ID A1KRV3_NEIMF Unreviewed; 766 AA.
AC A1KRV3;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=recQ {ECO:0000313|EMBL:CAM09582.1};
GN OrderedLocusNames=NMC0269 {ECO:0000313|EMBL:CAM09582.1};
OS Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS 15464 / FAM18).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=272831 {ECO:0000313|EMBL:CAM09582.1, ECO:0000313|Proteomes:UP000002286};
RN [1] {ECO:0000313|EMBL:CAM09582.1, ECO:0000313|Proteomes:UP000002286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700532 / DSM 15464 / FAM18
RC {ECO:0000313|Proteomes:UP000002286};
RX PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA Quail M.A., Achtman M., Barrell B., Saunders N.J., Parkhill J.;
RT "Meningococcal genetic variation mechanisms viewed through comparative
RT analysis of serogroup C strain FAM18.";
RL PLoS Genet. 3:230-240(2007).
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; AM421808; CAM09582.1; -; Genomic_DNA.
DR RefSeq; WP_002221588.1; NC_008767.1.
DR AlphaFoldDB; A1KRV3; -.
DR KEGG; nmc:NMC0269; -.
DR HOGENOM; CLU_001103_14_2_4; -.
DR Proteomes; UP000002286; Chromosome.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR GO; GO:0009432; P:SOS response; IEA:InterPro.
DR CDD; cd17920; DEXHc_RecQ; 1.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 1.10.150.80; HRDC domain; 3.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR006293; DNA_helicase_ATP-dep_RecQ_bac.
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 InterPro; IPR018982; RQC_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR01389; recQ; 1.
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; 3.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR Pfam; PF09382; RQC; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00341; HRDC; 3.
DR SMART; SM00956; RQC; 1.
DR SUPFAM; SSF47819; HRDC-like; 3.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50967; HRDC; 3.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:CAM09582.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAM09582.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 27..195
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 216..366
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 524..604
FT /note="HRDC"
FT /evidence="ECO:0000259|PROSITE:PS50967"
FT DOMAIN 610..690
FT /note="HRDC"
FT /evidence="ECO:0000259|PROSITE:PS50967"
FT DOMAIN 691..766
FT /note="HRDC"
FT /evidence="ECO:0000259|PROSITE:PS50967"
SQ SEQUENCE 766 AA; 85900 MW; 6EBB2A28AA3A111E CRC64;
MHRPTAKQIL HEVFGYPEFR GRQEAVINTL AGGGSLTVLM PTGGGKSLCY QIPALMREGV
AVVVSPLIAL MNDQVASLHV AGIEAAAVNS GTSADEAREI ADKLAQGRLK LLYVAPERLV
TDRFLRFLDQ QTVSLFAIDE AHCVSQWGHD FRPEYQQLGM LAERYPNVPR IALTATADAA
TRADIKHYLH LDDAPEFISS FDRPNIYYQV IEKNNGKKQL LEFIRKEMAG QSGIVYCLSR
KKVEDVAQFL RENGLNAIPY HAGLSMDVRE ENQRRFTHED NIIVVATVAF GMGIDKPDVR
FVAHLDMPQS VEHFYQESGR AGRDGLPAAS WLCYGLNDWV LLRERIAEGN SDEVQKQIEM
QKLDAMLSVC ETAACRRVLL LKHFGEESEP CGHCDNCLHP PVRFDGTVLV QKLLSCVYRA
GQRFAAGYIT NLLRGKSDDW IRGNRHEQLS TFGIGAELSD KEWRSVIRQC ISLGYLTVNI
ARYQALQLTE AAKKVLKGET EVMLRPLKRG KPAARTLKDN WLRTEREERL WQALRVWRMK
QAEAEGIPAY MIFGDKTLRD LVEKMPQNLN GLHDIYGLGE AKTERFGHGI LEVCRNAAGF
SRDAVIRPQT EREQQLRQKL EAWRYEQARA ENCALHAVLS DESLADMLAD TPETETDLEG
VHGLGSVRAA KYGRDILAVC RPFSDGIDET AKHKRRLMRA LIQWCNETAK HEQSEPYRIL
SKAALRAIAA KQPEGLAELA AVYGVGEEKA ARYGAAVLAV LERNAV
//
