ID A0A1E4RD75_9ASCO Unreviewed; 2485 AA.
AC A0A1E4RD75;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Cyclin-dependent kinases regulatory subunit {ECO:0000256|RuleBase:RU311113};
GN ORFNames=HYPBUDRAFT_163462 {ECO:0000313|EMBL:ODV65202.1};
OS Hyphopichia burtonii NRRL Y-1933.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Hyphopichia.
OX NCBI_TaxID=984485 {ECO:0000313|EMBL:ODV65202.1, ECO:0000313|Proteomes:UP000095085};
RN [1] {ECO:0000313|Proteomes:UP000095085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-1933 {ECO:0000313|Proteomes:UP000095085};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds to the catalytic subunit of the cyclin dependent
CC kinases and is essential for their biological function.
CC {ECO:0000256|RuleBase:RU311113}.
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 Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- SIMILARITY: Belongs to the CKS family. {ECO:0000256|RuleBase:RU311113}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC {ECO:0000256|ARBA:ARBA00010769}.
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DR EMBL; KV454545; ODV65202.1; -; Genomic_DNA.
DR RefSeq; XP_020074269.1; XM_020222620.1.
DR STRING; 984485.A0A1E4RD75; -.
DR GeneID; 30997169; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000095085; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0019219; P:regulation of nucleobase-containing compound metabolic process; IEA:UniProt.
DR CDD; cd00892; PIKKc_ATR; 1.
DR Gene3D; 3.30.170.10; Cyclin-dependent kinase, regulatory subunit; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000789; Cyclin-dep_kinase_reg-sub.
DR InterPro; IPR036858; Cyclin-dep_kinase_reg-sub_sf.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR012993; UME.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF124; SERINE_THREONINE-PROTEIN KINASE MEC1; 1.
DR Pfam; PF01111; CKS; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF08064; UME; 1.
DR PRINTS; PR00296; CYCLINKINASE.
DR SMART; SM01084; CKS; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00802; UME; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF55637; Cell cycle regulatory proteins; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00945; CKS_2; 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell cycle {ECO:0000256|RuleBase:RU311113};
KW Cell division {ECO:0000256|RuleBase:RU311113};
KW DNA damage {ECO:0000256|ARBA:ARBA00023204};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000095085};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1506..2042
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2147..2469
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2453..2485
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2485 AA; 286764 MW; 927447886B410FAC CRC64;
