XRN2_ASPOR
ID XRN2_ASPOR Reviewed; 1035 AA.
AC Q2UCP5;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=5'-3' exoribonuclease 2;
DE EC=3.1.13.-;
GN Name=rat1; ORFNames=AO090012000503;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(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; AP007161; BAE60670.1; -; Genomic_DNA.
DR RefSeq; XP_001727509.1; XM_001727457.2.
DR AlphaFoldDB; Q2UCP5; -.
DR SMR; Q2UCP5; -.
DR STRING; 510516.Q2UCP5; -.
DR EnsemblFungi; BAE60670; BAE60670; AO090012000503.
DR GeneID; 5987983; -.
DR KEGG; aor:AO090012000503; -.
DR VEuPathDB; FungiDB:AO090012000503; -.
DR HOGENOM; CLU_006038_1_1_1; -.
DR OMA; CLHYYVH; -.
DR Proteomes; UP000006564; Chromosome 4.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004534; F:5'-3' exoribonuclease activity; IEA:EnsemblFungi.
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: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..1035
FT /note="5'-3' exoribonuclease 2"
FT /id="PRO_0000249919"
FT ZN_FING 266..283
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 417..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 406..434
FT /evidence="ECO:0000255"
FT COMPBIAS 417..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1035 AA; 116864 MW; 16A3A71CA2E5933B CRC64;
MGVPALFRWL SNKYPKIISP VIEEQPYEVN GEQIPVDTTR PNPNGEELDN LYLDMNGIVH
PCTHPEGKPP PANEQEMMLE IFNYTDRVVN MVRPRKLLMI AVDGVAPRAK MNQQRARRFR
SAQEAKEADE KKEEFRKQFL KKSKGDQEIH EEVIQKTWDS NVITPGTPFM DILAASLRYW
IAYKLNTDPA WEKLKIIISD ATVPGEGEHK IMEFVRSQRA APEHDPNTRH VIYGLDADLI
MLGLATHEPH FRVLREDVFF QESKARTCHL CGQAGHKAEE CRGQAKEKNG QFDEKGKGTS
LKPFIWLNVS ILREYLAVEL YVPHQPFPFD LERALDDWVF MCFFVGNDFL PHLPSLDIRE
NGIDTLIAIW RDNIPVMGGY LTKDGHVEFK KAQLILQGLA KQEDAIFRRR RQVEEKKLAN
EKRRKEEAQA RDRARKRRRS SPNYEPSEPP ASNRARGGGG DSAPPNDVEL IIPGRGELSR
ENRELTHSMV VNRGAVYRAN MANKSAAAIL KSKLMKGSQE GDDTAESTPM PDADGASDSK
IEPTSPSVLG KRKAEEPEGE TDTPADNTDS TPKPSKDDEM PPDTVRLWEE GYADRYYEQK
FGVDPQDKEF RHKVARAYAE GLAWVLLYYF QGCPSWNWYY PYHYAPFAAD FVDIGDMELS
FEKGTPFKPF EQLMGVLPAS SNHAIPEVFH DLMQDPESEI IDFYPEDFAV DLNGKKFAWQ
GVILLPFIDE KRLLAAMEKK YPLLSDDERH RNTVGREVLL LSDGHPLYQD LVANFYSKKQ
GAPKYTLNMR VSEGLAGRVE RNETYIPHSS LVSSLEEYGM PTLEDDRSLT VNYEIPKSNH
IHKSMLLRGV KFPPPALDNA DIQATRSKAQ HSGRSFGGAP FRGGHGNRGG RINYASDRPN
PFAAHLDPNF MPPSNAGAQG MPSGWAPPVP GSANFSRGPP PPPRGNHRNH YGSGHAQQQG
YQQTNYGRND YYGRGQQGHQ HQGSYGNQSG QYSGRQSGYG GAEYRGGGYQ RGGYQGQGQG
RDYYNSRNQG GYGRY
