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DRS1_USTMA
ID   DRS1_USTMA              Reviewed;         932 AA.
AC   Q4P9P3; A0A0D1DWP5;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=ATP-dependent RNA helicase DRS1;
DE            EC=3.6.4.13;
GN   Name=DRS1; ORFNames=UMAG_03170;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATP-binding RNA helicase involved in ribosome assembly.
CC       {ECO:0000250}.
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   -!- SUBUNIT: Associates with pre-ribosomal particles. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX27/DRS1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CM003147; KIS68599.1; -; Genomic_DNA.
DR   RefSeq; XP_011389627.1; XM_011391325.1.
DR   AlphaFoldDB; Q4P9P3; -.
DR   SMR; Q4P9P3; -.
DR   STRING; 5270.UM03170P0; -.
DR   EnsemblFungi; KIS68599; KIS68599; UMAG_03170.
DR   GeneID; 23563715; -.
DR   KEGG; uma:UMAG_03170; -.
DR   VEuPathDB; FungiDB:UMAG_03170; -.
DR   eggNOG; KOG0338; Eukaryota.
DR   HOGENOM; CLU_003041_3_2_1; -.
DR   InParanoid; Q4P9P3; -.
DR   OMA; TNINEHA; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000000561; Chromosome 8.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IEA:EnsemblFungi.
DR   GO; GO:0006364; P:rRNA processing; IEA:EnsemblFungi.
DR   Gene3D; 3.40.50.300; -; 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   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Ribosome biogenesis; RNA-binding.
FT   CHAIN           1..932
FT                   /note="ATP-dependent RNA helicase DRS1"
FT                   /id="PRO_0000232248"
FT   DOMAIN          364..543
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          601..748
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          183..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          812..932
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           333..361
FT                   /note="Q motif"
FT   MOTIF           490..493
FT                   /note="DEAD box"
FT   COMPBIAS        16..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..223
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..297
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..334
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        845..860
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        900..923
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         377..384
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   932 AA;  102119 MW;  D6210D9C2D5DCD98 CRC64;
     MRVQQSKPSA AAKRKAAATS LTTSPQKKRA NTTPKRAKDD DFIMTLDSDD DVEDLDAAHV
     DADHVASDNS EREPEPEAEL EPEHSSTPPD GKLTKNQRKR KEKAHLVGKE KIIESLASRS
     KTNSAAAVKD AMALDKDFEF DIFGDGSAVD YTGAEANGWD MSVTGTRMHK KLNVDDIIEK
     RRKVLPTLPA PVEEEEENSD EDDQDDDLDD DIKYAEYQDS DDDEDRFGGG NGNIVGQNKD
     EDQQDAAELD SQEDPLSSDA ESASDDDDDN DNDDDDDELQ VAEQDEESNS SEDDSDLETE
     QEKARKAAFF AEDPIATSAD SSSKSKSTND AESSFGAFDL SRPVLRALSS LSFHKPTPIQ
     SRTIPIALAG KDIVAGAVTG SGKTAAFMIP TIERLTWRAK TRTPHEAKSR VLILAPTREL
     AIQCYSVGKS IAKFTDIRFC LCVGGLSVKS QEAELKLRPE VVIATPGRLI DHVRNSASFT
     LDDIEILVMD EADRMLEDGF ADELNEIVKS CPKGARQTML FSATMTDDVE QLVRLSLKRP
     VRLFVDPKRT TAKKLIQEFV RVRGTGTGGV AGADGLSGIQ DQPATWISGG RKSEDAQRPA
     LLLSLCTRTF TSQTMIFVRS KKLAHQLKIV FGLLGLSAGE LHGDLSQEQR IDALTDFRDG
     KTDFLLATDL ASRGLDIKGV QTVINYDMPG QFEAYLHRVG RTARAGRNGR AVTLVGEADR
     RMLKLAIKKS SAEQIKHRII PSAVAAHMCE TLERLKPEVD AVLREEKEEK ALRIAEMELK
     KGENMANHAD EIFSRPKRTW FQSGSEKTQA SALSKAGYQA TMDARSSSKQ KDKYAGLSRK
     KRRSKMMRQE IERERKDASG SAGAKTASGG GMDAGIRAAK KAQRPTKLGV APLKLANKSK
     GKQSGRNARP SATGGSKTKS SFNRDFSGNK RR
 
 
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