ID B7GIH0_ANOFW Unreviewed; 1059 AA.
AC B7GIH0;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=N-terminal HKD family nuclease fused to DNA/RNA helicase domain {ECO:0000313|EMBL:ACJ32717.1};
GN OrderedLocusNames=Aflv_0333 {ECO:0000313|EMBL:ACJ32717.1};
OS Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=491915 {ECO:0000313|EMBL:ACJ32717.1, ECO:0000313|Proteomes:UP000000742};
RN [1] {ECO:0000313|EMBL:ACJ32717.1, ECO:0000313|Proteomes:UP000000742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21510 / WK1 {ECO:0000313|Proteomes:UP000000742};
RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT "Encapsulated in silica: genome, proteome and physiology of the
RT thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL Genome Biol. 9:R161.1-R161.16(2008).
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; CP000922; ACJ32717.1; -; Genomic_DNA.
DR AlphaFoldDB; B7GIH0; -.
DR STRING; 491915.Aflv_0333; -.
DR REBASE; 38676; AflWKORF333P.
DR KEGG; afl:Aflv_0333; -.
DR eggNOG; COG1061; Bacteria.
DR eggNOG; COG3886; Bacteria.
DR HOGENOM; CLU_005588_1_1_9; -.
DR Proteomes; UP000000742; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR CDD; cd18032; DEXHc_RE_I_III_res; 1.
DR CDD; cd18799; SF2_C_EcoAI-like; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR021835; DUF3427.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1.
DR Pfam; PF11907; DUF3427; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50035; PLD; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:ACJ32717.1};
KW Helicase {ECO:0000313|EMBL:ACJ32717.1};
KW Hydrolase {ECO:0000313|EMBL:ACJ32717.1};
KW Nucleotide-binding {ECO:0000313|EMBL:ACJ32717.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000742}.
FT DOMAIN 206..237
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 325..476
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 531..682
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1059 AA; 124467 MW; 4E8E47E1577A9BA8 CRC64;
MVKFYKKYVR WFLLMEKSFF EELQLLAKQY PDTSVIQRLS PKDYIEVLVL HSAKQLAHKL
KSLAEENRFD EIIQLTKHIS TLVSNNEDSF SLPLSMITYT YGQREIPVIE DFFLSRLHLL
YNDKHTMKNF FKTLKYEMLT ADSVDFMVSF IRMSGLQLLI RPLLMLEKER IPVRIITSTY
LGITEPKALK KLMQFSNVQV KIIDTQQHSF HTKAYIFHRR SGLNTVIIGS SNISDSALIN
GHELNVKLPD TSFLPIYEHT KEMFEKIWNR ADTISLDYAF IETYQQQTIR KENKPLVAEP
KGEYNVTSSV KPNDMQKKAL KNLEHTRKNG NTKGVIIAAT GTGKTYLAAF DVKAYNPKKL
LFIAHREELL DKAIETFKHV IENDHLFGKI TGTVKQFDKP YLFSTVQSLS KDETLNRFKQ
HEFDYIIIDE FHHAEAPTYQ KVIRYFRPKF LLGLTATPER MDGRDVLAIC DHNVVYEIRL
REALDAQLLA PFHYFGISDR TVDYSQIPLK NGMFDEALLV KALKTNERTD FIIEMIRTYS
YDGDRIVGLA FCVNIDHAKY MSEQFNKRGY CTTYLTGEHS VEYREQIIKR LENPDDPLEF
IFTVNIFNEG IDIPSLNLLL FLRPTESSTV FIQQLGRGLR KVEGKEFVTV LDFVGNYQKS
FMIPLALAGQ LNDKAFDKDS LRVAITHEFA DLPGGAYVDL DPVTQREILD RIDSIKMNST
DMLKMLYQQF KNELGRSPEI LDFLYYEQSP SLTFFIYKYR SWVKTKEKMN DINELDQMIL
HYPLMCECVE RLENQLPIKW PYDFVILQLA LLQKVVSCED VVKQLARKFA IDVPLEKHEK
MIMQSMDRLS LPYKKQKWSF GQRNGQQFIL NDDILALTED TQFFNYIKDR IDYGLIEFRR
TYRPERFLTK GEKLTLYQNY TRNDLIFLFE AGLKEGSWRE GVSRVRNHYL LFVNLNKSER
VKEHLHYKDY FLDQKHFHWQ SQNQTSHSSS VGQHFIRHKE LGIHIHLFVR KFEEMHGMTL
PFTYLGEVDY VSSYGDKPMS ITWRLHHSVP EDLYIDLIR
//
