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Database: UniProt
Entry: A0A1A7REK5_9GAMM
LinkDB: A0A1A7REK5_9GAMM
Original site: A0A1A7REK5_9GAMM 
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
//
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