ID   A0A3B3QYA6_9TELE        Unreviewed;       488 AA.
AC   A0A3B3QYA6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=PX domain containing serine/threonine kinase like {ECO:0000313|Ensembl:ENSPKIP00000010625.1};
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:ENSPKIP00000010625.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000010625.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3B3QYA6; -.
DR   Ensembl; ENSPKIT00000034759.1; ENSPKIP00000010625.1; ENSPKIG00000025263.1.
DR   GeneTree; ENSGT00390000017669; -.
DR   Proteomes; UP000261540; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   PANTHER; PTHR22999:SF40; PX DOMAIN-CONTAINING PROTEIN KINASE-LIKE PROTEIN; 1.
DR   PANTHER; PTHR22999; PX SERINE/THREONINE KINASE PXK; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS50195; PX; 1.
PE   4: Predicted;
FT   DOMAIN          1..93
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   DOMAIN          116..410
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          403..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..442
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..462
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   488 AA;  55297 MW;  002304DB0DBCA9B6 CRC64;
     MAFLDKPSVA KLRLDDTVPL TAVIEASQSL QSHTISGINL PLPPKKLIGN MDREFIAERQ
     KGLQAYLNFI TSHHILSSSE LVKKFLDTNN YSANYTEIAL QQVSMFFRSD PKWEVVEPLK
     DIGWRIRKRY FLVKNKEQPK ERQVLSWVDL GPDKFLSDKD LQSAMKLLPT ISNPYIFPVT
     FASTSESSAL LIRVFSEKGT LRDHICKVKP REPFLKKYCN PKKIQGLELQ QIRTFGRQIL
     EVLKFLHDKG IPYGHLHASN VLIEDDTCKL LDIENSLLGL PSYYRSYITQ FRKINTTESI
     DVYSFGHVLY EMTYGRPPDT VPVDHFPPAP SPSVVSVLHS ILSTEACKTG MPTVGQLLQT
     PLFSDMLLMN SEKLQFKITA KLKDALKIAK ESLEKRLQEE QKVIHQHRRL TRAQSHHGSE
     EEKKKRKILA RKKSRQSAYE NEEDLSAKYN NNSGSGASSP LTSPSSPTPP PMTGKPLGHG
     TLFPTPPC
//