Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

RecBCD enzyme subunit RecB (EC 3.1.11.5) (Exonuclease V subunit RecB) (ExoV subunit RecB) (Helicase/nuclease RecBCD subunit RecB)

 A0A0B7D644_PSEFL        Unreviewed;      1229 AA.
A0A0B7D644;
01-APR-2015, integrated into UniProtKB/TrEMBL.
01-APR-2015, sequence version 1.
25-APR-2018, entry version 23.
RecName: Full=RecBCD enzyme subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485};
EC=3.1.11.5 {ECO:0000256|HAMAP-Rule:MF_01485};
AltName: Full=Exonuclease V subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485};
Short=ExoV subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485};
AltName: Full=Helicase/nuclease RecBCD subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485};
Name=recB_1 {ECO:0000313|EMBL:CEL27428.1};
Synonyms=recB {ECO:0000256|HAMAP-Rule:MF_01485};
ORFNames=SRM1_00755 {ECO:0000313|EMBL:CEL27428.1};
Pseudomonas fluorescens.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=294 {ECO:0000313|EMBL:CEL27428.1, ECO:0000313|Proteomes:UP000043897};
[1] {ECO:0000313|EMBL:CEL27428.1, ECO:0000313|Proteomes:UP000043897}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SRM1 {ECO:0000313|EMBL:CEL27428.1};
Lo R., Stanton-Cook M.J., Beatson S.A., Turner M.S., Bansal N.;
"Draft genome sequence of Pseudomonas fluorescens SRM1, an isolate
from spoiled raw milk.";
Genome Announc. 3:e00138-e00138(2015).
-!- FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for
recombinational DNA repair. Binds to DSBs and unwinds DNA via a
highly rapid and processive ATP-dependent bidirectional helicase
activity. Unwinds dsDNA until it encounters a Chi (crossover
hotspot instigator) sequence from the 3' direction. Cuts ssDNA a
few nucleotides 3' to the Chi site. The properties and activities
of the enzyme are changed at Chi. The Chi-altered holoenzyme
produces a long 3'-ssDNA overhang and facilitates RecA-binding to
the ssDNA for homologous DNA recombination and repair. Holoenzyme
degrades any linearized DNA that is unable to undergo homologous
recombination. In the holoenzyme this subunit contributes ATPase,
3'-5' helicase, exonuclease activity and loads RecA onto ssDNA.
{ECO:0000256|HAMAP-Rule:MF_01485}.
-!- CATALYTIC ACTIVITY: Exonucleolytic cleavage (in the presence of
ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-
phosphooligonucleotides. {ECO:0000256|HAMAP-Rule:MF_01485}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_01485};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_01485};
-!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits
contribute to DNA-binding. Interacts with RecA.
{ECO:0000256|HAMAP-Rule:MF_01485}.
-!- DOMAIN: The C-terminal domain has nuclease activity and interacts
with RecD. It interacts with RecA, facilitating its loading onto
ssDNA. {ECO:0000256|HAMAP-Rule:MF_01485}.
-!- DOMAIN: The N-terminal DNA-binding domain is a ssDNA-dependent
ATPase and has ATP-dependent 3'-5' helicase function. This domain
interacts with RecC. {ECO:0000256|HAMAP-Rule:MF_01485}.
-!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
{ECO:0000256|HAMAP-Rule:MF_01485, ECO:0000256|SAAS:SAAS00709641}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; CDMF01000001; CEL27428.1; -; Genomic_DNA.
RefSeq; WP_042557535.1; NZ_CDMF01000001.1.
EnsemblBacteria; CEL27428; CEL27428; SRM1_00755.
Proteomes; UP000043897; Unassembled WGS sequence.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:UniProtKB-UniRule.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
Gene3D; 3.90.320.10; -; 1.
HAMAP; MF_01485; RecB; 1.
InterPro; IPR014017; DNA_helicase_UvrD-like_C.
InterPro; IPR000212; DNA_helicase_UvrD/REP.
InterPro; IPR011604; Exonuc_phg/RecB_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR038726; PDDEXK_AddAB-type.
InterPro; IPR004586; RecB.
InterPro; IPR011335; Restrct_endonuc-II-like.
