XRN2_CANAL
ID XRN2_CANAL Reviewed; 968 AA.
AC Q5AMG5; A0A1D8PL69;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 4.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=5'-3' exoribonuclease 2;
DE EC=3.1.13.-;
GN Name=RAT1; OrderedLocusNames=CAALFM_C401080WA;
GN ORFNames=CaO19.12150, CaO19.4681;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017626; AOW28895.1; -; Genomic_DNA.
DR RefSeq; XP_722750.2; XM_717657.2.
DR AlphaFoldDB; Q5AMG5; -.
DR SMR; Q5AMG5; -.
DR STRING; 237561.Q5AMG5; -.
DR PRIDE; Q5AMG5; -.
DR GeneID; 3635686; -.
DR KEGG; cal:CAALFM_C401080WA; -.
DR CGD; CAL0000180194; RAT1.
DR VEuPathDB; FungiDB:C4_01080W_A; -.
DR eggNOG; KOG2044; Eukaryota.
DR HOGENOM; CLU_006038_1_1_1; -.
DR InParanoid; Q5AMG5; -.
DR OMA; ETWEYIV; -.
DR OrthoDB; 685597at2759; -.
DR PRO; PR:Q5AMG5; -.
DR Proteomes; UP000000559; Chromosome 4.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004534; F:5'-3' exoribonuclease activity; IGI:CGD.
DR GO; GO:0000150; F:DNA strand exchange activity; IGI:CGD.
DR GO; GO:0008017; F:microtubule binding; IGI:CGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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: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..968
FT /note="5'-3' exoribonuclease 2"
FT /id="PRO_0000249920"
FT REGION 498..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 113..140
FT /evidence="ECO:0000255"
FT COILED 387..416
FT /evidence="ECO:0000255"
FT COMPBIAS 498..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 968 AA; 111689 MW; 9614D86A3693586A CRC64;
MGVPALFRWL SRKYPKIISP VVEEEDHEIG GAKYENPNPN GEIDNLYLDM NGIVHPCSHP
EHKKPPETED EMFLDIFKYT DRVLMMARPR KVLMIAVDGV APRAKMNQQR ARRFRAAKDA
ELKAKQLEIE VQERELRGEI INDAIKGKKQ WDSNAITPGT PFMDRLAEAL RYWVAYKLSS
DPGWANLQVI ISDATVPGEG EHKLMSFIRS QRSDPQYDPN TKHCIYGLDA DLIFLGLATH
EPHFRVLRED VFASQDKKFT IKDQIADANS NGDTVAKEDK KPFLWLHVNV LREYLQVELF
TPRMSFPFEL ERAIDDWVFL CFFAGNDFLP HLPSLDVRDN GIDTLVQCWK RSLPILKDYV
TCDGKLNLKS VEVLMSNLAY KESEIFKNKH AAEQRREENN KRRKLAQEQE RALKRVYSSQ
VSKGKDKAPL TADVNMPLMD TSGQNVEGYA NLTNSDIVQN RAILTKANLA NSDAAAELKK
LIDSKKTQVT VVQDQIATDS SANSETTTSE SELEEIQSDN SLKRKLEPEE DKQTQSDDIK
LWEPGYNKRY YEAKFHCQSD EEIEQTKRDV VRHYVEGIAW VALYYYQGCP SWNWYFPYHY
APFAADFTNL EELFPEGVKF KLGEPFRPFE QLMSVLPAAS GHTLPQVFRD LMSNPDSEII
DFYPEEFEID MNGKKMSWQG IPLLPFIDEK RLLDAVQKKY ELLTPDEKSR NTNKEAELFI
SPANKNFSKF SEKLYKENEN EVTFKYAKSG LSGKIFKLGT FNPEGVFNFP LNEGYMPNVN
NSDYFQAIYH FPKTKTGKSM ILNGHIAPLP ALTTADKNDL LYQLDKFNNR RNGGRFNSTL
DNSDYINKGP AGKELYKTYS MRRGGYRSYL QYLTNGHHPD HQSQNSQYLS YGQQKPYGGQ
GSYNQQGYYN QQGRYNQQGN NYNQQGRYSQ QSQYNQYRSN TQRFNNNQNY NQSSNNSRSG
YLPPRPQR
