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Database: UniProt
Entry: A0A432WLK2_9GAMM
LinkDB: A0A432WLK2_9GAMM
Original site: A0A432WLK2_9GAMM 
ID   A0A432WLK2_9GAMM        Unreviewed;       730 AA.
AC   A0A432WLK2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=RecBCD enzyme subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487};
DE            EC=3.1.11.5 {ECO:0000256|HAMAP-Rule:MF_01487};
DE   AltName: Full=Exonuclease V subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487};
DE            Short=ExoV subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487};
DE   AltName: Full=Helicase/nuclease RecBCD subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487};
GN   Name=recD {ECO:0000256|HAMAP-Rule:MF_01487,
GN   ECO:0000313|EMBL:RUO34696.1};
GN   ORFNames=CWE14_01450 {ECO:0000313|EMBL:RUO34696.1};
OS   Aliidiomarina soli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Aliidiomarina.
OX   NCBI_TaxID=1928574 {ECO:0000313|EMBL:RUO34696.1, ECO:0000313|Proteomes:UP000287823};
RN   [1] {ECO:0000313|EMBL:RUO34696.1, ECO:0000313|Proteomes:UP000287823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4G10-17 {ECO:0000313|EMBL:RUO34696.1,
RC   ECO:0000313|Proteomes:UP000287823};
RX   PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA   Liu Y., Lai Q., Shao Z.;
RT   "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT   Idiomarinaceae.";
RL   Front. Microbiol. 9:2453-2453(2018).
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 has
CC       ssDNA-dependent ATPase and 5'-3' helicase activity. When added to pre-
CC       assembled RecBC greatly stimulates nuclease activity and augments
CC       holoenzyme processivity. Negatively regulates the RecA-loading ability
CC       of RecBCD. {ECO:0000256|HAMAP-Rule:MF_01487}.
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_01487};
CC   -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC       to DNA-binding. {ECO:0000256|HAMAP-Rule:MF_01487}.
CC   -!- SIMILARITY: Belongs to the RecD family. {ECO:0000256|HAMAP-
CC       Rule:MF_01487}.
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:RUO34696.1}.
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DR   EMBL; PIPO01000001; RUO34696.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A432WLK2; -.
DR   Proteomes; UP000287823; 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; cd17933; DEXSc_RecD-like; 1.
DR   CDD; cd18809; SF1_C_RecD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   Gene3D; 1.10.10.1020; RecBCD complex, subunit RecD, N-terminal domain; 1.
DR   HAMAP; MF_01487; RecD; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006344; RecD.
DR   InterPro; IPR041851; RecD_N.
DR   InterPro; IPR027785; UvrD-like_helicase_C.
DR   NCBIfam; TIGR01447; recD; 1.
DR   PANTHER; PTHR43788:SF6; DNA HELICASE B; 1.
DR   PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF13245; AAA_19; 1.
DR   Pfam; PF21185; RecD_N; 1.
DR   Pfam; PF13538; UvrD_C_2; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01487}; DNA damage {ECO:0000256|HAMAP-Rule:MF_01487};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_01487};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01487}; Exonuclease {ECO:0000256|HAMAP-Rule:MF_01487};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01487};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01487};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01487};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01487}; Reference proteome {ECO:0000313|Proteomes:UP000287823}.
FT   DOMAIN          660..707
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13538"
FT   BINDING         224..231
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01487"
SQ   SEQUENCE   730 AA;  80493 MW;  1A6B133B65987DA6 CRC64;
     MNKVVSNDVY NEGTALTELE AWYNAGWIRA LDLNLARFLQ SEQVADERVL VLAVLLSHQV
     GRGHVCLPLK ELFGSPQLLL NLPPAHSRFT DEEHELVSPL QLLTRLGVTT EADLEGALSA
     SEAVADSPQT DVTPLVYQHG ALYLRRYWHY EARIASALQE RMQLSGQGSR APDIAAETLQ
     QALDELFPHA ADSTTSSPTG IERVNWQKLA CANTLRSRFS VITGGPGTGK TYTVVRLLAM
     LQRLAAEPLR IRLAAPTGKA AARLKESISN ALHEMQQSTE LSEWQQVLQR IESDSSTLHK
     LLGVQQGTRK FRHHRGNPLS LDVLVVDEAS MVDIELMDAT LEALPAHAQL ILLGDKDQLA
     SVEAGAVLGQ LCQGAEQGGY NQQSFDYLQS FSDTPLPDFL RAADGPSYLQ HVVMLRVSRR
     FDGRSGVGHL AYAINAGDSK RAAQLLLGSQ AAEAAGASHE QQTANSFSDI AVLQSTGTET
     VSQRQLFAQQ QPALTEDLRR LCVQGFSGYL QQIKQRPDAQ ASDDDIDTWA RSVLAGYSNF
     QLLTPVREGE FGVAGLNAQI ERWLKSALQT LKKTAAGESE PLQPALATEK GNGANQASEQ
     WYEGRPVMIT ENDYSLNLRN GDIGMVLVSP RDGRKRVVFV DSDNTLRWIL PSRLREVQTV
     FAMTVHKSQG SEFTHTVMVL PEQDNPVLCR ELVYTGVTRA KKQLTMVVPD WHVFHQSVQR
     RTLRAGRLHL
//
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