ID A0A3N2BCH8_9MICO Unreviewed; 1201 AA.
AC A0A3N2BCH8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Replicative DNA helicase {ECO:0000256|ARBA:ARBA00021957, ECO:0000256|RuleBase:RU362085};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551, ECO:0000256|RuleBase:RU362085};
GN ORFNames=EDD31_1325 {ECO:0000313|EMBL:ROR72961.1};
OS Bogoriella caseilytica.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Bogoriellaceae;
OC Bogoriella.
OX NCBI_TaxID=56055 {ECO:0000313|EMBL:ROR72961.1, ECO:0000313|Proteomes:UP000280668};
RN [1] {ECO:0000313|EMBL:ROR72961.1, ECO:0000313|Proteomes:UP000280668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11294 {ECO:0000313|EMBL:ROR72961.1,
RC ECO:0000313|Proteomes:UP000280668};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Participates in initiation and elongation during chromosome
CC replication; it exhibits DNA-dependent ATPase activity.
CC {ECO:0000256|ARBA:ARBA00002835, ECO:0000256|RuleBase:RU362085}.
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 Evidence={ECO:0000256|ARBA:ARBA00001665,
CC ECO:0000256|RuleBase:RU362085};
CC -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC {ECO:0000256|ARBA:ARBA00008428, ECO:0000256|RuleBase:RU362085}.
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:ROR72961.1}.
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DR EMBL; RKHK01000001; ROR72961.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2BCH8; -.
DR Proteomes; UP000280668; Unassembled WGS sequence.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-UniRule.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR CDD; cd00081; Hint; 2.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 2.
DR Gene3D; 3.10.28.10; Homing endonucleases; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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 NCBIfam; TIGR00665; DnaB; 1.
DR NCBIfam; TIGR01443; intein_Cterm; 1.
DR NCBIfam; TIGR01445; intein_Nterm; 1.
DR PANTHER; PTHR30153:SF2; REPLICATIVE DNA HELICASE; 1.
DR PANTHER; PTHR30153; REPLICATIVE DNA HELICASE DNAB; 1.
DR Pfam; PF00772; DnaB; 1.
DR Pfam; PF03796; DnaB_C; 2.
DR Pfam; PF14890; Intein_splicing; 1.
DR Pfam; PF14528; LAGLIDADG_3; 2.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 2.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 2.
DR SUPFAM; SSF55608; Homing endonucleases; 2.
DR SUPFAM; SSF48024; N-terminal domain of DnaB helicase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 2.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
DR PROSITE; PS51199; SF4_HELICASE; 3.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362085};
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU362085};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362085};
KW Helicase {ECO:0000256|RuleBase:RU362085, ECO:0000313|EMBL:ROR72961.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362085};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362085}; Primosome {ECO:0000256|RuleBase:RU362085};
KW Protein splicing {ECO:0000256|ARBA:ARBA00023000};
KW Reference proteome {ECO:0000313|Proteomes:UP000280668};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 187..224
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT DOMAIN 363..549
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 640..806
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT DOMAIN 936..993
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 1121..1143
FT /note="Intein C-terminal splicing"
FT /evidence="ECO:0000259|PROSITE:PS50818"
FT DOMAIN 1143..1201
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
SQ SEQUENCE 1201 AA; 131789 MW; 95D2A530767C3DEF CRC64;
MTVAEERSSG QGFDRTPPQD IAAEQSVLGG MLLSKDAIAD VIEELRPNDF YRPAHEVIYE
AVIDLYGRGE PADAVTVSAE LSKRGEIARI GGAPYLHTLI SSVPTAANAG YYARLVREQA
VLRRLVEAGT RIVQLGYSTD GGEVDALVDN AQAEVYAVTE RRTSEDYVPL RETINPTMEE
IEAAADRGDG MVGVPTGFAD LDSLTNGLHG GQMVIIAARP AMGKALALET ALPTPSGWTT
MGEVREGDWL VAADGSPTRV VATTEVMADR PCFEIEFDDG TTVVADAEHQ WLTDTRASRK
SAQAAAVGYN GYRSQRTFAE VRTTEEIART VRCQTADKRM NHSVTNSLPL NLPEAELPID
PYVLGAWLGD GHSAGGRMTT ADPEIVARME AGGYVVKPGA GKYGYSITLP KPPALQERTC
DVCGATYLPK QAHVRTCGRQ CGGRRKTLKL PQVIPSCRDC GTPASGRGLC RDCYADHGSF
QVLLRKVGVL NNKHIPLTYL RASERQRREV LAGLLDTDGT VMKQGSVQIA LTHEPLARDT
RELIHSLGYR TGWYTKRVAG RSEDSSTSYV ITFTTDDDVF ALERKKLAHK RRRRPSTPRL
RSRYIKHVRS VPSVPVRCVQ IEHPSHLYLA TRSMVPTHNS TLAVDICRNA SVRHGQTSVI
FSLEMSRNEI TMRLLSAEGQ VPLQKMRNGT MREEDWTKMA SAMSKVSDAP LFIDDSPNMS
MMEIRAKCRR LKQRHDLKLV VVDYLQLMSS GKRVESRQQE VSEFSRALKL LAKEIEVPVI
AVAQLNRGPE QRTDKKPMMS DLRESGCLPA ETRILRADTG AESTIGELFL SGEKDVPVWA
LDDRLKYVRR HITSVFTTGT KPVYRMKLAS GREVRATPNH KFLTYNGWVA LGELEAGSRI
GVPRHIPAPE RETAWDDRKV IMLAHAVAAD RPSSAVPSDV FSLPKHQIAL FLRELWSLSG
TVGDGPGGGS VRLRTSSVRI AEAVMNLLLR FGLNSMRAGD GRTMAITGTQ EKRIFLERIA
VDGAAGPVAA SLRQRLTTGA VRRASTSSTP WHEVGEILSG PARVEDVVSG IGRSLRAAEA
RQGGALVKVA QTLDREDLEL MATNDLLWDR VVTIEYEGSE QVFDATVAGS HNFVANGVAV
HNSLEQDADI VMLLHREDAY DRESPRAGEA DIIVAKHRNG PTDTIVVAFQ GHYARFVDMA
R
//
