XRN2_EMENI
ID XRN2_EMENI Reviewed; 1032 AA.
AC Q5BFH3; C8VRD3;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=5'-3' exoribonuclease 2;
DE EC=3.1.13.-;
GN Name=rat1; ORFNames=AN0707;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000010; EAA65483.1; -; Genomic_DNA.
DR EMBL; BN001308; CBF88946.1; -; Genomic_DNA.
DR RefSeq; XP_658311.1; XM_653219.1.
DR AlphaFoldDB; Q5BFH3; -.
DR SMR; Q5BFH3; -.
DR STRING; 162425.CADANIAP00001962; -.
DR PRIDE; Q5BFH3; -.
DR EnsemblFungi; CBF88946; CBF88946; ANIA_00707.
DR EnsemblFungi; EAA65483; EAA65483; AN0707.2.
DR GeneID; 2876473; -.
DR KEGG; ani:AN0707.2; -.
DR eggNOG; KOG2044; Eukaryota.
DR HOGENOM; CLU_006038_1_1_1; -.
DR InParanoid; Q5BFH3; -.
DR OMA; CLHYYVH; -.
DR OrthoDB; 685597at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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 SMART; SM00343; ZnF_C2HC; 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..1032
FT /note="5'-3' exoribonuclease 2"
FT /id="PRO_0000249925"
FT ZN_FING 267..284
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 416..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 120..152
FT /evidence="ECO:0000255"
FT COILED 406..442
FT /evidence="ECO:0000255"
FT COMPBIAS 416..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1032 AA; 115795 MW; 7E5F419573EE6E6D CRC64;
MGVPALFRWL SKKYPKIISS VIEELPQEVN GEEIPVDITG PNPNGEEMDN LYLDMNGIVH
PCTHPEGKPP PANEQEMMIE IFKYTDRVVN MVRPRKLLMI AVDGVAPRAK MNQQRARRFR
SAQEAREQDE KKQEFQRMLA KQNGDKEQML QEEVIQKTWD SNVITPGTPF MDILAASLRY
WIAYKLNTDP AWEKLKIIIS DATVPGEGEH KIMEFIRSQR ASPEHDPNAR HVIYGLDADL
IMLGLATHEP HFRVLREDVF FQESKQRTCH LCGQPGHKAE ECRGQAKEKN GEFDEKGKGA
TLKPFIWLHV SILREYLAAE LYVPHQPFPF DLERALDDWV FMCFFVGNDF LPHLPSLDIR
EDGIDTLIAI WRDNIPLMGG YLTQDGRVDL KKAQLILQGL AKQEDAIFRR RRQAEERKLA
NEKRRKQEEK ARNEERARKR RRSSPSYDAI ESPTHAKPRS AGAAAAPPAG LELITPARGE
LARQTRELTH SMVVNRGNVY RANMANKSAA AVLKSKLLGG QDGQPSDDGE STAESDAQLD
AAGPVLGKRK ADEAEVGQLG TETPDKPEPA KADELPPDTV RLWEEGYADR YYEQKFGVDP
QDKEFRHKVA RAYAEGLAWV LLYYFQGCPS WTWYYPYHYA PFAADFVDIG DMELSFEKGT
PFKPYEQLMG VLPASSNHAI PKVFHSLMTE PDSEIIDFYP EDFPVDLNGK KFAWQGVVLL
PFIDEKRLLA AMSKKYPLLT EDEKARNTVG RDVLLLSESH PLYQDLVSNF YSKKQGAPKY
KLNMRVSDGL AGKVEKNEAY IPHSSLVSSL EEYGMPSLED DRSIMVNYEI PKSTNIHKSM
LLRGVKFGPP ALDNADIQAT KSRAQHSGRS YGGAPFRGGR GGRMNYAGDR QSHGNDRPNP
FAAHLDPKFM PGANPGAPMG MPSGWVPPSG NFSRGPPPPP RGGTSYGYGS QQYGSYGGYG
QQQSYQQSSH SQSDYYGRGP PAPYNNGPAD YYSGRPSGYG PQESRGGGYN RGGYRGGRDT
YSSSGHGGYG RY
