ID T1JVC9_TETUR Unreviewed; 978 AA.
AC T1JVC9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
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:tetur02g04140.1, 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:tetur02g04140.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636}.
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DR EMBL; CAEY01000792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1JVC9; -.
DR STRING; 32264.T1JVC9; -.
DR EnsemblMetazoa; tetur02g04140.1; tetur02g04140.1; tetur02g04140.
DR eggNOG; KOG0578; Eukaryota.
DR HOGENOM; CLU_015718_4_3_1; -.
DR Proteomes; UP000015104; Unassembled WGS sequence.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01093; CRIB_PAK_like; 1.
DR Gene3D; 3.90.810.10; CRIB domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
DR InterPro; IPR002452; Alpha_tubulin.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033923; PAK_BD.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR000217; Tubulin.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR PANTHER; PTHR48015:SF35; SERINE_THREONINE-PROTEIN KINASE PAK; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00091; Tubulin; 1.
DR PRINTS; PR01162; ALPHATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000015104}.
FT DOMAIN 235..248
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT DOMAIN 703..954
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 94..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..498
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 732
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 978 AA; 107880 MW; 4C57883E408CC6B9 CRC64;
MRECISIHVG QAGVQMGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGSGK
HVPRTVYVDL EPTVVDEVRT GTYHYSIHFS SPAQLSDTME DKPPQPPVRL TSQQNNHSKL
CNSRECHFVN HSNPASPHHY PHNYQTVNYA HQQSLYHTPL HQPYNSNSSV PVDLRPLPKE
PEKGNSVASK VIKKGLKVKP SKSHKNDKKD HNVNFGVHGS SNHNQSSSFV HKPFISSPTN
FEHTIHVRFD AHTGEFTGMP ESWNKLLQHS NISKIEQKNN PQAVLDVLNW YDSSNRETIG
NLPKYMTINR SLDVPQPNYV PDNKYVKKNA SCISVSTTST MLVSSNSASS CTSDAGLGSG
NLSATSSPVH SLIKISPSSN GSSCTPRESL QEPLSCTSSL SSNPPSTPEE DNTKSHSTQH
QIHQQNISHV HHSNYPIQSN LTTIGDKSSG SSSCNSSSSR DSNNIDDPHQ RSSPIDENHA
QTTPPSHPPP PPPPTRPEKT KSIYTRPICK SKFPGLTNSP VSVSNINNTT PSLNVSANNS
VPSQPKEVNS PTTPLATSHL NKPPTTPKNS DNNLNIHPTI DETIDAVNNL SIDPKPGHNN
NLTVLNNSVN KTKTITKECV NNNNINIAIN NNNNNNNINN LNNNKQTNLP NNIKSADKVN
ANNLGKLGKP DKNGLLEKKK MSDEEIMDKL RSIVTIGDPY RKYSKIEKIG QGASGVVYTA
IEVSTGMEVA IKQMKLVQQP NQELIINEIL VMKENKHPNI VNYLDSYLVG DELWVVMEYL
PGGSLVDVVT ETCMDEGQIA AVLREILQAL EFLHSNDVIH RDIKSDNILL GMDGSVKLTD
FGFCAQISPE HNKRTTLVGT PYWMAPEVVN KKQYGPKVDI WSLGILAIEM IEGEPPYLNE
HPLRALYLIA TTGKPEIKDK DKLSVLFQEF LDKCLEVDVD KRWSSSELLK HPFLKLGRPL
SSLHPLILAA KQAANTQP
//
