IRC3_YEAST
ID IRC3_YEAST Reviewed; 689 AA.
AC Q06683; D6VSW4;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Putative ATP-dependent helicase IRC3;
DE EC=3.6.4.-;
DE AltName: Full=Increased recombination centers protein 3;
GN Name=IRC3; OrderedLocusNames=YDR332W;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 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 [4]
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).
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 172 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the helicase family. IRC3 subfamily.
CC {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; U32517; AAB64767.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12174.1; -; Genomic_DNA.
DR PIR; S59797; S59797.
DR RefSeq; NP_010619.3; NM_001180640.3.
DR AlphaFoldDB; Q06683; -.
DR SMR; Q06683; -.
DR BioGRID; 32389; 80.
DR DIP; DIP-5241N; -.
DR IntAct; Q06683; 1.
DR MINT; Q06683; -.
DR STRING; 4932.YDR332W; -.
DR MaxQB; Q06683; -.
DR PaxDb; Q06683; -.
DR PRIDE; Q06683; -.
DR EnsemblFungi; YDR332W_mRNA; YDR332W; YDR332W.
DR GeneID; 851932; -.
DR KEGG; sce:YDR332W; -.
DR SGD; S000002740; IRC3.
DR VEuPathDB; FungiDB:YDR332W; -.
DR eggNOG; ENOG502QT4U; Eukaryota.
DR HOGENOM; CLU_014765_0_0_1; -.
DR InParanoid; Q06683; -.
DR OMA; WLCEGKF; -.
DR BioCyc; YEAST:G3O-29888-MON; -.
DR PRO; PR:Q06683; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06683; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0036121; F:double-stranded DNA helicase activity; IDA:SGD.
DR GO; GO:0061749; F:forked DNA-dependent helicase activity; IDA:SGD.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0000403; F:Y-form DNA binding; IDA:SGD.
DR GO; GO:0032042; P:mitochondrial DNA metabolic process; IMP:SGD.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Mitochondrion; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..689
FT /note="Putative ATP-dependent helicase IRC3"
FT /id="PRO_0000253816"
FT DOMAIN 46..211
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 265..438
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 158..161
FT /note="DEAH box"
FT BINDING 59..66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 689 AA; 78546 MW; E3303C88B00706CE CRC64;
MTSTLATRLS TYSISLILQR IKIIKRCYSA PVLRDYQQDA IDACVNSIRQ GTKRIGVSLA
TGGGKTVIFS NLINQLRQNY FKERQGNFKS LILVHRRELA LQATATLKKI FPDLKVHIEM
GKYDCDIEDS DVIVASVQTL IRRLHKYDTN SVNLIIIDEA HHSVANSYRS ILDHFKASTA
ETKIPVIGFS ATFERADKRA LSMVMDKIVY HRGILEMIDD KWLCEAKFTS VKIEADLSDV
KSTADDFQLA PLSSLMNTKE INEVILKTYL HKKQEKSLKS TLLFGVDKAH VQSLHKLFKD
NGINTDYVTS DTKQIERDNI IQKFKNGETE VLMNCGIFTE GTDMPNIDCI LLCRPTKSRS
LLIQMIGRGL RLHHSKDHCH IIDFIGASSV GVVSAPTLLG IRSDDIEFDD ATVEDLKAIQ
GEIIAKQQKI DERLRALFQT DEAAMENVTE RNSVADWIHS ANSVDLTLCS FDSFRNFTQS
NNSYPSGKEF DEASEAVKEM ELLMNSQYPW VKFASNAWGL PLKGKNHLRI YKEKSEDKLS
MVYHLKMYRQ LPCFITNKYA DYVPKSIIKD ANLWNVMSKV EKIINTLNSD LEGQTMQYQA
ISSKYSKWRQ TVPTSKQRDF VFRKLKKVYG ESSKDFIRLS LDDVTTYVNT KMTKGDASNL
IFASSLAPVY PLKSLLRILE YQKRRSFIK
