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Database: UniProt
Entry: M7WM09_RHOT1
LinkDB: M7WM09_RHOT1
Original site: M7WM09_RHOT1 
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
//
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