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Database: UniProt
Entry: A0A1Y0M5S1_9FLAO
LinkDB: A0A1Y0M5S1_9FLAO
Original site: A0A1Y0M5S1_9FLAO 
ID   A0A1Y0M5S1_9FLAO        Unreviewed;       773 AA.
AC   A0A1Y0M5S1;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=BTO04_02025 {ECO:0000313|EMBL:ARV05548.1};
OS   Polaribacter sp. SA4-10.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=754397 {ECO:0000313|EMBL:ARV05548.1, ECO:0000313|Proteomes:UP000195822};
RN   [1] {ECO:0000313|EMBL:ARV05548.1, ECO:0000313|Proteomes:UP000195822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA4-10 {ECO:0000313|EMBL:ARV05548.1,
RC   ECO:0000313|Proteomes:UP000195822};
RA   Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT   "Trade-off between light-utilization and light-protection in marine
RT   flavobacteria.";
RL   Submitted (DEC-2016) 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; CP019331; ARV05548.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y0M5S1; -.
DR   OrthoDB; 9810135at2; -.
DR   Proteomes; UP000195822; 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   CDD; cd18807; SF1_C_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:UP000195822}.
FT   DOMAIN          6..291
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          292..573
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         27..34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   773 AA;  88349 MW;  5FAAA08EB8A0DA5F CRC64;
     MNNYLDSLNE AQKQAVLQKD GPMIIIAGAG SGKTRVLTYR IAHLMKQGVD SFNILSLTFT
     NKAAKEMKER IASVVGASEA KNLWMGTFHS VFARILRSEA DKLGFPSNFT IYDSQDSVRL
     ISSIIKEMNL DKERYKPKQI LNRISSFKNS LITVRAYFNN SDLKEADLHA SRPEVGNIYK
     EYVDRCFKAG AMDFDDLLLR TNELLARFPE SLAKYQNRFR YIMVDEYQDT NHSQYLIVKA
     LADRFQNICV VGDDSQSIYS FRGANIQNIL SFQKDYPEVK TFKLEQNYRS TSTIVNAANS
     VIARNKTKLD KEVWTSNDAG ESINVMRTIS DGEEGRFVAQ SIWENKMNHQ LKNDQFAVLY
     RTNSQSRAIE DALRKKSIEY KIYGGISFYQ RKEIKDILSY LRILINPNDE EALKRIINYP
     ARGIGATTID KLTIAANHYK KSIFDILKYI DKIDLKINSG TKTKLQNFVN MMLRLQIESQ
     TKNAFEISEI VVKQTQLIKD LEKEGTPEAV SKVENVQELL NGIKDFITDK IEQGEDASLT
     TFLEDVALAT DFDSNKEDDK PSVSLMTIHQ SKGLEYSHVY VVGLEENLFP SAMSMSTRSE
     LEEERRLFYV ALTRAEKVAY LSYAQTRYRW GKLVDAEPSR FLEEIDDQYL HYITPKVPEP
     SINKFVDKSL FDDAPKGIRF QKPIQRKKVE RDLAKKKEIV VPKNLKKVTQ ATSSSNLFDN
     DIAVGNIIEH ERFGRGEVLS LEGKGPDKKA MIQFGTAGKK NLLLRFVKLK IIG
//
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