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XRN2_GIBZE
ID   XRN2_GIBZE              Reviewed;         980 AA.
AC   Q4HWE2; A0A0E0SQD3; V6S144;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=5'-3' exoribonuclease 2;
DE            EC=3.1.13.-;
GN   Name=RAT1; ORFNames=FGRRES_10716, FGSG_10716;
OS   Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS   / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=229533;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA   Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA   Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA   Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA   Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA   Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA   Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA   Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT   "The Fusarium graminearum genome reveals a link between localized
RT   polymorphism and pathogen specialization.";
RL   Science 317:1400-1402(2007).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA   Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA   Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA   Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA   Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA   King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA   Hammond-Kosack K.E.;
RT   "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT   graminearum.";
RL   BMC Genomics 16:544-544(2015).
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; DS231670; ESU18075.1; -; Genomic_DNA.
DR   EMBL; HG970334; CEF88646.1; -; Genomic_DNA.
DR   RefSeq; XP_011325697.1; XM_011327395.1.
DR   AlphaFoldDB; Q4HWE2; -.
DR   SMR; Q4HWE2; -.
DR   STRING; 5518.FGSG_10716P0; -.
DR   EnsemblFungi; ESU18075; ESU18075; FGSG_10716.
DR   GeneID; 23557604; -.
DR   KEGG; fgr:FGSG_10716; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G20287; -.
DR   eggNOG; KOG2044; Eukaryota.
DR   HOGENOM; CLU_006038_1_1_1; -.
DR   InParanoid; Q4HWE2; -.
DR   PHI-base; PHI:1671; -.
DR   Proteomes; UP000070720; Chromosome 3.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004534; F:5'-3' exoribonuclease activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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..980
FT                   /note="5'-3' exoribonuclease 2"
FT                   /id="PRO_0000249926"
FT   ZN_FING         269..286
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   REGION          111..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          413..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          491..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          845..980
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          121..145
FT                   /evidence="ECO:0000255"
FT   COILED          411..435
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        413..433
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        533..555
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        892..920
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   980 AA;  110362 MW;  53ECA1C9741B45E9 CRC64;
     MGIPAAFRWL STRYPKIISP VIEDQPLVME DGSTIPVDTT RPNPNGEEFD NLYLDMNGIV
     HPCSHPEDRP APKDEEEMMM EVFRYTDRVV NMVRPRKILM IAVDGVAPRA KMNQQRSRRF
     RSAQEAQEKE QDKQELIKML KQQNGGNLST ESLETVTKKA FDSNSITPGT PFMDILALSL
     RYWCQYKLNT DPGWAKLKII ISDATVPGEG EHKIMNFVRS QRASPDHDPN TRHVIYGLDA
     DLIMLGLATH EPHFRVLRED VFFQDQKARL CKICGQKGHD AQNCRGEEKK KDGEHDEKDK
     GVALKPFIWL HVAVLREYLA VELGVPNLPF RFDLERAVDD WIFMCCFVGN DFLPHLPALE
     IREHGIDTLT KIWKDNLPVM GGYVTKDGHI DLERAQVILD GLAQQEDNIF KRRKEQEDRR
     EANFKRRKLQ NEVNGRGGRQ GGPSHPKKIN GHENPENGLP LQAVGAYTGR HEQTLTHDMV
     VNRSTAPDAN VANKSAASVL KAQLQSQKSL SNPKPENPEQ ESPSALGKRK ASSIEEGNSS
     VPDAASVSTP STSAEEGPVD DVRLWEDGYA DRYYEKKFHK DPKDIEFRHG VGRAYVEGLA
     WVLLYYFQGC PSWEWYYPYH YAPFAADFKD IAKMNISFEK GRVSKPFEQL MSVLPAASRH
     ALPEVFHDLM LNPESNIIDF YPEDFEIDLN GKKFAWQGVA LLPFIEMPRL LAAVQSKYPE
     LSAADSARNE MGRDVLIFSE GHESLYDEVL TKFYSKKQGD SKFKLNPKKS DGLSGRVEKK
     EGYVPHSELK YPLERNSMPD LDYDRSVSVY YDFPQASQTH KSMLLRGVQL PTPALTQNDI
     QDMRSRANRG GRGGFGRGHD RGGYNGPGMT RGSQYNRNQG GYGRGNGHYP PAPASHVPPP
     PGAPGFGIGV PPPPPPNSYH NQPYDNRYGA SSGYNQYRGP PHPANGAPGY HGHGDASSER
     GRGSGGYSSR GRYRDNRSYR
 
 
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