ID H3AAW0_LATCH Unreviewed; 1069 AA.
AC H3AAW0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, 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};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000006781.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000006781.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AFYH01138566; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01138567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01138568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3AAW0; -.
DR STRING; 7897.ENSLACP00000006781; -.
DR Ensembl; ENSLACT00000006838.1; ENSLACP00000006781.1; ENSLACG00000006018.1.
DR eggNOG; KOG0199; Eukaryota.
DR GeneTree; ENSGT00940000165248; -.
DR HOGENOM; CLU_000288_7_39_1; -.
DR InParanoid; H3AAW0; -.
DR OMA; KSWMSKX; -.
DR TreeFam; TF316643; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000006018; Expressed in post-anal tail muscle and 5 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd05040; PTKc_Ack_like; 1.
DR CDD; cd09539; SAM_TNK-like; 1.
DR CDD; cd14274; UBA_ACK1; 1.
DR CDD; cd14328; UBA_TNK1; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR030220; Ack1_UBA_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR021619; Mig-6.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR049587; TNK-like_SAM.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR14254; GENE 33 POLYPEPTIDE; 1.
DR PANTHER; PTHR14254:SF6; NON-SPECIFIC PROTEIN-TYROSINE KINASE; 1.
DR Pfam; PF11555; Inhibitor_Mig-6; 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; SSF46934; UBA-like; 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|PIRSR:PIRSR630220-
KW 2}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR630220-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 121..380
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 498..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 247
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR630220-1"
FT BINDING 127..135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630220-2"
FT BINDING 153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630220-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1069 AA; 120417 MW; BC880619A5EA9578 CRC64;
MQSDEGTEWL LELLTEVQLQ QYFLRIRDDL NVTRLSHFDY VKNEDLEKIG MGRPGQRRLW
EAVKRRKALC KRKSWMSKVF SGKRPEMEFL PQPATTFRKA STPPPVEGQQ ALTCLISEKD
ITLFEKLGDG SFGVVKRGEW CAPTGKIISV AVKCLKTDML NQPDALDDFI WEVNAMHSLD
HPNLIRLYGV VLTHPMKMVT ELAPLGSLLD RLRKNQAHFL ISTLCLYAIQ IANGMAYLES
KRFIHRDLAA RNILLASSDL IKIGDFGLMR ALPKNDDHYV MQEHRKVPFA WCAPESLKTR
TFSHASDTWM FGVTLWEMFT YGQEPWVGLN GSQILHKIDK EGERLPRPED CPQDIYNVML
QCWAHKPEDR PTFMALRDFL VEAQPTDMRA LQDFEEPDKL LIQMNDVITV IEGSQGNVKF
QAFPTLFFMV RPFRRTPVTP PPRLNQRHVY APLSVIQQSL NDSDTKKSCF HFSFRLYLGN
PMDPPDVLGV DIHASRPTQL PGRAKKEPPP RPPQPAILVQ KSTYDPVADE EDATSMGLKK
LSMKKQGMVK GLKLAKPSAR VFATKIIEQQ PPFGNKGTGF QMGEVTLIDF GEELMPSTPS
PVVEATAPSL AKLATDACSL LDKTPPQSPT RALPRPLHPT PVVDWDSKPL PPPPAYDDVA
QDEEDIEVSS INSPEFVPVE EKTKYGTVHF QAAKEKKANI YAYVHEGEKA DKPKVEDILF
LPSKQAKQAN FSQTSEIFEE LQQECMKRLN VPIITSQAST PSPSASVANL TLSITDEKPQ
IPPRIPIPPR PMKRNDHGRW SGDLSPASGG EEDRPPQIPP RDPLSQPTSR TPSPMSLQVG
SPQQRSRSYL STSPGKLMPT TQSFASDPKY ATPKVITAQG KDPSAKGPCI LPIVKDGKKV
SSTHYYLLPE RPSYLDKYEK FFKDTENLDE VSAKRIVTTA TVRPMVHQTD FKGNFSSNNS
NPKPRCTIKT TCSLQKIMME GSENVRPSEK IKLVQENVHG VTIEECQAAL QNHGWNIEKA
IQYLKVEQLF CLGLKTRGEC HKILEMFDWN LQLASSHLLD PFGTSRVNY
//