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Database: UniProt
Entry: K7FTW2_PELSI
LinkDB: K7FTW2_PELSI
Original site: K7FTW2_PELSI 
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
//
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