ID W5MT98_LEPOC Unreviewed; 715 AA.
AC W5MT98;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=dual-specificity kinase {ECO:0000256|ARBA:ARBA00013203};
DE EC=2.7.12.1 {ECO:0000256|ARBA:ARBA00013203};
GN Name=TESK1 {ECO:0000313|Ensembl:ENSLOCP00000011607.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000011607.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000011607.1}
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; AHAT01015496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01015497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01015498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MT98; -.
DR STRING; 7918.ENSLOCP00000011607; -.
DR Ensembl; ENSLOCT00000011624.1; ENSLOCP00000011607.1; ENSLOCG00000009499.1.
DR eggNOG; ENOG502QTCP; Eukaryota.
DR GeneTree; ENSGT00940000157807; -.
DR HOGENOM; CLU_018577_0_0_1; -.
DR InParanoid; W5MT98; -.
DR OMA; TEENTFC; -.
DR Proteomes; UP000018468; Linkage group LG4.
DR Bgee; ENSLOCG00000009499; Expressed in ovary and 12 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IBA:GO_Central.
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:UP000018468}.
FT DOMAIN 44..307
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 305..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 715 AA; 77627 MW; 015C66E21B3EFEE7 CRC64;
MDRAEPDQES SDPSVIGAAG PNRLRPSSYR ALRSAVSSLA RIDDFYCEKI GSGFFSDVFK
VRHRITGQVM VLKMNKLASN RANMLREVQL MNRLCHPNIL RFLGVCVHEG QLHALTEYIN
GGNLEQLLDS DVYLSWAVRM GLSLDIARGL QYLHSKGIFH RDLTSKNCLV RCENGLFTAV
VGDFGLAEKI PDYSEGVEKQ PLAVVGSPYW MAPEVLRGEL YNEKADVFAY GIILCEIIAR
IQADPDFLPR AEDFGLDVES FQHMVGDCPP CFLQLAVNCC NMSADQRPSF SDIVVELERR
EREKQILKEE NGSPVRPLVA PGSSPARRRS VGLPHDRGLS RSQSDMLPPN SPPLLSGTPA
RVNPFSQRHD LNGGKIKLFD TPSKSVISLT FALPPPPDPF TGSSPTPPDL WQDSRGTPRR
CRSLPCTPEL PRPLRPVVAP TEKQGTPGQQ SRGVMIVSTF QDREGKGQEI PEDVGQMFGP
GHWDEPIRRQ PAVRPQDIGG RGQIAQDLGS GGETTEDSGT PVDLELVSLE MLGEGELETL
CLGEPMDCSS SPDTLEGSVF LEGTPAGQTW LTPPSPSSSI LANGWESPVF NGPPSLPPLP
PLDNNNTTVV VSRPLGWGGN GYHGHTGGPA YPLHGSSTAT LEQDEVISCP GCCLAGFSFP
SACLRPSRRN PPPYKNLNGE AARGLLCRNA KTLGPSQHTP GHSAEPSLPL PEAQT
//
