ID A0A258FST5_9CAUL Unreviewed; 1163 AA.
AC A0A258FST5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
DE AltName: Full=DNA 3'-5' helicase II {ECO:0000256|ARBA:ARBA00034923};
GN ORFNames=B7Z01_04545 {ECO:0000313|EMBL:OYX34812.1};
OS Brevundimonas subvibrioides.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=74313 {ECO:0000313|EMBL:OYX34812.1, ECO:0000313|Proteomes:UP000215595};
RN [1] {ECO:0000313|EMBL:OYX34812.1, ECO:0000313|Proteomes:UP000215595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32-69-9 {ECO:0000313|EMBL:OYX34812.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-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:OYX34812.1}.
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DR EMBL; NCEB01000007; OYX34812.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258FST5; -.
DR Proteomes; UP000215595; 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 Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR InterPro; IPR014151; DNA_helicase_AddA.
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; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR NCBIfam; TIGR02784; addA_alphas; 1.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
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 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 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}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 13..490
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 522..805
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 962..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1163 AA; 126698 MW; 5FE1E61822735A93 CRC64;
MSADASLSLD LGRILPDPAQ IDAADPRQSV FVTANAGSGK TSTLVDRVAR LLLAKVSAAE
ILCVTYTKAA AAEMQARLYQ RLGAWAVEDD AKLRQSLADL DNRDPERLSA DDLRQARKLF
AQALDTPGGL KIQTLHAFCE KLLRRFPLEA GVTPGFKVLE DQAAVALSRA AREDLARRAL
DNPDGAIGRA YAHFAVALAF ADFEALLARI EQDRAKLLDY VARWQDGRAP GPWMLAGAEE
GRDAATIEAE FMRYLDRAAW LSVAEQMATG GSDDTKCADR MWQADWTFEG VSSVFLTGGK
PRARIATSKA PPFARDWLTT LQDKVMATLG EVRKARLAED TLHVLTLAQA HGALYDQRKA
AKGALDFGDL VARTVELLTQ RTSAAWVLYK LDGGIEHVLI DEAQDTAPEQ WAIVSALTEG
FFAGVGSRRF GAGTVERTVF AVGDEKQSIY SFQGARPERL NQEAQRYDLM VRGAGFAFKA
VELATSFRST PEVLGFVDAV FDGPERTRAL VGEQVAAIPE HKAMRALDQG CVDLWPLYQD
EKAPERDAWD DPVDEEPVTG ARKRMAAALA QEIKRQVETG VAVQNKTDGE LRPAGYGDFL
ILVRRRDATF EEIIRALKSA GVPVAGADRL KLSTHIAFSD LISLARFALY PDDDLSLAEV
LRSPFCDVDE DGLFDLAGAR EKRGRLWREL RDRAAERPEW ARARDLLTFA IDTRGRDPFA
FFSGLLNGVD ETGLGGRARV LARLGREAEE ALDETLNQVL AAEDRGGLDL ETALSMLEQA
DVEVKRELEG ARGEVRVMTV HGAKGLEAPV VILPDTTSRA KGMGPALMPV ALDDGGEGWL
MCLGRKEEDC EAAAGARAAR EQRAVDESLR LLYVALTRAR DRIIVMGRGV GNQKDGFEPG
SWWSILTETF DRLGEQVRDI GDDRRRFGHD PQVLGRGSAA VAAPATVVPD WARHVPPVDP
SARYVSPSQA KGPTRAAAPS PLAVASGGEG APLGRFRRGD LIHLLLERLP EIAPDARPEA
ARRLLARERG LSDVQRSEMI AAAHRVLDDP RFAPVFGPGS RAEVALVGSA PELAPGVSIN
GRIDRLVVTP ERILVVDYKT NRPAPDRIED ADPAYVTQMA VYVAVLRTLY PDRPVEAALV
WTDGPRLMAV PEGMMAEALA GLR
//
