IRC20_YEAST
ID IRC20_YEAST Reviewed; 1556 AA.
AC Q06554; D6VYP5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Uncharacterized ATP-dependent helicase IRC20;
DE EC=3.6.1.-;
DE AltName: Full=Increased recombination centers protein 20;
GN Name=IRC20; OrderedLocusNames=YLR247C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP INDUCTION.
RX PubMed=10077188;
RX DOI=10.1002/(sici)1097-0061(199902)15:3<219::aid-yea349>3.0.co;2-3;
RA Shiratori A., Shibata T., Arisawa M., Hanaoka F., Murakami Y., Eki T.;
RT "Systematic identification, classification, and characterization of the
RT open reading frames which encode novel helicase-related proteins in
RT Saccharomyces cerevisiae by gene disruption and Northern analysis.";
RL Yeast 15:219-253(1999).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=18085829; DOI=10.1371/journal.pgen.0030228;
RA Alvaro D., Lisby M., Rothstein R.;
RT "Genome-wide analysis of Rad52 foci reveals diverse mechanisms impacting
RT recombination.";
RL PLoS Genet. 3:E228-E228(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-810, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Is probably involved in a pathway contributing to genomic
CC integrity.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: By heat shock and UV radiation.
CC {ECO:0000269|PubMed:10077188}.
CC -!- DISRUPTION PHENOTYPE: Displays increased levels of spontaneous RAD52
CC foci in proliferating diploid cells. {ECO:0000269|PubMed:18085829}.
CC -!- MISCELLANEOUS: Present with 143 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U20865; AAB67400.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09561.1; -; Genomic_DNA.
DR PIR; S59393; S59393.
DR RefSeq; NP_013348.1; NM_001182134.1.
DR AlphaFoldDB; Q06554; -.
DR BioGRID; 31515; 101.
DR DIP; DIP-6373N; -.
DR IntAct; Q06554; 10.
DR MINT; Q06554; -.
DR STRING; 4932.YLR247C; -.
DR iPTMnet; Q06554; -.
DR MaxQB; Q06554; -.
DR PaxDb; Q06554; -.
DR PRIDE; Q06554; -.
DR EnsemblFungi; YLR247C_mRNA; YLR247C; YLR247C.
DR GeneID; 850949; -.
DR KEGG; sce:YLR247C; -.
DR SGD; S000004237; IRC20.
DR VEuPathDB; FungiDB:YLR247C; -.
DR eggNOG; KOG0298; Eukaryota.
DR GeneTree; ENSGT00730000111123; -.
DR HOGENOM; CLU_001592_2_0_1; -.
DR InParanoid; Q06554; -.
DR OMA; WRTCKSK; -.
DR BioCyc; YEAST:G3O-32352-MON; -.
DR PRO; PR:Q06554; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06554; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; ISS:SGD.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:SGD.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IGI:SGD.
DR GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IMP:SGD.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Helicase; Hydrolase; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Stress response; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1556
FT /note="Uncharacterized ATP-dependent helicase IRC20"
FT /id="PRO_0000268181"
FT DOMAIN 378..583
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1363..1531
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 1239..1277
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 145..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1297..1319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1508..1534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1297..1312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 391..398
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 810
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1556 AA; 180344 MW; 6258491CE361EAC0 CRC64;
MSAVGALLAR EYNVTAEKCD FFLENGSFDS VIAALPALNQ EQETVTQKVS KNGKELINVA
SVNIEIPERI SLSNNGRQLF KFIVDIEILP CENDNEATLV VSSDSVSLFQ IGFKMENNSK
IAVDKQLPLI LDICAHKNQE RALRNQLENR KSLERKPSRK RRKKNSNVND PEKLLKSRIH
ELSLSYKDFE CSPVVFRYND SSLTWVLSFN LKLKFLNNKF NRFSVEANQI LDLTFSNRDE
NEFERYHKHS HIHSNFIQKQ FISQILEYSK DRLSKIKPFL PQSIPDLKVN LLPFQRESVE
WMLIKEGHGN SLSDTPTVID EVGLIDFMNE YYAYGYELIA RSPDEVGPSL LWNKLTGYIL
TTEDAAHLYN QYRKERLSGD YPVCAKGVLA EEMGLGKTIE ILSLILLNRR KLKDSEATFI
DDENRTITKT KTTLIICPNA ILKQWLEEIE LHANSLKWYT YRGYNEIMKD CKTVDEAVQQ
LCQYDIIVTS YNIIATEVHH AEFNRSIRSR RLKSPKYDYS SPLALMQFYR IILDEVQMLR
SSSTYSAKCT SLLHRIHTWG VSGTPIQNIY NFRMIMSYLK LHPFCDEVDF IRTLQEEIKL
RNEAKDYTSN DFVCQLKGVR FSIKDCMNIF YRYDLCIRHS KANVASQIHI PRQHNFIIPL
EFAPIEWDNY LNLWNNFLEL SGYNSDGSGS PRVSNAFLNE WLSRLRYICC HALFPEILST
RQKRLHGHLS RISNIDDILI SMRMDAFDSL IGYYRERFHL SIKQAQYELE ISNTPAKALE
SFIKIRDDLM IHIRQKFNVE DPFDKSLNLS EDEDEHMDER FGEKETSSGD ESDREINGAK
NHDNHNNDGM LSNHLKKKGL RAMMNLLHDC YFFLGSVYYN LGTRKLEEAD DKHRKEKTEE
VVYSDVFPKN ELEEIEENRL LEQENYANAE ILRKSILSSE ARKVDMTIKM ARTKFAPMTS
NIPLRLINIE FDHKNDYSSN LAVSRCFKSL SKLIEGLNEQ TKNFNELLDE LLIIIYEPVH
RTEDDDSTNK IIGNEEYSTS IDSQDKIFSL LGCLEIILQN RDNILTSESE VKIPKHLVPE
GSIISKYQKQ LLNSLRLISG TPLRTVFDEL KNSRIVRRIS SSNESESTIQ NFEDYLLQYE
VESKSLFKYN KQVRESLKIL GSIYNAKTEY YSQLQRISDS LVSLHSLSAP QLSHLIRTIN
KSLGGTLDAK INNIESRLIY LKNLSRLKDT LNDNQILSCS ICLGEVEIGA IIKCGHYFCK
SCILTWLRAH SKCPICKGFC SISEVYNFKF KNSTEKREKE IQEPRREGAD SSQDNSNENS
IISNMSEVEK LFGNKYEQFH QINEVHQIHI KESFGAKIDF VIKLISYLRL KSEQENADPP
QVILYSQKTE YLKVIGKVLK LYHIEHLACL SNTANVGETI NNFKRQPSVT CLLLNVKTLG
AGLNLINAKH IFLLDPILNN SDELQAMGRN NRIGQDEETF VWNFMIRNTV EENILRYKCI
LEERKRKEKS KKGDKYDEAQ DETDNEESDD AKFEISVVDQ EVSNEHLWNC FFHGSD
