HAL5_VANPO
ID HAL5_VANPO Reviewed; 758 AA.
AC A7TGR2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Probable serine/threonine-protein kinase HAL5-like;
DE EC=2.7.11.1;
GN ORFNames=Kpol_2001p30;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480388; EDO18525.1; -; Genomic_DNA.
DR RefSeq; XP_001646383.1; XM_001646333.1.
DR AlphaFoldDB; A7TGR2; -.
DR SMR; A7TGR2; -.
DR STRING; 436907.A7TGR2; -.
DR EnsemblFungi; EDO18525; EDO18525; Kpol_2001p30.
DR GeneID; 5546822; -.
DR KEGG; vpo:Kpol_2001p30; -.
DR eggNOG; KOG0590; Eukaryota.
DR HOGENOM; CLU_016904_0_0_1; -.
DR InParanoid; A7TGR2; -.
DR OMA; VGSEPYV; -.
DR OrthoDB; 872665at2759; -.
DR PhylomeDB; A7TGR2; -.
DR Proteomes; UP000000267; 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; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..758
FT /note="Probable serine/threonine-protein kinase HAL5-like"
FT /id="PRO_0000333583"
FT DOMAIN 442..744
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 595
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 448..456
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 485
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 758 AA; 84413 MW; A746312EA2B498FA CRC64;
MGTVEQKSTH TSPPTSPISR ARSISGSIKS LFKPSSVQNS TPTVSPHESS PPLGNSDNLK
KLVDTKRAEL SSSRGAPPVN VNNVSNLSIN TDVRPADDQP QVKSAKSPII QTPKMAMNIV
PQNIKSVLSS PRQSSSTNDR SSITSATSSV TSANDQKEKN YGSGNGSADD IPIAQLRLSE
QDRAQDYTID NALDTKDKSK PVKRNNSTSA FRGRKDKNFE SSEYEIRSNS LSRIHSTPQN
ESPTVNNIHR GRPYSESISI SSLKHIEQES KCILQVDNFK VFENGMHVHN LKIMPIVKSA
QADAANDHDS NELNKQKSMF SLTSIFKSHK EDSGVDNSPL ENLDNAVSLL PSIKNMAVYN
RKRNISSSTA GTGGSDSDSI PDDLSERMVN PCAAIGAEEL KLINTLSERI NDAILCKSGK
KSSHMLKEKD PDAMTFTQLY GKSMGVVLGH GAYGVVRLFS RNATERDPQY LQTYCNGQKM
FFAVKELKPK SSEPKEKFST RITSEFIIGH SLNHSEKKGG SKYSPNIIRV LDLLEISSGS
FIEVLEFCPS GDLYNILTRK TKNGTALHPL EADCFMKQLL TGVQYMHSHG VAHCDLKPEN
ILFHPNGLLK ICDFGTSCVF QTAWEKNVHF QTGAVGSEPY VAPEEFIHDF NYDPRLVDCW
SCGVVYCSMV LGHYLWKLAV KEKDPLYKAF YEEISSNKEF YVFEEMRHVN HEINRLRKIS
LYKIFQPNPD KRITIDQLLQ SPWMKNTRCC IDYKTISS
