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Database: UniProt
Entry: T1KJP1_TETUR
LinkDB: T1KJP1_TETUR
Original site: T1KJP1_TETUR 
ID   T1KJP1_TETUR            Unreviewed;       734 AA.
AC   T1KJP1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=107364991 {ECO:0000313|EnsemblMetazoa:tetur13g00640.1};
OS   Tetranychus urticae (Two-spotted spider mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC   Tetranychoidea; Tetranychidae; Tetranychus.
OX   NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur13g00640.1, ECO:0000313|Proteomes:UP000015104};
RN   [1] {ECO:0000313|Proteomes:UP000015104}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA   Rombauts S.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:tetur13g00640.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) 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=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
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=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR   EMBL; CAEY01000163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015787935.1; XM_015932449.1.
DR   AlphaFoldDB; T1KJP1; -.
DR   STRING; 32264.T1KJP1; -.
DR   EnsemblMetazoa; tetur13g00640.1; tetur13g00640.1; tetur13g00640.
DR   GeneID; 107364991; -.
DR   KEGG; tut:107364991; -.
DR   eggNOG; KOG2464; Eukaryota.
DR   HOGENOM; CLU_377822_0_0_1; -.
DR   OrthoDB; 5491350at2759; -.
DR   Proteomes; UP000015104; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0035173; F:histone kinase activity; IEA:UniProt.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR024604; GSG2_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   PANTHER; PTHR24419; INTERLEUKIN-1 RECEPTOR-ASSOCIATED KINASE; 1.
DR   PANTHER; PTHR24419:SF18; SERINE_THREONINE-PROTEIN KINASE HASPIN; 1.
DR   Pfam; PF12330; Haspin_kinase; 1.
DR   SMART; SM01331; DUF3635; 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.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          420..734
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          152..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..190
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         448
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   734 AA;  83331 MW;  41D7E583F55B4D47 CRC64;
     METVKSPLKA NYCRLPVKSR AEKLFDQFVT KTTFADRSND LNLLSQDSPT NHKEVKTRLK
     RKVTFATYAG DKQRKEVKKK TLVKRKEPTK CTKEAVLEAF MNAGLPDYDE IAALPLNIVV
     LSDANKQPEK YTEISRKQIV KPFMPLLKKI DSASKRKESN PAINIEEPSC ADNEVSSDHI
     EDRENKEEAS TPLPNAKARP KFDDISCINA NNTLDPNMDQ DVSFTTPKVP PPAKKKPWNV
     ADRRGTQLLP PHPVVFDEPL VISNTSIDVS NDQPLNWSTV HSLAKMDDSV HNVFSIDTKA
     NLATKIRESL GSLKSNMNEA EYPRGSVNFY RRSIVDTANV LRALGKSCRT IVREPSRRIT
     RKRKESLAEN QTVNFLVAFD KTIIEDVDVH LPLTTKEKVL ALCNPPQITT FNNVLNHSLM
     KSICKIGEGS YGEVFKSKTE DDKEVVIKVV PLVPTTSVED DLWAQVLPEL VISLTFSDLR
     SGLRNQTPNF VNTFRASCVN GSWPKELVKA WNEYNKLKKS ENDHPDKYGP NCNWLIILLN
     NGGIDLENHK FSSAVESLSV ILQTALSLAA AESEFEFEHR DLHTGNVLIM PCSESMLEYK
     IDGKNIMLPS VGLKVSVIDF TLARMAKDGY TVYDDLSKYE DLFTGTGDYQ FEIYRLMRIA
     NKNNWKVFTP YTNILWVHYL TYKLTKDKKY RSRSKAHHAA MKALKHLHNL LLDYKSTKQF
     VQSPYFNELF SKLS
//
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