ID F4H380_CELFA Unreviewed; 1166 AA.
AC F4H380;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN OrderedLocusNames=Celf_1166 {ECO:0000313|EMBL:AEE45301.1};
OS Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 /
OS NCIMB 8980 / NCTC 7547).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=590998 {ECO:0000313|EMBL:AEE45301.1, ECO:0000313|Proteomes:UP000008460};
RN [1] {ECO:0000313|EMBL:AEE45301.1, ECO:0000313|Proteomes:UP000008460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 /
RC NCTC 7547 {ECO:0000313|Proteomes:UP000008460};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA Woyke T.;
RT "Complete sequence of Cellulomonas fimi ATCC 484.";
RL Submitted (APR-2011) 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 -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
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DR EMBL; CP002666; AEE45301.1; -; Genomic_DNA.
DR AlphaFoldDB; F4H380; -.
DR STRING; 590998.Celf_1166; -.
DR KEGG; cfi:Celf_1166; -.
DR eggNOG; COG0210; Bacteria.
DR eggNOG; COG2887; Bacteria.
DR HOGENOM; CLU_003630_1_1_11; -.
DR Proteomes; UP000008460; 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 CDD; cd17932; DEXQc_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.30.160.800; -; 1.
DR Gene3D; 3.90.320.10; -; 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; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF55; DNA HELICASE; 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 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 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:UP000008460}.
FT DOMAIN 16..365
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 366..680
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1114..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1166 AA; 123721 MW; 51262DD373B76E0A CRC64;
MSLLPAARIA ALVGQPPPTP EQERVVEAPL SPALVVAGAG SGKTETMAAR VVWLLANGLV
APEQVLGLTF TRKAAAELAE RVRRRLRRLA RAAAQEGVEL PGGAALAGTT GDVLGSLARP
TVATYNAYAS SLVTDHALRL GLDPSARLLG EAAQWQLAHE VVEAWTGDVD TDAAVSTVVD
AVLSLCGALD EHLLTPAQAQ SGIAEIVEAI AATPDGPGRR REPYRDVQAL VRLLGERSRV
LDLVAEYRER KRAADAIDFG DQVALAARLA RDVPEVAAGE RDRFRVVLLD EYQDTSYAQL
TLLGALFGDG HPVTAVGDPH QSIYGWRGAS AGGLESFPTS FPAVDADGRR RPADVHVLST
SWRNDRRILD AANVVAGPLR AAAARVEVPV LAARPGAGDG RVHAHVADTV EDEARAVAEF
VAARWRPASP GTERVTAAVL CRKRSQFPAV QRALRAAGLP VEVVGLGGLL ATPEVVDLVA
ALQAAHDPSR GDALMRLLTG GRTRLGAADL HALGAWADEL AGRAGRRAGR DTGVQADVVD
ERSIVDALDD LPRSGWRSRN GRELSDAGRA RLAELARLLT ALRSHTYLAV PELVAEAERL
LGLDIEVAAR AGTTPGRARA NLDAFRDVAV EFARTADHPT LGGFLTWLDA AEVRESGLDM
PVAEPDPDAV QVITIHAAKG LEWDVVAVAG LVDGILPATR TRGQDGPKDS AWLTGLGTLP
YPLRGDRHDL PVLAYAGAAD HKDLDERRKQ FLLDAGLHQV AEERRLAYVA LTRARSDLLL
TAAWWGDSAR PRELSSFLEE LAEAGVVGSG SWVERPEQGV GNPRDELVLT AQWPADPFAV
DGGPGRRPAV EAAATLVRDA LAAGADSSGQ PGGSRWEDLA DRLLAEQERV RRPERGVELP
AHLSASSLVR LHADPAEFAR GLRRPVPREP SPQARRGTRF HAWVEGWYGA ATLVDLDALP
GADDDSDLVD LEEAALRASF LRTPWADRSP LAIEVDVETS VDGYVLRSRI DAVFADDEAG
REAAPQPAGA GAGAAVRPVV VVDWKTGAPP SDPAARASRE LQLAVYRLAW SRWTGTPLDL
VRAAFCYVGT GETVYPERLL AEPEITDLLR RATAASAQAP GDGPARGVGR TRSAPSNVDR
GGANPAVPGR ATESQSRRAP APPDRP
//
