ID A4ALD4_9ACTN Unreviewed; 1033 AA.
AC A4ALD4;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=A20C1_13261 {ECO:0000313|EMBL:EAR23821.1};
OS marine actinobacterium PHSC20C1.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=312284 {ECO:0000313|EMBL:EAR23821.1, ECO:0000313|Proteomes:UP000003868};
RN [1] {ECO:0000313|EMBL:EAR23821.1, ECO:0000313|Proteomes:UP000003868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHSC20C1 {ECO:0000313|EMBL:EAR23821.1,
RC ECO:0000313|Proteomes:UP000003868};
RA Murray A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) 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}.
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:EAR23821.1}.
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DR EMBL; AAOB01000014; EAR23821.1; -; Genomic_DNA.
DR AlphaFoldDB; A4ALD4; -.
DR STRING; 312284.A20C1_13261; -.
DR eggNOG; COG0210; Bacteria.
DR eggNOG; COG2887; Bacteria.
DR HOGENOM; CLU_004900_0_0_11; -.
DR OrthoDB; 5240387at2; -.
DR Proteomes; UP000003868; 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; 1.10.10.160; -; 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; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
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 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}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000003868}.
FT DOMAIN 18..321
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 313..617
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1033 AA; 111049 MW; 18D52B3A6D581096 CRC64;
MVNLLPERSD VAAPEPHTLD DSQRVVVELD EGVSAIVVGA PGSGKTETLV EVVAERVHSR
GWSPEQIVVL SATRQSATAL RDRLASRIDA PTLGPMARTA NSLAFEVIRE AAAVAGDGAP
TLLTGAEQDQ IIAELLAGEI ADGSGAPWPS HLDAEVRRLR GFRTELRDLM MRCVEFGVTP
RDLAQLGERN DRPEWVAASA FISVYDAVKA SYRDRHFDAS ELLAEAAALI AEGHYAAVDR
LRLVIVDDAH ELTEATISLL RALATRGITI IGFGDPDLTT GSFRGAQPGV LSRWAEQLEL
ENCQTLFLSS VHRHSASLRS AVIDVTQRVG VSGLIEQRKS MSVATEPSSI HSFQLSTPAE
EVAFIARHLR EKHVLESVPW SRMAVIVRTG SLIPSLARQL RTLEVVTSVS SARSAVRDEF
SVNGLIVLLE LALERRTLDA ASAVELLSSS VGGFDAVSLR RLKAALRHEA LGAEIYDSAD
QLIAQALAAP AGFTSIETRV SRQAAAVAKN LHETAAAGAA GDTIEELLWG AWQRSGLADR
WFTQALGSGV VAEEANRHLD AVVALFSSAK RFVERRPDAP ANVFLTEWLS ADVAEDTLAA
RSIVDSVTVG TPASVIGQEF DVVVVAGVQE NVWPNLRVRG SLLGAHDLPR VLAGEKLAVA
DRRREVLHDE LRMFAQAISR ATREVLVTAV EGDDNMPSPF LTLIPSPDEP VRARPPLSLR
GLVGVLRREL TTSANPGAAA SSLARLAREG VPGADPSSWY GLRSPSTTAP LVDLSEPDAK
VRVSPSRMES FESCPLHWAI DQLGGSTSNT ASNLGTLIHG VAETATDFNA EALFKAVEDR
WSEMSFEASW QSEAEKLRAK KLTQHLATYL RDFTANGGEL ISNEMGFTLP LEQALLSGKI
DRVEMYGGTT AVIVDLKTGK NEPSTDKAVA DHPQLAAYQL AFASGAVEGV PEGLENGGAK
LVVLSPSAKT RDYVDPKQQP MNDEELELFR QRVIEDARGM AGSVFVARVS SHCTDPWSFG
NCRIHVVPAV SAR
//
