ID A0A087XYP8_POEFO Unreviewed; 695 AA.
AC A0A087XYP8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=dual-specificity kinase {ECO:0000256|ARBA:ARBA00013203};
DE EC=2.7.12.1 {ECO:0000256|ARBA:ARBA00013203};
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:ENSPFOP00000010901.1, 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:ENSPFOP00000010901.1}
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=2.7.12.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000972};
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=2.7.12.1; Evidence={ECO:0000256|ARBA:ARBA00001076};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001687};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00005843}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AYCK01010251; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01010252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A087XYP8; -.
DR STRING; 48698.ENSPFOP00000010901; -.
DR Ensembl; ENSPFOT00000010917.1; ENSPFOP00000010901.1; ENSPFOG00000010874.1.
DR eggNOG; ENOG502QTCP; Eukaryota.
DR GeneTree; ENSGT00940000157807; -.
DR OMA; NECCLCN; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd14155; PKc_TESK; 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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR46485:SF3; DUAL SPECIFICITY TESTIS-SPECIFIC PROTEIN KINASE 1; 1.
DR PANTHER; PTHR46485; LIM DOMAIN KINASE 1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
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; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760}.
FT DOMAIN 53..309
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 335..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 695 AA; 75972 MW; D2A51878F9B6E4FB CRC64;
MDHYNECCLC NPEDGPGGLD EPPLHSIHAP NRIRPSSYRA LRSAVSSLAR IDDFFCEKIG
SGFFSEVFKV QHRITGQVMA LKMNTLASNK ANMLREVQLM NRLCHPNILR FLGVCVHEGQ
LHALTEYING GNLEQLLDSD LYLSWSARVG LSLDIARGLE YLHSKGIFHR DLTSKNCLVR
CENGTFTAVV GDFGLAEKIP DYSDGVEKQP LAIVGSPYWM APEVLRGELY DEKVDVFAFG
IILCEIIARI EADPDFLPRT EDFGLDVPAF ENMIGDCPAA FFSLAVTCCN MSAERRPSFS
DIVFTLEAMG GEDRQIPITL EPVTVNVSPY RRRSSPCHLG NHSQPRKGLA RSQSDMLPPA
ALTPPLLGTP PRVNPFSLRR DLNGGRCKLL DTPSKSVISL TFTLPALCDP CASPRLLRGT
TGMLAPPRRC QSLPCTPEIS RTAPFPCDTE QEEDGIGQVA GNEGDEKVLV SEEQTDGQSL
DTTEEDSGLP LELEMVSLGR LDEEEEEENN EESVCLAEPM DCTKSPEPAK RILNSTPLKP
LLTSTSCSNL RTKSWRLPCS NGPPSFPALP KLDNNNLSEL VIGQQVQWGG GRHSNGYGEG
QVPSSDLTGS SERDEVISCP SCCLVGLSFP SVCLRGSAAV PVSRRRASLP RQRQYQNLNA
SATAARTLLC RSTNGLVADQ SVPREPGRTL PEAQS
//
