ID T1KZD3_TETUR Unreviewed; 1374 AA.
AC T1KZD3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN Name=107368772 {ECO:0000313|EnsemblMetazoa:tetur28g01210.1};
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:tetur28g01210.1, 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:tetur28g01210.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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DR EMBL; CAEY01000738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015792140.1; XM_015936654.1.
DR STRING; 32264.T1KZD3; -.
DR EnsemblMetazoa; tetur28g01210.1; tetur28g01210.1; tetur28g01210.
DR GeneID; 107368772; -.
DR KEGG; tut:107368772; -.
DR eggNOG; KOG0579; Eukaryota.
DR HOGENOM; CLU_001965_3_2_1; -.
DR OrthoDB; 2880940at2759; -.
DR Proteomes; UP000015104; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR CDD; cd06611; STKc_SLK_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR022165; PKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR46538; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46538:SF3; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF12474; PKK; 2.
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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 39..297
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 322..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1346..1374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 984..1059
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1239..1273
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 342..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..401
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..773
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1349..1374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1374 AA; 157163 MW; 181A42EA47E2E44C CRC64;
MASFLDRIGK IFKGSSVNEV KRKKICHNIR FNENPEDFWT LVGELGDGAF GKVHKAQHKQ
TGRFAAAKIC ELKGEDELED FTVEIDILSE CCHENIVQLY EAFFFDDKLW ILIEFCEGGA
IDTIMLDLDK PLTEPQIRYV CHEICKGLSF LHKKKIIHRD LKAGNVLLTL DGGVKLADFG
VSAKNTHTLQ KRDSFIGTPY WMAPEVVKCE AFRDNPYDYK ADIWSLGATL IEFAEMNPPN
HEMAPMRVLL KIQKSDPPKL YRPQRWSKEF NNFLERCLTK DPSLRPSADE LLKHPFIAQA
TDSKPIRDLI SEYKAEIVEE VLTTDNEEES SEISSTNPLE SDLQTKKDES RVAANKKRID
YKEAATSESG NEMSNPPNNV KNKPKAPQPP PPPPLPPPTV PSTSLSSSST LASSTTTPSP
SSLSSSTTPS QTQPKSRDVL DRTKIIQSEQ NECNKVPSNS ESVSKEIKES TICNNNSNNK
RPAPKPPCTN SNLDNLAKDK KEDAPYLPYK DNIKNVEKPE KDRVSGTKEK LVTIRPKENE
LDHDLHSLNK NFENESKLAS SDDQGVTRFE LDGPRSDDKS PLANCDVNTA IGEVTVSSDH
STIIDNVHSD QNITDSSHVS IVSIDYGKDL AARSDRDKLE DLVDLMNSAN ETNVNGSSSV
ISSPKRYTPD LVRDEKTPEN DVIIISNDYD NLTDQFSGIS NQDRLHDLPT TTSVVTAFTT
NHHQRRDTTM DNEVDDHVSV KTISSDSSNS GKRIKVNLNL VSDRDETEAG AESSESENNR
NSYVSPRSSI SRQSVNSSST TSNIRNSLHE NVPTSSSSSS SATATITTND PKPSSITDSP
SRLNIHSRML KRESSNTGSC TSFASLNSDK ESRNGTDDDQ NCKRRSEKEN NNTNMKNHLK
KSNFNAAQKK TLTRVRKFVI DGETYTTTTS KVIYGDEDKP RDDHVLRKQE LRELKMLQKL
EQKQFQDLAL KAQLEREQAE KSFAQEMATL LRSYEADLEA LNRTQKNLVE KAEQQQELDL
KFASKKIRMD QEREMKAFKE ALKHEVKLLK AEIDQLPKEK RKDVWRVRKE ELDSDQNERE
RLFMEKLNET HDIAMRRMSE KFRKTIADLE KHFLQQKQVL LRRREAAIWE LEERQMYDKH
QLAKRQLEDI IKLQRIQIFT RHEKELEQLK RMSQRQEDQL LKRQAVERRQ LPKHIRAEMK
ARELMFRESL RCSSANLHNV EDERERIRKW QESEKLRYKA QQQEQENKHR KQLEDLRAAS
EAAIRELEHS QNEKRKSLLN YETIKVKQLK EEHNNEINNW NANLKPRKQK LENEFARQRE
EQERFYGNTN LLNDFATAIE KCNLHGHGHS HHTSSSNSPA STPGVDMPSN NYAL
//
