ID K7FTW2_PELSI Unreviewed; 603 AA.
AC K7FTW2;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=dual-specificity kinase {ECO:0000256|ARBA:ARBA00013203};
DE EC=2.7.12.1 {ECO:0000256|ARBA:ARBA00013203};
GN Name=TESK2 {ECO:0000313|Ensembl:ENSPSIP00000011472.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000011472.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
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).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000011472.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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}.
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DR EMBL; AGCU01047603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01047604; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01047605; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01047606; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01047607; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K7FTW2; -.
DR STRING; 13735.ENSPSIP00000011472; -.
DR Ensembl; ENSPSIT00000011529.1; ENSPSIP00000011472.1; ENSPSIG00000010305.1.
DR eggNOG; ENOG502QTCP; Eukaryota.
DR GeneTree; ENSGT00940000158765; -.
DR HOGENOM; CLU_018577_1_0_1; -.
DR OMA; SNQHLPW; -.
DR TreeFam; TF318014; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
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:SF6; DUAL SPECIFICITY TESTIS-SPECIFIC PROTEIN KINASE 2; 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:UP000007267}.
FT DOMAIN 58..315
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 322..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 603 AA; 67631 MW; BCAFD79C8F4DE725 CRC64;
MDRSKRNSIA GFPPRLERIE DFDGGGGGDG TVSQVGRVWT SSYRALISAF SRLTRLDDFT
CEKIGSGFFS EVFKVRHKTS DQVMALKMNM LSSNRANMLK EIQLMNRLSH PNILRFMGVC
VHQGQLHALT EYINCGNLEQ LLDSNQHLPW MVRVKLAYDI GLGVCYLHYK GIFHRDLTSK
NCLIRHDENG YSAVVGDFGL AEKIPDYSLN VKSEKLPVVG SPFWMAPEVL RDEPYNEKAD
VFSYGIILCE IIARIQADPD YLPRTENFGL DYDAFQHMVG DCPPDFLQLT FNCCNMDPKL
RPSFADIVRT LEEILNRLRN EESERERKLL SPKQKGLNEK AQGVKRLSSL DDKIPPKSPR
PRRNILLSRS QSDIFSRKPF RKINVQDPYY TPSKGAARKV NPFNAREDLK GGKIKFFDMP
SKSVISLVFD LHSPETGSCL KTSQPLSRQV YSTDGQEFSF PPGRRCRSLP VSPELLHKEY
VPFGGLSSMI SKCDSTQLGA EVRQKLLSSS KYGVSEIPPF QAKSHRPDSP LPPEQEDMDC
SDGLESQEEN GFCSSEEGSS PTVLSSCAAS EDMEVEDEPL GGVKETFSVS TFGAEPEMGH
SNG
//