ID G0P3H6_CAEBE Unreviewed; 664 AA.
AC G0P3H6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=CAEBREN_22094 {ECO:0000313|EMBL:EGT43990.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GL380044; EGT43990.1; -; Genomic_DNA.
DR AlphaFoldDB; G0P3H6; -.
DR STRING; 135651.G0P3H6; -.
DR EnsemblMetazoa; CBN22094.1; CBN22094.1; WBGene00160819.
DR eggNOG; KOG0670; Eukaryota.
DR HOGENOM; CLU_000288_5_5_1; -.
DR InParanoid; G0P3H6; -.
DR OMA; IMPIAMA; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24058; DUAL SPECIFICITY PROTEIN KINASE; 1.
DR PANTHER; PTHR24058:SF103; MITOGEN-ACTIVATED PROTEIN KINASE-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008068}.
FT DOMAIN 425..664
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..61
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..104
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 664 AA; 77319 MW; 2D81E533E6E3936D CRC64;
MEVEVKSDGG GATSSEEMAS ESDEKRVRTD SERSKGGEKK KKHKKEKKHK KDKKHKKEKK
HKRDKDAVEE EEPPTKKRGI EEDTRRQHRS RSPASRRRQV SPLRRARSKS GERRDRELKE
RREKERKEQE ELRDRRRQRE KTPPNARNVR DDRRRDDRDR DRRRSPDASR RRDSDRDHRD
RRHRSDEKKN ETVVEWNMDS DSDEEQKKIE EARKRRMQIM AKIEGGETGE NTPHDSSSPR
SDAVGSKKTE DTEDSSADSD SSEDEDDRKV AEARELIKAT RFGSEHGATS GTSTPASFQS
DNDTPTDFFE GLRDKMVHMK DADEHDVDET LKKEKEEEIR EDWQTKLKEQ EKKKAEEEAA
KKKKAEAASE DDDGFDMFAD NEDLPQDSNT IDGHSGAVHD TLKDNWDDQE GYYRVRIGEL
LDTRYRVVGF TGAGVFGNVC RCDDKVKGNT VAVKIIRNNE VMYKTGLREL EVLRKLNEAD
KDDKYHCLRL FRTFKHHNHL CLVFENLSMN LRELLKKYGQ KDGLHLKAVR SYAQQLLLAL
RLLKKLEFVH ADIKPDNILV TESKLTLKLC DFGSAGRVNE QELAPYLVSR FYRAPEIRPE
NSVSQDLTCF RDKSHSFPLK FHEKKIIFGF KNGKTPRNFF SISPAKIQKI PPKTSFPDSK
NNVK
//
