ID M7WM09_RHOT1 Unreviewed; 1085 AA.
AC M7WM09;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=RHTO_05443 {ECO:0000313|EMBL:EMS18875.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS18875.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS18875.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS18875.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
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=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034617};
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
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DR EMBL; KB722674; EMS18875.1; -; Genomic_DNA.
DR RefSeq; XP_016269994.1; XM_016419104.1.
DR AlphaFoldDB; M7WM09; -.
DR GeneID; 27369456; -.
DR eggNOG; KOG2108; Eukaryota.
DR HOGENOM; CLU_004585_4_1_1; -.
DR OrthoDB; 208346at2759; -.
DR Proteomes; UP000016926; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd18807; SF1_C_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Helicase {ECO:0000256|PROSITE-ProRule:PRU00560,
KW ECO:0000313|EMBL:EMS18875.1};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 59..342
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 343..703
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..954
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 80..87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1085 AA; 116263 MW; 4E8A1A1E04B1F9AD CRC64;
MEPSDDLSDS EYLPVTDNEP SNTNEVAQQP ARPAERATDG LKQSTLSFGR PSPSEYLAKL
NPAQREAVTA SAEGGLAIHA GPGSGKTAVL TTRVAYLVQK GGIKPEELVV VTFTNKAANE
MKVRLSKIVG AETVDKLVMG TFHSVCVRYL RKYAKLVNLA SNFLITDRDD CLGIIKRLLQ
ALPVPANLKR EMKPQTWLES ISKCKSRMMS PDQYRADRSA AVDQEKIEWV ARMYEAYEDA
LASGNALDFD DLLVRGYQLF RNHPRVIAKI KSVLIDEFQD TNSVQYDIVK LIAAPSGSLT
VVGDPDQSIY GWRNAEIENL EKMLKDFHPV RQIFLKENYR STGAILGAAL AVVRQDTKRI
NKSLTTSHPA GSSVVLHPAP SAQDEAAFVA STIKHLVAHL GGLVGYNDFA VLLRYGALSR
NIEVALQKAG IPSRMVGGHK FFERIEIKDM LCYLQLLSNP SYSPALMRVI NVPRRAIGDK
TIREIVATAE KKKISPFEVC VKIAKGQSIV QGMTTAQRKG IRTLVELVRD GRTKADEGVD
VASLIDLIVD RVGYRAHLEK QHSHDAAERW ENVEELKAYA TVVAQENPST ADLATAADPE
EGDSQFEEVA ILPKNGSLSI EDDDSDIEIV DSPKPKSRGR KGSEETEKLE VPLSSQAAVE
GAATPLEIFL ATSMLATDTE TQAAKGDAKL EKVTISTCHA AKGLEWPVVF IPACEDGTYP
FFRSTDANEV DEERRLLYVA ITRAQSFCFL SYAAQRMAGA EMKQKKPSPF IATASQTYPS
LFVKKLQKVT PKLRGEVAKV LGRTAPSEEV AKRMIDEYLA TMPVDPPVWD VASQPTGSRD
YGSFGSSSGR YGGFGSQGRY GGTFGSSQGQ SQGRWSTPVV PQSQAVPPGQ GGFRSALSTF
KSVAGGAGAG VNLTTAGFAP ASSSLSSKSG GFTAPRPAGS AAPFKPPTVA PSAAPRLPPT
SLAASVGALA PLPPKPPVDG APGVVETRAS RISDVVLVNP KLAPASLTTG GGRDLLASFQ
KGADDELEAF KRFAGESEED GTEVAQESAV GVQSGAPMSP KAKKKRSAAS SGGAATKAGG
KKAKR
//