ID F4H379_CELFA Unreviewed; 1077 AA.
AC F4H379;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN OrderedLocusNames=Celf_1165 {ECO:0000313|EMBL:AEE45300.1};
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:AEE45300.1, ECO:0000313|Proteomes:UP000008460};
RN [1] {ECO:0000313|EMBL:AEE45300.1, 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; AEE45300.1; -; Genomic_DNA.
DR RefSeq; WP_013770326.1; NC_015514.1.
DR AlphaFoldDB; F4H379; -.
DR STRING; 590998.Celf_1165; -.
DR KEGG; cfi:Celf_1165; -.
DR eggNOG; COG0210; Bacteria.
DR eggNOG; COG2887; Bacteria.
DR HOGENOM; CLU_004900_0_0_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 Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF59; DNA HELICASE; 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 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 30..339
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 347..646
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 798..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 51..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1077 AA; 112236 MW; 14F6DCFD5DC434A0 CRC64;
MTTTPALRLV RPALADGPSS GPGSRVVLDD AQAAAVDRAV HGPDPALLVL GAPGTGKTTV
ALETVVAAVD AGLSPQDVLV VSAGRRAAAD LRDRLAARLR TTSGRPLVQT APAVAFSVLR
SRAALLGDVP PTLVGGADQD LLLAELLAGH AAGEGVPLRW PPHVPADVPT MRAFRDELRD
LLMRAAERGL TPADLADLGR RHERPEWETA ARVYEEYLDV LVLRSATPDL GARLDPAVVV
EEAAQALVAW EDEVGDVPRP RWRLVVVDDH QESTSATARL LRVLTADGAR LLLLADPDTA
VQTFRGASPA LVGRAPVAGD GDGELGAATL VLGTVWRHGP AVREVTARVT ERIGSVGAVQ
HRRAASALRP DPAAPPQVQA AVLPSAAQEA AFVAHTLRTA HLEHGVGWDR MAVVARSGGQ
VTALRRALAG ASVPVTVVGS DVPLREEPAV RPLLEAVRVV VGDAPLDPAA AARLVCSPLG
GLDAVGLRRV RRALRAEELA AGGGRTSDVL LVEALEDVGR VASLPASVAR PVARLAEVLA
AGRRAAERPG ADAQTVLWSL WHASGLAEPW RRAALVGGVA GERADRDLDA VLALFRAAET
FVDRMPRATA GAFADWLAAQ DLPSDSLAAA ARRLAVPVLT PAGAAGQEWD VVVVAGVQDG
VWPDLRLRDS LLGSQALVDV VADRAVDGTD PGARAAQARA AVLADELRSF AVACSRARHR
LVVTAVADAD QQPSPFLDLV EPADDETDHR RTTAPAAADL RGLVAELRGT LEHAVASGAR
PDPAVVRTLA RLAREGVPGA DPAEWHGLAD PTTDSPLWAD DERVPVSPSR LETAQRCALR
WALEAAGGTA ADSSGQTLGT LVHAIAQELP TGTRTELAAE LDRRWSELGL GDGWPARATR
RRADAMIDRL AGYLQGAGAP LLVEGGFTLR TDRAVVRGTV DRVERDPAAP DDAGTPVRVV
DLKTGSTVPS KAKAEVNPQL GAYQLAVDGG AFAELPADAR STGAVLVYVG AGSNATERPQ
PALGGEDDGP SWARTLVDEV ADRMAASTFA ATTNDLCDRC PVRRSCPART EGSQVVA
//
