REXO3_YARLI
ID REXO3_YARLI Reviewed; 757 AA.
AC Q6CFE7;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=RNA exonuclease 3;
DE EC=3.1.-.-;
GN Name=REX3; OrderedLocusNames=YALI0B07689g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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: 3' to 5' exoribonuclease required for proper 3' end
CC maturation of MRP RNA and of the U5L snRNA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the REXO1/REXO3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382128; CAG82848.1; -; Genomic_DNA.
DR RefSeq; XP_500615.1; XM_500615.1.
DR AlphaFoldDB; Q6CFE7; -.
DR SMR; Q6CFE7; -.
DR STRING; 4952.CAG82848; -.
DR PRIDE; Q6CFE7; -.
DR EnsemblFungi; CAG82848; CAG82848; YALI0_B07689g.
DR GeneID; 2906951; -.
DR KEGG; yli:YALI0B07689g; -.
DR VEuPathDB; FungiDB:YALI0_B07689g; -.
DR HOGENOM; CLU_368108_0_0_1; -.
DR InParanoid; Q6CFE7; -.
DR Proteomes; UP000001300; Chromosome B.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004527; F:exonuclease activity; IBA:GO_Central.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR CDD; cd06145; REX1_like; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR034922; REX1-like_exo.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Nuclease; Nucleus; Reference proteome;
KW rRNA processing.
FT CHAIN 1..757
FT /note="RNA exonuclease 3"
FT /id="PRO_0000120936"
FT DOMAIN 597..751
FT /note="Exonuclease"
FT REGION 56..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 757 AA; 82343 MW; E45A571121CC9E53 CRC64;
MQFSGEGLFF HSPFNSPKKH MFSSSKGLFR GHPCPSIAAG QFCRLLCCPF DHPERVKRES
ENGSDSAEMV KRRKLEVGQG VARVAGDSSG GKLELPGARQ ALNQRDRPEI EGVGASPKTE
GGRAEGAEKK EFASSQSSQK EQQETPHASA TPQASVSPQT SAPPQHVSSS VSEDVLKQGK
NGITSKSEKS SVKQPGSRDI YQPSSSREPP VSSIDTRTSS SPKSALEAVM TTSASPSQSR
DGSRNTSASP SSSRDAEHLM PTTIFPCPAT VPQRIAYLKA IHSALTDKRK LKFPKRAAIL
EELAAAKRSA GNYMVYTNEC RVLVKSIKDG SWRGGKAGGT KTDSKTSGHI TSSISNQLDM
LASKTKPLLA QNGYPVNPDP LKSGLPSNIG IQHCDRCDKA FDVPKVDNYG SCKYHWARAR
MGGNSTMPEK FYPCCNQPVG MSEGCEEAPR HVYKLHDLND LAFVIPFRTV STSESLDTST
STSTSTSATT SAPSAKSTKT ASRPASTPTK SLTSSLDLEK SRQPFNKARR PRTIFNGPAV
NQREPDITLE TMKRGIGESR GQADSQERSS EPRERSARVR EQPSGSCDQA GSLQTSVVAV
DCEMLYTSLG MELCRVTCID YHGKKTLDRV VRPTGRILDY NTRFSGISDI NEPIITESGE
KGDSISFEEA HRLILKLINK QTILVGHGLE NDLIAMRLIH DRIIDTSILY PDFNPRYKTA
LKTLALKYLK RTIQTGEHDS MEDALAALDV VKCHLKG