位置:首页 > 蛋白库 > ADDA_LACP3
ADDA_LACP3
ID   ADDA_LACP3              Reviewed;        1234 AA.
AC   Q038V7;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=ATP-dependent helicase/nuclease subunit A {ECO:0000255|HAMAP-Rule:MF_01451};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01451};
DE            EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01451};
DE   AltName: Full=ATP-dependent helicase/nuclease AddA {ECO:0000255|HAMAP-Rule:MF_01451};
GN   Name=addA {ECO:0000255|HAMAP-Rule:MF_01451}; OrderedLocusNames=LSEI_1489;
OS   Lacticaseibacillus paracasei (strain ATCC 334 / BCRC 17002 / CCUG 31169 /
OS   CIP 107868 / KCTC 3260 / NRRL B-441) (Lactobacillus paracasei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=321967;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 334 / BCRC 17002 / CCUG 31169 / CIP 107868 / KCTC 3260 / NRRL
RC   B-441;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
CC   -!- FUNCTION: The heterodimer acts as both an ATP-dependent DNA helicase
CC       and an ATP-dependent, dual-direction single-stranded exonuclease.
CC       Recognizes the chi site generating a DNA molecule suitable for the
CC       initiation of homologous recombination. The AddA nuclease domain is
CC       required for chi fragment generation; this subunit has the helicase and
CC       3' -> 5' nuclease activities. {ECO:0000255|HAMAP-Rule:MF_01451}.
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:0000255|HAMAP-Rule:MF_01451};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01451};
CC   -!- SUBUNIT: Heterodimer of AddA and AddB/RexB. {ECO:0000255|HAMAP-
CC       Rule:MF_01451}.
CC   -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01451}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000423; ABJ70265.1; -; Genomic_DNA.
DR   RefSeq; WP_011674519.1; NC_008526.1.
DR   RefSeq; YP_806707.1; NC_008526.1.
DR   AlphaFoldDB; Q038V7; -.
DR   SMR; Q038V7; -.
DR   STRING; 321967.LSEI_1489; -.
DR   EnsemblBacteria; ABJ70265; ABJ70265; LSEI_1489.
DR   KEGG; lca:LSEI_1489; -.
DR   PATRIC; fig|321967.11.peg.1470; -.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   Proteomes; UP000001651; Chromosome.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 4.
DR   Gene3D; 3.90.320.10; -; 1.
DR   HAMAP; MF_01451; AddA; 1.
DR   InterPro; IPR014152; DNA_helicase_suAddA.
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; PTHR11070; 1.
DR   PANTHER; PTHR11070:SF48; PTHR11070:SF48; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF52980; SSF52980; 1.
DR   TIGRFAMs; TIGR02785; addA_Gpos; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW   Hydrolase; Nuclease; Nucleotide-binding.
FT   CHAIN           1..1234
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379277"
FT   DOMAIN          2..475
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          507..806
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   BINDING         23..30
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ   SEQUENCE   1234 AA;  136819 MW;  46B5EC69212BD213 CRC64;
     MTQFTTSQQA AITHDGHDVL VSASAGSGKT TVLVERIIQK ILKQHADITR MLIVTFTRAA
     TAEMRTKIQT ALKKALTERR HELSGEDRRH LANQIAMVNA AKISTLDAFS LQIVQTYYYV
     IDLDPGFRLL TDETERYMLQ ERVWDDLREQ LYASDEAPAF EQLTANFSGD RDDSGLQDLM
     FELIRQAGAT TDPKAYLEGL ATPYAPEKWE ATFSQQIWPR VKGQLLQIAT SLTQASALAN
     QLPNPIWYQQ IQADLAPLQT LLETNAPTYD TVRSVLISHE FAAWSRISKG LDDADKDTKN
     AAKDLRDAAK KTWQNKLAPT FALAAEQIGD LLREAQPLVA TLANVALKFE DALTAEKAAR
     HVQDYSDIAH NALRILQQKD PQTGAPIADN YRASFDEVMV DEYQDISPLQ EALLAAVSTT
     TPGDRFMVGD VKQSIYGFRL ADPQLFIHKY QTFQDAPTDP AAPERIILAE NFRSTKNVLA
     FTNLIFSQIM DPEVGDLSYD NAAALKYGAL DYGDAHPAVK VLLYSKATSD EDSSDASELP
     GDADDNEPVD IATGQTQLVL AEIQRLINDP DAQLWDRQAQ EYRRIHYRDI TLLTRQTSQN
     SLIQTQFAAA GVPLFVADTK NFFKTTELMV MLALLKVIDN QKQDIPLVAV LRSPIVGLSA
     DQLALIRLAA KQVPYYDAVT AFLQAEPKTP LAQRTHDMLT HFFNQLSHFR DLARENDLVT
     LLWAIYQDTG FLDYVGGTPG GSQRQANLQA LIDRARTYEA GGFKGLFAFI HFITLMQKQD
     QDLAMPAQVD PDNDAVKLMT IHKSKGLEFP VVFLMQANKH FNMSDQTGTA ILTKQGIGIK
     WLDPETRVEY ELPQYQAAKA ARQNQTLAEE MRLLYVALTR AQQRLYVVGA TMSGNQLTSA
     DKTVEKWAAA AEGEARVLAP QVRSGATSYL DWIGPALIRH PQARGLAETT IKPALVGDET
     EFTIEIDVNP QVTPTATPEK VSDDSGTMVD LSAWFKKAYP FQAATTTTGF QSVSEIKRAF
     DDPDTIDLVN ADRFLGPKPP MRDLTAPAFL TETPSGISPA AIGTATHLLL QLVDLAKPIT
     MASLRALRDQ LTTTQVIAVD VAKHIDLTAL IRFFETDLGR LLLAKPQQVH REVPFSMLLP
     ADQVFEALAD DPGEDVLIHG IIDGYVSDEQ GVTLFDYKTD HNPNTAVLVD RYRGQLNLYA
     QALQDLQPKP VLHRYLVFLR TGTVVDLVAS GAGK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024