ID A0A3Q3SV82_9TELE Unreviewed; 764 AA.
AC A0A3Q3SV82;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=LIM domain kinase 1 {ECO:0000256|ARBA:ARBA00040667};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000031175.1, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000031175.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001127};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000256|ARBA:ARBA00001127};
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:ARBA00001416};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000256|ARBA:ARBA00001416};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00005843}.
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DR AlphaFoldDB; A0A3Q3SV82; -.
DR STRING; 205130.ENSMAMP00000031175; -.
DR Ensembl; ENSMAMT00000031989.2; ENSMAMP00000031175.1; ENSMAMG00000020983.2.
DR GeneTree; ENSGT00940000156345; -.
DR InParanoid; A0A3Q3SV82; -.
DR OrthoDB; 5474815at2759; -.
DR Proteomes; UP000261640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_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; IPR001781; Znf_LIM.
DR PANTHER; PTHR46485; LIM DOMAIN KINASE 1; 1.
DR PANTHER; PTHR46485:SF7; LIM DOMAIN KINASE 1; 1.
DR Pfam; PF00412; LIM; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00132; LIM; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW ProRule:PRU00125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00125};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 46..108
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 125..211
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 327..602
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 737..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 764 AA; 86982 MW; 00C05CB9AC2D32D8 CRC64;
MSRRDQRFRR GMKGRCCECS CILYRWYYER EGQLYCKKHY WARYGEHCHG CKETIATGLV
MVAGEPKYHP ECFTCTSCQM IIGEGDTYTL VERSKLYCGH CFSQGVVSNV TEASQLTKSP
HIVALVSLPP CLGGHRGLEV VTDISQDKSP IVTVTELDSS VLSPNLLSSV HTGDQILEVN
GIPVHNISPD EIIRVIQDTS RPLQLTIEHN PPSPDDHLHS NNPQDIIGCP GPCAHDKLAA
THKLPSLEEE PSPEEEEHIQ LSLSADQHQG TVGMRSRHIL RSCSIDKCPQ SAGVLSLLSH
RRDMVRSESL RVDPGDRIHR IFRPSELIHG EVLGKGCFGQ AVKVTHQKTG EVMVIKELIS
CDEETQKTFL KEVKVMRCLD HPNVLKFIGL FYKDKRINFV SEYIQGGTLR ETIIKMDQDF
PWNVRVGYAK DIAAGMAYLH SMNVIHRDLN SYNCLVRENQ SVVVADFGLA RLVMEDRNQS
RTASMERPAK GTLSELRKPD RRKRYTVVGN PYWMAPEMIH GKSYDERVDI FSFGIMICEI
IGRVSADPDY LPRTNDFGLN VTAFLQQYLP PQCPLAFMPL AVLGCDIDAE KRPSFSKLEE
WLENLLMHLN IGLPLLSELE QLCRAFWEKH NHHDYFHTHC SPPQRQSPDH MQHSYNEKKH
IEHNQLSQGQ DQNSAPDSHL DTTQQHVCDD QAMSTDYGHS CLSRECENHS QDRNGFETYE
HSNPSRHKHS QLLQVRKQVP GQSNRPGRTH RALWDRSTED SSFL
//
