ID M7BN50_CHEMY Unreviewed; 1553 AA.
AC M7BN50;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Serine/threonine-protein kinase LMTK1 {ECO:0000313|EMBL:EMP39301.1};
GN ORFNames=UY3_03474 {ECO:0000313|EMBL:EMP39301.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP39301.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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DR EMBL; KB517139; EMP39301.1; -; Genomic_DNA.
DR STRING; 8469.M7BN50; -.
DR eggNOG; ENOG502QSRI; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 PANTHER; PTHR24417; SERINE/THREONINE-PROTEIN KINASE LMTK1; 1.
DR PANTHER; PTHR24417:SF0; SERINE_THREONINE-PROTEIN KINASE LMTK1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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:0000313|EMBL:EMP39301.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Transferase {ECO:0000313|EMBL:EMP39301.1}.
FT DOMAIN 1..272
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 453..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1241..1358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1413..1466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1338
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1413..1448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1450..1464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1553 AA; 168087 MW; 1102DDF90A124939 CRC64;
MLACLCCKKG DIGFKEFENA EGEDYVTEFS VQGSPATQNG PEVYILPLTE VSLPMAKQPG
RSVQLLKSTD LGRHTLLYLK EIGHGWFGKV FLGEVNSGLS SSQVVVKELK VSASVQDQMQ
FLEEAQPYSD LALRNCLLTA DLTVKIGDYG LSHCKYKGDY FVTADQLWVP LRWIAPELID
EVHGNLLIVD QTKSSNVWSL GVTIWELFEL GNQPYYCYSD RQVLTYAIKE QQLKLPKPQL
KLLLSERWYE VMQFCWLQPE QRPTAEEVHL LLSYLCAKGA TEAEEEFERR WNSMKPNSSS
SSSHRSTEVS SFPLLEQFSA EGFHSDGDDV LTVMETSQGL NFEYKWEPSK AECFQVPAGA
LSPSSAAPYQ DLYYPTSSMG RLSLGVSPSC YECKQQGCPS LHAPSVVPIL GARSPSLSSE
YYIRIEGPSE GRTELDYAMC SYSPNCEYGS PAKGSRWQAK GGQDSGTYDS DNSPTGSLTM
EPLLGPAPPS EGSWEHPDYY PYQCHSKEPP YYQPSPGNGA DHYLLEEEPL EAGSKEWQVP
SFRKNIFQDP LGISPSVNCA YGPPGYEEPH PASLGGRLLE CVGQKVASRT QGSRLDCITL
ELGEESPCGS PRCGSREHVS GLVPEDVNTE VQRQHWTSNS SANNNSSNCP PPPCEPPAND
SWCYRHMITF RGLMAEPLDS VPRDEAQLRD ALQERRSPLV KDLQLALQDQ PLTETHSFCL
DPGQRRTPSN KEDSSSSSSS SPHGLGDWES HDSSAFDLSE DTALAGVSGS RRASGAALPT
DSSAGAAAQT CLDDPSTVSR QAERGEGNHH AQMPQPRGMD PPGPVDMGHA ETGAACQLSE
STSVPAEGAA LLISPGEWAV PYAHTEGNSC ADCTQIPSEA SEAAGKVPGD IAVESGKSIT
SDLDRTPDKT FSSTSFPDMD DCSDEDTTEL TSGVFTDFSG DFVERVDVIP SFKSLQKQVG
TPDSLESLDI PSTASSCEVF SPISYIPSSQ PKALDSGYDT ENYESPEFIL KEPHEPREPE
TFTHLGKSPV GLAAGEGDVV ASEMHLSSSF SAELHGLSEK NPYRDSAYFS DYDTDAERYL
KEDEDSDGSE APDREAGCSQ LDAQDLGRAP SQNSDGEEPP QPRHTPDSPQ GAACTMGTGV
SGVGFSMAGE GVSPREGSVQ AAHPEPELEP EGAARAEETA AGHKPDSDCS RDTTWEECPA
IPSIPAASVP CKSFFLSPVV MSPEGPVLLV LAKAGGEELV QEGLSGPLGE AVAPSSEPEG
PEHPLEEPGV RVAPEGEAQE GPGRALAEEL SIAQGQQLSL PLSLRPAHAE LRPPGPERRE
EPEEEEEEDT EDSDESDEEL RCYNIQEQSE ESEDEPAAVP IVVAESHSAS NLRSLLKMPN
LLSQAFCEDL ERKKKAVSFY DDVTVYLFDQ ESPTRELSDQ TFPEVTAPSP QPVQSNSTSP
TGPVDRLSAS DDSSDGHASE ESSGFEWDDD FPLMPVKSSL MSSLTVTPVM PVSAVPSLPS
LVPVQKQVLP IQFSRFTVSA APVSRFSITH VSDSDIESVG GEDWGWVPSP IGS
//
