ID   ERI1_HUMAN              Reviewed;         349 AA.
AC   Q8IV48; A8K4U7; Q9NSX3;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 189.
DE   RecName: Full=3'-5' exoribonuclease 1;
DE            EC=3.1.-.- {ECO:0000269|PubMed:14961122, ECO:0000269|PubMed:16912046, ECO:0000269|PubMed:17135487};
DE   AltName: Full=3'-5' exonuclease ERI1;
DE   AltName: Full=Eri-1 homolog;
DE   AltName: Full=Histone mRNA 3'-end-specific exoribonuclease;
DE   AltName: Full=Histone mRNA 3'-exonuclease 1;
DE   AltName: Full=Protein 3'hExo;
DE            Short=HEXO;
GN   Name=ERI1; Synonyms=3'EXO, THEX1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-23; 43-48; 53-67;
RP   161-172; 200-208; 225-237; 263-269 AND 284-291, FUNCTION, ACTIVITY
RP   REGULATION, ENZYME ACTIVITY, AND RNA-BINDING.
RX   PubMed=14536070; DOI=10.1016/s1097-2765(03)00278-8;
RA   Dominski Z., Yang X.-C., Kaygun H., Dadlez M., Marzluff W.F.;
RT   "A 3' exonuclease that specifically interacts with the 3' end of histone
RT   mRNA.";
RL   Mol. Cell 12:295-305(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-16.
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   ENZYME ACTIVITY IN VITRO.
RX   PubMed=14961122; DOI=10.1038/nature02302;
RA   Kennedy S., Wang D., Ruvkun G.;
RT   "A conserved siRNA-degrading RNase negatively regulates RNA interference in
RT   C. elegans.";
RL   Nature 427:645-649(2004).
RN   [6]
RP   FUNCTION, IDENTIFICATION IN A TERNARY COMPLEX, ENZYME ACTIVITY, SUBCELLULAR
RP   LOCATION, MUTAGENESIS OF LYS-92; ARG-96; LYS-99; LYS-104; ARG-105; TYR-109;
RP   TYR-110; LYS-111; LYS-112; ASP-234; MET-235 AND ASP-298, AND RNA-BINDING.
RX   PubMed=16912046; DOI=10.1074/jbc.m602947200;
RA   Yang X.-C., Purdy M., Marzluff W.F., Dominski Z.;
RT   "Characterization of 3'hExo, a 3' exonuclease specifically interacting with
RT   the 3' end of histone mRNA.";
RL   J. Biol. Chem. 281:30447-30454(2006).
RN   [7] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=17135487; DOI=10.1261/rna.186706;
RA   Kupsco J.M., Wu M.J., Marzluff W.F., Thapar R., Duronio R.J.;
RT   "Genetic and biochemical characterization of Drosophila Snipper: A
RT   promiscuous member of the metazoan 3'hExo/ERI-1 family of 3' to 5'
RT   exonucleases.";
RL   RNA 12:2103-2117(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-62, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [11] {ECO:0007744|PDB:1W0H}
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 123-322 IN COMPLEX WITH MAGNESIUM
RP   IONS AND AMP, AND COFACTOR.
RX   PubMed=15451662; DOI=10.1016/j.jmb.2004.08.055;
RA   Cheng Y., Patel D.J.;
RT   "Crystallographic structure of the nuclease domain of 3'hExo, a DEDDh
RT   family member, bound to rAMP.";
RL   J. Mol. Biol. 343:305-312(2004).
CC   -!- FUNCTION: RNA exonuclease that binds to the 3'-end of histone mRNAs and
CC       degrades them, suggesting that it plays an essential role in histone
CC       mRNA decay after replication (PubMed:14536070, PubMed:16912046,
CC       PubMed:17135487). A 2' and 3'-hydroxyl groups at the last nucleotide of
CC       the histone 3'-end is required for efficient degradation of RNA
CC       substrates (PubMed:14536070, PubMed:16912046, PubMed:17135487). Also
CC       able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in
CC       vitro, suggesting a possible role as regulator of RNA interference
CC       (RNAi) (PubMed:14961122). Required for binding the 5'-ACCCA-3' sequence
CC       present in stem-loop structure (PubMed:14536070, PubMed:16912046). Able
CC       to bind other mRNAs (PubMed:14536070, PubMed:16912046). Required for
CC       5.8S rRNA 3'-end processing (By similarity). Also binds to 5.8s
CC       ribosomal RNA (By similarity). Binds with high affinity to the stem-
CC       loop structure of replication-dependent histone pre-mRNAs
CC       (PubMed:14536070, PubMed:17135487, PubMed:16912046). In vitro, does not
CC       have sequence specificity (PubMed:17135487). In vitro, has weak DNA
CC       exonuclease activity (PubMed:17135487). In vitro, shows biphasic
CC       kinetics such that there is rapid hydrolysis of the last three unpaired
CC       RNA nucleotides in the 39 flanking sequence followed by a much slower
CC       cleavage through the stem that occurs over a longer incubation period
CC       in the order of hours (PubMed:17135487). {ECO:0000250|UniProtKB:Q7TMF2,
CC       ECO:0000269|PubMed:14536070, ECO:0000269|PubMed:14961122,
CC       ECO:0000269|PubMed:16912046, ECO:0000269|PubMed:17135487}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:15451662, ECO:0000269|PubMed:17135487};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000269|PubMed:15451662};
CC   -!- ACTIVITY REGULATION: Although it can bind simultaneously with SLBP to
CC       the 3'-end of histone mRNA, the presence of SLBP prevents the
CC       exonuclease activity. {ECO:0000269|PubMed:14536070}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 37 degrees Celsius.
CC         {ECO:0000269|PubMed:17135487};
CC   -!- SUBUNIT: Identified in a histone pre-mRNA complex, at least composed of
CC       ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1. Interacts in a cooperative
CC       manner with SLBP to the mature 3'-end of histone mRNAs (By similarity).
CC       Binds to 40S and 60S ribosomal subunits and to 80S assembled ribosomes.
CC       Found in a ternary complex with SLBP and the stem-loop structure of the
CC       3'-end of histone mRNAs. {ECO:0000250, ECO:0000269|PubMed:15451662,
CC       ECO:0000269|PubMed:16912046}.
CC   -!- INTERACTION:
CC       Q8IV48; A9UHW6: MIF4GD; NbExp=2; IntAct=EBI-5459222, EBI-373498;
CC       Q8IV48; Q14493: SLBP; NbExp=2; IntAct=EBI-5459222, EBI-2696402;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16912046}. Nucleus
CC       {ECO:0000269|PubMed:16912046}. Nucleus, nucleolus
CC       {ECO:0000269|PubMed:16912046}.
CC   -!- DOMAIN: The SAP domain is necessary for binding to the stem-loop
CC       structure of histone mRNAs and to form the ternary complex with SLBP,
CC       but not for 3'-end histone mRNA exonuclease activity.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB70871.2; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAB70871.2; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AY310909; AAQ21219.1; -; mRNA.
DR   EMBL; AK291062; BAF83751.1; -; mRNA.
DR   EMBL; AL137679; CAB70871.2; ALT_SEQ; mRNA.
DR   EMBL; BC035279; AAH35279.1; -; mRNA.
DR   CCDS; CCDS5972.1; -.
DR   PIR; T46432; T46432.
DR   RefSeq; NP_699163.2; NM_153332.3.
DR   PDB; 1W0H; X-ray; 1.59 A; A=123-322.
DR   PDB; 1ZBH; X-ray; 3.00 A; A/B/C/D=51-349.
DR   PDB; 1ZBU; X-ray; 3.00 A; A/B/C/D=1-349.
DR   PDB; 4L8R; X-ray; 2.60 A; B/E=55-349.
DR   PDB; 4QOZ; X-ray; 2.30 A; B/E=55-349.
DR   PDBsum; 1W0H; -.
DR   PDBsum; 1ZBH; -.
DR   PDBsum; 1ZBU; -.
DR   PDBsum; 4L8R; -.
DR   PDBsum; 4QOZ; -.
DR   AlphaFoldDB; Q8IV48; -.
DR   SMR; Q8IV48; -.
DR   BioGRID; 124718; 56.
DR   DIP; DIP-61409N; -.
DR   IntAct; Q8IV48; 17.
DR   MINT; Q8IV48; -.
DR   STRING; 9606.ENSP00000250263; -.
DR   iPTMnet; Q8IV48; -.
DR   PhosphoSitePlus; Q8IV48; -.
DR   BioMuta; ERI1; -.
DR   DMDM; 45476938; -.
DR   EPD; Q8IV48; -.
DR   jPOST; Q8IV48; -.
DR   MassIVE; Q8IV48; -.
DR   MaxQB; Q8IV48; -.
DR   PaxDb; 9606-ENSP00000429615; -.
DR   PeptideAtlas; Q8IV48; -.
DR   ProteomicsDB; 70659; -.
DR   Pumba; Q8IV48; -.
DR   Antibodypedia; 8346; 338 antibodies from 31 providers.
DR   DNASU; 90459; -.
DR   Ensembl; ENST00000250263.8; ENSP00000250263.7; ENSG00000104626.15.
DR   Ensembl; ENST00000519292.5; ENSP00000430190.1; ENSG00000104626.15.
DR   GeneID; 90459; -.
DR   KEGG; hsa:90459; -.
DR   MANE-Select; ENST00000250263.8; ENSP00000250263.7; NM_153332.4; NP_699163.2.
DR   UCSC; uc003wsk.2; human.
DR   AGR; HGNC:23994; -.
DR   CTD; 90459; -.
DR   DisGeNET; 90459; -.
DR   GeneCards; ERI1; -.
DR   HGNC; HGNC:23994; ERI1.
DR   HPA; ENSG00000104626; Low tissue specificity.
DR   MIM; 608739; gene.
DR   neXtProt; NX_Q8IV48; -.
DR   OpenTargets; ENSG00000104626; -.
DR   PharmGKB; PA164719226; -.
DR   VEuPathDB; HostDB:ENSG00000104626; -.
DR   eggNOG; KOG0542; Eukaryota.
DR   GeneTree; ENSGT00530000063205; -.
DR   HOGENOM; CLU_037266_4_1_1; -.
DR   InParanoid; Q8IV48; -.
DR   OMA; MHSGQLM; -.
DR   OrthoDB; 443016at2759; -.
DR   PhylomeDB; Q8IV48; -.
DR   TreeFam; TF313449; -.
DR   PathwayCommons; Q8IV48; -.
DR   Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   SignaLink; Q8IV48; -.
DR   BioGRID-ORCS; 90459; 35 hits in 1168 CRISPR screens.
DR   ChiTaRS; ERI1; human.
DR   EvolutionaryTrace; Q8IV48; -.
DR   GenomeRNAi; 90459; -.
DR   Pharos; Q8IV48; Tbio.
DR   PRO; PR:Q8IV48; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q8IV48; Protein.
DR   Bgee; ENSG00000104626; Expressed in secondary oocyte and 143 other cell types or tissues.
DR   ExpressionAtlas; Q8IV48; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IDA:UniProtKB.
DR   GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IBA:GO_Central.
DR   GO; GO:0071207; F:histone pre-mRNA stem-loop binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR   GO; GO:0019843; F:rRNA binding; ISS:UniProtKB.
DR   GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProtKB-KW.
DR   GO; GO:0031125; P:rRNA 3'-end processing; ISS:UniProtKB.
DR   CDD; cd06133; ERI-1_3'hExo_like; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   Gene3D; 1.10.720.30; SAP domain; 1.
DR   InterPro; IPR047201; ERI-1_3'hExo-like.
DR   InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR003034; SAP_dom.
DR   InterPro; IPR036361; SAP_dom_sf.
DR   PANTHER; PTHR23044; 3'-5' EXONUCLEASE ERI1-RELATED; 1.
DR   PANTHER; PTHR23044:SF77; 3'-5' EXORIBONUCLEASE 1; 1.
DR   Pfam; PF00929; RNase_T; 1.
DR   Pfam; PF02037; SAP; 1.
DR   SMART; SM00479; EXOIII; 1.
DR   SMART; SM00513; SAP; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   SUPFAM; SSF68906; SAP domain; 1.
DR   PROSITE; PS50800; SAP; 1.
DR   Genevisible; Q8IV48; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Exonuclease; Hydrolase;
KW   Magnesium; Metal-binding; Nuclease; Nucleus; Phosphoprotein;
KW   Reference proteome; RNA-binding; RNA-mediated gene silencing;
KW   rRNA processing.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000305|PubMed:14536070"
FT   CHAIN           2..349
FT                   /note="3'-5' exoribonuclease 1"
FT                   /id="PRO_0000187007"
FT   DOMAIN          76..110
FT                   /note="SAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT   DOMAIN          130..306
FT                   /note="Exonuclease"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        136
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000269|PubMed:15451662,
FT                   ECO:0007744|PDB:1W0H"
FT   ACT_SITE        293
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000269|PubMed:15451662,
FT                   ECO:0007744|PDB:1W0H"
FT   BINDING         134
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:15451662,
FT                   ECO:0007744|PDB:1W0H"
FT   BINDING         134
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:15451662,
FT                   ECO:0007744|PDB:1W0H"
FT   BINDING         136
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000269|PubMed:15451662,
FT                   ECO:0007744|PDB:1W0H"
FT   BINDING         136
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:15451662,
FT                   ECO:0007744|PDB:1W0H"
FT   BINDING         137
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000269|PubMed:15451662,
FT                   ECO:0007744|PDB:1W0H"
FT   BINDING         234
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:15451662,
FT                   ECO:0007744|PDB:1W0H"
FT   BINDING         293
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000269|PubMed:15451662,
FT                   ECO:0007744|PDB:1W0H"
FT   BINDING         298
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:15451662,
FT                   ECO:0007744|PDB:1W0H"
FT   MOD_RES         59
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         62
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:23186163"
FT   VARIANT         16
FT                   /note="L -> P (in dbSNP:rs2288672)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_018107"
FT   MUTAGEN         92
FT                   /note="K->A: Does not inhibit RNA-binding to the stem-loop
FT                   structure. Does not inhibit RNA-binding to the stem-loop
FT                   structure, when associated with A-104."
FT                   /evidence="ECO:0000269|PubMed:16912046"
FT   MUTAGEN         96
FT                   /note="R->A: Does not inhibit RNA-binding to the stem-loop
FT                   structure."
FT                   /evidence="ECO:0000269|PubMed:16912046"
FT   MUTAGEN         99
FT                   /note="K->A: Reduces slightly RNA-binding to the stem-loop
FT                   structure."
FT                   /evidence="ECO:0000269|PubMed:16912046"
FT   MUTAGEN         104
FT                   /note="K->A: Does not inhibit RNA-binding to the stem-loop
FT                   structure. Does not inhibit RNA-binding to the stem-loop
FT                   structure, when associated with A-92."
FT                   /evidence="ECO:0000269|PubMed:16912046"
FT   MUTAGEN         105
FT                   /note="R->A: Inhibits RNA-binding to the stem-loop
FT                   structure."
FT                   /evidence="ECO:0000269|PubMed:16912046"
FT   MUTAGEN         109
FT                   /note="Y->A: Reduces slightly RNA-binding to the stem-loop
FT                   structure; when associated with A-110."
FT                   /evidence="ECO:0000269|PubMed:16912046"
FT   MUTAGEN         110
FT                   /note="Y->A: Reduces slightly RNA-binding to the stem-loop
FT                   structure; when associated with A-109."
FT                   /evidence="ECO:0000269|PubMed:16912046"
FT   MUTAGEN         111
FT                   /note="K->A: Reduces RNA-binding to the stem-loop structure
FT                   but not 3'-end histone mRNA exonuclease activity; when
FT                   associated with A-112."
FT                   /evidence="ECO:0000269|PubMed:16912046"
FT   MUTAGEN         112
FT                   /note="K->A: Reduces RNA-binding to the stem-loop structure
FT                   but not 3'-end histone mRNA exonuclease activity; when
FT                   associated with A-111."
FT                   /evidence="ECO:0000269|PubMed:16912046"
FT   MUTAGEN         234
FT                   /note="D->A: Inhibits 3'-end histone mRNA exonuclease
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:16912046"
FT   MUTAGEN         235
FT                   /note="M->A: Inhibits RNA-binding to the stem-loop
FT                   structure and 3'-end histone mRNA exonuclease activity."
FT                   /evidence="ECO:0000269|PubMed:16912046"
FT   MUTAGEN         298
FT                   /note="D->A: Inhibits 3'-end histone mRNA exonuclease
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:16912046"
FT   HELIX           47..49
FT                   /evidence="ECO:0007829|PDB:1ZBU"
FT   TURN            50..52
FT                   /evidence="ECO:0007829|PDB:1ZBU"
FT   STRAND          53..57
FT                   /evidence="ECO:0007829|PDB:1ZBU"
FT   HELIX           64..77
FT                   /evidence="ECO:0007829|PDB:4QOZ"
FT   HELIX           81..90
FT                   /evidence="ECO:0007829|PDB:4QOZ"
FT   HELIX           99..114
FT                   /evidence="ECO:0007829|PDB:4QOZ"
FT   STRAND          115..119
FT                   /evidence="ECO:0007829|PDB:1ZBU"
FT   STRAND          126..132
FT                   /evidence="ECO:0007829|PDB:1W0H"
FT   STRAND          151..160
FT                   /evidence="ECO:0007829|PDB:1W0H"
FT   TURN            161..163
FT                   /evidence="ECO:0007829|PDB:1W0H"
FT   STRAND          165..174
FT                   /evidence="ECO:0007829|PDB:1W0H"
FT   STRAND          177..179
FT                   /evidence="ECO:0007829|PDB:1W0H"
FT   HELIX           184..190
FT                   /evidence="ECO:0007829|PDB:1W0H"
FT   HELIX           194..198
FT                   /evidence="ECO:0007829|PDB:1W0H"
FT   STRAND          200..202
FT                   /evidence="ECO:0007829|PDB:1ZBU"
FT   HELIX           203..216
FT                   /evidence="ECO:0007829|PDB:1W0H"
FT   TURN            220..222
FT                   /evidence="ECO:0007829|PDB:1W0H"
FT   STRAND          225..231
FT                   /evidence="ECO:0007829|PDB:1W0H"
FT   TURN            232..235
FT                   /evidence="ECO:0007829|PDB:1W0H"
FT   HELIX           236..246
FT                   /evidence="ECO:0007829|PDB:1W0H"
FT   HELIX           252..254
FT                   /evidence="ECO:0007829|PDB:1W0H"
FT   STRAND          255..259
FT                   /evidence="ECO:0007829|PDB:1W0H"
FT   HELIX           260..268
FT                   /evidence="ECO:0007829|PDB:1W0H"
FT   HELIX           272..274
FT                   /evidence="ECO:0007829|PDB:1W0H"
FT   HELIX           277..283
FT                   /evidence="ECO:0007829|PDB:1W0H"
FT   HELIX           295..311
FT                   /evidence="ECO:0007829|PDB:1W0H"
FT   STRAND          320..323
FT                   /evidence="ECO:0007829|PDB:4QOZ"
FT   STRAND          326..329
FT                   /evidence="ECO:0007829|PDB:4QOZ"
FT   STRAND          332..334
FT                   /evidence="ECO:0007829|PDB:1ZBH"
SQ   SEQUENCE   349 AA;  40064 MW;  D5837AA05F09410C CRC64;
     MEDPQSKEPA GEAVALALLE SPRPEGGEEP PRPSPEETQQ CKFDGQETKG SKFITSSASD
     FSDPVYKEIA ITNGCINRMS KEELRAKLSE FKLETRGVKD VLKKRLKNYY KKQKLMLKES
     NFADSYYDYI CIIDFEATCE EGNPPEFVHE IIEFPVVLLN THTLEIEDTF QQYVRPEINT
     QLSDFCISLT GITQDQVDRA DTFPQVLKKV IDWMKLKELG TKYKYSLLTD GSWDMSKFLN
     IQCQLSRLKY PPFAKKWINI RKSYGNFYKV PRSQTKLTIM LEKLGMDYDG RPHCGLDDSK
     NIARIAVRML QDGCELRINE KMHAGQLMSV SSSLPIEGTP PPQMPHFRK
//