ID A0A3B3RAK2_9TELE Unreviewed; 521 AA.
AC A0A3B3RAK2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000015712.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000015712.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3B3RAK2; -.
DR STRING; 1676925.ENSPKIP00000015712; -.
DR Ensembl; ENSPKIT00000040185.1; ENSPKIP00000015712.1; ENSPKIG00000002321.1.
DR GeneTree; ENSGT00950000182988; -.
DR OrthoDB; 460351at2759; -.
DR Proteomes; UP000261540; Unplaced.
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 CDD; cd06655; STKc_PAK2; 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 InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR035064; STK_PAK2.
DR PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR PANTHER; PTHR48015:SF22; SERINE_THREONINE-PROTEIN KINASE PAK 2; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00220; S_TKc; 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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}.
FT DOMAIN 70..83
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT DOMAIN 246..497
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 521 AA; 57513 MW; C87C024BFFEF4211 CRC64;
MSDNGEMEDK PPAPPVRMSS TIFSSGGKDP LSANHSSKPL PSVPEERKRN KIISIFGVEK
GSKKKERPEI SPPSDFEHTI HVGFDAVTGE FTGMPEQWAR LLQTSNITKS EQKKNPQAVL
DVLKFYDSTG NNKQKYLSFS SEKDGFPSGA QPPAKKGTEP SVAQSQDLDD DDEEAPPPVV
APRPEHTKSV YTRSVIDPIP LPTTSPEGDA ASRAADKQKK KGKMTDEEIM DKLRTIVSIG
DPKKKYTRYE KIGQGASGTV FTAIDVATGQ EVAIKQINLQ KQPKKELIIN EILVMKELKN
PNIVNFLDSF LVGDELFVVM EYLAGGSLTD VVTETCMDEA QIAAVCRECL QALEFLHANQ
VIHRDIKSDN VLLGMDGSVK LTDFGFCAQI TPEQSKRSTM VGTPYWMAPE VVTRKAYGPK
VDIWSLGIMA IEMVEGEPPY LNENPLRALY LIATNGTPEL QNPEKLSPIF RDFLNRCLEM
DVEKRGGGKE LLQHPFLKLA KPLSSLTPLI LAAKEAMKSN R
//
