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XRN2_ASPFU
ID   XRN2_ASPFU              Reviewed;        1058 AA.
AC   Q8TFZ1; Q4WS77;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=5'-3' exoribonuclease 2;
DE            EC=3.1.13.-;
GN   Name=rat1; ORFNames=AfA35g10.12, AFUA_1G13730;
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=14998527; DOI=10.1016/j.fgb.2003.12.003;
RA   Pain A., Woodward J.R., Quail M.A., Anderson M.J., Clark R., Collins M.,
RA   Fosker N., Fraser A., Harris D.E., Larke N., Murphy L.D., Humphray S.,
RA   O'Neil S., Pertea M., Price C., Rabbinowitsch E., Rajandream M.A.,
RA   Salzberg S.L., Saunders D., Seeger K., Sharp S., Warren T., Denning D.W.,
RA   Barrell B.G., Hall N.;
RT   "Insight into the genome of Aspergillus fumigatus: analysis of a 922 kb
RT   region encompassing the nitrate assimilation gene cluster.";
RL   Fungal Genet. Biol. 41:443-453(2004).
RN   [2]
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: Possesses 5'->3' exoribonuclease activity. Required for the
CC       processing of nuclear mRNA and rRNA precursors. May promote termination
CC       of transcription by RNA polymerase II (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 5'-3' exonuclease family. XRN2/RAT1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BX649607; CAD29606.2; -; Genomic_DNA.
DR   EMBL; AAHF01000004; EAL90705.1; -; Genomic_DNA.
DR   RefSeq; XP_752743.1; XM_747650.1.
DR   AlphaFoldDB; Q8TFZ1; -.
DR   SMR; Q8TFZ1; -.
DR   STRING; 746128.CADAFUBP00001301; -.
DR   EnsemblFungi; EAL90705; EAL90705; AFUA_1G13730.
DR   GeneID; 3510193; -.
DR   KEGG; afm:AFUA_1G13730; -.
DR   VEuPathDB; FungiDB:Afu1g13730; -.
DR   eggNOG; KOG2044; Eukaryota.
DR   HOGENOM; CLU_006038_1_1_1; -.
DR   InParanoid; Q8TFZ1; -.
DR   OMA; CLHYYVH; -.
DR   OrthoDB; 685597at2759; -.
DR   Proteomes; UP000002530; Chromosome 1.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004534; F:5'-3' exoribonuclease activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IBA:GO_Central.
DR   GO; GO:0034428; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 5'-3'; IEA:EnsemblFungi.
DR   GO; GO:0051984; P:positive regulation of chromosome segregation; IEA:EnsemblFungi.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0106354; P:tRNA surveillance; IEA:EnsemblFungi.
DR   InterPro; IPR027073; 5_3_exoribonuclease.
DR   InterPro; IPR004859; Put_53exo.
DR   InterPro; IPR041412; Xrn1_helical.
DR   InterPro; IPR017151; Xrn2/3/4.
DR   InterPro; IPR001878; Znf_CCHC.
DR   PANTHER; PTHR12341; PTHR12341; 1.
DR   Pfam; PF17846; XRN_M; 1.
DR   Pfam; PF03159; XRN_N; 1.
DR   PIRSF; PIRSF037239; Exonuclease_Xrn2; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Exonuclease; Hydrolase; Metal-binding; mRNA processing;
KW   Nuclease; Nucleus; Reference proteome; rRNA processing; Transcription;
KW   Transcription regulation; Transcription termination; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..1058
FT                   /note="5'-3' exoribonuclease 2"
FT                   /id="PRO_0000249918"
FT   ZN_FING         268..285
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   REGION          418..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          881..908
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          935..1058
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          407..443
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        418..447
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..490
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..557
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..575
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        946..961
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        975..1012
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1037..1058
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1058 AA;  119121 MW;  3C4B3A50C2FCB657 CRC64;
     MGVPALFRWL SNKYPKIISP VIEELPYEVN GEEIPVDITK PNPNGEEMDN LYLDMNGIVH
     PCTHPEGKPP PANEQEMMVE IFKYTDRVVN MVRPRKLLMI AVDGVAPRAK MNQQRARRFR
     SAQEAKEADE KKEEFRKMLA KQNGNKVDEE LQEEVVKKTW DSNVITPGTP FMDILAASLR
     YWIAYKLNTD PAWEKLKIII SDATVPGEGE HKIMEFIRSQ RAAPEHDPNT RHVIYGLDAD
     LIMLGLATHE PHFRVLREDV FFQESRARTC HLCGQQGHKA EECRGQAKEK NGEFDEKQKG
     SSLKPFIWLH VSILREYLAA ELYVPHQPFP FDLERALDDW VFMCFFVGND FLPHLPSLDI
     RENGIDTLIA IWRDNIPVMG GYLTEDGHVD LKRAQLILQG LAKQEDAIFR RRRQAEERKL
     ANEKRRKQEA KAREEERARK RRRSSPTYEP MDSPVGHRAP RGGGDAAPPN QLELITPSRG
     ELSRQTRELT HSMVVNRGAV YRANMANKSA AAVLKSKLMQ GSQNGQNGEE KSEGATTNND
     EPSQDQPDQT EQTSPSVLGK RKADLVEEED TDAGTPGRDS PAVPVAAKED ELPPDTVRLW
     EEGYADRYYE QKFGVDPQDK EFRHKVARAY AEGLAWVLLY YFQGCPSWTW YYPYHYAPFA
     ADFVDIGDME ITFDKGVPFK PFEQLMGVLP ASSNHAIPKV FHDLMSSPDS EIIDFYPEDF
     AVDLNGKKFA WQGVILLPFI DEKRLLAAME KKYPLLTEDE KLRNSVGREV LLISEAHPLY
     QDLVANFYSK KQGVQKYKLN MRISDGLAGK VERNEAYIPH SSLPSSLEEY GMPSLEDDRS
     LTVNYEIPKS NHVHKSMLLR GVKFNPPALD NADIQAVKHK AQNSGRSYGG APLRGGQKGG
     RINYASDRPN PFAAHLDPGF IPPVPGNVGG GPIMPSGWVP PIPGSAGFSR GPPPPPHGGM
     SGSHHRPPYG QGPGQYQGNH GQGDHYGQGQ QGYYNQSSYY NQSNQYNGRS SDHGGSGGYR
     GGGGYHRGGN YRGGGYRDQR QYNQDQYSSR NSGGYGRY
 
 
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