XRN2_DEBHA
ID XRN2_DEBHA Reviewed; 1003 AA.
AC Q6BNU7;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 4.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=5'-3' exoribonuclease 2;
DE EC=3.1.13.-;
GN Name=RAT1; OrderedLocusNames=DEHA2E18898g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382137; CAG88393.2; -; Genomic_DNA.
DR RefSeq; XP_460123.2; XM_460123.1.
DR AlphaFoldDB; Q6BNU7; -.
DR SMR; Q6BNU7; -.
DR STRING; 4959.XP_460123.2; -.
DR PRIDE; Q6BNU7; -.
DR EnsemblFungi; CAG88393; CAG88393; DEHA2E18898g.
DR GeneID; 2902801; -.
DR KEGG; dha:DEHA2E18898g; -.
DR VEuPathDB; FungiDB:DEHA2E18898g; -.
DR eggNOG; KOG2044; Eukaryota.
DR HOGENOM; CLU_006038_1_1_1; -.
DR InParanoid; Q6BNU7; -.
DR OMA; ETWEYIV; -.
DR OrthoDB; 685597at2759; -.
DR Proteomes; UP000000599; Chromosome E.
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: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 PANTHER; PTHR12341; PTHR12341; 1.
DR Pfam; PF17846; XRN_M; 1.
DR Pfam; PF03159; XRN_N; 1.
DR PIRSF; PIRSF037239; Exonuclease_Xrn2; 1.
PE 3: Inferred from homology;
KW Coiled coil; Exonuclease; Hydrolase; mRNA processing; Nuclease; Nucleus;
KW Reference proteome; rRNA processing; Transcription;
KW Transcription regulation; Transcription termination.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..1003
FT /note="5'-3' exoribonuclease 2"
FT /id="PRO_0000249924"
FT REGION 107..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 389..419
FT /evidence="ECO:0000255"
FT COILED 690..730
FT /evidence="ECO:0000255"
FT COMPBIAS 113..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1003 AA; 116221 MW; 3416C11D7BF9AA04 CRC64;
MGVPALFRWL SRKYPKIISP VVEDDVTQEI GAAQFSDPNP NGELDNLYLD MNGIVHPCSH
PEHKLPPETE DEMFLDVFKY TDRVLLMARP RKVLMIAVDG VAPRAKMNQQ RSRRFRSAQD
AKIAHEEKER QIRERESRGE SIDDAIKGKK SWDSNAITPG TPFMDSLAQA LRYWVAYKLA
TDPGWANLQV IISDATVPGE GEHKLMSFIR SQRSDPEYDP NTKHCIYGLD ADLIFLGLAT
HEPHFRVLRE DVFANQSRQM RISDQLSMTQ DQKDSIAEQD AKKPFLWLHV NVLREYLEIE
LYNPHLSFPF DLERAIDDWV FMCFFVGNDF LPHLPSLDVR DNGIDILVNC WKRMLPKLRD
YITCDGNLNL ESVEKLLSSL SYKEDEIFRK RHEGEKRREE NDKRRKLAQE EEKALKNQYI
PQVSKGSDKA PLTADINMPL LSTSGDAVEG YAQLSNKDIV ENRDVITKAN MSNADAAAAL
KKLLDSKNNK ESDKNVSASA AIQEQQNKSD INTTENSKKR PIDQVEAELP KPDENGDSVR
MWEPGYRQRY YQSKFGVVSE EEINKIRRDM VRCYLEGISW VLLYYYQGCP SWQWYYPYHY
APFAADFVNI NDIIGEQGIK FTLGEPFKPY EQLMSVLPAA SGHNLPEVLR ILMSDPSSEI
LDFYPEEFQI DMNGKKMSWQ GIALLPFIDE NRLLEALEKR YHLLTDDERE RNTLKNEVLF
ISNQNKNYKR FYNELYDNNV KELKFRFSRS SLAGTVIKNE YFVPDGITKF PLSEGDMPDL
NNIEFFQSSY KMPTKKMGKS MLINGYISHT RTLTQEDRDS ILHGNQRNGG YNRFRTPNDN
SGYVNKGPSG KEDYLIYSMR RGGYRAFMHN LKNQNQQHQQ PVPMNAMANN SYDNQYNSYS
NNNNYNNNYN GGYPNQSNNN YSNQNSYNNY SNQNSYNNYN NQNSYNNYNN RNNHGNYNNY
NRYNNQGSNY DRQGQGNASS NRSGYIPAPN RTGNFRNRNG YNR
