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Database: UniProt
Entry: Q0RLS5_FRAAA
LinkDB: Q0RLS5_FRAAA
Original site: Q0RLS5_FRAAA 
ID   Q0RLS5_FRAAA            Unreviewed;      1011 AA.
AC   Q0RLS5;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   SubName: Full=Putative ATP-dependent RNA helicase {ECO:0000313|EMBL:CAJ61529.1};
GN   OrderedLocusNames=FRAAL2885 {ECO:0000313|EMBL:CAJ61529.1};
OS   Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ61529.1, ECO:0000313|Proteomes:UP000000657};
RN   [1] {ECO:0000313|EMBL:CAJ61529.1, ECO:0000313|Proteomes:UP000000657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACN14a {ECO:0000313|Proteomes:UP000000657};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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DR   EMBL; CT573213; CAJ61529.1; -; Genomic_DNA.
DR   RefSeq; WP_011604031.1; NC_008278.1.
DR   AlphaFoldDB; Q0RLS5; -.
DR   STRING; 326424.FRAAL2885; -.
DR   KEGG; fal:FRAAL2885; -.
DR   eggNOG; COG4581; Bacteria.
DR   HOGENOM; CLU_002902_4_1_11; -.
DR   OrthoDB; 3229913at2; -.
DR   Proteomes; UP000000657; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 1.10.3380.30; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
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; IPR012961; Ski2/MTR4_C.
DR   PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR   PANTHER; PTHR12131:SF8; HELICASE SKI2W; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF08148; DSHCT; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01142; DSHCT; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:CAJ61529.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000657}.
FT   DOMAIN          27..188
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          376..573
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          239..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          725..764
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..294
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        750..764
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1011 AA;  108072 MW;  EE2C842C751B0ACE CRC64;
     MSSTPEALVE FAASLPFGFD PFQLEALSAL AAGEGVLVAA PTGAGKTVVG EFAAHLALST
     GTRCFYTTPI KALSNQKYTD LVARYGADRV GLLTGDTSRN GSAPVVVMTT EVLRNMLYAG
     PVGGGGLDTL AYVVMDEVHY LADRQRGAVW EEVIIHLPAH VRLVSLSATV SNAEEFGEWL
     VTVRGHTRVI VSDHRPVPLW QHVLADRTLH DLFLEDGSGA PAPSAGAAVA RAVSGEELAR
     PGWGAPPTSG SARAVPPATG SARTVPPGAG GRSGDRGRGG ERARRRDGRG RADDAARTST
     PAVPAARAGG NGAARGDGAA RGATAKVGGR VVNPDLVRLA REENRAMPGG YGRGRGGPGA
     PRRRMWVPGR PEVVERLDRD GLLPAIVFVF SRAGCDDAVT SCVRAGLRLV GPAEQQRIRT
     IVRERTTGIP DADLGVLGYW AWLEGLERGI ASHHAGMLPT FKEIVEELFV QGLARVVFAT
     ETLALGINMP ARTVVLERLT KFNGESRVDI TPGEYTQLTG RAGRRGIDVE GHAVVLWQPG
     LDPLALAGLA STRTYPLRSS FRPSYNMAVN LVGRLGADRA RTVLESSFAQ FQADRDVVGL
     ARVVARNTEA IDEMRAQLSC DRGDAAEYDR IRRDIREREA ALSREGTARR RAESAAALGR
     LRTGDIVRVP AGRRSGLAVV LDADAGAVGA EGPRPVVLTA DKQVRRLSLV DFPVAVEPLG
     RVRVPRSFNP RSPQSRRDLA SSLRAADVDP DGPPGRRAKA RSAAADDAEL ARLRRALRAH
     PVHDCPRREE HLRSAEQVNR LAKETAAISR KVEGRTNTVA KTFDRVRAAL AELGYLDGDT
     VTDAGRVLAR IYSDQDLLVA ECLRAGIWED LTAPALAAAV SSLVFEPRGD DVGVPALPGG
     AALRDCLDEM SRLAFRLAAT EQGHRLSFLR PPELGFVPAA HDWAVGRPLE RVLTDSGLEL
     TAGDFVRWMR QLLDLLDQIA KVAPDDSRVR RTARSAMDAL RRGVVAYASS V
//
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