RAG8_KLULA
ID RAG8_KLULA Reviewed; 536 AA.
AC P40230; Q6CR85;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Casein kinase I homolog RAG8;
DE EC=2.7.11.1;
GN Name=RAG8; OrderedLocusNames=KLLA0D11044g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210;
RA Wesolowski-Louvel M.;
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Casein kinases are operationally defined by their
CC preferential utilization of acidic proteins such as caseins as
CC substrates.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
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DR EMBL; X79679; CAA56127.1; -; Genomic_DNA.
DR EMBL; CR382124; CAH00650.1; -; Genomic_DNA.
DR PIR; S47131; S47131.
DR RefSeq; XP_453554.1; XM_453554.1.
DR AlphaFoldDB; P40230; -.
DR SMR; P40230; -.
DR STRING; 28985.XP_453554.1; -.
DR EnsemblFungi; CAH00650; CAH00650; KLLA0_D11044g.
DR GeneID; 2892738; -.
DR KEGG; kla:KLLA0_D11044g; -.
DR eggNOG; KOG1165; Eukaryota.
DR HOGENOM; CLU_019279_1_0_1; -.
DR InParanoid; P40230; -.
DR Proteomes; UP000000598; Chromosome D.
DR GO; GO:0032153; C:cell division site; IEA:EnsemblFungi.
DR GO; GO:0051286; C:cell tip; IEA:EnsemblFungi.
DR GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR GO; GO:0005937; C:mating projection; IEA:EnsemblFungi.
DR GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000902; P:cell morphogenesis; IEA:EnsemblFungi.
DR GO; GO:0006897; P:endocytosis; IEA:EnsemblFungi.
DR GO; GO:0010255; P:glucose mediated signaling pathway; IEA:EnsemblFungi.
DR GO; GO:1904846; P:negative regulation of establishment of bipolar cell polarity; IEA:EnsemblFungi.
DR GO; GO:1903067; P:negative regulation of protein localization to cell tip; IEA:EnsemblFungi.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Lipoprotein; Nucleotide-binding; Palmitate;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..536
FT /note="Casein kinase I homolog RAG8"
FT /id="PRO_0000192860"
FT DOMAIN 77..361
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 26..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 196
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 83..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT LIPID 535
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 536
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 531
FT /note="Missing (in Ref. 1; CAA56127)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 536 AA; 60547 MW; 03A113CF3A155A78 CRC64;
MSITAGPKVT TTAALVNTDR KMNNHHSTQV LHGSGQHGMQ PSGNNVLNGL ANGATGLQSS
ASSTSTRDDS TIVGLHYKIG KKIGEGSFGV LFEGVNMINN VPVAIKFEPR KTDAPQLKDE
YRTYKILSGS EGIPQAYYFG QEGLHNILVI DLLGPSLEDL FDWCGRRFSI KTVVHVAIQM
ITLIEELHDH DLIYRDIKPD NFLIGRPNQP DANMVHLIDF GMAKLYRDPK TKQHIPYREK
KSLSGTARYM SINTHLGREQ SRRDDMEALG HVFFYFLRGQ LPWQGLKAAN NKLKYEKIGE
KKRSTNVYDL SQGLPVQFGR YLEIVRNLGF EETPDYEGYR KLLLSVLDEL GQKLDGEYDW
MKLNGGRGWD LAINKKPNLH GYGHPTPPNE KSKRHRNKFN QVPLAVNNLN GSNVPLQSHS
PLPGGTDLTQ GVSNAPQQPQ QIMSQQQYQQ HTQQRLDPMS YEAYKQQVQQ RYAQQPQPTQ
QKAQKSPNND TSQQQFSQNR QQQPQYQFQQ NQPQNGKVQV ADSNSEKGFF SKLGCC
