ID A0A1Y6L6G7_9GAMM Unreviewed; 1153 AA.
AC A0A1Y6L6G7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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:SMY18108.1};
GN ORFNames=PAQU9191_03441 {ECO:0000313|EMBL:SMY18108.1};
OS Photobacterium aquimaris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=512643 {ECO:0000313|EMBL:SMY18108.1, ECO:0000313|Proteomes:UP000196485};
RN [1] {ECO:0000313|Proteomes:UP000196485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=type strain: CECT 9192 {ECO:0000313|Proteomes:UP000196485};
RA Rodrigo-Torres L., Arahal R. D., Lucena T.;
RL Submitted (JUN-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}.
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DR EMBL; FYAH01000011; SMY18108.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6L6G7; -.
DR Proteomes; UP000196485; 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:UP000196485}.
FT DOMAIN 846..1076
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1153 AA; 130297 MW; ED52AAA4D4FEC0DF CRC64;
MFTVYHSNQL DLLKSLLVEL IRLQPLANPF EKEQILVQSP GMSQWLKMEL ATSFGVAANI
DFPLPATFIW KMFTQVLADV PERSAFNKEA MTWKLMQVLP QQFDQPEFEP LKRYLDSDSD
SLKCYQLSEK IADIFDQYLV YRPEWIQQWE AGETVAELND EHPWQPILWQ ALYDQTLALE
QSPYHRANLY DHFIETLNNY SGSEGKAALL AAGLPQRLFV FGISSLPPRY LDALAAIGEH
IDVHLMFTNP CKYYWGDIRD RKHLARLAAR QRVQLQHITT DDELNELLSV LKDTDQTNYD
DDMHNDVVGN SLLASMGKLG RDNMYLLSAM EVNEVDAGFV DIEPDTLLHA IQADILNLQD
RQDDTQLDSS LHKFPIATND HSITIHACHS PMREVEVLHD KLLAMFATNS NLKPRDIIVM
VADINAYSPA IQAVFGNAPG NRYIPFSISD RTAEQENPIL LAFLRLLTLP ESRCHASELL
ELLEVPAVME KFGFDSASFE KIKKWIEEVG IRWGLDQHTS SQFDLPEQLQ NTWLFGIQRM
LLGYAMPHDT GLFAGISAYE QVQGLDAELA GQLAGFIDSL IEYRCALAQP QTVNQWAELL
HQLLDDFFAV ELEGELILKS IRDNLQRLHQ QLQDAGYQAQ ITPAVLTQYL QDKLSGERVS
QRFLAGQVNF CTLMPMRSIP FNVVCLLGMN DGAYPRNIAP EGFDLMNGRT KAGDRSRRDD
DRYLFLEALL SAQQSLYISY VGRSIQDNAS KVPSVLVSEL IEYCQQGYCC DGDQSLAVDV
SADNIKHQLV QHHSLVPFSP SAFVGDDPSF AIEWLPAANR EGQASAPFQL DALAAEPMAD
EQALILELAE LQRFWRLPVK YFFNRRLKVY FEPPLGLLED DEPFVLNGLE SYLIRDQLLE
LLLDAKLKNA DPDVIYRQFA AEQRAAGTLP VAAFGDLDLA ASRQAVANLT DVIEPLIHAP
LADQEVAITV MVAGHKVLLQ GWLKKRYQSG LLRYRTGKIR PQDLLTAWFD HLCLAVSAPE
KAQVTHVIGT DKHFQLQVIE PLQALAYLQQ LIELYYQGLN QPLAYFPKTA MAAIQAHIGR
DGSWKDDADT EQKALMKMAE CFNDGYLFSG EGCDEYINRV WPKWSEDLAS EANQLAALVL
QAAVVNAKEI KPE
//
