UVRD_HAEIN
ID UVRD_HAEIN Reviewed; 727 AA.
AC Q02322;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=DNA helicase II;
DE EC=3.6.4.12;
GN Name=uvrD; Synonyms=mutB; OrderedLocusNames=HI_1188;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8294031; DOI=10.1016/0378-1119(93)90444-8;
RA Walter R.B., Morton K.A., Stuy J.H.;
RT "The sequence of the Haemophilus influenzae mutB gene indicates it encodes
RT a DNA helicase II-like protein.";
RL Gene 136:35-40(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [3]
RP CHARACTERIZATION.
RX PubMed=3259573; DOI=10.1128/jb.170.6.2537-2542.1988;
RA Walter R.B., Stuy J.H.;
RT "Isolation and characterization of a UV-sensitive mutator (mutB1) mutant of
RT Haemophilus influenzae.";
RL J. Bacteriol. 170:2537-2542(1988).
CC -!- FUNCTION: May process damage occurring in non-replicating regions of
CC DNA to produce recombinational intermediates for sister strand
CC recombinational exchange.
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 -!- INTERACTION:
CC Q02322; Q02322: uvrD; NbExp=2; IntAct=EBI-7817147, EBI-7817147;
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
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DR EMBL; M99049; AAC36867.1; -; Unassigned_DNA.
DR EMBL; L42023; AAC22841.1; -; Genomic_DNA.
DR PIR; H64188; H64188.
DR RefSeq; NP_439344.1; NC_000907.1.
DR AlphaFoldDB; Q02322; -.
DR SMR; Q02322; -.
DR MINT; Q02322; -.
DR STRING; 71421.HI_1188; -.
DR EnsemblBacteria; AAC22841; AAC22841; HI_1188.
DR KEGG; hin:HI_1188; -.
DR PATRIC; fig|71421.8.peg.1240; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_5_2_6; -.
DR OMA; YQDTNRT; -.
DR PhylomeDB; Q02322; -.
DR BioCyc; HINF71421:G1GJ1-1219-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0033202; C:DNA helicase complex; IBA:GO_Central.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro.
DR GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR005753; DNA_helicase_ATP-dep_UvrD.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070; PTHR11070; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01075; uvrD; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; DNA replication; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..727
FT /note="DNA helicase II"
FT /id="PRO_0000102074"
FT DOMAIN 9..290
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT DOMAIN 291..568
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00617"
FT BINDING 33..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT BINDING 288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 18
FT /note="R -> A (in Ref. 1; AAC36867)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="H -> R (in Ref. 1; AAC36867)"
FT /evidence="ECO:0000305"
FT CONFLICT 240..242
FT /note="ILA -> FLP (in Ref. 1; AAC36867)"
FT /evidence="ECO:0000305"
FT CONFLICT 389..400
FT /note="RQEIKDALAYLR -> LKKLKMRYAIFV (in Ref. 1; AAC36867)"
FT /evidence="ECO:0000305"
FT CONFLICT 459..460
FT /note="ST -> QQ (in Ref. 1; AAC36867)"
FT /evidence="ECO:0000305"
FT CONFLICT 638..643
FT /note="AELPRE -> GRITER (in Ref. 1; AAC36867)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 727 AA; 83712 MW; 67FD98A7E455677E CRC64;
MMDISELLDG LNDKQRERVA APLGNHLVLA GAGSGKTRVL THRIAWLIAV ENISEGSIMA
VTFTNKAAAE MRHRIQSTLA KHAQHQLFGM WIGTFHSIAH RLLRAHHLDV GLPQDFQILD
SEDQLRLIKR LLKLHNFDEK AFPPKQACWY INNKKDEGLR PNDIEDFNDR QEREWIKIYQ
IYQDTCDRAG LVDFAELLIR VYELFEKKPL ILQRYQQRFQ HILVDEFQDT NKIQYKWIKI
LAGKTGQVMI VGDDDQSIYG WRGAQIENIQ KFLKDFKAET IRLEQNYRST ANILNSANEL
IANNSDRLGK NLWTEGEKGD PVGIYSAFNE LDEAKFVASQ IQDWVEHGGK LDDCAVLYRS
NSQSRVIEEA LIRCQIPYRI YGGMRFFERQ EIKDALAYLR LINNRQDDAA FERVINTPTR
GIGDRTLDIL RNLTRERQIT LWQAVQVATQ ENMLAGRAST ALLRFQELIN SLQLDTAEMP
LFAQTDFVIK HSGLYEMYQQ EKGEKGEVRI ENLEELVTAT REFIKPDNAE EMTELTAFLT
HASLEAGEEQ ASPHQSCVEM MTLHSAKGLE FPRVFMVGVE EGLFPSFRSF EEPGRLEEER
RLAYVGITRA KKKLTISYAE SRRLYAKEER HLPSRFIAEL PRECIQEIRL RGTVTRAMNL
AKVGSLSNTS AVENEWKMGQ KVKHEKFGFG TVINVEGSEN NTRLQIAFQA QGIKWLIAHL
AKLEKVR
