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Database: UniProt
Entry: K0JVL9_SACES
LinkDB: K0JVL9_SACES
Original site: K0JVL9_SACES 
ID   K0JVL9_SACES            Unreviewed;       874 AA.
AC   K0JVL9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   OrderedLocusNames=BN6_09180 {ECO:0000313|EMBL:CCH28248.1};
OS   Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC
OS   15066 / NRRL 15764).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH28248.1, ECO:0000313|Proteomes:UP000006281};
RN   [1] {ECO:0000313|EMBL:CCH28248.1, ECO:0000313|Proteomes:UP000006281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764
RC   {ECO:0000313|Proteomes:UP000006281};
RX   PubMed=22958348; DOI=10.1186/1471-2164-13-465;
RA   Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J.,
RA   Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.;
RT   "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and
RT   comparison to the other completely sequenced Pseudonocardiaceae.";
RL   BMC Genomics 13:465-465(2012).
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DR   EMBL; HE804045; CCH28248.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0JVL9; -.
DR   STRING; 1179773.BN6_09180; -.
DR   KEGG; sesp:BN6_09180; -.
DR   PATRIC; fig|1179773.3.peg.923; -.
DR   eggNOG; COG0513; Bacteria.
DR   eggNOG; COG3064; Bacteria.
DR   HOGENOM; CLU_003041_27_0_11; -.
DR   Proteomes; UP000006281; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:CCH28248.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006281}.
FT   DOMAIN          98..126
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          129..300
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          328..474
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          496..874
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           98..126
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        572..586
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        708..722
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"
FT   COMPBIAS        808..863
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   874 AA;  92314 MW;  C1CA41ECF56899EF CRC64;
     MPRADYGGTV PPGEGARIPR RPSRATRPAA SRGREAVGAV EWPVQAVRAG TREAIILTAT
     NEQTQLDPVA LEHSELGVPD VDTSHPLVAN APVRTDSPTF AELGVHAEIV RALAEAGIER
     AFAIQELTLP LALAGDDVIG QARTGTGKTL GFGIPLLQRI TVPGDGTPQA LVVVPTRELC
     LQVTHDLTDA AKHLGVRVMA IYGGRPYEPQ INALRKGVDL VVGTPGRLLD LAEQRHLVLG
     KVRGLVLDEA DEMLDLGFLP DIERILRMVP DERQTMLFSA TMPGPIITLA RTFLNQPTHV
     RAEENDAGAI HERTEQFVYR AHALDKTELL ARALQARDRG LCMIFTRTKR TAQKVADEMV
     ERGFAAAAVH GDLGQGAREQ ALRAFRSGKI DVLVATDVAA RGIDVEGVTH VINYQCPEDE
     KTYVHRIGRT GRAGRTGVAV TLVDWDEMPR WKSISDALNL GKPEPVETYS TSDHLFAELH
     IPAGSTGRLP LGLRTRAGLD AEPEENLKGE RKPRKRGRKR GAPGSPGSPT TSGEPAATED
     GTENGGGRTR RRRRSRGGVP AEGVTAEGGS PNGQAEGGSP NGEAGSTEHT RSRRRRRRGS
     SAGEAAAVAD GSAPEAVAVN GTAVEHAPVE AATPAEAVAI PDAPKAEAPA DAAPTRSRRR
     SRAGASTDAP ADAAPQAPAA DAVAAPVAEP VAAPVAEAPA EAPAEAVTPR RTRTRKKAEP
     APAEAVTEPA AEPVAEPVAE PVAEPVAEAA PKRTRTRKKA VEAPAEATPA DAEPAVETAV
     EPAAPKRART RKAAAPAEVA ETSDQPAEAA PKRTRTRKTA EATAEAQPEE ADTRSRTRRK
     AEPADAEETE RPRTRRRATR TETEGSADAP PSAD
//
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