InterPro; IPR014016; UvrD-like_ATP-bd.
InterPro; IPR034739; UvrD/AddA_N.
PANTHER; PTHR11070; PTHR11070; 1.
PANTHER; PTHR11070:SF23; PTHR11070:SF23; 1.
Pfam; PF12705; PDDEXK_1; 1.
Pfam; PF00580; UvrD-helicase; 1.
Pfam; PF13361; UvrD_C; 1.
SUPFAM; SSF52540; SSF52540; 5.
SUPFAM; SSF52980; SSF52980; 1.
TIGRFAMs; TIGR00609; recB; 1.
PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01485,
ECO:0000256|SAAS:SAAS00938801};
Complete proteome {ECO:0000313|Proteomes:UP000043897};
DNA damage {ECO:0000256|HAMAP-Rule:MF_01485,
ECO:0000256|SAAS:SAAS01033119};
DNA repair {ECO:0000256|HAMAP-Rule:MF_01485,
ECO:0000256|SAAS:SAAS01033119};
DNA-binding {ECO:0000256|HAMAP-Rule:MF_01485,
ECO:0000256|SAAS:SAAS00745286};
Exonuclease {ECO:0000256|HAMAP-Rule:MF_01485,
ECO:0000256|SAAS:SAAS01033115};
Helicase {ECO:0000256|HAMAP-Rule:MF_01485,
ECO:0000256|SAAS:SAAS00938801};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_01485,
ECO:0000256|SAAS:SAAS00938801, ECO:0000256|SAAS:SAAS01033115};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01485};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01485};
Nuclease {ECO:0000256|HAMAP-Rule:MF_01485,
ECO:0000256|SAAS:SAAS01033115};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01485,
ECO:0000256|SAAS:SAAS00938801}.
DOMAIN 1 461 UvrD-like helicase ATP-binding.
{ECO:0000259|PROSITE:PS51198}.
DOMAIN 490 769 UvrD-like helicase C-terminal.
{ECO:0000259|PROSITE:PS51217}.
REGION 1 874 DNA-binding and helicase activity,
interacts with RecC. {ECO:0000256|HAMAP-
Rule:MF_01485}.
REGION 926 1229 Nuclease activity, interacts with RecD
and RecA. {ECO:0000256|HAMAP-
Rule:MF_01485}.
ACT_SITE 1121 1121 For nuclease activity.
{ECO:0000256|HAMAP-Rule:MF_01485}.
METAL 992 992 Magnesium; via tele nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01485}.
METAL 1108 1108 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01485}.
METAL 1121 1121 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01485}.
SEQUENCE 1229 AA; 138018 MW; DEF2BA35085C7B9B CRC64;
MSTKTPLALA FPLRGSQLIE ASAGTGKTFT ISALYLRLIL GHGGELSGFA RELLPPQILV
VTFTDAATKE LRERIRTRLA EAARFFRDET PAPDGLIADL RDQFDPQQWP GCANRLDIAA
QWMDEAAVST IHSWCQRMLR EHAFDSGSLF SQSLETDHSD LLGEVLRDYW RLFCYPMQGD
ALNWVRSNWG GPAALLPRVR GLFASERDSD EGKAPAELIE ECLQERRSAL IELKMPWRQW
ADELLAICHQ GVASKTVDGR KMQARYFEPW FEKLKAWAED ESLEQLDIGT GFTRLTPDGM
AEAWKGPAPS HPGLDAMSGL KSSLDALPTP DAAVLQHAAN WVGTRFEEEK RRRAEMGFDD
MLLRLDAALQ SDGGERLATL IREQFPVALI DEFQDTDPVQ YRIFESIYRI EDNNPDTGLF
LIGDPKQAIY AFRGADIYTY LRARQATTGR LHTLGTNFRS SHGMVKAVNH VFERAESREL
GRGAFLFREK NGENPVPFQP VESQGRKEKL QIAGQDIGAL NVWHLSTDQP LSGAVYRQQL
AAACASQITA LLNGGQTGSA GFVQDGEDFR GLRPSDIAIL VRDGKEAQAV RGELAARGVR
SVYLSDKDSV FAAQEAHDLL SWLKACAEPD VERSLKAALA CITLNLPLAE LERLNQDELV
WEARVMQFRG YRELWRKQGV LPMLRRLLHD FHLPQTLMTR SDGERVLTNL LHLSELMQQA
