ID A0A2U9R7L5_PICKU Unreviewed; 830 AA.
AC A0A2U9R7L5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Serine/threonine-protein kinase RAD53 {ECO:0000256|PIRNR:PIRNR000661};
DE EC=2.7.12.1 {ECO:0000256|PIRNR:PIRNR000661};
GN ORFNames=C5L36_0D00560 {ECO:0000313|EMBL:AWU77317.1};
OS Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=4909 {ECO:0000313|EMBL:AWU77317.1, ECO:0000313|Proteomes:UP000249293};
RN [1] {ECO:0000313|EMBL:AWU77317.1, ECO:0000313|Proteomes:UP000249293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS573 {ECO:0000313|EMBL:AWU77317.1,
RC ECO:0000313|Proteomes:UP000249293};
RA Douglass A.P., Offei B., Braun-Galleani S., Coughlan A.Y., Martos A.,
RA Ortiz-Merino R.A., Byrne K.P., Wolfe K.H.;
RT "Population genomics shows no distinction between pathogenic Candida krusei
RT and environmental Pichia kudriavzevii: One species, four names.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Controls S-phase checkpoint as well as G1 and G2 DNA damage
CC checkpoints. Phosphorylates proteins on serine, threonine, and
CC tyrosine. Prevents entry into anaphase and mitotic exit after DNA
CC damage via regulation of the Polo kinase CDC5.
CC {ECO:0000256|PIRNR:PIRNR000661}.
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=2.7.12.1; Evidence={ECO:0000256|PIRNR:PIRNR000661};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR000661}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CHEK2 subfamily. {ECO:0000256|ARBA:ARBA00005575,
CC ECO:0000256|PIRNR:PIRNR000661}.
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DR EMBL; CP028776; AWU77317.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9R7L5; -.
DR STRING; 4909.A0A2U9R7L5; -.
DR VEuPathDB; FungiDB:C5L36_0D00560; -.
DR OrthoDB; 2045964at2759; -.
DR Proteomes; UP000249293; Chromosome 4.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0009202; P:deoxyribonucleoside triphosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.200.20; -; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000253; FHA_dom.
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 InterPro; IPR016256; Ser/Thr_kinase_Rad53.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR24347:SF412; CALCIUM_CALMODULIN DEPENDENT PROTEIN KINASE I; 1.
DR PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF00498; FHA; 2.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000661; Ser/Thr_PK_RAD53; 1.
DR SMART; SM00240; FHA; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 2.
DR PROSITE; PS50006; FHA_DOMAIN; 2.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000661};
KW Cell cycle {ECO:0000256|PIRNR:PIRNR000661};
KW DNA damage {ECO:0000256|PIRNR:PIRNR000661};
KW Kinase {ECO:0000256|PIRNR:PIRNR000661};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000661}; Nucleus {ECO:0000256|PIRNR:PIRNR000661};
KW Reference proteome {ECO:0000313|Proteomes:UP000249293};
KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000661};
KW Transferase {ECO:0000256|PIRNR:PIRNR000661};
KW Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR000661}.
FT DOMAIN 114..178
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 237..511
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 655..736
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT REGION 24..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 358
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000661-50"
FT BINDING 243..251
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000661-51"
FT BINDING 266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000661-51,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 830 AA; 93786 MW; C1F544C7A6E0A84E CRC64;
MESKRSPLKQ SRIENIAIKS TSISSNKLMM TKPTMKKPYT SEPKGPVDTV TQPTQPSSYN
PRTDPIEQDL IEQGILCRLI GRTVDESFQI DVKFKDAQRK SVLDDGVENI QQEWTFGRNG
NTCCYQLPVH STRISNKHFR LWMNLDSKNT SAGKYTKDNN IMIQDLSTNG TWLNNSKLAP
KQNFILTQGD EIAVGIGVEQ DVIRFIVHFP NPSIQGEEQD ATHTDYEEEA GINKDFIIRD
EIVGSGAFAT VKKAIERSTG ITFAAKIISK KKALGGLDGV ARELQILKKL NHPGIVRLKA
SYEDDDNYYL VMEFISGGDL MDFVACNGAI DESASKEIAR QILEAIKYVH SKGISHRDLK
PDNIMIAQDD PVIVKITDFG LAKSQENESR MKTFCGTLAY LAPEVITNKK NQLKNKKRYL
GNGRITEDLY SNKVDMWSIG CLLFVIMTAH LPFSGSTQDM LFKHITNGDY HSKLLETMNI
SIEGRDFIHR LLEVDVTLRL NANDALKHPW FKDNLEYPSQ VSLSQHLSQS QKIIKSQPKP
PTQAPQILSR ISSSEEGVDN MENSRDFKIP VIPSQRNNDI PALPLDISSS ETENHGELTR
VVDPIPSEER TSRTTYLGEP FNPIPKATFI MLKPLTKLSG KETPIMYIPQ GIPTFYIGRL
NNLNVVMSDE RISKIHCVIL KRRHPTNDSD ATGDNSPLNI NEETNPNIFS SPAMGLDDVW
LLDFSTNTCY LNNLKIGKGK KIKLRDQDII SLFIDKKNGV KLNYQVNFID TTGLFIEDAN
LERIRVPIDE NDRRMFETKL KEGMKPIMDR STKKRQQVKS IGDFPNKRRA
//
