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Database: UniProt
Entry: I3JLM2_ORENI
LinkDB: I3JLM2_ORENI
Original site: I3JLM2_ORENI 
ID   I3JLM2_ORENI            Unreviewed;       657 AA.
AC   I3JLM2;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000009766.2, ECO:0000313|Proteomes:UP000005207};
RN   [1] {ECO:0000313|Proteomes:UP000005207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Broad Institute Genome Assembly Team;
RG   Broad Institute Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSONIP00000009766.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; I3JLM2; -.
DR   STRING; 8128.ENSONIP00000009766; -.
DR   Ensembl; ENSONIT00000009772.2; ENSONIP00000009766.2; ENSONIG00000007751.2.
DR   eggNOG; KOG0578; Eukaryota.
DR   GeneTree; ENSGT00940000158656; -.
DR   HOGENOM; CLU_000288_26_6_1; -.
DR   InParanoid; I3JLM2; -.
DR   OMA; QENGDPQ; -.
DR   TreeFam; TF105352; -.
DR   Proteomes; UP000005207; Linkage group LG14.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01093; CRIB_PAK_like; 1.
DR   Gene3D; 3.90.810.10; CRIB domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000095; CRIB_dom.
DR   InterPro; IPR036936; CRIB_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR033923; PAK_BD.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR   PANTHER; PTHR48015:SF17; SERINE_THREONINE-PROTEIN KINASE PAK 4; 1.
DR   Pfam; PF00786; PBD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00285; PBD; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005207}.
FT   DOMAIN          12..25
FT                   /note="CRIB"
FT                   /evidence="ECO:0000259|PROSITE:PS50108"
FT   DOMAIN          387..638
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          94..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..145
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..217
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..273
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..348
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         417
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   657 AA;  73651 MW;  B29083D72D18F8C6 CRC64;
     MFAKKKKSRI QISAPSNFEH RVHTDFDEQE QKFVGLPRQW QSLIEDTAQR PKPFIDATII
     TTVEPRKTIV RGSRMGTESL TWLLDEFDTM SVTRSNSLRR GSPPTHPRRD SSSSGGGGGQ
     ENGDPQYRHY SDRQDRDRPR QDQQSGGDPR HQGQRGVRPP QADEVIQGRP QQQPRGQEPS
     RAQRDRQAPP PPPHRDRQPR DRDQRDQPGD HRPKSSYVAR DGSPQSPRDK RPLSGPNIRT
     PNLPMSEGVM KTAQQASRPF NTYPRTESDG GRSPTGQVGV GRHHESSPQN GPSSGSVRGS
     SGSKPPISHP HPHHSSHPIL APESSQLPHT PHPNVPAPRP PVPSGPAASG APPQGRSPQR
     EPQRVSHEQF RAALQMVVDP GDPRTYLDHY IKIGEGSTGI VCIATMKNTG KLVAVKKMDL
     RKQQRRELLF NEVVIMRDYH HENVVEMYNS YLVGDELWVV MEFMEGGALT DIVTHTRMNE
     EQIATVCLSV LKALSVLHTQ GVIHRDIKSD SILLTHDGRV KLSDFGFCAQ VSKEVQRRKS
     LVGTPYWMAP ELISRLPYGP EVDIWSLGIM VIEMVDGEPP YFNEPPLKAM KMIRDNLPPK
     LKNLHKVSPL LKSFLDRMLV RDPAQRATAS ELLKHPFLSK GGPPSCIVPL MRQNRMK
//
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