DNAB_RHOMR
ID DNAB_RHOMR Reviewed; 941 AA.
AC O30477; O50478;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Replicative DNA helicase;
DE EC=3.6.4.12;
DE Contains:
DE RecName: Full=Homing endonuclease PI-Rma43812IP {ECO:0000303|PubMed:12654995};
DE EC=3.1.-.-;
DE AltName: Full=Rma dnaB intein;
GN Name=dnaB {ECO:0000303|PubMed:9223276};
OS Rhodothermus marinus (Rhodothermus obamensis).
OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC Rhodothermaceae; Rhodothermus.
OX NCBI_TaxID=29549;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INTEIN SPLICING IN E.COLI.
RX PubMed=9223276; DOI=10.1073/pnas.94.15.7851;
RA Liu X.Q., Hu Z.;
RT "A DnaB intein in Rhodothermus marinus: indication of recent intein homing
RT across remotely related organisms.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7851-7856(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Politz O.;
RT "Cloning of a dnaB homolog gene from Rhodothermus marinus with high
RT similarity to the E.coli helicase but not able to complement a dnaBts
RT mutation.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NOMENCLATURE.
RX PubMed=12654995; DOI=10.1093/nar/gkg274;
RA Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT endonucleases and their genes.";
RL Nucleic Acids Res. 31:1805-1812(2003).
CC -!- FUNCTION: Participates in initiation and elongation during chromosome
CC replication; it exhibits DNA-dependent ATPase activity. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- PTM: Upon expression in E.coli this protein undergoes self splicing
CC that involves a post-translational excision of the intervening region
CC (intein) followed by peptide ligation. {ECO:0000269|PubMed:9223276}.
CC -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC {ECO:0000305}.
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DR EMBL; AF006675; AAB66912.1; -; Genomic_DNA.
DR EMBL; Y13813; CAA74140.1; -; Genomic_DNA.
DR AlphaFoldDB; O30477; -.
DR SMR; O30477; -.
DR MEROPS; N10.002; -.
DR REBASE; 4095; PI-Rma43812IP.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
DR CDD; cd00984; DnaB_C; 1.
DR Gene3D; 1.10.860.10; -; 1.
DR Gene3D; 3.10.28.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR036185; DNA_heli_DnaB-like_N_sf.
DR InterPro; IPR007692; DNA_helicase_DnaB.
DR InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR InterPro; IPR007693; DNA_helicase_DnaB-like_N.
DR InterPro; IPR016136; DNA_helicase_N/primase_C.
DR InterPro; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00772; DnaB; 1.
DR Pfam; PF03796; DnaB_C; 1.
DR Pfam; PF14528; LAGLIDADG_3; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF48024; SSF48024; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF55608; SSF55608; 1.
DR TIGRFAMs; TIGR00665; DnaB; 1.
DR TIGRFAMs; TIGR01443; intein_Cterm; 1.
DR TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
DR PROSITE; PS51199; SF4_HELICASE; 2.
PE 3: Inferred from homology;
KW ATP-binding; Autocatalytic cleavage; DNA replication; DNA-binding;
KW Endonuclease; Helicase; Hydrolase; Intron homing; Nuclease;
KW Nucleotide-binding; Primosome; Protein splicing; Repeat.
FT CHAIN 1..421
FT /note="Replicative DNA helicase, 1st part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000013285"
FT CHAIN 422..849
FT /note="Homing endonuclease PI-Rma43812IP"
FT /evidence="ECO:0000255"
FT /id="PRO_0000013286"
FT CHAIN 850..941
FT /note="Replicative DNA helicase, 2nd part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000013287"
FT DOMAIN 214..484
FT /note="SF4 helicase; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
FT DOMAIN 534..683
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT DOMAIN 646..915
FT /note="SF4 helicase; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..941
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 245..252
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
FT CONFLICT 30
FT /note="R -> RR (in Ref. 2; CAA74140)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="K -> KA (in Ref. 2; CAA74140)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="C -> CA (in Ref. 2; CAA74140)"
FT /evidence="ECO:0000305"
FT CONFLICT 293..317
FT /note="ASMPRRPAPDGCATRTGVSWPARRP -> RVDAQAARTGRLRDEDWRKLARA
FT AGR (in Ref. 2; CAA74140)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 941 AA; 104883 MW; 9145C41066152B29 CRC64;
MAEFEERPRL SIGEEEAPPY PLEKLTGGRR TRAQIHALHQ QAGRVPPQAV ELEQAVLGAM
LIEPEAIPRA LEILTPEAFY DGRHQRIFRA IVRLFEQNRG VDLLTVTEEL RRTGELEQAG
DTIYLSELTT RVASAANVEY HARIIAEKLL RRMIEVMTLL VGRAYDPAAD AFELLDEVEA
EIFRLSDVHL RKAARSMNEV VKETLERLEA IHGRPGGITG VPSGFHQLDA LTGGWQRGDL
IIIAARPSMG KTAFALSCRN AALHPHYGTG VAIFSLEMGA EQLAQRLLTA EAASMPRRPA
PDGCATRTGV SWPARRPLSD APIFIDDTPS LGVLELRAKC RRLKAEHDIG LVIVDYLQLM
QASHMPRNAN REQEIAQISR SLKALAKELN VPVVALSQLS RAVETRGGDK RPQLSDLRES
GCLAGDTLIT LADGRRVPIR ELVSQQNFSV WALNPQTYRL ERARVSRAFC TGIKPVYRLT
TRLGRSIRAT ANHRFLTPQG WKRVDELQPG DYLALPRRIP TASTPTLTEA ELALLGHLIG
DGCTLPHHVI QYTSRDADLA TLVAHLATKV FGSKVTPQIR KELRWYQVYL RAARPLAPGK
RNPISDWLRD LGIFGLRSYE KKVPALLFCQ TSEAIATFLR HLWATDGCIQ MRRGKKPYPA
VYYATSSYQL ARDVQSLLLR LGINARLKTV AQGEKGRVQY HVKVSGREDL LRFVEKIGAV
GARQRAALAS VYDYLSVRTG NPNRDIIPVA LWYELVREAM YQRGISHRQL HANLGMAYGG
MTLFRQNLSR ARALRLAEAA ACPELRQLAQ SDVYWDPIVS IEPDGVEEVF DLTVPGPHNF
VANDIIAHNS IEQDADVVLF IYRPERYGIT VDENGNPTEG IAEIIIGKQR NGPTGTVRLA
FINQYARFEN LTMYQPEPGT PLPETPDETI LPSGPPDEAP F
