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MRD1_ASPFU
ID   MRD1_ASPFU              Reviewed;         825 AA.
AC   Q4WJT7;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Multiple RNA-binding domain-containing protein 1;
GN   Name=mrd1; ORFNames=AFUA_1G04840;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- FUNCTION: Involved in pre-rRNA processing. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RRM MRD1 family. {ECO:0000305}.
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DR   EMBL; AAHF01000007; EAL88195.1; -; Genomic_DNA.
DR   RefSeq; XP_750233.1; XM_745140.1.
DR   AlphaFoldDB; Q4WJT7; -.
DR   SMR; Q4WJT7; -.
DR   STRING; 746128.CADAFUBP00000512; -.
DR   PRIDE; Q4WJT7; -.
DR   EnsemblFungi; EAL88195; EAL88195; AFUA_1G04840.
DR   GeneID; 3507335; -.
DR   KEGG; afm:AFUA_1G04840; -.
DR   VEuPathDB; FungiDB:Afu1g04840; -.
DR   eggNOG; KOG0110; Eukaryota.
DR   HOGENOM; CLU_008479_0_0_1; -.
DR   InParanoid; Q4WJT7; -.
DR   OMA; TALIEYC; -.
DR   OrthoDB; 1428854at2759; -.
DR   Proteomes; UP000002530; Chromosome 1.
DR   GO; GO:0030686; C:90S preribosome; IEA:EnsemblFungi.
DR   GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0032040; C:small-subunit processome; IEA:EnsemblFungi.
DR   GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0042134; F:rRNA primary transcript binding; IEA:EnsemblFungi.
DR   GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR   GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR   GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR   GO; GO:0034462; P:small-subunit processome assembly; IEA:EnsemblFungi.
DR   CDD; cd12568; RRM3_MRD1; 1.
DR   Gene3D; 3.30.70.330; -; 5.
DR   InterPro; IPR034482; Mrd1_RRM3.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR003954; RRM_dom_euk.
DR   Pfam; PF00076; RRM_1; 5.
DR   SMART; SM00360; RRM; 5.
DR   SMART; SM00361; RRM_1; 1.
DR   SUPFAM; SSF54928; SSF54928; 3.
DR   PROSITE; PS50102; RRM; 5.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW   rRNA processing.
FT   CHAIN           1..825
FT                   /note="Multiple RNA-binding domain-containing protein 1"
FT                   /id="PRO_0000081637"
FT   DOMAIN          4..76
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          301..379
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          484..556
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          597..680
FT                   /note="RRM 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          702..779
FT                   /note="RRM 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          80..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..208
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..257
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   825 AA;  92395 MW;  D7E75A56557141B9 CRC64;
     MENTRVFVSG LPPTFTNDQL RMHFSSRFQI TDAHVLPKRR IGFVGFKSSE AAQQAASYFN
     KTYVKMSKIS VEIAKPIDSE PVKKAEKHRK GSTSNDSTAG KALKRKRDGD NTQKDPQLQE
     YLSVIERPSK TKTWANGDDF LNTIQNQPAT SELREEQRDD TSEKVEEHSH KQRKKPRVDD
     VPKAAHDREP EPMVLDKTEE EHERANADGQ VEAIPPTQEE AEPVSDADWL RSKTSRLLGL
     LDEDEQAEFD STAQRKPDPS SEPETVSKAG AQHSDDDKAA VESSVEEEEV DTNIEHIRLS
     SRLFVRNLPY DASESDLEPV FSKFGKIEEI HVAFDTRSTT SKGFAYVQYI EPDAAVQAYK
     ELDGKHFQGR LMHILPATAK KTYKIDEHEL SKLPLKKQKQ IKRKLEASSS TFSWNSLYMN
     TDAVMSSVAE RLGVSKADLL DPTSADAAVK QAHAETHVIQ ETKAYFTANG VNLDAFKQRE
     RGNTAILVKN FSYGVKVDDL RKLFEPYGQI TRLLMPPSGT IAIVEFARPD EAQKAFKGLA
     YRKVGDSILF LEKAPANLFD ATTAPQTSVL ETKAVSQGFS TADTFAAEDG DEPVVTSTLF
     VKNLNFSTTN ERFTEVFKPL DGFVSARIKT KPDPKRPGKT LSMGFGFVDF RTKAQAQAAL
     AAMDGYKLDQ HELVVRASNK AMDAAEERRR EDTAKKIAAR RTKIIIKNLP FQATKKDVRS
     LFGAYGQLRS VRVPKKFDRS ARGFGFADFV SAREAENAMD ALKNTHLLGR RLVLEFANEE
     AVDPEQEIEQ IEKKVGEQLD RVKLQKLTGT GRKKFTVGAQ EDEEA
 
 
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