ID A0A4W6BSC5_LATCA Unreviewed; 770 AA.
AC A0A4W6BSC5;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Tyrosine kinase non receptor 2 {ECO:0000313|Ensembl:ENSLCAP00010001354.1};
GN Name=TNK2 {ECO:0000313|Ensembl:ENSLCAP00010001354.1};
OS Lates calcarifer (Barramundi) (Holocentrus calcarifer).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangaria incertae sedis; Centropomidae; Lates.
OX NCBI_TaxID=8187 {ECO:0000313|Ensembl:ENSLCAP00010001354.1, ECO:0000313|Proteomes:UP000314980};
RN [1] {ECO:0000313|Proteomes:UP000314980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sai Rama Sridatta P.;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLCAP00010001354.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A4W6BSC5; -.
DR Ensembl; ENSLCAT00010001415.1; ENSLCAP00010001354.1; ENSLCAG00010000808.1.
DR GeneTree; ENSGT00940000160853; -.
DR Proteomes; UP000314980; 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 CDD; cd00174; SH3; 1.
DR CDD; cd14328; UBA_TNK1; 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 InterPro; IPR015940; UBA.
DR PANTHER; PTHR24418:SF458; 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 Pfam; PF14604; SH3_9; 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.
DR PROSITE; PS50030; UBA; 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 Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000314980};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 121..379
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 382..442
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 722..763
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 84..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..507
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..610
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 770 AA; 86353 MW; 6BAF3AD7C1D888C0 CRC64;
MQCEEGTEWL LELLTDVQLQ QYFLRIRDEL NVTRLSHFDY VKNEDLEKIG MGRPGQRRLW
EAVKRRRALY KRKSWMSKVF PVKRSDADPQ QPLPQGASSS QAPANSESGA SLTCLIRESE
LQLFERLGDG TFGVVRRGEW TGPNGRVLSV AVKCLKAGVL DSDGLDDFIR EVNAMHSLSH
QNLIRLYGIV LTQPMKMVTE LAPLGSLLDR LRKRQGHILI SSLCNYAVQV ACGMAYLEQR
RFLHRDLAAR NVLLSTNETV KIGDFGLMRA LPTHTDQYIM EEGHKIPFPW CAPESLKSRT
FSHASDTWMF GVTLWEMFTH GQEPWLGLNG SQILHKVDVE AERLCKPDDC PQDVYNVMLQ
CWSPKPEDRP TFIALRDFLL ETMPTDMRAL QDFEEEDKLQ IKMNDVITII EGRAEHYWWR
GQNRGTLRVG QFPRHVVTSV AGLSAHDISR PLKHSFIHTG HGDTDPHRSW GHADRIDRLT
RHSRSLPSSP LPMPLAPLGP HRQICLPPPS PSSTSTSSFT SCFEDRPVLP PRSPVPPLRP
SKYNLSSRAT QPQARSSSIS LGDEEDTPPQ IPPRDHAFSQ PGSRSSSPLP LVPPLSSSPV
VLPPPPLSVS PRRASGLLGP LLSSNSTSSS SPPQATSHHT RLAAPGPSTY SSTSLLDPLT
FREGRGLSSL IDSSQSSSPT PLPERPAFLE RCVSDIKYSV HGVTLEECQA ALQSHNWIIP
QAINHLKVEQ LFRLGLRSRA ECEELLQRCQ WNLEQASSIM LDTYGPHRNR
//
