ID A0A1A7REK5_9GAMM Unreviewed; 1265 AA.
AC A0A1A7REK5;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=A9J31_00120 {ECO:0000313|EMBL:OBX29959.1};
OS Acinetobacter gandensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1443941 {ECO:0000313|EMBL:OBX29959.1, ECO:0000313|Proteomes:UP000185753};
RN [1] {ECO:0000313|EMBL:OBX29959.1, ECO:0000313|Proteomes:UP000185753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 4275 {ECO:0000313|EMBL:OBX29959.1,
RC ECO:0000313|Proteomes:UP000185753};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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}.
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:OBX29959.1}.
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DR EMBL; LZDS01000001; OBX29959.1; -; Genomic_DNA.
DR RefSeq; WP_067761254.1; NZ_VZOF01000013.1.
DR AlphaFoldDB; A0A1A7REK5; -.
DR STRING; 1443941.A9J31_00120; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000185753; 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; 3.40.50.10930; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_01486; RecC; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006697; RecC.
DR InterPro; IPR041500; RecC_C.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
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}; DNA damage {ECO:0000256|HAMAP-Rule:MF_01486};
KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01486};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01486}; Exonuclease {ECO:0000256|HAMAP-Rule:MF_01486};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_01486};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01486};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01486};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01486}.
FT DOMAIN 953..1166
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1265 AA; 146351 MW; 732A00BEF5CD93AB CRC64;
MAIHVIQSQR IEVLVDCLID QLKTQQSTNA LSVLQERHIV VPDQAIATWL EQQISEKISI
SANIKHHRKI LGLQWKAYEW ALPTKQDRER IKGINTPPLI MQWRIYHGLA QFIQSDSLDT
ANTPADLQVL LQRVYDNSAN LSDLNKRKSK RQEMLYWIAA QVTRLFTNYA TYRGSCIHTP
DEGVETWVCP HCDTDWLSAW TKNKPLDVLQ LTGFKPDQAA EYLPTQAAQL EQWQRWLWHA
LFQKDFNDRF EIDNKFWQAL HQAKYHHQQQ LEFSLGDGSV DEDDERHQTY NGLPAQIFVF
TTLELPPAQL KFLYRLGEFT EVHLLYFNPS REYWADMVDP VWKDRYNLKL QQRYIERNPK
VTTEQIQAYL NTTNAELRES QHSLLTRLGK RARDNFSLLV NMSGGEGWED VFPEDEPNTL
LGQIQHDIMT LQEPEKHGYA LAQEDQSIQF HVCHSSLRQL EVLRDQLVRW LAAGTPEAPR
HPSDVLILVP NLKELEPHIR TVFSTTRGIA RTAQDLPYIP VKIAGVISQD VNNAWQAFVG
RIEISQGRFS AEDFHDWLNL NAVQHYYQLD HVQMERMMEL LINAGFRRGL DEQHMQAYLA
ENDQDYRYTF KFALDRLVLG VAIPQHMVFA GTLSFAGVLS ADFELVQTLI QIYQDIAERR
EWLNPQATTL PCHSVQQWLE HLDADLKPFA ETGGRAFEDI RKVLRAVIQR LHNAQSEKVG
SLPESFDLPL MLILKEIQQS LEASAEQAEP TGSVTFADIG KVRQVPYDLV VLMNMDSGKF
PRRDQQVPFD LMELLKPVLG DRSRLEDDKG AFLDALLFAR QSLWLFYNGF DVNDGESREP
SSVLYEFSQF LAKMICPQTL DQPHEAMLDL EGLRIPQQLE ALYHVHPLQP FDPKGFQPSK
SLRFQDQWFA VAEQIQHSAG PRQPWINRDY PVVEDTEIRV LDGQEWIKDV VFPARLYLKT
LGVASVYTGD QLPQQEPLLL DKLQQYHVRE LLQKHYVQPN AVLHTTTQTD DETDGRIEPN
IALFQDVLPV GHTRTGTWKI SLAEQAQLVQ RLDGRQITAT TQQNLNIEDN LLLSIQVPED
QHATLWLSCM ASSAKPKRQT QTWLEYLLWL SYLDLGEDGA QYVREVICND KTIICHGLSS
AQAKQQLASW FGLWRHAQKR PVILPAALIR QEKTHWVENE NGQVIPDNLQ KLQDKWLNNH
SFGIELESDE ANCHHRDWRF ILQQQAADEL FQLSSTYYAE RLYQVMDGEQ DGVKKLELIK
PEGKK
//