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Database: UniProt
Entry: A0A158H9V1_9BURK
LinkDB: A0A158H9V1_9BURK
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ID   A0A158H9V1_9BURK        Unreviewed;      1126 AA.
AC   A0A158H9V1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   11-DEC-2019, entry version 17.
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=AWB69_04112 {ECO:0000313|EMBL:SAL40759.1};
OS   Caballeronia udeis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=1232866 {ECO:0000313|EMBL:SAL40759.1, ECO:0000313|Proteomes:UP000054683};
RN   [1] {ECO:0000313|EMBL:SAL40759.1, ECO:0000313|Proteomes:UP000054683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 27134 {ECO:0000313|EMBL:SAL40759.1};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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; FCOK02000027; SAL40759.1; -; Genomic_DNA.
DR   RefSeq; WP_062087861.1; NZ_FCOK02000027.1.
DR   EnsemblBacteria; SAL40759; SAL40759; AWB69_04112.
DR   GeneID; 33101494; -.
DR   OrthoDB; 1320159at2; -.
DR   BioCyc; GCF_001544555:G1EQ2-4059-MONOMER; -.
DR   Proteomes; UP000054683; 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}.
FT   DOMAIN          820..1070
FT                   /note="RecC_C"
FT                   /evidence="ECO:0000259|Pfam:PF17946"
SQ   SEQUENCE   1126 AA;  124497 MW;  A3F7AA9EAF579D40 CRC64;
     MLELFYSNRH ETLSQALLDD VAAFALNGGD PFARQTIIVP SAAVRRRLEL DMAARFGICA
     NVDLCYLAQW LWARIGGVLP VPEHSPFAPD RLVWRCFRLL GAMTQTAPES SSRLRAYLDA
     ADDSMRYELA RRIATVFDHY LTYRPEWLLH WQAGGSILAS AGGAADANGP RLPNATAIQR
     EDERWQAALW RALLADLAQD AGEHDPTPPA YRFLSESPKL DLDAVMKAEW PERVSVFALP
     TMPSLHIALL RELSRWIDVR IYAIDPCREF WFDIVSEARV EQLELAGKLD FQEVGHPLLA
     EWGRQTQAQL HMLRELTESA ASREASHFEE NPAPTWLAHV QNAILNLNEV AEPGEALEPG
     IEIHVCHSLS RQLEVLHDRL LGWFDEIDGL QPSDVLVAFP DLAAAGPLID GVFGTAPAGV
     AGERRRIPYR ITGLPPSQAN PVARVLLDWL ALPERSVGAP ELIEWLRVDA VAARYGIDAV
     ALETAQTWLA AAGARRGLTP SAVTAADVPA ARHTFSDALT RLFLGYALPD GGAPVDEWLP
     VGGAQGSDAE LLGRLTRFID DIEAFGERIA TARTPQAWTQ LLLDALTQFF DAGLPFADSI
     ADVRSTLDAL MLSMSEGAVD TEIAADVLRT ALTDALDDAA RGGVPWGGVT FSSLTSLRGL
     PYRVVCLLGM DDGMLPSLTR ADEFDLMASF GKLGDRQRRD DERNLFLDLL LSARDRLMIA
     YTGRSIRDNA ALPPAALIDE LLDYLAETVA GEGASPKELE RARSRFVFEH PLQPFAPEYF
     SAPLFTYEPE RAELARTLAL GRVEPSVKFF SEPLPAEDVE PVAFDDFERF WRHPARAILR
     DRLGISLFDA ETELGDTEPF ELQYPGRAAL ADRVLPALLE LTADNESHGL DRARRVARAS
     PEMPGGATGG VWQSREIGAL HSLANRVRVA TSEGAARLPF TLDIKPIWPD AELFGRHDAT
     LQADALQPMQ LHGTLNLLTD EGQIIYRYDV PRARDYLSAW LAHLAYCAAL PDGPRRTVWH
     GRGAQSSGFE LMPVDDPHAH LATLAALYRA GRRLPLRFFP KSAWTWVRES ESKAQSVWIS
     DRTRGESDDP ALRIAFRGAE LRLDETFVTS ARIVFDPLIQ HMRSDA
//
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