ID A0A1G7B414_9NOCA Unreviewed; 1105 AA.
AC A0A1G7B414;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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 ORFNames=SAMN05444580_11269 {ECO:0000313|EMBL:SDE21848.1};
OS Rhodococcus tukisamuensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=168276 {ECO:0000313|EMBL:SDE21848.1, ECO:0000313|Proteomes:UP000199417};
RN [1] {ECO:0000313|EMBL:SDE21848.1, ECO:0000313|Proteomes:UP000199417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 11308 {ECO:0000313|EMBL:SDE21848.1,
RC ECO:0000313|Proteomes:UP000199417};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FNAB01000012; SDE21848.1; -; Genomic_DNA.
DR RefSeq; WP_072845716.1; NZ_FNAB01000012.1.
DR AlphaFoldDB; A0A1G7B414; -.
DR STRING; 168276.SAMN05444580_11269; -.
DR Proteomes; UP000199417; 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};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_01486, ECO:0000313|EMBL:SDE21848.1};
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:UP000199417}.
FT DOMAIN 800..1026
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1105 AA; 118565 MW; F57C8E4298E9024F CRC64;
MLTLHRAERS DTLAAALAEL LAVPLADPFA AEVVAVPAKG VERWLTQRLS MTLGARDGDG
VAANIEFPSP ARLVDAALAA ATGVDADADP WHPARVLWTL LAVIDDSLDE PWCAVLARHL
GHGADDHRAG RRYATAAHLA GLFRSYGAQR PGMLVAWADG RDVDAGDDKS EPLDDDQLWQ
PQLWRRLRAR IGSPSPAERL DGACARLRAE PGLLDLPGRL SLFGPTRLSA DQIAVLSAIG
VNHDVHLWIP HPSPAMWTKL DGASQPTLRA DDDRALAAGH PLLASLARDV RELQARIAGL
DLVDVHHPAP APPADTLLGR IQGDLAADRP PVAFPLAADD TSVQVHGCHG PARQVEVLRE
CLLHLFQDDP TLEPRDVLVM CPDVEAYAPL VRAAFGQDPY GQNTFGHPGH RLRVRLADRA
LHQTNPVLSV VSTLLGLADA RVAASSVLDL AATEPVRRRF RFGDSDLERL REWAGAAGAR
WGIGPRQRGA FGLGDFKQNT FGTALDRILL GAAADESDAQ WLSLALPLDD VESNDITLAG
GLAEYIDRLD VALRGLAGPQ TAAQWSANLA RALDLLVDVS PTDAWQLGQA RRELAGAVEH
SGEGGDPTLR LADVRALFAT RLAGRPGRTN FRTGELTVCT MVPMRSVPHR VVVLLGLDDE
VFPRGAGVDG DDVLARSPRL GERDPRSEDR QLLLDAIMSA TERLLLFYTG KDPVTGSRRA
PAIPLSELTD VIEQMVGADA SESVVRHGHP LQPFDPRNFA PGSPFSFDTA ALAGARAAQH
PAAAETDFLP RPLDPRPEQP EAVDLADLIA FLVHPTQAFL RQRLGLRVPD LDEDLADALD
LELDPLAKWN VGERMLAARL AGVSVEEFRD AEWRRGTLPP ARLGGRALAD IEGQVHSLFS
ASRRDGRATT VDVDLDLGGG RRLTGTVGGV YGAVVARSTF SRLAPKHRLP VWANLLALAA
SGPPPEGERW RAVTTGRGRG RAPVQQSTLV APDDALAHLV RLVALRDRGL DVLAPIATAS
SAAYAELRFQ GRSVEQAMTY AGKEWGGDFG DGKDRHIGYV YGDSAPLSVL TARPAPSGSP
EPTVFGMAAR QLWEPLLSAE TLETP
//
