ID A0A5A8CX54_CAFRO Unreviewed; 829 AA.
AC A0A5A8CX54;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 02-APR-2025, entry version 23.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KAA0157535.1};
GN ORFNames=FNF29_00111 {ECO:0000313|EMBL:KAA0157535.1};
OS Cafeteria roenbergensis (Marine flagellate).
OC Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Bicosoecida;
OC Cafeteriaceae; Cafeteria.
OX NCBI_TaxID=33653 {ECO:0000313|EMBL:KAA0157535.1, ECO:0000313|Proteomes:UP000323011};
RN [1] {ECO:0000313|EMBL:KAA0157535.1, ECO:0000313|Proteomes:UP000323011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BVI {ECO:0000313|EMBL:KAA0157535.1,
RC ECO:0000313|Proteomes:UP000323011};
RA Fischer M.G., Hackl T., Roman M.;
RT "Genomes of Cafeteria roenbergensis.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
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:KAA0157535.1}.
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DR EMBL; VLTN01000001; KAA0157535.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5A8CX54; -.
DR Proteomes; UP000323011; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IEA:InterPro.
DR Gene3D; 1.10.2020.20; -; 1.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR Gene3D; 2.30.29.70; Proteasomal ubiquitin receptor Rpn13/ADRM1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR044867; DEUBAD_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR044868; Rpn13/ADRM1_Pru.
DR InterPro; IPR038633; Rpn13/ADRM1_Pru_sf.
DR InterPro; IPR032368; RPN13_DEUBAD.
DR InterPro; IPR038108; RPN13_DEUBAD_sf.
DR InterPro; IPR047173; STRAD_A/B-like.
DR PANTHER; PTHR48014; SERINE/THREONINE-PROTEIN KINASE FRAY2; 1.
DR PANTHER; PTHR48014:SF21; SERINE_THREONINE-PROTEIN KINASE FRAY2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF04683; Rpn13_ADRM1_Pru; 1.
DR Pfam; PF16550; RPN13_C; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51916; DEUBAD; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS51917; PRU; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000323011}.
FT DOMAIN 23..297
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 402..525
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT DOMAIN 692..804
FT /note="DEUBAD"
FT /evidence="ECO:0000259|PROSITE:PS51916"
FT REGION 585..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..620
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..645
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..829
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 829 AA; 86197 MW; 4003986B947020E2 CRC64;
MAAAAASGAL GEADGWPTTA SAYKLGGVIG QGAFAKVYRA ECTSRSETVA VKIIELDKVQ
TPIEVIMNEV RAMALCHHEN VLPLHAAFVS GSDLWLVSPL MSKGSAFWLV RMLNRDSPTR
TPPFIPEPAI KAIMSQALHG LAYLHSQKQI HRDIKAGNIL IGAAGEVMIG DFGVAGWMAD
GLSREDGRRD TFVGTPCWMA PEVMEQSKGY NERADIWSLG ITALELTMGK APYASLPPMQ
VLLETLNKDP PTLESYRSGD VEVPKMSADF HKFVARCLCR NPTKRPSATE LLSDRFIRTA
KLEDLVALLP DVGEVGPDTA AALSDKPGYE AAGMVRPADS KFAEGTTWVL WKGSGSVTIS
AGAEVQPSAV SDDMFEAALS SMAQGRPYPC GAACTSAPMS LDAKAPSFRI KAGLLVPSEV
EGSGGRRFRV TADPRRGYLE ITANQDEGTL SIGWRTRNAQ DTEFSLIIMA DSLRVARVAT
GRDGDRVYSL ISKGSSSRRF FWLQEPDADG DEARIRRLRA MLKSPPQVRA PGMGALAGGM
GMMQAMAAAS RAARGGASPD PHASASELLQ RQLQGLDPAA RQRVMQALQA ARPGGAASVD
APGRGAPPSS ASPGMMPGAS SIGGPGGEAA APASRAEVPA GGSAASHAAS SSAAATAGSA
GDGGAGGAGG DPSADAAHAL VMQAMLAQAR AQAEAPRTAP LPLVLNTSDA LDVATGSDEA
AERLIRRLPE SQRSREQLEA AIRSPQLRQA LSALSAALGT ENYETVFANF DLDPADGADE
LAHGDAVGAF LAALRAKVSR ADGAGPAGDE GDSAGTDDAD EEGDHGEAE
//
