ID A0A1H6Q6A4_9GAMM Unreviewed; 1241 AA.
AC A0A1H6Q6A4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, 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 ORFNames=SAMN05421831_10138 {ECO:0000313|EMBL:SEI37416.1};
OS Allopseudospirillum japonicum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Allopseudospirillum.
OX NCBI_TaxID=64971 {ECO:0000313|EMBL:SEI37416.1, ECO:0000313|Proteomes:UP000242999};
RN [1] {ECO:0000313|Proteomes:UP000242999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7165 {ECO:0000313|Proteomes:UP000242999};
RA Varghese N., Submissions S.;
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; FNYH01000001; SEI37416.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6Q6A4; -.
DR STRING; 64971.SAMN05421831_10138; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000242999; 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};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_01486, ECO:0000313|EMBL:SEI37416.1};
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:UP000242999}.
FT DOMAIN 877..1156
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1241 AA; 143452 MW; 54D091B8B08D68E3 CRC64;
MYAQACHNTA PLTPGFMVLH SHRMEALRDL VLEWISQHPL APLENEVFLV QSNGIAQWLK
LALAQDEACG IAAAVDIQLP ARFFWQVYRA YLGDRQVPKH SPMDKAPLTW RLFQLLPQLS
QDPRFAELEA QQALNHQDAN ARYALAQSLA DLFDQYQVYR AHWLQDWQQN RFILQHPMRA
QAFPLPEEHQ WQAYLWQEVQ ASLPKYARTN NRAHLHQAFL QTAAKGHLPL NKLPRRVLVF
GISSLPVQSV QILQALAKHL QVIICVHNPC RFYWGDLISD QNLVWQLNKQ ARRQAEHHHV
ALAPSLPPLS KAPRHPSKFS FHNLADLHQH AHPLLAAWGR QGRDYIHLLE EADHKEAYAH
LFQRIDLFDY PPADSMLAVI QEDILELRSL QEIQAQPRNW QAATDHSIRF HSAHTKHREV
EILQDQLLAL FQQHPDLQPK DVIVMMPQVD TYVAAIQAVF GQVDPQDPRY LPYALADRQH
AQHQNLILAL ESLLNLQEHK CTFSQLFQLL EVPAIRARFG LQEKDLPLIR TWLEQAGARW
GLNAHHRKAL GLQTEFNQNT WAFALERLWL GYALGDQSQP WQGLYPYADI GGLDAPVLGL
LDAWFRRLLS YVQHVQEARE PQAWVSFLHQ VLEDFFLAQE SSEALLLEHL HQTLDAWLET
CQRAEFSQPL PIKLVAHVWL QSLQTDGVAQ RFLGGAINFC TLMPMRAIPF QVVCLLGMNE
ADYPRQRTVQ AFDLMALYPQ AGDRARRDDD RYLFLEALLS ARRHLHISWL GRDAQDNSER
MPSVLVGQLR DYIQQGWQLP PELAKHNKSL LDYLTYEHPL QAFSPQYFLQ AAHTCDQHSL
FSYNPHWRAL YTGEMHTQGL PLPHTHAGCL AGESTETKLD LETLSRFFAH PVDYFCRHHL
GAPFYYQELI YEDLEPFTLD PLQNYQIRDF LLKQVLSTLI DTNQPHTLSE PEHAPIQQHQ
IQHSLQQALD QLQGQGRLPC LHFAQPLREA FGYQITQLVE NYQEVRRLWF QQDQHPVQVS
MAAHTYQAAD LAEISLEDAP QAYPELLDWV DALHQDHQGK MARIHLYPHT LATNKDKIFK
INSLASFWLE YLALCVQQPQ PSFHYLVLAL DQTLCWPAMP PQQAQALLHD ICSAWQYSQH
TPLPLAPRSS MTWLHTYYHK QGDTNEALAQ ARQVYHAETQ IWSRPECAPG SALSEIFPHF
EDLQTADEGF VYWTQKLYQP LFAHLKKSLP LTQLLHCNKD A
//
