ID A0A1B8P6L9_HALEL Unreviewed; 1231 AA.
AC A0A1B8P6L9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, 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 ECO:0000313|EMBL:OBX37853.1};
GN ORFNames=A8U91_02232 {ECO:0000313|EMBL:OBX37853.1};
OS Halomonas elongata.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=2746 {ECO:0000313|EMBL:OBX37853.1, ECO:0000313|Proteomes:UP000092504};
RN [1] {ECO:0000313|EMBL:OBX37853.1, ECO:0000313|Proteomes:UP000092504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HEK1 {ECO:0000313|EMBL:OBX37853.1,
RC ECO:0000313|Proteomes:UP000092504};
RA Gaba S., Singh R.N., Abrol S., Kaushik R., Saxena A.K.;
RT "Genome sequence of halotolerant plant growth promoting strain of Halomonas
RT elongata HEK1 isolated from salterns of Rann of Kutch, Gujarat, India.";
RL Submitted (JUN-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}.
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:OBX37853.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MAJD01000001; OBX37853.1; -; Genomic_DNA.
DR RefSeq; WP_065241040.1; NZ_MAJD01000001.1.
DR AlphaFoldDB; A0A1B8P6L9; -.
DR PATRIC; fig|2746.7.peg.2288; -.
DR Proteomes; UP000092504; 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}; Helicase {ECO:0000256|HAMAP-Rule:MF_01486};
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}.
FT DOMAIN 883..1128
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1231 AA; 138190 MW; 02F89E6595910353 CRC64;
MLATPDTTLQ PGFMVVHGNR LEDLRDLAVT WMRSHPLTPL EDETILVQSN GISQWLKLAL
AADDPQGSGV AAALDVTLPA RFLWQAYRSV LVHRDGEGAV PPESPLDKPR LIWRLMRLLP
ALLDDPLFAP LSRFLADDDD LRKRHQLAER LADLFDQYQV YRADWLAAWA EGRDELIDAR
GQAWPLDEDQ RWQPALWRYL RDDIGAAGLA TSRALVHSRF LEACKELTPE TRPPGLPRRV
MVFGISSLPR QTLEALAAIA RVSQVILCVH NPCRHYWADI IEHKDLLRAA RKRQQRRPGM
PIELDDTQLH LHAQPLLAAW GKQGRDYLRL LDEFDDQESY RARFEAESLR IDLFESPLER
CDAPGLLQQL QDDILELRPP SESRDTWPAV DPERDTSLRF HVAHSALREV EILHDQLLAA
FDADPSLKPR DILVMVPDID TYTAAVQAVF GRLAPDDPRH IPFTLSDQTS RHRQPLLIAL
EALLHLPESR LSVGELLDLL EVPALRQRFG LDAEALPILR RWIEGAGIRW GLSADQRARL
DLPDGLTANT WAFGLRRLLL GYAVGDNADG PWHGIEPFGD IGGLEAALAG PLVDLLDTLD
TLWRRLSEPA DVASWCQRLR ELLADCFSAA DEADLSTLTR LEELLDEWRD TTEDAGLEEP
LPLSVVREHW LGQIDGNNLS QRFLAGAVNI ATLMPMRAIP FRHVCLLGMN DGDYPRTQRP
LDIDLMGHDY RPGDRSRRED DRYLFLEALL SARERLMISW VGRSIHDNAL QPPSVLLGQL
RDHLADGWRL AGHAADEQDD DGQALLDALT TEHPLQPFSR DYFRQPNHPD ATDTQAADKG
LFTYAHEWRA IHTGQPDANE HLEPGFNAVS PSTASLPAMT QETPLTLKQL GAFLKDPVKA
FFNTRLGVYL EREAAESPDH EPFDLDGLAH WQLQNELIGA GRRAVEASEP PMPVVDETLA
RLEREGRLAM GGFAQRMRED LVAPLDDLFT KYAELLEAWP HARPMPAPVS LSLDAEGGEL
AVEDWLGELR ENDQGETCRL LLLTSSLINQ SKYNWKHWLT PWVEHLAAQI AVGPVITELR
SRAGEGTLYP LPADEARARL TAIASAWQAG MTAPLPLARD TAFAWIEKGG DASGIERYLG
DVEKAEETDL KAGKAAAQTL EGNDHQGGEL SRDAYLARQW RDFDELARHQ AAGRRFGELA
ERLYGPLHYA VKVTQKQKAG TTKRQPRGDK S
//
