ID C4ZAK4_AGARV Unreviewed; 659 AA.
AC C4ZAK4;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=ATP-dependent DNA helicase RecQ {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=EUBREC_0261 {ECO:0000313|EMBL:ACR74065.1};
OS Agathobacter rectalis (strain ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835
OS / VPI 0990) (Eubacterium rectale).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Agathobacter.
OX NCBI_TaxID=515619 {ECO:0000313|EMBL:ACR74065.1, ECO:0000313|Proteomes:UP000001477};
RN [1] {ECO:0000313|EMBL:ACR74065.1, ECO:0000313|Proteomes:UP000001477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835 / LMG 30912 / VPI
RC 0990 {ECO:0000313|Proteomes:UP000001477};
RX PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA Hettich R.L., Gordon J.I.;
RT "Characterizing a model human gut microbiota composed of members of its two
RT dominant bacterial phyla.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
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|ARBA:ARBA00001665};
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446}.
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DR EMBL; CP001107; ACR74065.1; -; Genomic_DNA.
DR RefSeq; WP_012741186.1; NC_012781.1.
DR AlphaFoldDB; C4ZAK4; -.
DR STRING; 515619.EUBREC_0261; -.
DR PaxDb; 515619-EUBREC_0261; -.
DR KEGG; ere:EUBREC_0261; -.
DR HOGENOM; CLU_001103_14_1_9; -.
DR Proteomes; UP000001477; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR CDD; cd17920; DEXHc_RecQ; 1.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 1.10.150.80; HRDC domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF105; BLOOM SYNDROME PROTEIN; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00570; HRDC; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00341; HRDC; 1.
DR SUPFAM; SSF47819; HRDC-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50967; HRDC; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 24..193
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 220..375
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 432..512
FT /note="HRDC"
FT /evidence="ECO:0000259|PROSITE:PS50967"
SQ SEQUENCE 659 AA; 73991 MW; 1F729920F8729404 CRC64;
MNINQTLKQY FGYDSLRTGQ EELINGILAG HDVLGIMPTG AGKSLCYQLP ALMLKGITLV
ISPLISLMSD QVKALNQAGV HAAYINSSLT ENQIRMALSY ASQGRYKIIY VAPERLNTPR
FLDFACNADI SMLTVDEAHC ISQWGQDFRP SYLEIAGFLT RLPRRPIVSA FTATATERVK
NDIVASLGLN NPVTMVTGFD RPNLFFRVVT RKGGSQKDNS IINYVKKHED ESGIIYCATK
KNVDKLYTLL NEQGISAGRY HAGLSNDERK QNQEDFTYDR IRVMVATNAF GMGIDKSNVR
YVLHYNMPQS LEYYYQEAGR AGRDGEEAEC VLFFSKQDIM INKFLLQNKA SAGDVASDMQ
KTANDRRKLQ QMINYCETDK CLREFILSYF GDTTPCICNK CSNCVVVEDE EEETYVETGK
KRKKAAQLAG LNELGAALFE KLRSVRTELA AEKSVPPYII CSDKTLKDMC AKLPRDKEQL
ADVYGMGEQK IQNYGEAFVT AVNSFVADNP NPSGSTTGER PQTVLSDEEA VEIGSTRKKK
LPFYIEPQRL DEVELTDKCR LTELTNKINE LCPADKEHKK LAASFINELL IAEGYLEEVT
EDGNKIKRVT EKGRSVGIDE EERKAKFGGS YYAITHSKQS QQVIIEMLKK HYGSIKPQE
//
