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Database: UniProt
Entry: L0A2L4_DEIPD
LinkDB: L0A2L4_DEIPD
Original site: L0A2L4_DEIPD 
ID   L0A2L4_DEIPD            Unreviewed;       477 AA.
AC   L0A2L4;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=DNA/RNA helicase, superfamily II {ECO:0000313|EMBL:AFZ68108.1};
GN   OrderedLocusNames=Deipe_2643 {ECO:0000313|EMBL:AFZ68108.1};
OS   Deinococcus peraridilitoris (strain DSM 19664 / LMG 22246 / CIP 109416 /
OS   KR-200).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=937777 {ECO:0000313|EMBL:AFZ68108.1, ECO:0000313|Proteomes:UP000010467};
RN   [1] {ECO:0000313|Proteomes:UP000010467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19664 / LMG 22246 / CIP 109416 / KR-200
RC   {ECO:0000313|Proteomes:UP000010467};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Pukall R., Steenblock K., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "Complete sequence of chromosome of Deinococcus peraridilitoris DSM
RT   19664.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC       {ECO:0000256|RuleBase:RU000492}.
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DR   EMBL; CP003382; AFZ68108.1; -; Genomic_DNA.
DR   RefSeq; WP_015236410.1; NC_019793.1.
DR   AlphaFoldDB; L0A2L4; -.
DR   STRING; 937777.Deipe_2643; -.
DR   KEGG; dpd:Deipe_2643; -.
DR   PATRIC; fig|937777.3.peg.2652; -.
DR   eggNOG; COG0513; Bacteria.
DR   HOGENOM; CLU_003041_28_3_0; -.
DR   OrthoDB; 9805696at2; -.
DR   Proteomes; UP000010467; Chromosome.
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:InterPro.
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   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
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.
DR   PROSITE; PS51195; Q_MOTIF; 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:UP000010467}.
FT   DOMAIN          7..35
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          38..209
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          220..380
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          406..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           7..35
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
SQ   SEQUENCE   477 AA;  51477 MW;  0DAE079DE8380C7A CRC64;
     MTTTFADAFS ALDLHASLQR AVGELGYAKP TPIQALALPP ALQGRDVLGA AQTGSGKTAA
     FLLPILQRLQ GLPRGKTRAL VLAPTRELAA QIEESALALA KFTDVRVASV FGGVSMKPQE
     KAFRGGTDLI IATPGRLLDH FQHPYARLEA LEVLVLDEAD RMLDMGFLPD IRRVLRHLPA
     RRQTLFFSAT MPAPILQLSR ELLRDPVMVG AERKAAPAQG VTQSIYPVPE ELKTDLLLEL
     LRQPSMESAI VFTRTKHRAN RLAEKLIKAG VKAERIHGNR SQAARTEALA GFKSGKYRVL
     VATDIAARGI DVEALGHVVN FDVPEIPEDY IHRVGRTARA EMTGEALTFV APQEEGDLKA
     IERAVGRKLD RVTLPDFDYR ARPSERFEVP IGERIAEIRA RKSEERARAK AKAERKAAQD
     PQPGGRGPAG SGAGRAATPS RSSASGPASA AQPAREGGRT GPSRPSRGRG RGGSRSS
//
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