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Database: UniProt
Entry: G8RJW9_MYCRN
LinkDB: G8RJW9_MYCRN
Original site: G8RJW9_MYCRN 
ID   G8RJW9_MYCRN            Unreviewed;       494 AA.
AC   G8RJW9;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   OrderedLocusNames=MycrhN_0354 {ECO:0000313|EMBL:AEV70994.1};
OS   Mycolicibacterium rhodesiae (strain NBB3) (Mycobacterium rhodesiae).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=710685 {ECO:0000313|EMBL:AEV70994.1, ECO:0000313|Proteomes:UP000005442};
RN   [1] {ECO:0000313|EMBL:AEV70994.1, ECO:0000313|Proteomes:UP000005442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBB3 {ECO:0000313|EMBL:AEV70994.1,
RC   ECO:0000313|Proteomes:UP000005442};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A.,
RA   Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT   "Complete sequence of Mycobacterium rhodesiae NBB3.";
RL   Submitted (DEC-2011) 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; CP003169; AEV70994.1; -; Genomic_DNA.
DR   RefSeq; WP_014208814.1; NC_016604.1.
DR   AlphaFoldDB; G8RJW9; -.
DR   STRING; 710685.MycrhN_0354; -.
DR   KEGG; mrh:MycrhN_0354; -.
DR   PATRIC; fig|710685.3.peg.360; -.
DR   eggNOG; COG0513; Bacteria.
DR   HOGENOM; CLU_003041_27_2_11; -.
DR   OrthoDB; 9805696at2; -.
DR   Proteomes; UP000005442; 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; PTHR47963:SF8; ATP-DEPENDENT RNA HELICASE DEAD; 1.
DR   PANTHER; PTHR47963; DEAD-BOX ATP-DEPENDENT RNA HELICASE 47, MITOCHONDRIAL; 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:UP000005442}.
FT   DOMAIN          6..34
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          37..227
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          255..401
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          411..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           6..34
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        420..438
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   494 AA;  53657 MW;  BC088C79778DD7A7 CRC64;
     MTHLNPTFAE LGVRDEIVRA LSEDGKEHPF AIQELTMPLA LAGDDLIGQA RTGMGKTLAF
     GVPLLQRITT DPEKELSGIP RALVVVPTRE LCLQVHSDLS IAAKYLTTGG APAPTSGTAD
     RKLVVTSIYG GRPYEPQIEA LQKGVDVVVG TPGRLLDLAQ QGHLQLGGLS MLVLDEADEM
     LDLGFLPDIE RILRQIPTDR QAMLFSATMP DPIITLARTF MNQPTHIRAE APHSAATHDT
     TEQFAYRAHA LDKVEMVARI LQAEGRGATM IFTRTKRTAQ KVSDELAERG FKVGAVHGDL
     GQGAREKALK SFRTGDIDVL VATDVAARGI DIDDITHVIN YQIPEDEQAY VHRIGRTGRA
     GKTGIAVTLV DWDELPRWTM IDKALGLNTP DPAETYSSSP HLYEELNIPA ETTGTFGEPR
     KAHAAKRPPA EKSADRPARN RNRNRRRTRA GEPVSAHSPA PSTDIAAPDA EASADGAPKR
     RRRRRPRTAA ASTG
//
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