC   Mizuhopecten.
OX   NCBI_TaxID=6573 {ECO:0000313|EMBL:OWF51025.1, ECO:0000313|Proteomes:UP000242188};
RN   [1] {ECO:0000313|Proteomes:UP000242188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PY_sf001 {ECO:0000313|Proteomes:UP000242188};
RX   PubMed=28812685; DOI=10.1038/s41559-017-0120;
RA   Wang S., Zhang J., Jiao W., Li J., Xun X., Sun Y., Guo X., Huan P.,
RA   Dong B., Zhang L., Hu X., Sun X., Wang J., Zhao C., Wang Y., Wang D.,
RA   Huang X., Wang R., Lv J., Li Y., Zhang Z., Liu B., Lu W., Hui Y., Liang J.,
RA   Zhou Z., Hou R., Li X., Liu Y., Li H., Ning X., Lin Y., Zhao L., Xing Q.,
RA   Dou J., Li Y., Mao J., Guo H., Dou H., Li T., Mu C., Jiang W., Fu Q.,
RA   Fu X., Miao Y., Liu J., Yu Q., Li R., Liao H., Li X., Kong Y., Jiang Z.,
RA   Chourrout D., Li R., Bao Z.;
RT   "Scallop genome provides insights into evolution of bilaterian karyotype
RT   and development.";
RL   Nat. Ecol. Evol. 1:120-120(2017).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OWF51025.1}.
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DR   EMBL; NEDP02002403; OWF51025.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A210QQL5; -.
DR   STRING; 6573.A0A210QQL5; -.
DR   EnsemblMetazoa; XM_021496757.1; XP_021352432.1; LOC110449715.
DR   Proteomes; UP000242188; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd13990; STKc_TLK; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR22974; MIXED LINEAGE PROTEIN KINASE; 1.
DR   PANTHER; PTHR22974:SF23; TOUSLED-LIKE KINASE, ISOFORM G; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OWF51025.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000242188};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          395..673
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          38..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          189..237
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          344..380
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        38..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..90
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..155
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         424
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   757 AA;  86636 MW;  CAB047AE62E8763A CRC64;
     MNTELTEAVN NSMENVNLQS LDPRKQELLE ARFYGSRFQP LNITQQQDNS NLSAGSAERD
     DELIGVVHTP EKHARTPSER KRKRKATSEG TESNTPKSNR PEANGKKINE YFKQNQSPSR
     SANSQSAGTK SPSPQGMSYS YTAPSPSNHS NSDSIGYPPV PLYHCNKTIQ TDLNLQQILV
     LENKSSSHIE QKDSKIDDLL RQNDELRRQL TAQQKLIEKH KENLQKCLNV NKSLLIEKSK
     LEKKTTRQKC MGDRLRLGQF VTQRQGATFV ENWVDGWAFT DLMKQQERIS SDREEIEKQR
     KLLTKKKPTP TVMKNSKHDA FLKPGGDKPM TLAEFYEQDE ILKLRQASLK KEDADLQLEL
     EKLERERNLH IRELKRIHNE DNSRFKEHPT LHDRYLLLCL LGKGGFSEVH KGFDLKEQRY
     VACKIHQLNR EWKDDKKANY IKHALREYNI HKSLNHPRIV RLYDVFEIDN NSFCTVLEYC
     EGNDLDFYLK QNKSIPEKEA RSIISQTVSA LRYLNEIKPP VIHYDLKPGN ILLGSGSVSG
     EIKITDFGLS KVMDDDNLTP DGMDLTSQGA GTYWYLPPEC FVVGSNPPKI SSKVDVWSVG
     VIFYQCLYGK KPFGHNLSQA AILEENTILK ATEVEFPAKP QISTEAKGFI RQCLQYKKEH
     RPDVLLLAHQ DYLRPAPLKS KGHRCRSTNL PALRLGTEHD NSVLDVDPRE ITDLHLQFHV
     LAEPRQLCMG QAPCSHVAVT NCLEVAQMDR RAPRQVP
//
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