ID J8PMR0_SACAR Unreviewed; 725 AA.
AC J8PMR0;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000256|HAMAP-Rule:MF_03177};
DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_03177};
DE AltName: Full=rDNA recombination mutation protein 3 {ECO:0000256|HAMAP-Rule:MF_03177};
GN Name=RRM3 {ECO:0000256|HAMAP-Rule:MF_03177};
GN ORFNames=SU7_1427 {ECO:0000313|EMBL:EJS43410.1};
OS Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1160507 {ECO:0000313|EMBL:EJS43410.1, ECO:0000313|Proteomes:UP000006968};
RN [1] {ECO:0000313|EMBL:EJS43410.1, ECO:0000313|Proteomes:UP000006968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H-6 / AS 2.3317 / CBS 10644
RC {ECO:0000313|Proteomes:UP000006968};
RX PubMed=23368932; DOI=10.1186/1471-2164-14-69;
RA Liti G., Nguyen Ba A.N., Blythe M., Mueller C.A., Bergstroem A.,
RA Cubillos F.A., Dafhnis-Calas F., Khoshraftar S., Malla S., Mehta N.,
RA Siow C.C., Warringer J., Moses A.M., Louis E.J., Nieduszynski C.A.;
RT "High quality de novo sequencing and assembly of the Saccharomyces
RT arboricolus genome.";
RL BMC Genomics 14:69-69(2013).
CC -!- FUNCTION: 5' to 3' DNA replicative helicase recruited to paused
CC replisomes to promote fork progression throughout nonhistone protein-
CC DNA complexes, naturally occurring impediments that are encountered in
CC each S phase where replication forks pauses. Required for timely
CC replication of the telomere and subtelomeric DNA and for wild-type
CC levels of telomeric silencing. Involved in DNA repair during stalled
CC replication fork, regulation of fragile sites expression and essential
CC for genome stability. Plays also a role in mtDNA replication. Has G-
CC quadruplex (G4) unwinding activity and can suppress G4-induced genome
CC instability when PIF1 levels are low. {ECO:0000256|HAMAP-
CC Rule:MF_03177}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03177};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03177}.
CC Chromosome, telomere {ECO:0000256|HAMAP-Rule:MF_03177}.
CC -!- SIMILARITY: Belongs to the helicase family. PIF1 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03177}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJS43410.1}.
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DR EMBL; ALIE01000098; EJS43410.1; -; Genomic_DNA.
DR AlphaFoldDB; J8PMR0; -.
DR HOGENOM; CLU_001613_0_2_1; -.
DR OrthoDB; 5474774at2759; -.
DR Proteomes; UP000006968; Chromosome VIII.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005657; C:replication fork; IEA:UniProtKB-UniRule.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051880; F:G-quadruplex DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR CDD; cd18037; DEXSc_Pif1_like; 1.
DR CDD; cd18809; SF1_C_RecD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_03176; PIF1; 1.
DR HAMAP; MF_03177; RRM3; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR010285; DNA_helicase_pif1-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR048293; PIF1_RRM3_pfh1.
DR InterPro; IPR028880; Rrm3.
DR PANTHER; PTHR47642; ATP-DEPENDENT DNA HELICASE; 1.
DR PANTHER; PTHR47642:SF5; ATP-DEPENDENT DNA HELICASE; 1.
DR Pfam; PF05970; PIF1; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03177}; Chromosome {ECO:0000256|HAMAP-Rule:MF_03177};
KW DNA damage {ECO:0000256|HAMAP-Rule:MF_03177};
KW DNA repair {ECO:0000256|HAMAP-Rule:MF_03177};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_03177}; Helicase {ECO:0000256|HAMAP-Rule:MF_03177};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03177};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03177};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03177};
KW Reference proteome {ECO:0000313|Proteomes:UP000006968};
KW Telomere {ECO:0000256|HAMAP-Rule:MF_03177}.
FT DOMAIN 248..396
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DNA_BIND 684..703
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03177"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 256..263
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03177"
SQ SEQUENCE 725 AA; 81818 MW; ADDC358EEEAAF44A CRC64;
MFRSNASGNK KQWSKRTANG NASAESASGS HFYRQQTLSS FLMGPNKRTA VVAKNSATII
DLENGHEGDQ TKTVPPRPRL VRNNSSILFS QPQGSFGDED PEAEFKKLVN VPRLNSYKKT
SKSSSVTTSL RKTTSSTSTT HKTYRYGEDE TLREVTSVKS NSRQLSFTST INIGDSGAGL
PADLERPAKR SKPSMEFQGL KLTVPKRIKP LLRKTASNLE SMNHRNAFLS PVVLTKEQEM
VVNLIIKKRT NIFYTGSAGT GKSVILQTII RQLSSLYGKE SIAITASTGL AAVTIGGSTL
HKWSGIGIGN KTIDQLVKRI QSQKDLLAAW RYTKVLIIDE ISMIDGNLLD KLEQIARRIR
KTDDPFGGIQ LVLTGDFFQL PPVVKKDEDK VVKFCFESDM WKRCVQKTIL LTKVFRQQDN
ELIDILNAIR FGELTVDMTK TIRNLNRDIG YPDGIAPTEL YATRREVESS NVRKLQSLPG
DLYEFKAVDN APERYQALLD SSLMVDKVVA LKEDAQVMML KNRPDVELVN GSLGKVLFFV
TESLVVKMKE IYKIIDDDVV MDMRLVSRVI GNPLLKESKE FRQDVNARPL ARLERLKILI
NHATKISPHK EKFPYVRWTA GKNKYIHELM VPERFPIDIP RENVGLERTQ IPLMLCWALS
IHKAQGQTIQ RLKVDLRRIF EAGQVYVALS RAVAMDNLQV LNFDPGKIRT NEKVKDFYKH
LETLK
//
