FOB1_YEAST
ID FOB1_YEAST Reviewed; 566 AA.
AC O13329; D6VS96; Q04587;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=DNA replication fork-blocking protein FOB1 {ECO:0000303|PubMed:9078378};
GN Name=FOB1 {ECO:0000303|PubMed:9078378};
GN Synonyms=HRM1 {ECO:0000303|PubMed:10230397};
GN OrderedLocusNames=YDR110W {ECO:0000312|SGD:S000002517}; ORFNames=YD9727.06;
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], AND FUNCTION.
RX PubMed=9078378; DOI=10.1046/j.1365-2443.1996.d01-256.x;
RA Kobayashi T., Horiuchi T.;
RT "A yeast gene product, Fob1 protein, required for both replication fork
RT blocking and recombinational hotspot activities.";
RL Genes Cells 1:465-474(1996).
RN [2]
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 [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 FUNCTION.
RX PubMed=9869636; DOI=10.1101/gad.12.24.3821;
RA Kobayashi T., Heck D.J., Nomura M., Horiuchi T.;
RT "Expansion and contraction of ribosomal DNA repeats in Saccharomyces
RT cerevisiae: requirement of replication fork blocking (Fob1) protein and the
RT role of RNA polymerase I.";
RL Genes Dev. 12:3821-3830(1998).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=10230397; DOI=10.1016/s1097-2765(00)80472-4;
RA Defossez P.A., Prusty R., Kaeberlein M., Lin S.J., Ferrigno P.,
RA Silver P.A., Keil R.L., Guarente L.;
RT "Elimination of replication block protein Fob1 extends the life span of
RT yeast mother cells.";
RL Mol. Cell 3:447-455(1999).
RN [6]
RP FUNCTION, DNA-BINDING, AND MUTAGENESIS OF HIS-159; HIS-164; CYS-193;
RP CYS-196 AND ASP-291.
RX PubMed=14645529; DOI=10.1128/mcb.23.24.9178-9188.2003;
RA Kobayashi T.;
RT "The replication fork barrier site forms a unique structure with Fob1p and
RT inhibits the replication fork.";
RL Mol. Cell. Biol. 23:9178-9188(2003).
RN [7]
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 [8]
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 [9]
RP INTERACTION WITH NSI1.
RX PubMed=22362748; DOI=10.1093/nar/gks188;
RA Ha C.W., Sung M.K., Huh W.K.;
RT "Nsi1 plays a significant role in the silencing of ribosomal DNA in
RT Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 40:4892-4903(2012).
CC -!- FUNCTION: Required for replication fork blocking activity at the
CC replication fork barrier (RFB) site in rDNA and for recombination hot-
CC spot (HOT1) activity, regulating the recombination rate and the number
CC of rDNA copies. Binds directly to two separated sequences in the RFB.
CC {ECO:0000269|PubMed:14645529, ECO:0000269|PubMed:9078378,
CC ECO:0000269|PubMed:9869636}.
CC -!- SUBUNIT: Interacts with NSI1. {ECO:0000269|PubMed:22362748}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10230397,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1510 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; AF013245; AAB66897.1; -; Genomic_DNA.
DR EMBL; Z48758; CAA88664.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11956.1; -; Genomic_DNA.
DR PIR; S52676; S52676.
DR RefSeq; NP_010395.1; NM_001180418.1.
DR AlphaFoldDB; O13329; -.
DR BioGRID; 32168; 116.
DR DIP; DIP-870N; -.
DR IntAct; O13329; 35.
DR MINT; O13329; -.
DR STRING; 4932.YDR110W; -.
DR iPTMnet; O13329; -.
DR MaxQB; O13329; -.
DR PaxDb; O13329; -.
DR PRIDE; O13329; -.
DR EnsemblFungi; YDR110W_mRNA; YDR110W; YDR110W.
DR GeneID; 851688; -.
DR KEGG; sce:YDR110W; -.
DR SGD; S000002517; FOB1.
DR VEuPathDB; FungiDB:YDR110W; -.
DR eggNOG; ENOG502R9VR; Eukaryota.
