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Database: UniProt
Entry: A0A0R2N8N9_9LACO
LinkDB: A0A0R2N8N9_9LACO
Original site: A0A0R2N8N9_9LACO 
ID   A0A0R2N8N9_9LACO        Unreviewed;       433 AA.
AC   A0A0R2N8N9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=II DNA RNA helicase {ECO:0000313|EMBL:KRO22182.1};
GN   ORFNames=IV88_GL001278 {ECO:0000313|EMBL:KRO22182.1};
OS   Pediococcus argentinicus.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=480391 {ECO:0000313|EMBL:KRO22182.1, ECO:0000313|Proteomes:UP000051249};
RN   [1] {ECO:0000313|EMBL:KRO22182.1, ECO:0000313|Proteomes:UP000051249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23026 {ECO:0000313|EMBL:KRO22182.1,
RC   ECO:0000313|Proteomes:UP000051249};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC       {ECO:0000256|RuleBase:RU000492}.
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:KRO22182.1}.
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DR   EMBL; JQCQ01000040; KRO22182.1; -; Genomic_DNA.
DR   RefSeq; WP_057800382.1; NZ_JQCQ01000040.1.
DR   AlphaFoldDB; A0A0R2N8N9; -.
DR   PATRIC; fig|480391.4.peg.1297; -.
DR   OrthoDB; 9805696at2; -.
DR   Proteomes; UP000051249; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProt.
DR   CDD; cd00268; DEADc; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   PANTHER; PTHR47959:SF13; ATP-DEPENDENT RNA HELICASE RHLE; 1.
DR   PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000492};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051249}.
FT   DOMAIN          25..194
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          220..364
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          377..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..391
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..413
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..433
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   433 AA;  48301 MW;  71F316CBA39D411E CRC64;
     MNEIFEQHFN EKGFKARTLI QKQTFDLLLD GQSVIGLSPT GSGKTLAFAL PLLEKIIPGD
     GIQLLVLSPS QELAVQTTDV FREWASLLKL KVSSVTGGAN LQRQIERLKK KPEIIVGTPG
     RVLTLVNEGR LKTSEINTLV VDEADELLVG ETLGDIRQIE DQLPGSLQYG FFSATSADSL
     FQISNWFGID PVTVDVRADD HTQGMVKHGW MVTSDASKLK LLRKLSHLKH FQALVFFNHV
     STLEKVAATL KHEGVHAGKI AGHQVQTDRA TALRDFRKGK LDLLLVTEVA ARGLDIQKLP
     AVINYDVPEK AINYTHRVGR TGRMGESGFV INFGNDHDIR DVKKIGRSLN LEMNSLVIMN
     DEVMTSEEAK DVQPIKKTAV KNDNDRQSTR PKARAKIKKT NVQKDSDIRE TPLKKKKHSK
     KHSKRKGMRQ KKS
//
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