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Database: UniProt
Entry: E6UGK9_RUMA7
LinkDB: E6UGK9_RUMA7
Original site: E6UGK9_RUMA7 
ID   E6UGK9_RUMA7            Unreviewed;       752 AA.
AC   E6UGK9;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=ATP-dependent RecD-like DNA helicase {ECO:0000256|HAMAP-Rule:MF_01488};
DE            EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_01488};
GN   Name=recD2 {ECO:0000256|HAMAP-Rule:MF_01488};
GN   OrderedLocusNames=Rumal_2657 {ECO:0000313|EMBL:ADU23132.1};
OS   Ruminococcus albus (strain ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 /
OS   7).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=697329 {ECO:0000313|EMBL:ADU23132.1, ECO:0000313|Proteomes:UP000006919};
RN   [1] {ECO:0000313|EMBL:ADU23132.1, ECO:0000313|Proteomes:UP000006919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 / 7
RC   {ECO:0000313|Proteomes:UP000006919};
RX   PubMed=21914885; DOI=10.1128/JB.05621-11;
RA   Suen G., Stevenson D.M., Bruce D.C., Chertkov O., Copeland A., Cheng J.F.,
RA   Detter C., Detter J.C., Goodwin L.A., Han C.S., Hauser L.J., Ivanova N.N.,
RA   Kyrpides N.C., Land M.L., Lapidus A., Lucas S., Ovchinnikova G.,
RA   Pitluck S., Tapia R., Woyke T., Boyum J., Mead D., Weimer P.J.;
RT   "Complete genome of the cellulolytic ruminal bacterium Ruminococcus albus
RT   7.";
RL   J. Bacteriol. 193:5574-5575(2011).
CC   -!- FUNCTION: DNA-dependent ATPase and ATP-dependent 5'-3' DNA helicase.
CC       Has no activity on blunt DNA or DNA with 3'-overhangs, requires at
CC       least 10 bases of 5'-ssDNA for helicase activity. {ECO:0000256|HAMAP-
CC       Rule:MF_01488}.
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=3.6.4.12;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01488};
CC   -!- SIMILARITY: Belongs to the RecD family. RecD-like subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01488}.
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DR   EMBL; CP002403; ADU23132.1; -; Genomic_DNA.
DR   RefSeq; WP_013499259.1; NZ_JHYT01000019.1.
DR   AlphaFoldDB; E6UGK9; -.
DR   STRING; 697329.Rumal_2657; -.
DR   KEGG; ral:Rumal_2657; -.
DR   eggNOG; COG0507; Bacteria.
DR   HOGENOM; CLU_007524_0_2_9; -.
DR   OrthoDB; 9803432at2; -.
DR   Proteomes; UP000006919; Chromosome.
DR   GO; GO:0043139; F:5'-3' DNA helicase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   CDD; cd17933; DEXSc_RecD-like; 1.
DR   CDD; cd18809; SF1_C_RecD; 1.
DR   Gene3D; 1.10.10.2220; -; 1.
DR   Gene3D; 2.30.30.940; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   HAMAP; MF_01488; RecD_like; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR006345; DNA_helicase_RecD-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029493; RecD-like_HHH.
DR   InterPro; IPR041451; RecD-like_SH13.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR027785; UvrD-like_helicase_C.
DR   NCBIfam; TIGR01448; recD_rel; 1.
DR   PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR43788:SF6; RECBCD ENZYME SUBUNIT RECD; 1.
DR   Pfam; PF13604; AAA_30; 1.
DR   Pfam; PF14490; HHH_4; 1.
DR   Pfam; PF14520; HHH_5; 1.
DR   Pfam; PF18335; SH3_13; 1.
DR   Pfam; PF13538; UvrD_C_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF47781; RuvA domain 2-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01488}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_01488};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01488, ECO:0000313|EMBL:ADU23132.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488, ECO:0000313|EMBL:ADU23132.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01488}.
FT   DOMAIN          335..519
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   BINDING         346..350
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ   SEQUENCE   752 AA;  84015 MW;  891FAD3EBB26A5C3 CRC64;
     MSEAEKIEGE VDRVQFKSDD GSFCVIDVNT GDDLIKAVGE LGNIEEGESV ILTGEYVKHR
     TFGKQFRVQM FERSLPTGEA SILRYLVSGA LDSVKPVTAK RLVAAFGSDT LEIIENEPER
     LTEVNGIDAK KADAIHEDFK KTFAARALLV YMSKNGVATK YGVRAWRKLG NSAEELIKSN
     PYLLCTDGIE LGFSKADEIA EAEFIPRDSE QRIRAGMAFV LRNAAREGGH TCIPVETLKR
     DTVRLLDINA ELFDKVKEIA LEEQDIFELD ISGVKYAMLH CYYKAEEYIS RRLDVMRSIT
     YDNKIDYSEI IDMEEQESGI KYEEKQRKAI NLAISEGFLV LTGGPGTGKT TTLNAIISLF
     EQQGLDVMIA APTGRAAKRI SDMTGCEAKT IHRLLEVIPS DGDRMLFVHD EDDLLDCEVM
     VVDEMSMVDS VLFEALLRAL SVTCKLILVG DSDQLPPVGP GNVLRDIIDS GVMSVVRLTE
     VFRQAQESDI VMNAHRIVSG EMIDLKKRDR DFVYLRRPEA EDIYTTLVEL CSDRLPKKYG
     FSPIRDIQVL SPTRQGRIGT PELNKILQAE LNPPDKKKAE LKTAYGIYRV GDKVMQTRNN
     YEISWTRTDG GKEENGKGVY NGDIGIVTAV RTSLKIVTID FDGRIADYSG EILDDLELAY
     AVTVHKSQGS EYDAVILTLY DGMDNLYYRN LLYTAVTRAK KLLVILGTAQ RVGFMIMNNG
     KNRRCTALRT MLMQAVSGDD MGQLQLEDLN GQ
//
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