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Database: UniProt
Entry: A0A291JPL9_9GAMM
LinkDB: A0A291JPL9_9GAMM
Original site: A0A291JPL9_9GAMM 
ID   A0A291JPL9_9GAMM        Unreviewed;      1187 AA.
AC   A0A291JPL9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   11-DEC-2019, entry version 10.
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   ECO:0000313|EMBL:ATH76161.1};
GN   ORFNames=CLM76_00410 {ECO:0000313|EMBL:ATH76161.1};
OS   Halomonas hydrothermalis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=115561 {ECO:0000313|EMBL:ATH76161.1, ECO:0000313|Proteomes:UP000217920};
RN   [1] {ECO:0000313|EMBL:ATH76161.1, ECO:0000313|Proteomes:UP000217920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y2 {ECO:0000313|EMBL:ATH76161.1,
RC   ECO:0000313|Proteomes:UP000217920};
RX   PubMed=27315164; DOI=10.1007/s00792-016-0852-8;
RA   Cui Y., Cheng B., Meng Y., Li C., Yin H., Xu P., Yang C.;
RT   "Expression and functional analysis of two NhaD type antiporters from the
RT   halotolerant and alkaliphilic Halomonas sp. Y2.";
RL   Extremophiles 20:631-639(2016).
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}.
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DR   EMBL; CP023656; ATH76161.1; -; Genomic_DNA.
DR   KEGG; hhh:CLM76_00410; -.
DR   KO; K03583; -.
DR   Proteomes; UP000217920; Chromosome.
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}; Coiled coil {ECO:0000256|SAM:Coils};
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}.
FT   DOMAIN          863..1108
FT                   /note="RecC_C"
FT                   /evidence="ECO:0000259|Pfam:PF17946"
FT   COILED          650..670
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1187 AA;  133638 MW;  C4E070DBE8774154 CRC64;
     MPANALLSPT SLTPGFMVVH ANRLEDLRGL AVEWMRRHPL GPLENETILV QSNGIGQWLK
     LALAEDPGNG GAGIAAALDV MLPARFLWQA YRRVLTHVSH DADAVPETSP FDKSRLVWRL
     LRLLPTLAGQ PVFEPLAQFL QTDRDQRKHY QLAERLADLF DQYQVYRADW LDAWANGHDV
     LITARGEHRP LEEHQCWQPA LWRILRDDVA ATQGDAGLNS SRAQVHQRFL KATEQLEGQA
     CPPGLPRRLI IFGISSLPQQ TLEALAALSR CCQIVLCVHN PCQFYWADII EHKDLLRAQR
     YRQRRKTGMP DTLDVLGTGD ADDALHLHAQ PLLAAWGKQG RDYLRLLDEH DDAGNYQTLF
     EQQALRIDMF EPFSGEERHC LLSQLQDDIR ELRPVAETQA QWPALSATDD SIVFHIAHGP
     QREVEILHDQ LLATFSADPA LRPRDIIVMV PDIDRYAPHI EAVFGQLPTD DPRHIPYTLS
     DQASRHRLPL MIALEKLLRL PELRLTVSDV LDLLEVPALR QRFGLEERDL PVLERWMEGA
     GIRWGLNAQQ RQRLELPSGL SQNTWAFGLR RLLLGYTVGD GHAWQGIEPF DDIGGLEASL
     AGPLATLLEK LDATWETFCQ PTDAATWVAR LRALLETFFL TDDAQESIML TKLENGLQQM
     LESSQEAELD DPLPLSMVRE HWLAQIDEHS LSQRFLAGAV NFATLMPMRA IPFKRVCLLG
     MNDGDYPRSQ PPLDFDLMGS DYRPGDRSRR EDDRYLFLEA LLSARDQLYI SWMGRSQIDN
     SPLPPSVLVG QLRDHLEAGW QTHTGAPLLE RLTTEHPLQP FSRAYFNHPA GRLFTYAHEW
     REVHAPRRPP AVERMLPAPE NAPTSLSLAQ LGGFLREPVR SFFNTRLGVY FEQETIAELD
     AEPFALDGLQ NWQLQDQLIA AQRHAVDHGQ PRIEALHDAL ERFQGQGVLA MGAFGERMRD
     ALADPMEELF NAYEEALTAW PHALPDAQVQ FEAHGLTLEE PLGELRQDEA GQRCRLLLLS
     SSLISQGSGR GQYRWSHLLR PWVAHLAGNL SGPMTTLLLS KAGHVTLEPV AADTARQHLE
     TQLAAWQAGL QTPLPLAPQA GFAWLAKQGT PEIAQEKGRD SDAFAAAEAA YEGGYKVTGE
     AAQSAYLSHQ WPRFERLFFE QANGHTFATL TESLYAPLFF AVKGKKE
//
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