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Database: UniProt
Entry: C6X052_FLAB3
LinkDB: C6X052_FLAB3
Original site: C6X052_FLAB3 
ID   C6X052_FLAB3            Unreviewed;      1064 AA.
AC   C6X052;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   OrderedLocusNames=FIC_00264 {ECO:0000313|EMBL:ACU06737.1};
OS   Flavobacteriaceae bacterium (strain 3519-10).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=531844 {ECO:0000313|EMBL:ACU06737.1, ECO:0000313|Proteomes:UP000001512};
RN   [1] {ECO:0000313|EMBL:ACU06737.1, ECO:0000313|Proteomes:UP000001512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3519-10 {ECO:0000313|EMBL:ACU06737.1,
RC   ECO:0000313|Proteomes:UP000001512};
RX   PubMed=18622572; DOI=10.1007/s00792-008-0178-2;
RA   Raymond J.A., Christner B.C., Schuster S.C.;
RT   "A bacterial ice-binding protein from the Vostok ice core.";
RL   Extremophiles 12:713-717(2008).
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};
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DR   EMBL; CP001673; ACU06737.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6X052; -.
DR   STRING; 531844.FIC_00264; -.
DR   KEGG; fba:FIC_00264; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_010638_0_0_10; -.
DR   Proteomes; UP000001512; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.320.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   Gene3D; 1.10.3170.10; Recbcd, chain B, domain 2; 1.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011604; PDDEXK-like_dom_sf.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070:SF64; ATP-DEPENDENT DNA HELICASE REP; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 2.
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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000001512}.
FT   DOMAIN          1..485
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          496..761
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         21..28
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   1064 AA;  122896 MW;  B1CF26009928D54C CRC64;
     MLLLKSIYNS MVQKNYRVIN ASAGSGKTYA LVQNLLVICL KHPSQPDKIR NILALTFTNK
     AANEMKQRII KWLREFSSAE YANNQDLKNI QQKMKVQGIE LSLETLHKRS RKILDYVLHN
     YSTLNIGTID KFNSRLVRSF SYELGLAQNF NLEINAEPYL VEAVEKMLAD IGAENDVSDA
     FMDFVNYSLD NNERVNLNKT LYDSAKEFVQ DKHYFRLSQN KEFDWKVYGE AKQRLRDNIK
     SLKEDSLKIT ETCINLLNEK NLEIADFSGG SKNSIAKFII EAARFYKKER ADFPFPSNEE
     TALTNFQSGA SSKSKNRQSE ILEILDFLIE SRSKIIKNYI ETQREEKILH ALLPLKVNKD
     IQDKLAEIEE KNDVVLLSKF NILIHENLRE EPSSFIYEKV GTQFSHYFFD EFQDTSFLQW
     QNFIPLRDHA VSSDEMSFTL VGDPKQSIYR FRGGDSQLML DIINKQEKSL VLADLENLGD
     NWRSAKNIVD FNNQLYQFLS AHTQEAHCDI FGKGSQQTPK SESSGRVRIN LIENSTKAIY
     YEDVAEKMCE DLQACVDNGF RFADITILCR GNFDIFSFSN LLGNLKINYN GKEEFIKTIS
     ESGLTLNLSS TLLALTEFLR WEQNPKNFQF PVKMLYYLNI LGRITIEDFS ADMMEMLAFK
     TKPEIQDFIE NRYGIRLRNE TLLQLNLYNF VEHFLQEFSV AGKETDFLFN YLEMLYAFSQ
     NAGANLKDFL RFWDEEAQEA TIQASDNLDA VKLMTIHKAK GLEFPVVFLP MANSHKDGKF
     SNWLDIKDHA GLAAVNVPSF GKELEVYDED MAKFNQENNY QNKIDRFCLQ YVATTRAAEQ
     IFLYIEKPNK TTNNLEIYEF LEPNIPLNEH LEPLSSFDLY EVSPEILKKK ESDKAETAVT
     QAVRFKNEKV PNPAAIQIAT PSKSYQNRVE KVRTGIFTHE ILAKINSKDD VEKTLENYLL
     DGIITQTEKQ YISERLLTII NDGRYAQYFA PNQRVINEKD IMISAGGESK IYRPDRLIDT
     GDGYIIIDFK TGGVKEKHQQ QVDEYQSVLE KLGMKVRETA IVYV
//
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