AAELDGEQAL IRHLAELLAL SGQAGEEQIL RLESDEQLVK VVTIHKSKGL EYPLVFLPFI
CSAKPVDGSR LPLHYHDATG KAQVSLKPTV ELIAQADEER LAEDLRLLYV ALTRAQHACW
LGVTDLKRGN NNSSVLHLSA LGYLLGGGAS LGESSGLNRW LQDLQQDCPA IDIGEMPQPT
DEHYQPPRNE AVLSVTLLPK RKASENWWIA SYSALRISDV LSVGSDEAPD SPQAQKLFDD
ERLDPDAPRE IITGGADIHR FPRGPNPGTF LHGLLEWAGD DGFAVSREAL EDAIGRRCNL
RGWEGWITTL SDWLQHLLKS PLPIADERPP VILEQLTQYR VEMEFWFASH KVDVLKLDEL
VRQFTHNGVA RVGAEPVQLN GMFKGFIDLT FEHDGRYYVA DYKSNWLGVD DLAYTEHAME
QSILDNRYDL QYVLYLLALH RQLKARLPDY DYDRHVGGAL YLFLRGTRSD SRGVYFARPP
RELIERLDRM FQGKPEPKAE PAWEQGVLL


Related products :

Catalog number Product name Quantity
EIAAB46584 86 kDa subunit of Ku antigen,ATP-dependent DNA helicase 2 subunit 2,ATP-dependent DNA helicase II 80 kDa subunit,CTC box-binding factor 85 kDa subunit,CTC85,CTCBF,DNA repair protein XRCC5,G22P2,Homo s
EIAAB46583 ATP-dependent DNA helicase 2 subunit 2,ATP-dependent DNA helicase II 80 kDa subunit,CTC box-binding factor 85 kDa subunit,CTC85,CTCBF,DNA repair protein XRCC5,G22p2,Ku autoantigen protein p86 homolog,
EIAAB46585 5'-deoxyribose-5-phosphate lyase Ku70,5'-dRP_AP lyase Ku70,ATP-dependent DNA helicase 2 subunit 1,ATP-dependent DNA helicase II 70 kDa subunit,CTC box-binding factor 75 kDa subunit,CTC75,CTCBF,DNA rep
18-003-42479 ATP-dependent DNA helicase 2 subunit 1 - EC 3.6.1.-; ATP-dependent DNA helicase II 70 kDa subunit; Lupus Ku autoantigen protein p70; Ku70; 70 kDa subunit of Ku antigen; Thyroid-lupus autoantigen; TLAA 0.1 mg Protein A
EIAAB46586 5'-deoxyribose-5-phosphate lyase Ku70,5'-dRP lyase Ku70,70 kDa subunit of Ku antigen,ATP-dependent DNA helicase 2 subunit 1,ATP-dependent DNA helicase II 70 kDa subunit,CTC box-binding factor 75 kDa s
18-003-42478 ATP-dependent DNA helicase 2 subunit 1 - EC 3.6.1.-; ATP-dependent DNA helicase II 70 kDa subunit; Lupus Ku autoantigen protein p70; Ku70; 70 kDa subunit of Ku antigen; Thyroid-lupus autoantigen; TLAA 0.1 mg Protein A
EIAAB34355 A1 40 kDa subunit,Activator 1 40 kDa subunit,Activator 1 subunit 2,Homo sapiens,Human,Replication factor C 40 kDa subunit,Replication factor C subunit 2,RF-C 40 kDa subunit,RFC2,RFC40
EIAAB34363 A1 36 kDa subunit,Activator 1 36 kDa subunit,Activator 1 subunit 5,Homo sapiens,Human,Replication factor C 36 kDa subunit,Replication factor C subunit 5,RF-C 36 kDa subunit,RFC36,RFC5
EIAAB34361 A1 37 kDa subunit,Activator 1 37 kDa subunit,Activator 1 subunit 4,Homo sapiens,Human,Replication factor C 37 kDa subunit,Replication factor C subunit 4,RF-C 37 kDa subunit,RFC37,RFC4
EIAAB34360 A1 38 kDa subunit,Activator 1 38 kDa subunit,Activator 1 subunit 3,Homo sapiens,Human,Replication factor C 38 kDa subunit,Replication factor C subunit 3,RF-C 38 kDa subunit,RFC3,RFC38
EIAAB29619 Homo sapiens,Human,PAF acetylhydrolase 29 kDa subunit,PAF-AH 29 kDa subunit,PAFAH subunit gamma,PAF-AH subunit gamma,PAFAH1B3,PAFAHG,Platelet-activating factor acetylhydrolase IB subunit gamma