DR HOGENOM; CLU_030376_1_0_1; -.
DR InParanoid; O13329; -.
DR OMA; FSHFANI; -.
DR BioCyc; YEAST:G3O-29712-MON; -.
DR PRO; PR:O13329; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; O13329; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0033553; C:rDNA heterochromatin; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043110; F:rDNA spacer replication fork barrier binding; IDA:SGD.
DR GO; GO:0006325; P:chromatin organization; IGI:SGD.
DR GO; GO:0007059; P:chromosome segregation; IGI:SGD.
DR GO; GO:0006310; P:DNA recombination; IMP:SGD.
DR GO; GO:0043570; P:maintenance of DNA repeat elements; IMP:SGD.
DR GO; GO:0043007; P:maintenance of rDNA; IGI:SGD.
DR GO; GO:0008156; P:negative regulation of DNA replication; IDA:SGD.
DR GO; GO:0045911; P:positive regulation of DNA recombination; IMP:SGD.
DR GO; GO:0034503; P:protein localization to nucleolar rDNA repeats; IMP:SGD.
DR GO; GO:0070550; P:rDNA chromatin condensation; IMP:SGD.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; IDA:SGD.
DR GO; GO:0031582; P:replication fork arrest at rDNA repeats; IMP:SGD.
PE 1: Evidence at protein level;
KW DNA recombination; DNA replication; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..566
FT /note="DNA replication fork-blocking protein FOB1"
FT /id="PRO_0000087323"
FT ZN_FING 159..196
FT /note="C2H2-type"
FT /evidence="ECO:0000305|PubMed:14645529"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 159
FT /note="H->A: Abolishes RFB-binding, replication fork
FT blocking activity and reduces recombination rate."
FT /evidence="ECO:0000269|PubMed:14645529"
FT MUTAGEN 164
FT /note="H->A: Abolishes RFB-binding, replication fork
FT blocking activity and reduces recombination rate."
FT /evidence="ECO:0000269|PubMed:14645529"
FT MUTAGEN 193
FT /note="C->A: Abolishes RFB-binding, replication fork
FT blocking activity and reduces recombination rate."
FT /evidence="ECO:0000269|PubMed:14645529"
FT MUTAGEN 196
FT /note="C->A: Abolishes RFB-binding, replication fork
FT blocking activity and reduces recombination rate."
FT /evidence="ECO:0000269|PubMed:14645529"
FT MUTAGEN 291
FT /note="D->A: No effect."
FT /evidence="ECO:0000269|PubMed:14645529"
FT CONFLICT 103
FT /note="T -> A (in Ref. 1; AAB66897)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 566 AA; 65318 MW; 2DC064120C5E7331 CRC64;
MTKPRYNDVL FDDDDSVPSE SVTRKSQRRK ATSPGESRES SKDRLLILPS MGESYTEYVD
SYLNLELLER GERETPIFLE SLTRQLTQKI YELIKTKSLT ADTLQQISDK YDGVVAENKL
LFLQRQYYVD DEGNVRDGRN NDKIYCEPKH VYDMVMATHL MNKHLRGKTL HSFLFSHFAN
ISHAIIDWVQ QFCSKCNKKG KIKPLKEYKR PDMYDKLLPM ERIHIEVFEP FNGEAIEGKY
SYVLLCRDYR SSFMWLLPLK STKFKHLIPV VSSLFLTFAR VPIFVTSSTL DKDDLYDICE
EIASKYGLRI GLGLKSSARF HTGGILCIQY ALNSYKKECL ADWGKCLRYG PYRFNRRRNK
RTKRKPVQVL LSEVPGHNAK FETKRERVIE NTYSRNMFKM AGGKGLIYLE DVNTFALANE
ADNSCNNNGI LHNNNIGNDN FEEEVQKQFD LTEKNYIDEY DDLAHDSSEG EFEPNTLTPE
EKPPHNVDED RIESTGVAAP MQGTEEPEKG DQKESDGASQ VDQSVEITRP ETSYYQTLES
PSTKRQKLDQ QGNGDQTRDF GTSMEL
