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Database: UniProt
Entry: A0A180GQV5_PUCT1
LinkDB: A0A180GQV5_PUCT1
Original site: A0A180GQV5_PUCT1 
ID   A0A180GQV5_PUCT1        Unreviewed;      1205 AA.
AC   A0A180GQV5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=PTTG_03386 {ECO:0000313|EMBL:OAV94343.1};
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:OAV94343.1};
RN   [1] {ECO:0000313|EMBL:OAV94343.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV94343.1};
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:OAV94343.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV94343.1};
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   -!- 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|ARBA:ARBA00001556};
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:OAV94343.1}.
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DR   EMBL; ADAS02000040; OAV94343.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A180GQV5; -.
DR   STRING; 630390.A0A180GQV5; -.
DR   VEuPathDB; FungiDB:PTTG_03386; -.
DR   OrthoDB; 3682876at2759; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
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:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   CDD; cd21691; GH2-like_DHX8; 1.
DR   CDD; cd05684; S1_DHX8_helicase; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR049588; DHX8_GH2-like.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR048333; HA2_WH.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR049621; S1_DHX8_helicase.
DR   InterPro; IPR003029; S1_domain.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF85; ATP-DEPENDENT RNA HELICASE DHX8; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF04408; HA2_N; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50126; S1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          241..311
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          551..714
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          739..912
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          83..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          160..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          462..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..225
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..476
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1205 AA;  135087 MW;  56CC9F6CE6F64E69 CRC64;
     MDQEFEKLEI LSLVNSITKE LHNHVGLQDS TLAEYLISLH EESTSFENFK LKLQEIGAEF
     PESFITNMDR LVTSLHPKYK KKKLPAEGKG KEKDIDPAED EEELERKKRR AQALFPALAL
     PDRSWEPSFV PDPKDATAKN TSTADQLLEE LEHVGRRHRE LQAVREEEQE DDASSDYNRP
     TKMPRRDRSA SRERGRRSPE PRSGRFRDDY SGGRFDDRGR QRDNGYGNRA SKAPDTRPVL
     YKIYDGTVAS IKDFGCFVTL KGVAGKAEGL VHVNAIAAGR VNHPSDLVSR GQPVKVKVVS
     IAGERIGISM KDVDQNTGAD LTPHLRIKSD AEMAEEEAQY AARHVNHSVG AGFADDNRSS
     SARRLTSPER WEIKQLIASG AASAADYPNL DDDLTTPGST NGMAAAATAE EELDIEMRED
     EAPFLKGAHR RVLDLSPVKI VKAPDGTLNR AALAGAGLAK ERRELRQQEA NERADAETQD
     TSTAWLDPVA KPHERLFAQD ARDNTMGKKQ EESGWKQATF NQATTYGKIT SLSITEQRAS
     LPIYKLRDAL VKAVKENQIL VVVGDTGSGK TTQMTQYLAE EGLADEKKIA CTQPRRVAAM
     SVAKRVAEEV GCRLGQDVGY TIRFEDCTSS ETKIKYMTDG MLQREALVDP NLSAYSVIML
     DEAHERTIAT DVLFGLLKKS IMRRPDLKLI VTSATLDAEK FSKYFYSCPI FTIPGRTYPV
     EVLYTKEPES DYLDAALITI MQIHISEPPG DILLFLTGQE EIDTSAEILY ERMKALGSHV
     PELIVLPVYS ALPSEMQSKI FDPAPPGARK VILATNIAET SITIDGIYYV VDPGFVKQKA
     WDPRLGMDSL VVTPISQAQA RQRSGRAGRT GPGKCYRLYT EAAYRNEMLP TSIPDIQRQN
     LAHTILMLKA MGINDLLNFD FMDPPPQQTM ITALENLYAL SALDDEGLLT RLGRKMADFP
     MDPELSKMLI ASVDLGCSEE VLTIVAMISG ATNVFYRPKE KQAQADAKKA KFHQPEGDHL
     TLLAVYDGWK NNKFSNPWCH ENYIQSRAMR RAQDVRKQLL GIMDRYKHDI VSCGTNYDRV
     RRAICSGYFR HAAKKDPQEG YKTLVEGTPV FIHPSSALFN RAPEWIIYHE LVLTTKEYCR
     DVTAIEPKWL TEVAPTFFKV ADAKTMSKRK RNERVQPLFD RFAKSENEWR ISKVKRSTRT
     SQTFG
//
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