ID V4AAW4_LOTGI Unreviewed; 491 AA.
AC V4AAW4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN ORFNames=LOTGIDRAFT_139861 {ECO:0000313|EMBL:ESP01144.1};
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:ESP01144.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESP01144.1, 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 -!- 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; KB200538; ESP01144.1; -; Genomic_DNA.
DR RefSeq; XP_009048194.1; XM_009049946.1.
DR AlphaFoldDB; V4AAW4; -.
DR STRING; 225164.V4AAW4; -.
DR EnsemblMetazoa; LotgiT139861; LotgiP139861; LotgiG139861.
DR GeneID; 20234241; -.
DR KEGG; lgi:LOTGIDRAFT_139861; -.
DR CTD; 20234241; -.
DR HOGENOM; CLU_000288_7_39_1; -.
DR OMA; NIDGDRK; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000030746; 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 CDD; cd05040; PTKc_Ack_like; 1.
DR CDD; cd09539; SAM_TNK-like; 1.
DR Gene3D; 4.10.680.10; Cdc42-like binding domain; 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; IPR001452; SH3_domain.
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; SM00326; SH3; 1.
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.
DR PROSITE; PS50002; SH3; 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:UP000030746};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 124..391
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 386..446
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 83..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 491 AA; 55407 MW; 95C0A27B19541E63 CRC64;
MSDGGEDEGQ EWLYELLSEV QLEKFFTKLR DDLQVTRLTH FDYVKVEDLE KIGMGKPAIR
RLLDAIKKKK AMKKKGLLDK ILPGSKSLDK TSSRKLSSTS SSVSPSSPRT NDPSLTCLID
QKFLYIYGKL GNGSFGVVRR GEWVTPTQNK VNVAIKILKN DALAQPGAFE DFVKEVNSMH
TLNHPNLIKL FGVVLSSPLM MVTELAEHGA LLGKLREEGP KLLICTLLEY AIQIANGMGF
LESKRFIHRD LACRNVLLSA NDKVKIGDFG LMRALPSQVD HYVMSEQKKV PFAWCAPESL
KSRQFSHASD MWMFGVTLWE MFTYGQEPWL GLNGSQILQK IDVDNERLPE PAYCPTGLYQ
LILQCWAHKP AERPSFVAIK ESLCEVQPPE VKSLQNYDEK DKLKIEEGDH IIIISGKSEN
FFWNGQNKRT TEIGLFPRQL VDPLRKRASQ DISKPLKNSF IHAGHGDVFG KTWGDPATID
ELVSNISFHL L
//
