ID A0A254SJR8_9BACT Unreviewed; 1258 AA.
AC A0A254SJR8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=B7982_06910 {ECO:0000313|EMBL:OWV23202.1};
OS Fibrobacter sp. UWB2.
OC Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC Fibrobacter.
OX NCBI_TaxID=1964358 {ECO:0000313|EMBL:OWV23202.1, ECO:0000313|Proteomes:UP000197741};
RN [1] {ECO:0000313|EMBL:OWV23202.1, ECO:0000313|Proteomes:UP000197741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWB2 {ECO:0000313|EMBL:OWV23202.1,
RC ECO:0000313|Proteomes:UP000197741};
RA Neumann A.P., Suen G.;
RT "Draft genomes of novel Fibrobacter strains.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:OWV23202.1}.
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DR EMBL; MWQK01000003; OWV23202.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A254SJR8; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000197741; 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:0008854; F:exodeoxyribonuclease V activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.3170.10; Recbcd, chain B, domain 2; 1.
DR HAMAP; MF_01485; RecB; 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; IPR004586; RecB.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF23; RECBCD ENZYME SUBUNIT RECB; 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 SUPFAM; SSF52980; Restriction endonuclease-like; 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}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
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}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 1..435
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 458..740
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 19..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1258 AA; 143503 MW; A6321790C2DDC6AF CRC64;
MENFSLQKFD PSKSLFIEAS AGTGKTYTIQ LMVAKLISLG TPLKKILIVT YTEKAAGELK
DRIRKKIDEV LVSRKLDKTN EAEKELDDAT LALFSKAYQD VDNAAIFTIH SFCQKALKEY
AYDAGRPFDM SMIDDSEVHD LVEQFIRDKW SDNSNFQFLL KTDSAQSIAN KVATGLENIV
NVYRGSEGDR EIIPLDKPEQ ITFGDTALSD DDIRTIAIAK TFDDILGIPV FGDAFSTLEK
HPAEKFGKTS KNCISDFLSA LKLWEKDKTL FSGVSFKDSD FVRTTWPTDA YEAFLSFKAL
KELLPSINNV LLNNFLISQA ASVFDEWQKY KTEKKCQSFN DMILSVHRAA LDTSKGDSLL
KSRLRAQYTY AIIDEFQDTN QLQWDIFSAI FDKIFVVGDP KQSIYSFQSA DVNVYQKAIH
EIKNGMSLQT NFRSTTGIIN GCNELFKGDF FTPNEGATKL VDFEPSLPPQ NEKQVKAPPK
INDNEVAPIW ISEQDINEVD FARAAVQKII DWCTFVDGKT VLQVFKKEDC TQYRNVTFKD
FAVLARSRSE MDAIEDAMRS AGVPFSRYKD SNLFSCRECA EWIAIFKAIN APDFSAWNRR
LLSEALITDF FRIARQDIHY AESKAFDDPN NPVRQKLNTW TELAQKRRYA EMLERIYSDT
QVEERLTEIS RLQNLARLRQ IGNYAIEYLY NHNCSIEDLV RHLEALASYS ENADDEDGNL
VEKSSDYDAV QVMTIHASKG LEFPVVISVA GFKGKRPATV PFLYHDNDEI RLGFSEHAKT
TREREELEEW KRLFYVDFTR ASSILMLPRY EKWKNTKGVK PEYVFLESSI NRLIEKASEL
TAILPKAENR NPQQLSETVK ERILKPLNEN SEIGKALSTD EIRDNIIQQK CAMASLQGKL
ADASIMQYSY SSLSGKADTL VDADDGNRTN REGEEIATSR TSTVQIRDID TAAVNCTIAA
DASLDYQTHL NESAHKFPRG SHAGNALHRI FECTQFQKFG LENKTLEDAL ANPQTRNIIE
EEFKRESLPI WNHRDAWIDI ATRYTWNTLN ARLPEIAGNS VQYTEQDSAG NAKQDAPQTF
ALIDIPLSDH KPEVQFNQNA TDENDEKCTS DEKRAESDIL KRFCKGFIDL LFVRTINSQK
YYSILDWKSD MLENNNYTPE ALKEKVDNDY SIQRVLYSYC LIQWLKQFYG EGTAENLSED
DIFKKHFGGI YYAFIRGTEG GTPKGIYAQT WNSYTELANA YQKVKDLMSK PSIVKEEN
//
