ID G4CIX4_9NEIS Unreviewed; 1061 AA.
AC G4CIX4;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
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:EGY52211.1};
GN ORFNames=HMPREF9371_1563 {ECO:0000313|EMBL:EGY52211.1};
OS Neisseria shayeganii 871.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=1032488 {ECO:0000313|EMBL:EGY52211.1, ECO:0000313|Proteomes:UP000003019};
RN [1] {ECO:0000313|EMBL:EGY52211.1, ECO:0000313|Proteomes:UP000003019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=871 {ECO:0000313|EMBL:EGY52211.1,
RC ECO:0000313|Proteomes:UP000003019};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (MAY-2011) 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:EGY52211.1}.
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DR EMBL; AGAY01000057; EGY52211.1; -; Genomic_DNA.
DR RefSeq; WP_009119253.1; NZ_JH164926.1.
DR AlphaFoldDB; G4CIX4; -.
DR STRING; 1032488.HMPREF9371_1563; -.
DR PATRIC; fig|1032488.3.peg.1474; -.
DR HOGENOM; CLU_007513_0_0_4; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000003019; 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 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:UP000003019}.
FT DOMAIN 771..989
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1061 AA; 118380 MW; FB54A466C6252F0A CRC64;
MLHLYQSNRL EILAETAVAL MQHAPLQGAF APEEIVVQSQ GMRRYLNHYL AERSGIAANL
RFSLPAALSW RLTRTFLPDT PALNPFAPEV MRWRLLQLLQ GDHLPAAVHT ALTGYLNSSR
TAPYRLAGKL ADVFDQYLVY RPDWVAAWES GESMGLGADE IWQAELWRLL AADGTDGGHR
AEQRRRLLAA LSADKLPERY LVFGIATLAP MYLDLLQRLA EHTEVHIFAV NPSSRYWGDI
ESARRQAFSG LPDAEAAGHP LLASLGKQGR DFFDMLTAEG RVDEQHDWFP APPAAPSLLQ
RVQQDIQTLS LPERGSAAMD GSITIQSAHS RLRELQILKE WLLGVLAENA DLQPHHIAVL
TPDIESYAPY IHAVFGEEQP GSPALPYSVA DVKISRRSAL MQLAEQLLAL MQSRFETDYV
LPLLDSPAVC RHWHFSERDA DHLRHSIAEL NIRWGSDADM RRRYGGSGEA FTWQQGSERT
ALGWLMPENS GLWQGVLPWT ADWSHTAVQA RWQQLLACLR RHHALWQTDA APAEWCARLH
ALLDDLAGSE PADADDQAAR QQLHNDLAAW QAESALAGYL KPLPPETACE HLARFFTGSG
EAGFLRGGIT FCGMVPMRSL PFDTLCLLGL NDGRFPRQTQ IPAFDLISRH PRKGDRARRD
DDRYLFLESL LSARRRLYLS YIGRDSRKDE ALAPSPLLSE LADVLALMGG QSSAEFAEQH
IRQHPLQPYS PRYFSGSPSS SRQDYAEALN RLPQPPAPFA GDCPPAADCP DPIPLEHLLR
FWRNPVRHWL GRALQWREPY ADEAAESAEP YAIEASNEVA RQYLDARRRH QDFADTEAHL
AAQGLVPAGL LGHLLQAPDI RAVKRLDGEL LHSPRLPAQA FELACGGRRL TGSLSQLYQH
GQILYRSGAP TAPDTVELWL LHLVYCAAGS GSQPRETHWL SAAAPHTLPP IEREQAQAWL
ASWLDYYALG HSRPLPFFAK TSLAAARAYT EDSDTPPDAA VKAARGDYRS GRFSTGQAER
TEVAQVFGRD EAEPIETPLF WNLVRELLVP LHLYFAAAEA T
//
