ID A0A269PR26_9GAMM Unreviewed; 1123 AA.
AC A0A269PR26;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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:PAJ74703.1};
GN ORFNames=CJF42_09060 {ECO:0000313|EMBL:PAJ74703.1};
OS Pseudoalteromonas sp. NBT06-2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=2025950 {ECO:0000313|EMBL:PAJ74703.1, ECO:0000313|Proteomes:UP000215836};
RN [1] {ECO:0000313|EMBL:PAJ74703.1, ECO:0000313|Proteomes:UP000215836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBT06-2 {ECO:0000313|EMBL:PAJ74703.1,
RC ECO:0000313|Proteomes:UP000215836};
RA Wei Y.;
RT "Pseudoalteromonas hadalis sp. nov., a facultative psychrophile isolated
RT from New Britain Trench.";
RL Submitted (AUG-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:PAJ74703.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NQMR01000034; PAJ74703.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A269PR26; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000215836; 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; 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:UP000215836}.
FT DOMAIN 830..1065
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1123 AA; 129280 MW; D87A2FD9565BE3BB CRC64;
MLHIIQSNRL EALQFQLNSL IKQNPLSSPF SQEAILVQSP GMSQWIKIGL AQELGIVAQV
DFPLPSSFIW RLYQKLLPDV PAESAFNKNN MAWKIFDILP GFLNEPLFES LKSYLANDAQ
FENNNEDGIF SYEQQKLYML CEKIADVYDQ YLMYRPNWLE TWQEGEDSLN DVDTSHVLWQ
PELWRRLVNH TINILQQSAY HRGNMHEALL AALGNTSKAQ LKNLLPERLT IFGISALPNA
QLEVFVALAA KIDVFLYFFN PSEHYWGDLV DEKTLAKIEV KYSVKPVLEA QGKDYYFVGN
PLLSSWGKLG RDYLEQLLQL DANWHDYFID DFNPRLLSQI QQEIYQLAFK GESLSSNKNW
FISNEGKLAV DSQDNSIHLN DCHTPLREVE VLHDHLLNLF EQDKTLSPKD IIVMMPDVAS
YSPYIEAVFG SAVNERFIPY GLADLAIEQE KPILSSFNQL VNLPFSRFGV SDILDLLQVS
HIADNFDIEE NELDQIRHWL EKVGVKWGIN GEHKTEFEQD AIALNTWLQG LNKLLLGVVQ
RDESTSFNNI YAADHVEGMA ANTLGKLLSF FDKLVKFKNL LMHDGTLLNK ALILEQMIIT
FYDTQSEQSW DLMVLENLMT SIKTHFDNKD YQGIISQKVM CYLVKQGLKE KGVGQRFLIG
KINFCTLMPM RSVPFKVVCM LGLNDADYPR SVQPMGFDLL PQSRRQKGDR SRKLDDRYLF
LEALLSAREH LYISYIGRSC FDNTQRVPST LVSELLEYIS RSFYQLKPDS EQENNHFPNN
LIQQHHLQPF NKAYYLTDNL SNDQSYNPTW MITDYQLAKD AKPLAITPAK EIELELFIST
LCQPQKRFYQ SSLALKLPQG DEINKDEEPF SLDHLERYFY LDEFLTKALK GENVAQNQIL
QRGNLPLANV GELTLEKIEG RIAQMQLNIQ SHDFKLRDDP LDINVTLTNF ASEHTQEVQS
TIVGWLKNVS QVNSETQTAK QLFYRPASVK AKDLIKAWLY HLTAHASGHK LDTFILGLDE
QYQFTHLSKE AANERLQSWF ILYANALTQP VPFFPQSALE YAKTQDIGKA KLKFSGGQYI
GRGESEDPYI RLNFKSLDDV QQEFMQLSDD LLIPLLQQLE DIN
//
