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Database: UniProt
Entry: H0J4Q3_9GAMM
LinkDB: H0J4Q3_9GAMM
Original site: H0J4Q3_9GAMM 
ID   H0J4Q3_9GAMM            Unreviewed;      1189 AA.
AC   H0J4Q3;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   11-DEC-2019, entry version 36.
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   ORFNames=MOY_13089 {ECO:0000313|EMBL:EHK60248.1};
OS   Halomonas sp. GFAJ-1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1118153 {ECO:0000313|EMBL:EHK60248.1, ECO:0000313|Proteomes:UP000004512};
RN   [1] {ECO:0000313|EMBL:EHK60248.1, ECO:0000313|Proteomes:UP000004512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GFAJ-1 {ECO:0000313|EMBL:EHK60248.1,
RC   ECO:0000313|Proteomes:UP000004512};
RX   PubMed=22408239; DOI=10.1128/JB.06664-11;
RA   Phung le T., Silver S., Trimble W.L., Gilbert J.A.;
RT   "Draft Genome of Halomonas Species Strain GFAJ-1 (ATCC BAA-2256).";
RL   J. Bacteriol. 194:1835-1836(2012).
CC   -!- FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for
CC       recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly
CC       rapid and processive ATP-dependent bidirectional helicase activity.
CC       Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator)
CC       sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the
CC       Chi site. The properties and activities of the enzyme are changed at
CC       Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and
CC       facilitates RecA-binding to the ssDNA for homologous DNA recombination
CC       and repair. Holoenzyme degrades any linearized DNA that is unable to
CC       undergo homologous recombination. In the holoenzyme this subunit
CC       recognizes the wild-type Chi sequence, and when added to isolated RecB
CC       increases its ATP-dependent helicase processivity. {ECO:0000256|HAMAP-
CC       Rule:MF_01486}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage (in the presence of ATP) in either
CC         5'- to 3'- or 3'- to 5'-direction to yield 5'-
CC         phosphooligonucleotides.; EC=3.1.11.5; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01486};
CC   -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC       to DNA-binding. {ECO:0000256|HAMAP-Rule:MF_01486}.
CC   -!- SIMILARITY: Belongs to the RecC family. {ECO:0000256|HAMAP-
CC       Rule:MF_01486}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHK60248.1}.
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DR   EMBL; AHBC01000043; EHK60248.1; -; Genomic_DNA.
DR   RefSeq; WP_009100516.1; NZ_CP016490.1.
DR   STRING; 1118153.MOY_13089; -.
DR   EnsemblBacteria; EHK60248; EHK60248; MOY_13089.
DR   KEGG; hag:BB497_15750; -.
DR   PATRIC; fig|1118153.6.peg.2662; -.
DR   KO; K03583; -.
DR   OrthoDB; 1320159at2; -.
DR   BioCyc; GCF_000236625:G1EEI-859-MONOMER; -.
DR   Proteomes; UP000004512; Unassembled WGS sequence.
DR   GO; GO:0009338; C:exodeoxyribonuclease V complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003678; F:DNA helicase activity; 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;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01486,
KW   ECO:0000256|SAAS:SAAS00992480};
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   ECO:0000256|SAAS:SAAS00992482};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_01486};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01486, ECO:0000256|SAAS:SAAS00992489};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01486, ECO:0000256|SAAS:SAAS00992512};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01486};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01486,
KW   ECO:0000256|SAAS:SAAS00992504};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004512}.
FT   DOMAIN          863..1106
FT                   /note="RecC_C"
FT                   /evidence="ECO:0000259|Pfam:PF17946"
SQ   SEQUENCE   1189 AA;  134098 MW;  3FE91044DE11A6C7 CRC64;
     MPANALFSPT PLPPGFMVVH ANRLEDLRGL AVEWMRRQPL GPLENETILV QSNGIGQWLK
     LALAEDPKNG GAGIAAALDV MLPARFLWQA YRTVLTHVSQ NADAVPETSP FDKSRLVWRL
     LRLLPTLAGQ PVFEPLAQFL EIDRDQRKHY QLAERLADLF DQYQVYRADW LDAWANGHDV
     LITAKGEHRP LEEHQRWQPA LWRILRDDVA ATQGDAGLNS SRAQVHQRFL KATEHLEGQD
     CPPGLPRRLI IFGISSLPQQ TLEALAALSR CCQIVLCVHN PCQFYWADII EHKDLLRAQR
     YRQRRKTGMP EALDVLGTGD ADDALHLHAQ PLLAAWGKQG RDYLRLLDEH DDSGNYQTLF
     EQQALRIDMF EPFSGEDRHC LLSQLQDDIR ELRPVAETQG HWPALPASDD SIVFHIAHGP
     QREVEILHDQ LLAAFSADPH LRPRDIIVMV PDIDRYAPHI EAVFGQLPTD DPRHIPYTLS
     DQASRHRLPL MIALEKLLRL PELRLSVSDL LDLLEVPALR QRFGLEERDL PVLERWMEGA
     GIRWGLNAKQ RQKLELPGGL SQNTWAFGLR RLLLGYTVGD GHAWQGIEPF DDIGGLEAGL
     AGPLATLLEK LEATWETFCQ PTDAATWVAR LRELLETFFL TDDAQESVML SKLESGLQQM
     LESSREAELN DPLPLSMVRE HWLAQIDEHN LSQRFLAGAV NFATLMPMRA IPFKRVCLLG
     MNDGEYPRSQ PPLDFDLMGS DYRPGDRSRR EDDRYLFLEA LLSARDQLYV SWVGRSQIDN
     TPLPPSVLVG QLRDHLEAGW QTEDGAPLLE TLTTEHPLQP FSRAYFTPST SRLFTYAHEW
     REVHAPRTPT AASRTLPPPE NAPTTLSLGQ LGGFLREPVR SFFNTRLGVY FEQEAIAELD
     AEPFALDGLQ NWQLQDQLIA AQRHAVDNGQ PRIEALHEAL ERFQGQGVLA MGAFGERMRD
     TLAEPMEALF NDYEEALAAW PIALNEPEAI YLESHEGSVL EDWLNELRQD EAGQRCRLLL
     LSSSLIKNSK YQWHLLLRPW VAHLAGNLSG PMTTQLLSKA GHVTLEPVDA ETARQHLETQ
     LAAWKAGLAT PLPLSPHAAF AWLTKQGTPE IAQETDRDSD AFAAAEAAYE GGYKVTGEVA
     QSAYLGHQWP RFERLFFEQA NGHTFATLAE ALYAPLFKAV KKPNISKTQ
//
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