ID V4BFM8_LOTGI Unreviewed; 393 AA.
AC V4BFM8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 08-NOV-2023, entry version 38.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
DE Flags: Fragment;
GN ORFNames=LOTGIDRAFT_91758 {ECO:0000313|EMBL:ESP04677.1};
OS Lottia gigantea (Giant owl limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESP04677.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESP04677.1, ECO:0000313|Proteomes:UP000030746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC {ECO:0000256|RuleBase:RU000304}.
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DR EMBL; KB199652; ESP04677.1; -; Genomic_DNA.
DR RefSeq; XP_009044576.1; XM_009046328.1.
DR AlphaFoldDB; V4BFM8; -.
DR STRING; 225164.V4BFM8; -.
DR EnsemblMetazoa; LotgiT91758; LotgiP91758; LotgiG91758.
DR GeneID; 20252927; -.
DR KEGG; lgi:LOTGIDRAFT_91758; -.
DR CTD; 20252927; -.
DR HOGENOM; CLU_000288_5_15_1; -.
DR OMA; KNANEHE; -.
DR OrthoDB; 3122824at2759; -.
DR Proteomes; UP000030746; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR CDD; cd14211; STKc_HIPK; 1.
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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24058; DUAL SPECIFICITY PROTEIN KINASE; 1.
DR PANTHER; PTHR24058:SF17; HOMEODOMAIN INTERACTING PROTEIN KINASE, ISOFORM D; 1.
DR Pfam; PF00069; Pkinase; 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.
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}; Kinase {ECO:0000256|RuleBase:RU000304};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000030746};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304};
KW Transferase {ECO:0000256|RuleBase:RU000304}.
FT DOMAIN 1..328
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ESP04677.1"
FT NON_TER 393
FT /evidence="ECO:0000313|EMBL:ESP04677.1"
SQ SEQUENCE 393 AA; 45471 MW; 5F887F43FC285965 CRC64;
VLEFLGRGTF GQVVKCWKKG TNEIVAIKIL KNHPSYARQG QIEVQILKQL SQENADDYNF
VRTYEYFQHQ NHACLVFEML EQNLYDFLKQ NKFQPLPLKY IRPVTQQVLT ALLKLKDLGL
IHADLKPENI MLVDPVRFPY RVKVIDFGSA SQVTKAVPST YLQSRYYRAP EILLGLPFCE
AIDMWSLGCV IAELFLGWPL YPGSSEYDQI RYISQTQGLP AEHMLSSATK TSRFFMRDNT
DTSYPFWRLK SPEEHEAETK IKSKEARKYI FNCLDDIGQI NVPTDLEGSE LLAEKVDRRE
FIDLLKRMLI LDQERRILPI DALNHPLISM KHLMDYPHCN ITKQSVQSME ICRRPRQSSV
YDVNQNSNGM MTNVVPSSNG NFTVTFNNQI NAL
//
