ID A0A1X1MQ43_9VIBR Unreviewed; 1164 AA.
AC A0A1X1MQ43;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=ST37_12410 {ECO:0000313|EMBL:ORT49237.1};
OS Vibrio sp. qd031.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1603038 {ECO:0000313|EMBL:ORT49237.1, ECO:0000313|Proteomes:UP000193432};
RN [1] {ECO:0000313|EMBL:ORT49237.1, ECO:0000313|Proteomes:UP000193432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=qd031 {ECO:0000313|Proteomes:UP000193432};
RA Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ORT49237.1, ECO:0000313|Proteomes:UP000193432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=qd031 {ECO:0000313|Proteomes:UP000193432};
RA Chen G.;
RT "Denovo assembling a bacteria genome.";
RL Submitted (MAY-2017) 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}.
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:ORT49237.1}.
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DR EMBL; JXQD01000025; ORT49237.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1MQ43; -.
DR STRING; 1603038.ST37_12410; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000193432; 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 CDD; cd22353; RecC_C-like; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 1.10.10.990; -; 1.
DR Gene3D; 3.40.50.10930; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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 NCBIfam; TIGR01450; recC; 1.
DR PANTHER; PTHR30591; RECBCD ENZYME SUBUNIT RECC; 1.
DR PANTHER; PTHR30591:SF1; RECBCD ENZYME SUBUNIT RECC; 1.
DR Pfam; PF04257; Exonuc_V_gamma; 1.
DR Pfam; PF17946; RecC_C; 1.
DR PIRSF; PIRSF000980; RecC; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01486};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01486};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01486};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01486};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01486}; Helicase {ECO:0000256|HAMAP-Rule:MF_01486};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01486};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01486};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01486}; Reference proteome {ECO:0000313|Proteomes:UP000193432}.
FT DOMAIN 852..1083
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1164 AA; 132455 MW; BB531B60893E018B CRC64;
MFTVYHSNQI DLLNSLMIEL IRNDPLPNPL QAEVILVQSP GMSQWLKLSI AQQQGVAGNI
EFPLPATFIW QLFEKVLPDV PSKSAFNKES MTWRLNAILP NYLDTEEFAP LSRYLNDADP
LKQLQLAEKI ADTFDGYLVY RPDWIAAWEG HQEVEEVPAE QSWQPILWRA LFDHTVASGA
SPYHRANLYD DFIDTLAHYQ GRIEGLPSRL FVFGISSLPP RYLEALHAIG QHIDVHFMFA
NPCRYYWGDV RDQKTIAKMA AQTRKHIQWQ GDHSVVGNEA HVLKGSEAQN IEDPTQQAQV
GNALLASMGK LGCDNLLLLS QLECQEIEAF VDHDLNAATL LQRIQSDILE LDQRDISDDD
SIRPKHIVAD SDRSLTLHQC HSPTREVEVL HDQLLHLFDS DPSLTPRDVI VMVPDINRYT
PAIEAIFGQA NDERRIPYSI SDRTTTEANP LLNAFFSLLD LPNSRAQSSL MLELLETPAV
LRRFELSVQE FERIKLWVEE VGIRWGLTEK TAAELGFEAP LNTWQFGLQR MLMGYSLHPD
VGLYEQDDRV ISPFNHIQGM DADVAGRLAQ YIDNLIEFQQ RFAQSHSIEA WMDIINQLLS
QFFTPELDEE LMVSAIRDAL VSLKQPLSEL DDAPQLDIDL IRYCLKQKLD QSRVSQRFLA
GQVNFCTLMP MRSIPFKVVC LLGMNDGAYP PAEMVEGFDL MQNKSRPGDR SRRIDGRYMF
LEALLSAQHT LYISYVARSI RDNSVSEPSI LVSELLEYCE QNYSVQLDIQ ADDNTNMGAD
NELTDFITYS HSMTPYSRHA FDSDTPSYAR EWLPVAQANS GNDASHTEVK PLAEDQWQLP
SFTDEIDGEL IVELDVLSRF WTLPVKRYMN QRLGVYFDPF DIKIEDDEPF AMGGLGSYLL
RQQLLEHSLE QSIQAGEVVT DPQSYLKHKR AEGVLPVGAF GELDIVSSEQ QIAMLLERIL
PYCSRPQPAR SIDLHLSPLS DTRSVFLQGW LDNQYEQGMV RYRCGQLSAK YVLGFWIDHL
AAMATGEQRS TQLFGLAKQN VVEWTLLPLT SENAKHHLET LIQLYVEGLD LPLPFFVDTA
WEGALVIEKA GLVLDNPPAD SDDGLKAMAK MQQTFEGNSF RPGESDNPYI QRVWPQWNDQ
VAEKCYQLML AVMLPLLSHC EREK
//