MSKPRYLSDS ERAKILEFQD MIHYSPRYSD DSNEYRHVML PKNMLKAIPQ DYFNPETGTL
RILLEEEWRG LGITQSLGWV HYETHAPEPH ILLFKRPINY VHQKISDAEL SAFLDDVNKN
ISVDDKADFK KLTLHLFGFT HSRLKFIKKN VYQTNNSSEP IHILERLMST IELVFSKRKH
LLNTHLADHE LAQLKKLFYG NDVNYESDMM YELSILFALS WLPEFSLDNT MVNIIKSFII
GVTNIISIQL HNYKYKNSLK SKLLMVLQDN VSFLLSSVQL INIPTEFNQV YGPKLACTIH
LLSIINDYDI SNKLLLNSPQ NQLAFDSIIR KLWFIINSVD FNMILTSNNG DEPNLLLIDN
LKSILILNLT NNIVLNISGN WDSIALILKW ILDYVKAFDS KVDGSPFNKF LKSFNRSISY
SLLKIFQLCR DKSLIHNLFN FLQLHTIPMI FQLDDLSSND LNLQYPIIIL KTLHIIYYQY
NTIIENKSMI DSYHASPKFK FISQPFVDEE LNYLRNNVIG YDSNDTYKIT VDLLDFIIKP
EFRFENSYSN DLINDKFDFK LWLKHIKYLK DLSLKKPNNF NILSDKSSLY TFITAMGNFP
CLFSGHFHFR VGECIKCGIS PMNKNYYSNI LPNRKNVNEI VEVSEFYNDM IISYLLNQRF
QEVVSDPLIS SNLLLTIFKI FASYSPPRDS NRIVDPVLKF VIDSVSSNLN RNVRMLAARI
LPLYLIQQKD LDLDSTFKTI FSKLSQIKFN NGSKKTYLAE STVKALSELA IISEGEWLCV
ILIKLVDMFN EYNDQHVNLA YNGLLYIASN KRITPYKMLS PFLPSIAERI VKRPRSLTKI
AELLGITKTS FLFRTRVYTT PRLLEHYGYD YVQEIATASS MTKLKLIQKL LPRILATYFV
KDEKIDENYI LAVLGNASSE YRSVGIMDLM TSIGNMTWYI LLQISDDADG NILNEDRINN
ALTYVAKMNL KINNEPKKRV RDYVEYLLGE YVLELVQRFS ETIHQTQGTS PFLEKLTSLK
AIEFLINKNI NAVASALGQI STCLQATLEN PDFEYVAIRC CNVLVQKLET NHLISLFDII
ISLLFQKFPD LEPRSKFEAA KIFKKLFGEL SDRPNNYTCY SFSLPFIKDL DQYYTPEPKF
MNSMKLFGKN HSFSEFTRRL KTSNKYVVQQ ALDDLILYIR LYQKSLQTED LKDSTLERTF
SDLVRTIFDT AVHFKSKNDK ISTSCATALS IMGALDANKF NFKTIKNRIV IIHDFSDYKE
NADFLRHFME DIVIKVFWAS NDPSKQLFSA YVMQKFLQVL KLDVKVLDPS TQDYFSEVWN
SFSDVAKSTL APLLSSKYFT SNPKYEQLTL PYYRVGMRHE KWLADFTSNL LKRPSFTSND
DSIKDTIFKI CSLLIKDQDI SICHYLLKYA ALSHIISGDE DISNGIKDEF LAILGMDTHG
TFSSDRLELI RSCYQSIFEV LDYFNEWRSV VTQYLSNNKL TKVESNRLKG NLNLVDSFLS
KIPTNLIALK SAECDSYERT ILYLEKCYRD GQLDDFNKIQ DLDAVSALQS MYASINDYDA
LDGILKKFST NNLNEKLQTF QYNENWWLAQ ESFQVLSEVG IKKIENNTNL FKSLSDHALY
DEVLSTLSSR VNFDKPNKIP IEWSMVGLQA ASVSGDIDQI NKWLFVSDSC GKAHDIETLI
NYRFAQALKA LFGRDTEKFN EEVNDLYKII GQSLVPSISS SFSRNSTLMS QLHSIYDVSM
ISGSRVNDEI NQTYEHILRD RLSNVDQGFD SQWKILSMHR VANMAVGNSD KISDILLFCS
KVARKNDRLD ISTRCIMKSM ALNDQEANLE YAELLWAQDK QTEAIKSLSQ IIDEDVFKNK
KQKARAQLQY AIWLDESNHT SSSTIINEYE QARQLEPTWE KPYYDLGKYY NKIMESRHDS
TGYYEVQTIR YFLKSLGLRP TFIFEALPKF ITIWLDFAQK VRKNKDSNRR EVERKLNQIT
SDIKRFHSSI PIYVWYTSIT QMLSRISHSH SDSVELLKAI ISKVAEAYPE HSLWYILSHL
NSNDLNRKAR VGQILSQVES ASSSLSDKVL GAKTLFSTLI SIVNFKVDKR NLKPMSLSSD
FNIKNLGEPY DCLAIPVASN LEIKSPTLKY DYRNAFPKSS MITFDGFDDV VNVFHSLQVP
KQLTVRGSDA KPYRLMVKKD DTRKDAKVVE FTTMINRLLL ASTEARKRNL VIHNYAVIPL
AENMGVIEFV QNVTTFKSII ADTQKKLGKV VNERSIFHKM SDAHKLLKVN SKSNLSSAMD
DVIKLFEKIC HDNQPVSHKW FIDQFSDPTA WYIARYKFTR SAAVMSIVGY IIGLGDRHCE
NILIFKNTGS VLHIDFDCLF DKGLSLPTPE IVPFRLTQNI TDAMGISGIE GVFRIACEVT
GSLLRENEAP LMNILETLLY DPLLDWKTQQ NPQEHLKKVQ RKIRGLVDEK EGLPMNIHGQ
VDVLIQESTS IENLSRMYPG WSPYL
//
