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Database: UniProt
Entry: H9GCQ5_ANOCA
LinkDB: H9GCQ5_ANOCA
Original site: H9GCQ5_ANOCA 
ID   H9GCQ5_ANOCA            Unreviewed;       605 AA.
AC   H9GCQ5;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 3.
DT   24-JAN-2024, entry version 70.
DE   RecName: Full=LIM domain kinase 1 {ECO:0000256|ARBA:ARBA00040667};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000007341.4, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000007341.4}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000007341.4};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000007341.4}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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 {ECO:0000256|ARBA:ARBA00004496}.
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; H9GCQ5; -.
DR   STRING; 28377.ENSACAP00000007341; -.
DR   Ensembl; ENSACAT00000007497.4; ENSACAP00000007341.4; ENSACAG00000007383.4.
DR   eggNOG; KOG1187; Eukaryota.
DR   GeneTree; ENSGT00940000156345; -.
DR   HOGENOM; CLU_000288_7_23_1; -.
DR   InParanoid; H9GCQ5; -.
DR   TreeFam; TF318014; -.
DR   Proteomes; UP000001646; Unplaced.
DR   Bgee; ENSACAG00000007383; Expressed in adrenal gland and 12 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0051496; P:positive regulation of stress fiber assembly; IBA:GO_Central.
DR   CDD; cd09464; LIM2_LIMK1; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   CDD; cd14221; STKc_LIMK1; 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; 2.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00132; LIM; 2.
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}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          48..110
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          131..219
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          300..562
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          224..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          260..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..278
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         329
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   605 AA;  68681 MW;  4FC60AA1B6203DBE CRC64;
     MLSAVLKGSR FLTAGAKCSE CGTSLSHQYY EKDGRLYCKK DYWAHFGEMC HGCSEQITKG
     LVMVAGEQKY HPECFSCLNC RVFIGDGDTY ALVERSKLYC GRCYYQMVVT PVMDQLLPES
     PGPRIPHTVT LVSIPASSEG KRGFSISIDQ HSSSEHAHTV RVRELDPDCI SPDMKNSIHV
     GDRILEINGT PIRHVPLDEI DLLIQETSRL LQLTIEHDPH EVLESSPLSE LRSPLRSPSR
     TPCPDPAAIR QRTIMRSCSI DKSPCSSTLG SPASQRKDIG RSESLRVVSR HHRIFRPSDL
     IHGEVLGKGC FGQAIKVTHR ETGEVMVMKE LIRFDEETQR TFLKEVKVMR CLEHPNVLRF
     IGVLYKDKRL NFITEYIKGG TLRGIIKNMD SQYPWTQRVS FAKDIASGMA YLHSMNIIHR
     DLNTHNCLVR ENKSVVVADF GLARLMVDEK NQLASLKKPD RRKRYTVVGN PYWMAPEMIN
     GRSYDEKVDV FSFGIILCEI IGRVSADPDY LPRTLDFGLN VRGFLDRYCP PNCPPSFFPI
     AVRCCDLDPE KRPSFCRLEQ WLEALRMHLA MALPLSPQLE QLDQAFWETH RRADGGLSVH
     PEVSE
//
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