EIAAB29611 Homo sapiens,Human,PAF acetylhydrolase 30 kDa subunit,PAF-AH 30 kDa subunit,PAFAH subunit beta,PAF-AH subunit beta,PAFAH1B2,PAFAHB,Platelet-activating factor acetylhydrolase IB subunit beta
EIAAB29612 Mouse,Mus musculus,PAF acetylhydrolase 30 kDa subunit,PAF-AH 30 kDa subunit,PAFAH subunit beta,PAF-AH subunit beta,Pafah1b2,Pafahb,Platelet-activating factor acetylhydrolase IB subunit beta
EIAAB29614 Bos taurus,Bovine,PAF acetylhydrolase 30 kDa subunit,PAF-AH 30 kDa subunit,PAFAH subunit beta,PAF-AH subunit beta,PAFAH1B2,PAFAHB,Platelet-activating factor acetylhydrolase IB subunit beta
EIAAB29617 Bos taurus,Bovine,PAF acetylhydrolase 29 kDa subunit,PAF-AH 29 kDa subunit,PAFAH subunit gamma,PAF-AH subunit gamma,PAFAH1B3,PAFAHG,Platelet-activating factor acetylhydrolase IB subunit gamma
EIAAB29618 Mouse,Mus musculus,PAF acetylhydrolase 29 kDa subunit,PAF-AH 29 kDa subunit,PAFAH subunit gamma,PAF-AH subunit gamma,Pafah1b3,Pafahg,Platelet-activating factor acetylhydrolase IB subunit gamma
EIAAB34364 A1 36 kDa subunit,Activator 1 36 kDa subunit,Activator 1 subunit 5,Mouse,Mus musculus,Replication factor C 36 kDa subunit,Replication factor C subunit 5,RF-C 36 kDa subunit,RFC36,Rfc5
EIAAB34354 A1 40 kDa subunit,Activator 1 40 kDa subunit,Activator 1 subunit 2,Mouse,Mus musculus,Replication factor C 40 kDa subunit,Replication factor C subunit 2,RF-C 40 kDa subunit,Rfc2,RFC40
EIAAB34359 A1 38 kDa subunit,Activator 1 38 kDa subunit,Activator 1 subunit 3,Mouse,Mus musculus,Replication factor C 38 kDa subunit,Replication factor C subunit 3,RF-C 38 kDa subunit,Rfc3,RFC38
EIAAB34358 A1 38 kDa subunit,Activator 1 38 kDa subunit,Activator 1 subunit 3,Bos taurus,Bovine,Replication factor C 38 kDa subunit,Replication factor C subunit 3,RF-C 38 kDa subunit,RFC3,RFC38
E1345m ELISA Epiligrin subunit alpha,Kalinin subunit alpha,Lama3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subunit alpha,Mouse,Mus musculus,Nicein subunit alpha 96T
U1345m CLIA Epiligrin subunit alpha,Kalinin subunit alpha,Lama3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subunit alpha,Mouse,Mus musculus,Nicein subunit alpha 96T
E1345m ELISA kit Epiligrin subunit alpha,Kalinin subunit alpha,Lama3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subunit alpha,Mouse,Mus musculus,Nicein subunit alpha 96T
E1345h ELISA E170,Epiligrin 170 kDa subunit,Epiligrin subunit alpha,Homo sapiens,Human,Kalinin subunit alpha,LAMA3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subunit al 96T
U1345h CLIA E170,Epiligrin 170 kDa subunit,Epiligrin subunit alpha,Homo sapiens,Human,Kalinin subunit alpha,LAMA3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subunit alp 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur