XRN2_SCHPO
ID XRN2_SCHPO Reviewed; 991 AA.
AC P40848;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=5'-3' exoribonuclease 2;
DE EC=3.1.13.-;
DE AltName: Full=Protein dhp1;
GN Name=dhp1; ORFNames=SPAC26A3.12c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-29.
RC STRAIN=ATCC 38365 / 975;
RX PubMed=8190062; DOI=10.1007/bf00283869;
RA Sugano S., Shobuike T., Takeda T., Sugino A., Ikeda H.;
RT "Molecular analysis of the dhp1+ gene of Schizosaccharomyces pombe: an
RT essential gene that has homology to the DST2 and RAT1 genes of
RT Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 243:1-8(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP CHARACTERIZATION.
RX PubMed=11238999; DOI=10.1093/nar/29.6.1326;
RA Shobuike T., Tatebayashi K., Tani T., Sugano S., Ikeda H.;
RT "The dhp1+ gene, encoding a putative nuclear 5'3' exoribonuclease, is
RT required for proper chromosome segregation in fission yeast.";
RL Nucleic Acids Res. 29:1326-1333(2001).
CC -!- FUNCTION: Required for the processing of nuclear mRNA and rRNA
CC precursors. May promote the termination of transcription by RNA
CC polymerase II (By similarity). Essential for vegetative cell growth and
CC chromosome segregation. Possesses 5'->3' exoribonuclease activity.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P40848; O13836: din1; NbExp=2; IntAct=EBI-15755578, EBI-15755601;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the 5'-3' exonuclease family. XRN2/RAT1
CC subfamily. {ECO:0000305}.
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DR EMBL; D17752; BAA04601.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA93235.1; -; Genomic_DNA.
DR PIR; S43891; S43891.
DR RefSeq; NP_594155.1; NM_001019579.2.
DR PDB; 3FQD; X-ray; 2.20 A; A=1-885.
DR PDBsum; 3FQD; -.
DR AlphaFoldDB; P40848; -.
DR SMR; P40848; -.
DR BioGRID; 279127; 26.
DR DIP; DIP-59743N; -.
DR IntAct; P40848; 1.
DR STRING; 4896.SPAC26A3.12c.1; -.
DR iPTMnet; P40848; -.
DR MaxQB; P40848; -.
DR PaxDb; P40848; -.
DR PRIDE; P40848; -.
DR EnsemblFungi; SPAC26A3.12c.1; SPAC26A3.12c.1:pep; SPAC26A3.12c.
DR GeneID; 2542674; -.
DR KEGG; spo:SPAC26A3.12c; -.
DR PomBase; SPAC26A3.12c; dhp1.
DR VEuPathDB; FungiDB:SPAC26A3.12c; -.
DR eggNOG; KOG2044; Eukaryota.
DR HOGENOM; CLU_006038_1_1_1; -.
DR InParanoid; P40848; -.
DR OMA; CLHYYVH; -.
DR PhylomeDB; P40848; -.
DR PRO; PR:P40848; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0090730; C:Las1 complex; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0004534; F:5'-3' exoribonuclease activity; IDA:PomBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000448; P:cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IC:PomBase.
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:0071028; P:nuclear mRNA surveillance; ISO:PomBase.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0000294; P:nuclear-transcribed mRNA catabolic process, endonucleolytic cleavage-dependent decay; EXP:PomBase.
DR GO; GO:0034428; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 5'-3'; IDA:PomBase.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; IMP:CACAO.
DR GO; GO:0106354; P:tRNA surveillance; IGI:PomBase.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Exonuclease; Hydrolase;
KW mRNA processing; Nuclease; Nucleus; Reference proteome; rRNA processing;
KW Transcription; Transcription regulation; Transcription termination.
FT CHAIN 1..991
FT /note="5'-3' exoribonuclease 2"
FT /id="PRO_0000071398"
FT REGION 404..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 264..268
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 404..419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:3FQD"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:3FQD"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:3FQD"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 75..93
FT /evidence="ECO:0007829|PDB:3FQD"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 109..143
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 167..184
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:3FQD"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 206..218
FT /evidence="ECO:0007829|PDB:3FQD"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 238..244
FT /evidence="ECO:0007829|PDB:3FQD"
FT STRAND 248..255
FT /evidence="ECO:0007829|PDB:3FQD"
FT TURN 269..273
FT /evidence="ECO:0007829|PDB:3FQD"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 297..308
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 319..329
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:3FQD"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 350..365
FT /evidence="ECO:0007829|PDB:3FQD"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 377..388
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 391..402
FT /evidence="ECO:0007829|PDB:3FQD"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 591..598
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 608..629
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 647..649
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 668..675
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 678..683
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 686..693
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 700..702
FT /evidence="ECO:0007829|PDB:3FQD"
FT STRAND 712..715
FT /evidence="ECO:0007829|PDB:3FQD"
FT STRAND 719..722
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 729..737
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 740..742
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 745..749
FT /evidence="ECO:0007829|PDB:3FQD"
FT STRAND 757..761
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 767..774
FT /evidence="ECO:0007829|PDB:3FQD"
FT STRAND 776..778
FT /evidence="ECO:0007829|PDB:3FQD"
FT STRAND 780..782
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 788..791
FT /evidence="ECO:0007829|PDB:3FQD"
FT STRAND 796..800
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 819..824
FT /evidence="ECO:0007829|PDB:3FQD"
FT STRAND 828..830
FT /evidence="ECO:0007829|PDB:3FQD"
FT STRAND 833..839
FT /evidence="ECO:0007829|PDB:3FQD"
FT HELIX 864..873
FT /evidence="ECO:0007829|PDB:3FQD"
SQ SEQUENCE 991 AA; 112368 MW; 83FA34D93DADAD00 CRC64;
MGVPALFRLL SRKFAKVITP VIEAPTEKLP DGTEIEPDLS LPNPNGVECD NLYLDMNGIV
HPCSHPEDRP APETEDEMMV AVFEYTDRIL AMVRPRQLLF IAIDGVAPRA KMNQQRSRRF
RSSREAALKE EELQAFIEEA KQQGIPIDEN ATKKKSWDSN CITPGTPFMD TLAKSLRYYI
INKLNSDPCW RNVRFILSDA SVPGEGEHKI MEFIRSQRVK PEYDPNTHHV VYGLDADLIM
LGLATHEPHF RVLREDVFFQ QGSTKKTKEE RLGIKRLDDV SETNKVPVKK PFIWLNVSIL
REYLEVELYV PNLPFPFDLE RAIDDWVFFI FFVGNDFLPH LPSLDIRDGA VERLTEIWRA
SLPHMGGYLT LDGSVNLARA EVILSAVGNQ EDDIFKRLKQ QEDRRNENYR RRQQRESNQE
SESYVDNVVI QRSVETQSTE VVTSSKSTSV DTKPPKKTQK IDAPAPVDLV NLSEKTSNRS
LGATNRELIN NRAANRLGLS REAAAVSSVN KLAASALKAQ LVSNETLQNV PLEDSIASSS
AYEDTDSIES STPVVHPIDT KVSNVGQKRK APDSTEENEN TDTVRLYEPG YRERYYEQKF
HISPDEPEKI REAVKHYVHG LCWVLLYYYQ GCPSWTWYYP YHYAPFAADF KDLASIDVKF
ELNQPFKPYE QLLGVLPAAS KNNLPEKLQT LMTDENSEII DFYPENFTID LNGKKFEWQG
VALLPFIDEN RLLNAVSKIY PQLTEEESKR NEDGSTLLFI SEHHPMFSEL VKQLYSKKRQ
GKPLKLSGKM AHGLFGKVNT NDSVIPNVSV QCPIDVTSAD ALQKYGSIDD NQSISLVFEV
PKSHFVHKSM LLRGVKMPNR VLTPEDINQV RAERSFSSRR NNGNSYRGGH QSYGVRRSYQ
SQSYSSRQSY TGVTNGFANG GVQPPWSGNG NFPRSNASYN SRGGHEGYGG RSRGGGYSNG
PPAGNHYSSN RGKGYGYQRE SYNNNNRNGY Y
