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Database: UniProt
Entry: A0A1U9NLS4_9BACT
LinkDB: A0A1U9NLS4_9BACT
Original site: A0A1U9NLS4_9BACT 
ID   A0A1U9NLS4_9BACT        Unreviewed;       720 AA.
AC   A0A1U9NLS4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   Name=pcrA {ECO:0000313|EMBL:AQT68859.1};
GN   ORFNames=STSP2_02035 {ECO:0000313|EMBL:AQT68859.1};
OS   Anaerohalosphaera lusitana.
OC   Bacteria; Planctomycetota; Phycisphaerae; Sedimentisphaerales;
OC   Anaerohalosphaeraceae; Anaerohalosphaera.
OX   NCBI_TaxID=1936003 {ECO:0000313|EMBL:AQT68859.1, ECO:0000313|Proteomes:UP000189674};
RN   [1] {ECO:0000313|Proteomes:UP000189674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST-NAGAB-D1 {ECO:0000313|Proteomes:UP000189674};
RA   Spring S., Bunk B., Sproer C.;
RT   "Comparative genomics and description of representatives of a novel lineage
RT   of planctomycetes thriving in anoxic sediments.";
RL   Submitted (FEB-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   -!- 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; CP019791; AQT68859.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1U9NLS4; -.
DR   STRING; 1936003.STSP2_02035; -.
DR   KEGG; alus:STSP2_02035; -.
DR   OrthoDB; 9810135at2; -.
DR   Proteomes; UP000189674; Chromosome.
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   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; 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; PF21196; PcrA_UvrD_tudor; 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};
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}; Reference proteome {ECO:0000313|Proteomes:UP000189674}.
FT   DOMAIN          9..285
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          286..558
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   720 AA;  81232 MW;  125C5BDA9AC6C2E9 CRC64;
     MTRQAFTTDQ LTESQRRAVF HKDGPLLVIA GPGSGKTRVI TSRIAALIDA GVRPWNICAI
     TFTNKAAEEM RERLAAGGGG EGVHTSTFHS LCVRLLRMYA DAAGISNNFS IYDTDDQRRC
     VKEAIKNSNI DSKTFTPAKV LSAISNFKND LETPEQILER ADEFYLKTAG RVYEQYQKLL
     KKNNALDFDD LLINTAFLLR DNPDIRQALG NRYQYLLVDE YQDTNHAQYQ IAKGLALEHR
     NICVTGDPDQ SIYKWRGADI QNILMFEKDW PDAVVVKLEE NFRSTPNILE MADVLIANNT
     QRKEKRLVAT HDRGADAEIE CYGDGLEESV EVAGKIQALI EEGADPNEIA VFYRVNSMSR
     TVEEAFVRQQ IPYQVVRGVE FYARKEIRDM LSYMKVIANP SDDMALLRAV GTHSRGIGKM
     TLSRVQHYAS QYGITMFNAM NQADAIDTIT PRTQTKVKAF AAMIEKWRAD ADGPVAPLME
     RVFDESGLLD SLRAGGEDEE SAIENIDELI NSASRYDEMT EEPSLIDYLQ SIALYSDTDA
     YDAEAGRVSL MTLHAAKGLE FDNVFIIGLE EGLLPHERSL VGGEEELEEE RRLFFVGITR
     ARKVLHISHA RYRTMRGQHL RTTPSKFLYE IGYTPKEEQF ESYTYDTEFS QVAPSGFGSK
     IEKKEAPFRT GELVEHRKFG TGRVKEFQDM GDNSIIVVRF QSGQVKTLML KYANLTKLSG
//
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