HAL5_KLULA
ID HAL5_KLULA Reviewed; 772 AA.
AC Q6CXN5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Probable serine/threonine-protein kinase HAL5-like;
DE EC=2.7.11.1;
GN OrderedLocusNames=KLLA0A06820g;
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 [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 -!- 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. CAMK Ser/Thr
CC protein kinase family. NPR/HAL subfamily. HAL5 sub-subfamily.
CC {ECO:0000305}.
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DR EMBL; CR382121; CAH02892.1; -; Genomic_DNA.
DR RefSeq; XP_451304.1; XM_451304.1.
DR AlphaFoldDB; Q6CXN5; -.
DR SMR; Q6CXN5; -.
DR STRING; 28985.XP_451304.1; -.
DR EnsemblFungi; CAH02892; CAH02892; KLLA0_A06820g.
DR GeneID; 2896336; -.
DR KEGG; kla:KLLA0_A06820g; -.
DR eggNOG; KOG0590; Eukaryota.
DR HOGENOM; CLU_016904_0_0_1; -.
DR InParanoid; Q6CXN5; -.
DR Proteomes; UP000000598; Chromosome A.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..772
FT /note="Probable serine/threonine-protein kinase HAL5-like"
FT /id="PRO_0000333582"
FT DOMAIN 454..758
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 609
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 460..468
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 498
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 772 AA; 85538 MW; 96F6DED61B7EA482 CRC64;
MASSNVDSSE PRISRESSLK RSLSISKSLK GLFKSGGGNA NTGPTTAAAA AAPSSISTPE
VPTLATKDKQ DRLKNLAANK EKELQTSRRG VASPSLSPTR HVSLSNLAKL SLTSRAGTGQ
VDPNVIHETS PLASDEESTD LAFGKRQSSS NRSSSFSNEE QEPNNKYPLL EKLMGDLDEM
VCGSIDTQLS KSPDTVEASS LRRSRSTQRK RLNSFSLRPR ALSNPGQNPN HPVENRERSN
TSSIDLLMSH ESESRAIYKS DQFSVYPDGH HAHHLKVVPI VHDLEQSLNK PKSSFSFSGF
FKTHRTIADD GENLATALSL LPANRFSFHK RLSQIIDEEN GNHNADEELE HNGNNGVDSD
SDADYDNQSS GNSNPSDDES ESDEDGYKGP NKSANVPKIV NEKSVIGANE LKLINQLTEK
IDNGFCLKGS KSDAVSSNEP SSAPRKQHLC EKYGKSIGII GQGAYGVVKL CYKFIDPDEP
DLKDNTYFHD NKLFYAVKEL KPRPDEPPKK FSTRLTSEFV IGLSLSGGNK SRRSSARTHP
NILNVIDLMQ TPNAFYEVME FCPSGDLYSL ITRSSKSDSV LHPLEADCFM KQLLHGIQYM
HAHGVAHCDI KPENLLFLPT GVLKICDFGT SSVFQTAWEK KAHFQTGPAG SEPYVAPEEF
IPKQQYDPRL VDCWSCGIIY CVMVLGHYLW KIAIKGKDSV YDAFLEDMEK HGQYYVFDEM
KHVSPGMNRY RTAALYHIFQ VDPNKRITVD SLLKSSWMKR TKCCVTYPPR PV
