ID K6XF80_9MICO Unreviewed; 737 AA.
AC K6XF80;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
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:GAB97494.1};
GN ORFNames=KILIM_072_00030 {ECO:0000313|EMBL:GAB97494.1};
OS Kineosphaera limosa NBRC 100340.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Kineosphaera.
OX NCBI_TaxID=1184609 {ECO:0000313|EMBL:GAB97494.1, ECO:0000313|Proteomes:UP000008366};
RN [1] {ECO:0000313|EMBL:GAB97494.1, ECO:0000313|Proteomes:UP000008366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100340 {ECO:0000313|EMBL:GAB97494.1,
RC ECO:0000313|Proteomes:UP000008366};
RA Yoshida I., Isaki S., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y.,
RA Ohji S., Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Kineosphaera limosa NBRC 100340.";
RL Submitted (AUG-2012) 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 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:GAB97494.1}.
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DR EMBL; BAHD01000072; GAB97494.1; -; Genomic_DNA.
DR RefSeq; WP_006594026.1; NZ_BAHD01000072.1.
DR AlphaFoldDB; K6XF80; -.
DR STRING; 1184609.KILIM_072_00030; -.
DR eggNOG; COG0507; Bacteria.
DR Proteomes; UP000008366; 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_sf.
DR InterPro; IPR027785; UvrD-like_helicase_C.
DR NCBIfam; TIGR01447; recD; 1.
DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR PANTHER; PTHR43788:SF6; RECBCD ENZYME SUBUNIT RECD; 1.
DR Pfam; PF13245; AAA_19; 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|HAMAP-Rule:MF_01487};
KW 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:UP000008366}.
FT DOMAIN 656..703
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13538"
FT REGION 85..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 216..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01487"
SQ SEQUENCE 737 AA; 76300 MW; 443ED2251EC274CE CRC64;
MSLLEVFEPA DARDRRLALG ATGQLAAFNE AGVLSAADVH IARAVARASR EQDEVAVLAA
AFATRAVRLG SVAVDLADLA AAGRQTESPA PAGVAGSGAS EPGGDVGVEP ERPDASGGVA
DLPWPDPATW QPRVQASKLV AQGVLVVEHD LVYLQRYHHQ EVQVVDDLNR RAAGPPPPVD
EARLQAGLER YFAEGDSDQR AAAQTAVRSW TTVITGGPGT GKTTSAATIL ALLAEQGQQD
HSTAGKARPL RIGLAAPTGK AAARMQEALR EALTGSPERP GVIAATANAD AATRAAVAGL
GDLEAVTLHR LLGVRPDRGT RFRHHRGNRL PHDVVLIDEA SMVSLTHMAR LLEALRPTTR
LILVGDPDQL VSVDAGAVLA DLVAGAQLAE GKQAIGADSG TGAGTGTESG TGSGGGADGA
TAGGATGGPL RVAGLRRVHR YGAQIGEVAQ ALREGDADAV MALLRGPRAA GADAEVLWID
DSDPATSLQA LEPLLTRQAR AIYDLAQVGD APGALAAAAR HRLLCAHREG PFGVRTWNAR
VEGWLRQATG DGLYDPMYIG RPLLITANDY ATGVVNGDTG VIVRATGRGS QRVAVIAGQE
TRGHAPPAPP GQPADLQSSR PAEQEQRSSP EGTAFAGLGG GFRVFAPSRL GEVQTLHAMT
VHKSQGSQAD AVTVLLPERG SPLLTRELLY TGVTRARNQV RVVGSEAVIR EAVQRRVVRA
SGLRRRLAPP QGEGGLP
//
