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Database: UniProt
Entry: A0A4Q0MB51_9SPHI
LinkDB: A0A4Q0MB51_9SPHI
Original site: A0A4Q0MB51_9SPHI 
ID   A0A4Q0MB51_9SPHI        Unreviewed;      1064 AA.
AC   A0A4Q0MB51;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   18-JUN-2025, entry version 17.
DE   RecName: Full=RecBCD enzyme subunit RecC {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:RXF70049.1};
GN   ORFNames=EKH83_09165 {ECO:0000313|EMBL:RXF70049.1};
OS   Arcticibacter tournemirensis.
OC   Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
OC   Sphingobacteriales; Sphingobacteriaceae; Arcticibacter.
OX   NCBI_TaxID=699437 {ECO:0000313|EMBL:RXF70049.1, ECO:0000313|Proteomes:UP000290848};
RN   [1] {ECO:0000313|EMBL:RXF70049.1, ECO:0000313|Proteomes:UP000290848}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R1 {ECO:0000313|EMBL:RXF70049.1,
RC   ECO:0000313|Proteomes:UP000290848};
RA   He J.;
RT   "The Draft Genome Sequence of the Soil Bacterium Pedobacter tournemirensis
RT   R1.";
RL   Submitted (DEC-2018) 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   -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC       to DNA-binding. {ECO:0000256|HAMAP-Rule:MF_01486}.
CC   -!- MISCELLANEOUS: In the RecBCD complex, RecB has a slow 3'-5' helicase,
CC       an exonuclease activity and loads RecA onto ssDNA, RecD has a fast 5'-
CC       3' helicase activity, while RecC stimulates the ATPase and processivity
CC       of the RecB helicase and contributes to recognition of the Chi site.
CC       {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:RXF70049.1}.
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DR   EMBL; RXOC01000005; RXF70049.1; -; Genomic_DNA.
DR   RefSeq; WP_128769122.1; NZ_RXOC01000005.1.
DR   AlphaFoldDB; A0A4Q0MB51; -.
DR   Proteomes; UP000290848; 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|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01486};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01486, ECO:0000313|EMBL:RXF70049.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000290848}.
FT   DOMAIN          778..989
FT                   /note="RecC C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17946"
SQ   SEQUENCE   1064 AA;  121825 MW;  0CFB7FAB65280054 CRC64;
     MALYLQVSNS LSQLAKKLCS DLQAQGNQVF QPYYIVTQTE GMNNWLKLQL ADSMGIAANY
     RFLRPNDIVF KIYQLLGGRY SQSLSPENLS WVFYKLLNDK EFKERFGNIA AYFGEGSDKE
     VKRLALAEKV ADLLDQYQIY RPEMVQEWNR ASIADVKDDE WQKFLWIRAK ELTKDRLPDR
     TLMGQFILQA LQQGDRIDDL QRGMPAVHIF GLSVITSYHL QLFSELSRHI DFSFHILNPA
     PSEYWFEDRS EKQMLFLKKK GLVNADEPVP GNPLLTSWGR LIQNTFSLFF QNDALINAYD
     EVGIEEPGDK TLLQCIQQDI FYNRNNADRR LISPDHIRDG SVTINACYTA AREVEALYNY
     LVHLIDKHGE VLSARDIVVM VSDIDAYAPY IRAVFNNAPY SFHYTIADES FAANDSLSNA
     LQSVLRMNRQ TFKAEEVLQL LDSGYIRKRF AISDLNLIRK AVDRANIRFG MEGDKDDDTI
     YVSWKYGIER IIYGICMSGD EEFKDEDGTG FYPLELTEGH ASAELIRFCH FVQVLMDSVK
     ERERSRSVSE WVGYVESVLY DLVSEPGEDA GEDYDILLKQ LENYNALNEL ITENISYEVF
     SHNFLQSISS ATRSSSFATG GVTFCSLIPM RSIPFRVVAL LGLNFDKFPR KENPSNFNLM
     EREKRKGDRN IKENDKHLFL ETILSARDYL YISYIGQSTK DNTVLPPSAL VDELVDYIEA
     GVAAEEHVPI VIRQPLHSFS RKYNLADDRL YNYLNYKQGN GETDVQGERK DPPAFDPEVV
     SLDALVNFFK NPVKGYYNDV LGIYFNNDEV LLSDTELFEL DGLSKWSLKQ DLLLLPPEDI
     EILKDKLVKK GVLPLKNMAD IALRDVEAEV SAIRGLFNEC TGGMPGRSLQ VEVNVGDVLL
     KGRVNRIFGD RMICISWSRK ETKYLLEAYL RYLAVRASGT LVDLYFISAK EGRVFEASAI
     TSADALSRLE ELLDLYKQGH KDMLAFFPDF EIEPPKLADL DEAVFQSIAE KKLNSYPFPC
     TDAYVMREAV NGFYKREGVF EEYKMAAEML LLPLAEIFPG YYQN
//
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