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Database: UniProt
Entry: A0A1M6HFR4_9BACT
LinkDB: A0A1M6HFR4_9BACT
Original site: A0A1M6HFR4_9BACT 
ID   A0A1M6HFR4_9BACT        Unreviewed;       719 AA.
AC   A0A1M6HFR4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=SAMN05720471_12115 {ECO:0000313|EMBL:SHJ21026.1};
OS   Fibrobacter sp. UWP2.
OC   Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC   Fibrobacter.
OX   NCBI_TaxID=1896216 {ECO:0000313|EMBL:SHJ21026.1, ECO:0000313|Proteomes:UP000184414};
RN   [1] {ECO:0000313|EMBL:SHJ21026.1, ECO:0000313|Proteomes:UP000184414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UWP2 {ECO:0000313|EMBL:SHJ21026.1,
RC   ECO:0000313|Proteomes:UP000184414};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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   -!- 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; FQYM01000021; SHJ21026.1; -; Genomic_DNA.
DR   RefSeq; WP_073190724.1; NZ_FQYM01000021.1.
DR   AlphaFoldDB; A0A1M6HFR4; -.
DR   STRING; 1896216.SAMN05720471_12115; -.
DR   OrthoDB; 9806690at2; -.
DR   Proteomes; UP000184414; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   CDD; cd07989; LPLAT_AGPAT-like; 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; 2.
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; IPR002123; Plipid/glycerol_acylTrfase.
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; PF01553; Acyltransferase; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 2.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000313|EMBL:SHJ21026.1};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Transferase {ECO:0000313|EMBL:SHJ21026.1}.
FT   DOMAIN          8..271
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   BINDING         32..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   719 AA;  82504 MW;  1B8441EE188AC619 CRC64;
     MDAQSILDGL NSDQRAAVLH DHQKGAQLLI LAGAGSGKTS VLTKRIQYRI AMGVDPEKIL
     ALTFTAKAAA EMRERVQKLF PKAGVRLCTF HSLALFMLKQ KIGSRFAYEM VGFKKPPVPQ
     ESAERDFLTK LSRLRIPSGK LNREELFADT YPASLVPKLK TLRQGVLDSG SVVFEDLIYL
     AISLLEKHRE ARDYFRAQWS EILVDEYQDI NPSQYRLVKA LLGSRKELFV VGDDDQAIYG
     FRGADIGNIN RFCEDFKESS LIRLEWNYRS VPEILHLANS IFENKPLRLR KVLRAGNTRG
     SGGNPLYREN RRPEVWYSEN PVEEMLKIVG WIKELRESYE LEWKNFAILV RYNRQRLYYE
     AALKDAGLPI AGVELDEGET LENGVHVETV HASKGLQYAV VFYAGLAEGL TPGECQGSRA
     ERQRQLDEER RLYYVGVTRA EAYLILLYCK QRFWKGKLRK FKKSRFLPQA RPKNEELKLP
     LILFKIYVVV RVLFVMFEHI LKLPFVYLFH KNEVDLWVDK KIQWFSNFCM DIINIDLTIE
     DQALLGKVDW TRPVFVMGNH NSFVDIPVVF LTIERTIGFI AKAQLGRIPF LNFWMHKIGC
     IFINREKGGG ADLVREALAH GRVPRISVFP EGTRGKSDDL APFKSGSFRL AIEAQATILP
     VVIKGSAGAW ERRRDCGRKK VTSRVLEPID VRALMQEKGE LEPRRDLMNV IRERMETAL
//
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