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Database: UniProt
Entry: A0A0L6VRC9_9BASI
LinkDB: A0A0L6VRC9_9BASI
Original site: A0A0L6VRC9_9BASI 
ID   A0A0L6VRC9_9BASI        Unreviewed;       844 AA.
AC   A0A0L6VRC9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE            EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN   ORFNames=VP01_1227g2 {ECO:0000313|EMBL:KNZ62745.1};
OS   Puccinia sorghi.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ62745.1, ECO:0000313|Proteomes:UP000037035};
RN   [1] {ECO:0000313|EMBL:KNZ62745.1, ECO:0000313|Proteomes:UP000037035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ62745.1,
RC   ECO:0000313|Proteomes:UP000037035};
RA   Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA   Sacco F.;
RT   "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT   Schw, the Causal Agent of Maize Common Rust.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATP-dependent RNA helicase required for ribosome biogenesis.
CC       Involved in the release of U14 snoRNA in pre-ribosomal complexes.
CC       Required for pre-rRNA cleavage at site A2.
CC       {ECO:0000256|ARBA:ARBA00037374}.
CC   -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC         Evidence={ECO:0000256|RuleBase:RU365068};
CC   -!- SUBUNIT: Interacts with the U3 and U14 snoRNAs. Associates with pre-
CC       ribosomal complexes. {ECO:0000256|ARBA:ARBA00038587}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000256|ARBA:ARBA00004604}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC       family of RNA helicases and controls ATP binding and hydrolysis.
CC       {ECO:0000256|RuleBase:RU365068}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX10/DBP4
CC       subfamily. {ECO:0000256|ARBA:ARBA00038084}.
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:KNZ62745.1}.
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DR   EMBL; LAVV01002532; KNZ62745.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6VRC9; -.
DR   STRING; 27349.A0A0L6VRC9; -.
DR   VEuPathDB; FungiDB:VP01_1227g2; -.
DR   OrthoDB; 149428at2759; -.
DR   Proteomes; UP000037035; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd17941; DEADc_DDX10; 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; IPR025313; DUF4217.
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; PTHR24031:SF54; ATP-DEPENDENT RNA HELICASE DDX10-RELATED; 1.
DR   PANTHER; PTHR24031; RNA HELICASE; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF13959; DUF4217; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01178; DUF4217; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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:RU365068};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU365068};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365068};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU365068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037035};
KW   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552}.
FT   DOMAIN          45..73
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          76..250
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          280..439
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          488..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          528..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          723..827
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           45..73
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        1..18
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..557
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..572
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        723..742
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        790..813
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   844 AA;  93772 MW;  7F2E48E6137A6B70 CRC64;
     MKTSKHKKNT QKHTKHRKLK RQTEEEELKK LASDSLAFDL TKPPTLFTDL PISRATLKGL
     QAAKFEKLTP IQALAIPRAL KGRDVLGAAR TGSGKTLAFL IPVLEMLYRQ KWGAMDGLGA
     LIISPTRELA VQIFEVLKSI GKFHAFSAGL VIGGKSLEDE RDRLGRMNIL VSTPGRLQQH
     LEQTTNFDSD NLQLLVLDEA DRILDMGFAN SINAIISGLP TSRQSLLFSA TQTKSVKDLA
     RLSLTGDPEY VSARETGVDR DLTTPKELLQ SYMVTPLECK IDYLWGFVKT HLKTKMIVFL
     SSCKQVRFVH EVFRHLRPGI PLLHLHGKQK QIKRLEIYER FSSSPQVCLF ATDIAARGLD
     FPFVDWVVQV DCPEDVDTYI HRVGRTARYQ SGGKALLLLL PSEEEGMLKK WESRGIVVTK
     VKPNESKKQS IQTPIQAQMF KFPELKFLGQ RAFISYVRSI HLQKNKEIFK LKELDLVKFA
     ESLGLPGAPQ VRFSGSGAGG ASGGTGESAK AKKNAPRDLE TLKKLTLAQN SAGAQTASQG
     DGKTNEKESG SNPASSDDDS DSNDESSEDG SSDAEEERQA AILHPSAPQP TSEKPTVRTK
     YERMFQRQNQ DILSQHYAKL VDRSADGAVD GEKDDGADDF LQLKRADHDL DASEAAIPDS
     AYLSKRKLKM ATSKKAIATS GIGLGKKVIF DEEGEAHEAY KILEEEEYKQ THDMQTEIHE
     FVTREKEKVQ QADQTDKLVA KNKRTEKKRK RKLASEGVLN DVQGGRVAEL VSNDEDDGYV
     SPEFDLPSES ESDPDGHPPP SKKKHRPDLL PTCDGAGDDE GEEEEQDLEA LALQKLTQRI
     NPPR
//
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