ID A0A180G9M1_PUCT1 Unreviewed; 845 AA.
AC A0A180G9M1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=PTTG_01980 {ECO:0000313|EMBL:OAV88603.1};
OS Puccinia triticina (isolate 1-1 / race 1 (BBBD)) (Brown leaf rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=630390 {ECO:0000313|EMBL:OAV88603.1};
RN [1] {ECO:0000313|EMBL:OAV88603.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV88603.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAV88603.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV88603.1};
RA Cuomo C.A., Bakkeren G., Szabo L., Khalil H., Joly D., Goldberg J.,
RA Young S., Zeng Q., Fellers J.;
RT "Comparative analysis highlights variable genome content of wheat rusts and
RT divergence of the mating loci.";
RL Submitted (MAY-2016) 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:OAV88603.1}.
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DR EMBL; ADAS02000165; OAV88603.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A180G9M1; -.
DR VEuPathDB; FungiDB:PTTG_01980; -.
DR OrthoDB; 149428at2759; -.
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 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 267..439
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..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..17
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 845 AA; 94209 MW; CEC46EBBA5266743 CRC64;
MKASNQKKKN KHHAKPRQLK RQTEEEEIKK LASESLSFDL AKPPTLFTDL PISRATLKGL
QAAKFEKLTP IQALAIPRAL KGRDVLGAAR TGSGKTLAFL IPVLEMLYRQ KWGAMDGLGA
LIISPTRELA VQIFEVLRSI GKFHAFSAGL VIGGKNLEDE RERLGRMNIL VSTPGRLQQH
LEQTTNFDSD NLQVLVLDEA DRILDMGFAN SVNAIISSLP NSRQSLLFSA TQTKSVKDLA
RLSLTGDPEY VSARETGVER DLTTPKELVQ SYMVTPLECK IDYLWGFVRT HLKTKMIVFL
SSCKQVRFVH EIFRHLRPGI PLLHLHGKQK QIKRLEIYER FSSSPQVCLF ATDIAARGLD
FPSVDWVVQV DCPEDVDTYI HRVGRTARYQ SGGKALLLLL PSEEEGMLKK WETRGIVVSK
VKPNESKKQS IQTQIQAQMF KFPELKFLGQ RAFISYVRSI HLQKNKDIFK LKEMDLVKFA
ESMGLPGAPQ VRFSGSGAGG AAGGTGESAK AKKNAPRDLE TLKKLTLNQN IASAQTVNKD
GRDENEAASG SDSASSDSGS NSDSDEEGDD DESSDGEEKT HSDTAVAHPS ATNSEAAKPA
VRTKYDRMFQ RQNQDILSQH YAKLVDRTAD GMEDQEKGDE EDDFIQLKRA DHDLDAAEAA
IPDSAYLSKR KLKLATSKKA VAMSGIGLGK KVIFDDEGEA HQAYEILQEE EYKKNHNVES
EIKDFVVREK EKVKQADQTD KLVAKNKRAE KKRKRKLNPE GNQNEAIHGA RVAELVSNDE
DDGYISPEFD LPSESESGSD GDGDPHRHRP KKFKALGRRE SLDEEEDDLE ALALQKLQQR
IKPTL
//
