(data stored in SCRATCH zone)

SWISSPROT: A0A0E1NY90_YERPA

ID   A0A0E1NY90_YERPA        Unreviewed;      1123 AA.
AC   A0A0E1NY90;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   10-APR-2019, entry version 20.
DE   RecName: Full=RecBCD enzyme subunit RecC {ECO:0000256|HAMAP-Rule:MF_01486};
DE            EC=3.1.11.5 {ECO:0000256|HAMAP-Rule:MF_01486};
DE   AltName: Full=Exonuclease V subunit RecC {ECO:0000256|HAMAP-Rule:MF_01486};
DE            Short=ExoV subunit RecC {ECO:0000256|HAMAP-Rule:MF_01486};
DE   AltName: Full=Helicase/nuclease RecBCD subunit RecC {ECO:0000256|HAMAP-Rule:MF_01486};
GN   Name=recC {ECO:0000256|HAMAP-Rule:MF_01486};
GN   OrderedLocusNames=YPA_0490 {ECO:0000313|EMBL:ABG12458.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12458.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12458.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12458.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for
CC       recombinational DNA repair. Binds to DSBs and unwinds DNA via a
CC       highly rapid and processive ATP-dependent bidirectional helicase
CC       activity. Unwinds dsDNA until it encounters a Chi (crossover
CC       hotspot instigator) sequence from the 3' direction. Cuts ssDNA a
CC       few nucleotides 3' to the Chi site. The properties and activities
CC       of the enzyme are changed at Chi. The Chi-altered holoenzyme
CC       produces a long 3'-ssDNA overhang and facilitates RecA-binding to
CC       the ssDNA for homologous DNA recombination and repair. Holoenzyme
CC       degrades any linearized DNA that is unable to undergo homologous
CC       recombination. In the holoenzyme this subunit recognizes the wild-
CC       type Chi sequence, and when added to isolated RecB increases its
CC       ATP-dependent helicase processivity. {ECO:0000256|HAMAP-
CC       Rule:MF_01486}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage (in the presence of ATP) in
CC         either 5'- to 3'- or 3'- to 5'-direction to yield 5'-
CC         phosphooligonucleotides.; EC=3.1.11.5;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01486};
CC   -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits
CC       contribute to DNA-binding. {ECO:0000256|HAMAP-Rule:MF_01486}.
CC   -!- SIMILARITY: Belongs to the RecC family. {ECO:0000256|HAMAP-
CC       Rule:MF_01486}.
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DR   EMBL; CP000308; ABG12458.1; -; Genomic_DNA.
DR   RefSeq; WP_002220072.1; NZ_CP009906.1.
DR   EnsemblBacteria; ABG12458; ABG12458; YPA_0490.
DR   EnsemblBacteria; AJJ81876; AJJ81876; CH58_3339.
DR   KEGG; ypa:YPA_0490; -.
DR   PATRIC; fig|360102.15.peg.3509; -.
DR   KO; K03583; -.
DR   OMA; PHIRAVF; -.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0009338; C:exodeoxyribonuclease V complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.160; -; 1.
DR   HAMAP; MF_01486; RecC; 1.
DR   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006697; RecC.
DR   InterPro; IPR041500; RecC_C.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   Pfam; PF17946; RecC_C; 1.
DR   PIRSF; PIRSF000980; RecC; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF52980; SSF52980; 1.
DR   TIGRFAMs; TIGR01450; recC; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0E1NY90.
DR   SWISS-2DPAGE; A0A0E1NY90.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01486};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_01486};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_01486};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01486};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_01486};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01486,
KW   ECO:0000313|EMBL:ABG12458.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01486,
KW   ECO:0000313|EMBL:ABG12458.1};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01486};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01486}.
FT   DOMAIN      831   1050       RecC_C. {ECO:0000259|Pfam:PF17946}.
SQ   SEQUENCE   1123 AA;  129605 MW;  B78AEA99E32412DA CRC64;
     MFTVYHSNQL DLLKALTTAL IEREPLDNPF QQEVVLVQSP GMAQWLQMQL AQQFSIAANI
     VFPLPATFIW DMFTRVLPDI PKESAFSKEA MTWKLMWLLP DLLENPLFSP MKRYLSDDGD
     RRKIHQLAAR VADLFDQYLV YRPEWLESWE RGQLIEGLDD AQQWQALLWV ELTRYTRQLE
     QPEWHRANLY QRFIHQLLKS DVCPQGLPKR VFICGISALP PIYLQALQAL GKHIDIHLMF
     TNPCRYFWGD IQDYTFLAKL QSRKRRHYRE SIELSLFRHP QQAEQLFNTD GEQNLSNPLL
     ASWGRLGRDH MYLLSQIDEI QEVHAFVDIE PDNLLHGIQH DMLELEDHAV IGTTPETLAR
     SDQKRRLDLD DRSLSFHVCH SPQREVEVLQ DHLLGLLAAD PELTPRDIIV MVVDIDSYTP
     YIQAAFGNAP SERYLPFAIS DRKASQAHPA LHAFITLLDL PQSRFTAEQV LALLEVPALA
     TKFGITEDGL RRLRQWVGES GIRWGLDDDN VRELSLPATG QHTWRFGLTR MLLGYAMDST
     AGDWQGILPY DESSGLAAEL AGQLADMLMH LSQWRQQLGQ PRELSEWLPI CRQLLDTFFD
     QDNDTEAALV LIEQQWQKVI GYGIAAQYPD VVPLNLLRDE LAARLDNERI SQRFLAGPIN
     FCTLMPMRSI PFKVVCLLGM NDGVYPRTLP PQGFDLMAKK VRRGDRSRRD DDRYLFLEAL
     LSAQQQLYIS YIGRSIQDNS KRYLSVLVSE LIEYVAQSYH LPGDEKLSAD DSAQRVTQHL
     LCWHARMPFS AENFIKNSEL QSYAAEWLPS AESKGHAHPN FNQPLQAEPL AEITLDELVR
     FYRHPVRAFF QLRLGVNFVI EETELPDEEP FTLDNLSRYQ FNTQLLNALI NEDDINSVFA
     RARAAGVLPY GSFGELYWES QQDEMVPLAE QIRSERKENH SIELNIEFAD ITVTGWIHQV
     QDDGLVRWRP SILTAVDGLL LWLEHLVYCS AGGEGESRIY GRKGTAWRYA PMAADEARPY
     LQQLIKGYQQ GLCEPLMLLS KSGWAWLSQC FDRESGQILW DEETQGKARM KLLQVWQGDQ
     RVTGEGEDHY IQRVCRRMDN QHLDIILHET ERYLLPIARH NKA
//

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