HAL5_YEAS7
ID HAL5_YEAS7 Reviewed; 855 AA.
AC A6ZQG7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Serine/threonine-protein kinase HAL5;
DE EC=2.7.11.1;
DE AltName: Full=Halotolerance protein 5;
GN Name=HAL5; ORFNames=SCY_3128;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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-TRK2 potassium transport system in
CC response to potassium starvation. Stabilizes TRK1 in the plasma
CC membrane by preventing its vacuolar sorting and degradation. Also
CC stabilizes other plasma membrane nutrient transporters like CAN1, FUR4
CC and HXT1. May itself be subject to regulation by ARL1 (By similarity).
CC {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; AAFW02000044; EDN63219.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZQG7; -.
DR PRIDE; A6ZQG7; -.
DR EnsemblFungi; EDN63219; EDN63219; SCY_3128.
DR HOGENOM; CLU_016904_0_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
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; Phosphoprotein;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..855
FT /note="Serine/threonine-protein kinase HAL5"
FT /id="PRO_0000333584"
FT DOMAIN 503..837
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 688
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 509..517
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 546
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38970"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38970"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38970"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38970"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38970"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38970"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38970"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38970"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38970"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38970"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38970"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38970"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38970"
SQ SEQUENCE 855 AA; 95456 MW; 29F2D00C6880278C CRC64;
MGDEKLSRHT SLKRARSLSE SIKGLFKPSG ISGSNNAAAP SSRPGQDQAH SHQTARIITS
NVSSPSISPV HSPVLQAAPK HHKLGVPNIA KLSLSPSREP SLNSENEMFS QESFISEKDE
DEANLLERED LQNKKEEKAR AKHVRSKEAY VPHHRYTGGS DEVERQPRER LKNFPQNAGS
SNPANSNANH VLDQENNFSI DAMLDYDEES KLRRRNSLGV RNHSNRTRSR KNSLSTPRSP
PMKNGNDGMN SNATNNVGNG TGNRIYMRGR NQSDSISASS LPKFQEIECK CILDLGHFKV
FENGYHEHSL RVLPIITNNK NVDSGDEKDA DASVNSGDDG DNDSEANMHK QKSVFSLSGL
FKSHKDGNQQ QQQQQQQEEN GEQINLEKAF SIIPSQRFIK SQTVKKSRTS NLKNGNNDEL
MKNDGKNIPQ IVNPNAAVGA EELKLINALS EKIRKGLKSE NTKGNNGEGR SNSNKQEDSD
DTEGKAGTTN DDTSHKPCSQ KYGKYIGVVG AGAYGVVKIC ARCKTAKDVL PYSTYSNGKK
LFFAVKELKP KPGDQIDKFC TRLTSEFIIG HSLSHPHFEA NAMIAGNVSR TTPPKHVFNA
PNILKILDLM EYSNSFVEVM EFCASGDLYS LLTRNNISNE SNNGSSRLIQ TVKEGSGSPL
HPLEADCFMK QLLNGVQYMH DHGIAHCDLK PENILFQPNG LLKICDFGTS SVFQTAWEKH
VHFQSGAMGS EPYVAPEEFI RDAEYDPRLV DCWSCGIVYC TMVMGQYLWK IAIPEKDSLF
KSFLSEIKDD GQFYLFEELR HVSSELNRLR KIALYRTFQV DPTKRITIEQ LLQSSWMRKT
KCCVVYRPLH TKVSK
