ID R4SJB4_9PSEU Unreviewed; 1085 AA.
AC R4SJB4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN Name=uvrD {ECO:0000313|EMBL:AGM03714.1};
GN ORFNames=AORI_1125 {ECO:0000313|EMBL:AGM03714.1};
OS Amycolatopsis keratiniphila.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis; Amycolatopsis japonica group.
OX NCBI_TaxID=129921 {ECO:0000313|EMBL:AGM03714.1, ECO:0000313|Proteomes:UP000013968};
RN [1] {ECO:0000313|EMBL:AGM03714.1, ECO:0000313|Proteomes:UP000013968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HCCB10007 {ECO:0000313|EMBL:AGM03714.1,
RC ECO:0000313|Proteomes:UP000013968};
RX PubMed=23627759; DOI=10.1186/1471-2164-14-289;
RA Tang B., Wang Q., Yang M., Xie F., Zhu Y., Zhuo Y., Wang S., Gao H.,
RA Ding X., Zhang L., Zhao G., Zheng H.;
RT "ContigScape: a Cytoscape plugin facilitating microbial genome gap
RT closing.";
RL BMC Genomics 14:289-289(2013).
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; CP003410; AGM03714.1; -; Genomic_DNA.
DR RefSeq; WP_016331522.1; NC_021252.1.
DR AlphaFoldDB; R4SJB4; -.
DR KEGG; aoi:AORI_1125; -.
DR PATRIC; fig|1156913.3.peg.1151; -.
DR HOGENOM; CLU_003630_1_1_11; -.
DR Proteomes; UP000013968; 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:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR CDD; cd17932; DEXQc_UvrD; 1.
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; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF55; 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:UP000013968}.
FT DOMAIN 22..367
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 368..674
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 43..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1085 AA; 118922 MW; 12F8CE9AF82C38FA CRC64;
MISELQRRQV EPGEIARALG LHSPTDEQAE VIAAPIEPSL VVAGAGAGKT ETMAARVVWL
VANSVVPPER VLGLTFTRKA ARQLADRVRT RLRRLVGSGL LDKIDPTGDL RTTVTAGEPT
VLTYHAYAGR LLSEHGLRLP VQPGVRLLSE TSSWQFSHRV VSTWDNDLDT DRVPSTVTAQ
LLALAGELGE HLVETERLAQ YTSWLCEVIE NAPRAKGQRA SLPQKLAEVM TAQRFRLALL
PLVEAYHARK RAEGALDFAD QMSLAAQLAS SYPAVVAGER ERYGAVLLDE YQDTGHAQRI
LLRSLFGGVE HPPMPVTAVG DPAQAIYGWR GASAANLPRF TTDFPRDNGE RLVPALDFGL
LTSFRNPPEV LELANAISEP LRERGLGVAR LRALEGAGTA DIAAALLPDI RAEREWVADA
VAKRWFETME ETGKPPTAAV LVRRRADMAP IAAEMRARGL PVEVVGLGGL LDEPEVADLV
STLRVLADPL AGSAAARLLT GARWRIAAAD LAALWRRAGE LSSPVPPSGK SDVDEPVLVT
ERVEQAGLAD AIDDPGAPER YSPEGYRRIR RIGAELSALR RRLDQSLPEL VADVERTMLL
DVESLARPGP AGRAHLDAFA DVVTDFAETS PTATLLSFVD YLNTAAHAED GLTPGEVEVV
PDRVQVLTVH SAKGLEWRIV AIPHLVKEVF PGRRRSSSWL RTSTSLPAAL RGDSEDLPEL
RIPEGADRKE VQEALELHEE GFVAREADEE RRLCYVALTR SEHTMLISGH WWNESSARPK
GPSEFLLEIG EVMRANSVGR IEHWADEPET DGENPLVADS RRSRWPVDPL WPRREGVTNG
VDMVLGAMED AEHAEEEEED DPDGWISDTK VLLEERARAR DRVQQVVLPP HLSVSQLVEL
SADPAELAKR LRRPLPVRPN TYARRGTAFH GWLEQRFGGE QLLEIHDLPG AADVDEAPDT
ELEALQAAFE KSEWAHRVPH AVEVPFSADV VGVTVRGRMD AVFADADGGW TVVDWKTGAV
PEADRLESLA VQLAAYRLAW AALKNIPVEK VRAAFHYVKH DKTVRPADLL DAEGLRQLLR
SVPTV
//
