ID A0A076H8S4_9SYNE Unreviewed; 1194 AA.
AC A0A076H8S4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=KR49_03695 {ECO:0000313|EMBL:AII45563.1};
OS Synechococcus sp. KORDI-49.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=585423 {ECO:0000313|EMBL:AII45563.1, ECO:0000313|Proteomes:UP000028589};
RN [1] {ECO:0000313|EMBL:AII45563.1, ECO:0000313|Proteomes:UP000028589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KORDI-49 {ECO:0000313|EMBL:AII45563.1,
RC ECO:0000313|Proteomes:UP000028589};
RA Choi D.H., Kwon K.-K., Lee J.-H., Noh J.H.;
RT "Genome sequences of Synechococcus sp. KORDI-49.";
RL Submitted (JUN-2013) 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};
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DR EMBL; CP006270; AII45563.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A076H8S4; -.
DR STRING; 585423.KR49_03695; -.
DR KEGG; synr:KR49_03695; -.
DR PATRIC; fig|585423.3.peg.703; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_6_1_3; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000028589; Chromosome.
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:0008854; F:exodeoxyribonuclease V activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR CDD; cd22352; RecB_C-like; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.3170.10; Recbcd, chain B, domain 2; 1.
DR HAMAP; MF_01485; RecB; 1.
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; IPR004586; RecB.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF23; RECBCD ENZYME SUBUNIT RECB; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 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}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 1..466
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 467..734
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 21..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1194 AA; 133883 MW; E4D31E08A849F399 CRC64;
MVQRFEANSY PLVPGLRLLE ASAGTGKTFA LAHLCLRLIT EAQHPLEQLL VVTYTEAAAD
ELRSRIGQRF QAALEGLEAL ETEAAPPAAD PVLENWLEHA ADTTLRRQWI SCLLLALEQL
DRADITTIHG FCRRTLRRMA LSSGAAMDPE LETDSTDLLQ QVVQDIWRDQ LLTLPADQLI
GLRQSGLSPE AMVQALRVLD GEPHPCVLAE RDDFDPDEPL AAQLQLWMGR CWERFLILWK
RDGESLETRF RSSAAQWKAQ GCRDTKPYSG KPRTDRCALL DRWIADQNGI PSLTAIRAQK
GLLRDYFHPG CWCSTARRCG ESDPSLAAAE LQQVMAALWD GPPERVWRFV LNRALRELAA
RRTRRGVISF PGLLAALDPG EEDAPWLEPL RCRYRAVMVD EFQDTDPLQW RLLRRTFAER
GNHLLLLVGD PKQAIYRFRG GDLDTYLQAR RQADRIDALQ ENFRTTPTLM RALNDLMRPG
LVRSELPVPA VEPRGSAQAP PRGCPLQLLH WCGETPLTKT ALVEELPLRL ADAVLRLLQE
RDDLTPAQLC LLVSTHRQAT ELRRALSSRG LPTRLVSQGD VFETEAAVVL QRLLDALAQP
GDERRLRLLA CSPLMGWPPD DLSIDGRLDQ LALRLRAWAV QMPTIGLLGC LSDLLDGERM
AELSDRGRML GDLQQAARLV QEVMHRQGLD IASAATWLRR ERLHPADPVP EPRQPHSDLV
ESAIAVVTVH RSKGLEYPVV ICPTLWEGPR VGGGPLWRDG GEGSWRLLLD SRWGRGLDLA
QQEETAAMAE AERLAYVALT RARSQLVLVW ARVTRQEGSP LVSWLFGADA VGQPIDQLTD
ERLSAELAER ALAIELTSLE PPDPAPRRWR SPAPTDRLCI GAVPQRIDRR WGRSSYSAWT
ATSEDPARHE QGRDADPEGE EILDEVDDHW PEDGPLRDFP RGASAGDCLH RILEQVSYQP
STPDPELVEA ELRRAGLDIS WVPAVQQGLR LVVETPLGGP LGDLSLDQLA PEQRHPELGF
DLPVEQVRTA DLVKAFQAEP EARFGEDYLE RLASLSVNSR GFLTGSIDLV FVDPNLRWWV
LDWKSNWIGE RSGDGSDDRC GPRHYTDAAM GLQMIHHHYP LQAHLYLVAL HRHLRWRLPG
YLPERHLGGY VYAFLRGMPG SRQPGSRAAP GRIVEPAPLR RVLALDRLLQ EGGR
//
