HAL5_CANGA
ID HAL5_CANGA Reviewed; 813 AA.
AC Q6FQH2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Serine/threonine-protein kinase HAL5;
DE EC=2.7.11.1;
GN Name=HAL5; OrderedLocusNames=CAGL0I06248g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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: Protein kinase involved in salt tolerance and pH sensitivity,
CC probably by regulating plasma membrane potential and cation influx.
CC Positively controls the TRK1 potassium transport system in response to
CC potassium starvation. Stabilizes plasma membrane nutrient transporters
CC in the plasma membrane by preventing their vacuolar sorting and
CC degradation (By similarity). {ECO:0000250}.
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; CR380955; CAG60459.1; -; Genomic_DNA.
DR RefSeq; XP_447522.1; XM_447522.1.
DR AlphaFoldDB; Q6FQH2; -.
DR SMR; Q6FQH2; -.
DR STRING; 5478.XP_447522.1; -.
DR EnsemblFungi; CAG60459; CAG60459; CAGL0I06248g.
DR GeneID; 2889154; -.
DR KEGG; cgr:CAGL0I06248g; -.
DR CGD; CAL0132660; CAGL0I06248g.
DR VEuPathDB; FungiDB:CAGL0I06248g; -.
DR eggNOG; KOG0590; Eukaryota.
DR HOGENOM; CLU_016904_0_0_1; -.
DR InParanoid; Q6FQH2; -.
DR Proteomes; UP000002428; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; 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: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..813
FT /note="Serine/threonine-protein kinase HAL5"
FT /id="PRO_0000333580"
FT DOMAIN 477..800
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 27..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 651
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 483..491
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 520
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 813 AA; 90151 MW; 4509EAF0459816F5 CRC64;
MGESNTAAPP SRSRSLSASI KGLFGKNSIS SNEINGKKEA FVQSGTREDQ RYNEEHHLKK
IDTKASVPKK DTQLSPLSAP GSYLKKSTSI ASSLHLNSGK QSVTSSRAQS ISSDGNGFLS
QESFISEEHE DDIDDTTYYD KSTRGFTNLS KEVESYSISR KNSIQQSRKA SVDDNEVDKR
NAHFPDSDTT IDSVLGDKNK NQKVMNQINS ISNISRSGSV PANPPILSSK SRRGSNAMSI
RSPSVRSTAS IVSGNSNSEV ITPSSKPATQ NISEDGNIKK TDNTLKCVIN SKHFKVYENG
FHEHHLPVID LVKGDSTDSL NSSTVSKGTE GIEINRQKSS FSLTGIFKKK NGDKMNELLD
TEPFGNASSL MPTKAFCPRY KTKDGSMIEE PLEQETTHKK IPKIVNPYAA VGSEELKLIT
TLSDKIKKGL KNKDGQSRSG SQSGSASSSL HTSPVASSTS LSSKFHHALV TCSEKYGDPV
GVIGHGTYGV VRVCSRPLLI SDSAPFPSYC NDKKLFFAIK VLKPKDDEQL EKFSTRVTSE
FIIGHSLSRR HKAHALQNKV CPSKRLAHKA QRKLDWECPN ILRVIDLMET NNTFIEVMEL
CPAGDLHSLL VSRSQSGNAI GSLHPLEADC FMKQLLRGVQ YMHDHGIAHC DLKPENLLFH
PNGLLKICDF GTSSVFQTAW EKHVHFQNGV IGSEPYVAPE VFQLGKDYDP RLIDCWSCGI
VYCTMVFGQY LWKIAIENKD SLYASFISQM KDENQFSLFE ELRHVNADLN KLRKNVLYNM
FQTNPEKRIT VDKILHSSWM KHTRCCVSYN HSV
