ID   IRC5_YEAST              Reviewed;         853 AA.
AC   P43610; D6VTS1;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   27-MAR-2024, entry version 178.
DE   RecName: Full=Uncharacterized ATP-dependent helicase IRC5;
DE            EC=3.6.4.-;
DE   AltName: Full=Increased recombination centers protein 5;
GN   Name=IRC5; OrderedLocusNames=YFR038W;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   PubMed=8686381;
RX   DOI=10.1002/(sici)1097-0061(199602)12:2<177::aid-yea896>3.0.co;2-a;
RA   Eki T., Naitou M., Hagiwara H., Abe M., Ozawa M., Sasanuma S., Sasanuma M.,
RA   Tsuchiya Y., Shibata T., Watanabe K., Ono A., Yamazaki M., Tashiro H.,
RA   Hanaoka F., Murakami Y.;
RT   "Fifteen open reading frames in a 30.8 kb region of the right arm of
RT   chromosome VI from Saccharomyces cerevisiae.";
RL   Yeast 12:177-190(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7670463; DOI=10.1038/ng0795-261;
RA   Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA   Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA   Eki T.;
RT   "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT   cerevisiae.";
RL   Nat. Genet. 10:261-268(1995).
RN   [3]
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   [4]
RP   IDENTIFICATION OF FRAMESHIFT.
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA   Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA   Gates K., Gaffney T.D., Philippsen P.;
RT   "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT   comparison to the genome of a related fungus: Ashbya gossypii.";
RL   Genome Biol. 4:R45.1-R45.13(2003).
RN   [5]
RP   IDENTIFICATION OF FRAMESHIFT.
RX   PubMed=12748633; DOI=10.1038/nature01644;
RA   Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT   "Sequencing and comparison of yeast species to identify genes and
RT   regulatory elements.";
RL   Nature 423:241-254(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   IDENTIFICATION BY MASS SPECTROMETRY [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:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Displays increased levels of spontaneous RAD52
CC       foci in proliferating diploid cells. {ECO:0000269|PubMed:18085829}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA09277.1; Type=Frameshift; Evidence={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; D50617; BAA09277.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; BK006940; DAA12481.1; -; Genomic_DNA.
DR   PIR; S56293; S56293.
DR   RefSeq; NP_116696.2; NM_001180003.1.
DR   AlphaFoldDB; P43610; -.
DR   SMR; P43610; -.
DR   BioGRID; 31196; 73.
DR   DIP; DIP-5300N; -.
DR   IntAct; P43610; 1.
DR   MINT; P43610; -.
DR   STRING; 4932.YFR038W; -.
DR   GlyGen; P43610; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; P43610; -.
DR   MaxQB; P43610; -.
DR   PaxDb; 4932-YFR038W; -.
DR   PeptideAtlas; P43610; -.
DR   EnsemblFungi; YFR038W_mRNA; YFR038W; YFR038W.
DR   GeneID; 850599; -.
DR   KEGG; sce:YFR038W; -.
DR   AGR; SGD:S000001934; -.
DR   SGD; S000001934; IRC5.
DR   VEuPathDB; FungiDB:YFR038W; -.
DR   eggNOG; KOG0385; Eukaryota.
DR   GeneTree; ENSGT00940000173484; -.
DR   HOGENOM; CLU_000315_17_3_1; -.
DR   InParanoid; P43610; -.
DR   OMA; PNIFTDW; -.
DR   OrthoDB; 5482994at2759; -.
DR   BioCyc; YEAST:G3O-30485-MONOMER; -.
DR   BioGRID-ORCS; 850599; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P43610; -.
DR   Proteomes; UP000002311; Chromosome VI.
DR   RNAct; P43610; Protein.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS:SGD.
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:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006312; P:mitotic recombination; IMP:SGD.
DR   GO; GO:0044030; P:regulation of DNA methylation; IBA:GO_Central.
DR   CDD; cd18009; DEXHc_HELLS_SMARCA6; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR044753; HELLS_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR10799:SF923; PASG; 1.
DR   PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Coiled coil; DNA-binding; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..853
FT                   /note="Uncharacterized ATP-dependent helicase IRC5"
FT                   /id="PRO_0000074385"
FT   DOMAIN          234..401
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          607..758
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          43..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          158..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          548..580
FT                   /evidence="ECO:0000255"
FT   MOTIF           352..355
FT                   /note="DEGH box"
FT   BINDING         247..254
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   853 AA;  96966 MW;  91EF0E200197FF28 CRC64;
     MSRCSNAALM TVVEDAVGAR VAARTRNMSN GVNYREKEVN DLTADISDSD SDLDSEDNKH
     GKGDNDTAPI WLQDDVHSDE DIQLDSEDDS DTEAVQAQVV DKLAKDTKSE QKSLDDELSE
     MDTKTVSLKL KKLNEFVRQS QVYSSIIADT LLHRSNEVAN ANTKDNSNSD DEEHSSKKRK
     TKKKSITDFF KKQKKNEDTT TQNGAPDDAA IKQPRLLKNC ILKPYQLEGL NWLITLYENG
     LNGILADEMG LGKTVQSIAL LAFIYEMDTK GPFLVTAPLS TLDNWMNEFA KFAPDLPVLK
     YYGTNGYKER SAKLKNFFKQ HGGTGIVITS YEIILRDTDL IMSQNWKFLI VDEGHRLKNI
     NCRLIKELKK INTSNRLLLT GTPLQNNLAE LWSLLNFIMP DIFADFEIFN KWFDFDSLNL
     GSGSNSEALN KLINDELQKN LISNLHTILK PFLLRRLKKV VLANILPPKR EYIINCPMTS
     AQEKFYKAGL NGKLKKTMFK ELIKDFFTLN DEYIGHVSNR SIRDFINYKL SGNETSNTDN
     KINPTLLQMD KLYKKNLQME ISNKKLQNMM MQLRQIIDST FLFYFPYLHP EDLTLETLLK
     TSGKLQILQK LIPPLISEGH KVLIYSQFVN MLDLIEDWCD LNSFATFRID GSVNNETRKD
     QLEKFNSSKD KHNIFLLSTR AAGLGINLVG ADTVVLFDSD WNPQVDLQAM DRCHRIGQES
     PVIVYRLCCD NTIEHVILTR AANKRNLERM VIQMGKFNNL KKLALNEGSF LKANKAGVNV
     TNKDLVQELS MLLMSDESNI GFENGGQKEN KATEGQLTDK EVEELTNRSL EAYKANRVVD
     LPHVKLFETT SGL
//