ID A0A075B4E3_ROZAC Unreviewed; 426 AA.
AC A0A075B4E3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=O9G_003438 {ECO:0000313|EMBL:EPZ36280.1};
OS Rozella allomycis (strain CSF55).
OC Eukaryota; Fungi; Fungi incertae sedis; Cryptomycota;
OC Cryptomycota incertae sedis; Rozella.
OX NCBI_TaxID=988480 {ECO:0000313|EMBL:EPZ36280.1, ECO:0000313|Proteomes:UP000030755};
RN [1] {ECO:0000313|EMBL:EPZ36280.1, ECO:0000313|Proteomes:UP000030755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSF55 {ECO:0000313|EMBL:EPZ36280.1,
RC ECO:0000313|Proteomes:UP000030755};
RX PubMed=23932404; DOI=10.1016/j.cub.2013.06.057;
RA James T.Y., Pelin A., Bonen L., Ahrendt S., Sain D., Corradi N.,
RA Stajich J.E.;
RT "Shared signatures of parasitism and phylogenomics unite Cryptomycota and
RT microsporidia.";
RL Curr. Biol. 23:1548-1553(2013).
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DR EMBL; KE560603; EPZ36280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A075B4E3; -.
DR STRING; 988480.A0A075B4E3; -.
DR EnsemblFungi; EPZ36280; EPZ36280; O9G_003438.
DR HOGENOM; CLU_000288_26_6_1; -.
DR OMA; KEGWISY; -.
DR OrthoDB; 460351at2759; -.
DR Proteomes; UP000030755; Unassembled WGS sequence.
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 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 PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR PANTHER; PTHR48015:SF6; SERINE_THREONINE-PROTEIN KINASE CLA4-RELATED; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00285; PBD; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000030755}.
FT DOMAIN 174..407
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 74..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 426 AA; 48295 MW; A4D9CD1A625B0E3A CRC64;
MYRGDTIRAN RVGISKISNV KRNVHVGFDE ASGEFTNLPK QWQDILIGSK LTKEDMQKDP
QAVLDVLNYY AGNNDETQTP EKVEKHKISP PTPHRPKLPQ KSQYPMKEVI FIKPVPPIND
IPSSRKNVDS RISENDELPS PSIVADRRVS ILRDDEVLDV LKEICSRDDP NKFYAQMKRI
GQGASGSVYV ARSEATGKRV AIKKIDLKEQ PKKNLSVNEI ITMKACRHEN IINMFETYLV
NQILWIVMEY MDAGSLTDLI DSQSQLTEPE ISTICFETLK GLEYLHIIFN KADFGFCAQL
SAEKAKRQTL VGTPYWMSPE VVRQQKYGAK VDIWSLGIMA IEMLEGEPPY LDEEPLKALY
MIASNGKPKL RDSSRPSELF RSFLDACLTV DVSKRPNATE LLAHPFLKLS APKSSIKNLI
QRKNII
//
