ID E3MAJ9_CAERE Unreviewed; 1339 AA.
AC E3MAJ9;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN Name=Cre-kin-25 {ECO:0000313|EMBL:EFO97406.1};
GN ORFNames=CRE_16705 {ECO:0000313|EMBL:EFO97406.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; DS268432; EFO97406.1; -; Genomic_DNA.
DR RefSeq; XP_003106800.1; XM_003106752.1.
DR STRING; 31234.E3MAJ9; -.
DR EnsemblMetazoa; CRE16705.1; CRE16705.1; WBGene00070106.
DR eggNOG; KOG0199; Eukaryota.
DR HOGENOM; CLU_009070_0_0_1; -.
DR InParanoid; E3MAJ9; -.
DR OMA; FLESKHC; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0035194; P:regulatory ncRNA-mediated post-transcriptional gene silencing; IEA:EnsemblMetazoa.
DR CDD; cd09539; SAM_TNK-like; 1.
DR CDD; cd00174; SH3; 1.
DR Gene3D; 4.10.680.10; Cdc42-like binding domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR015116; Cdc42-bd-like.
DR InterPro; IPR037085; Cdc42-bd-like_dom_sf.
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; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR049587; TNK-like_SAM.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24418:SF294; NON-SPECIFIC PROTEIN-TYROSINE KINASE; 1.
DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR Pfam; PF09027; GTPase_binding; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 107..369
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 456..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1239..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1097
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1339 AA; 146126 MW; 1DCE64F11DC25A88 CRC64;
MASTSGVLVD DNVLELLRKA QLDDYTNKFV FIFNVRRFDH FSHVRDKDMQ SIGMQQQQIR
QFHEQVLKMS REMWNRSDPK QVFVASDQST PNQSSIDEKA LIPNEQIKLF ELLGEGSFAV
VKRGTWTQSN GQRVEVAVKI LRDISPNIMD DLRVEASHLL KLQHPSLIRL YGIVRQPAMM
VFELCEGGSL LDRLRDDKKP IPLVSRLHDY CSQIAKALQF LESKHCVHRD VAARNILLAR
DEKTVKICDF GLMRALKENE QMYTMAPQKK VPFAWCPPEA LRHRKFSHAS DVWSYGVTIW
ELFTFGEEPW VGCRAIDVLK NIDAGERLEK PKYCSNRIYQ IMTDCWKSNP AERCKFSAIR
EDLKAAMFLD ATARETYNSI QPGALILTKG DEVVVVENTG QDWFGQNKKN QKFGTFPRSV
VFAQTNHAVA AASAVTPQKV PTAPTIRMRP EQSLQPTPLA YTSKPLNNNT KTSLNDRTSR
ISMPVAGSFI HTGHGDPLGG QSWGNPSTID DTYLKNPVKG VPLSRFVLMS FPSVNQPHVF
SMSNGAQVIA SKELLTNGGR STHTPAAPST SDMSKIRGLS LDLPEYDDFD RAFDDGFSPS
KIELPRDFGN DSIISNGSNF RSEDLSSTIL IKGEERRDPT FDIRGNVLKP TPIAPVQVPS
TTHAPRPILL APTSTGVMSM QLPDGFITPQ PHGSAVVVDK PDPLRNQPRH VNSAGSRLDS
MAQPNIPTHF TQQSQKQSMP TNLIPELQHR LNAGSDMMRP RPASSIGLQN NAMDSYNPQM
NRPFSVVNVP SVPIVPQQPA SIPCLVPTPA PIPAHSSAPK TSVNGQQQNP LQKALTEELR
GNLNRRPTSA GASTTSNGAS NLRNGVNTSI PPTTQPSLQP QKLPTAVVQK PFQPQQVKLP
PPTQTMPSTS APITTVPSVV STNVPVQQVS TPRPMTASTA PIKKTSVPAS TVLGSSAPTT
TASTSSSQNV VTRRPTQTIT MSDEERRSRI IQDVASALPA PSALLLGSQS AASLPSAAVP
AATSSGSSNR DRPGRTTPPS QPQVTMPPKK SSEPVLSTEV LQPTRLPSAA SSVPKPVSQP
VPQAIQQPVR NPSPPVINTN RQSTFVDKKQ TIPSHSTNVP LFNITNSSNM YPQLNSYPNY
GNGYQPYGYG MNYHSGGIQY NITFLVFCII VGYPGYTGYT PYTSGMGQLA LTHNAVSSLP
PLVPSENTGT AQPLDDAAIM ELLGEQNRQA AAAQAAAHTS RVASSAPTSA PVTAPSTARS
NDLSMADRME VLYKEADFTD SGNCDTMVMR CNGDTEMALK LLKQNHLVQI GVAKNEMAAL
QALESRQYDL TAAANLLLG
//
