ID A0A267GZL6_9PLAT Unreviewed; 740 AA.
AC A0A267GZL6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=BOX15_Mlig028886g1 {ECO:0000313|EMBL:PAA91490.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA91490.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA91490.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA91490.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA91490.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAA91490.1}.
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DR EMBL; NIVC01000085; PAA91490.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267GZL6; -.
DR STRING; 282301.A0A267GZL6; -.
DR Proteomes; UP000215902; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48016; MAP KINASE KINASE KINASE SSK2-RELATED-RELATED; 1.
DR PANTHER; PTHR48016:SF29; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 1A; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 3.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00248; ANK; 9.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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}; Reference proteome {ECO:0000313|Proteomes:UP000215902}.
FT DOMAIN 469..736
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 432..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 497
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 740 AA; 82631 MW; 394731C0A96C9DB0 CRC64;
MATQMERKLR AALEAGDSEE LQRLCGEVGS NIELEVGGFD KQDFPFREIL KMPLAHHVAC
KPVSSSCLEL LIDRFGPDCL THGNDRGKTP VHLAAQHQDQ SWMKLVKEKG GRGCLRTVDR
WEQTVAHFAA MNRKSNSCLK WLVKELGSDC LTVPDGWGDT AVHLAAQHQG IESLEWIKRQ
IGTDCFRLKR RWERTAFYFA AQKSDNSNLK WLVKELGSDC LTVPDSRGDT AVHFAALHQG
IELLEWIKRQ IGTDCFRLKG DDDRTAFHFA AEKSDNSNLK WLVKELGSDC LAVPDKFGHT
AVHLAAEHQG IESLEWIKRQ IGTDFFRMKG DDDRTAFHFA AQKSDNSNLK WLVKKLGSDC
LTVPDRLGDT AVHLAARRQP VDSLQFFFDQ IGAEMFSLKN NKGETPADIV ESRWCYTDQS
AKRAWISSTQ RRLEASRPSA GSSAPTAASA GAKKQLDPSF TDWDFILQDN KKQLIGRGGF
GEVYKALTDR NQTVAVKVLP LSGTGQSGKL QKAVELEKRG VEILKRLSHP NILQFLKCEQ
KSDGLYIFTE LVSGHSLFEL MQRQNKPFKE SGVRDFSRQI CSGLNFLHCQ PEGAILHRDI
KSSNVMLTSK GVIKLIDFGL AKEIVGTCGL STGVDPKGTP YFMAPELFMG EGDSIPYSAK
TDVWAFGCTV YELTAMQPPD ANVQQFRIAV LRCGGRAMPR IADGFSAGLK DFYLRCVDYD
PRKRADTAEL LRHSFLSASS
//
