PAN2_YEAST
ID PAN2_YEAST Reviewed; 1115 AA.
AC P53010; D6VU51;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=PAN2-PAN3 deadenylation complex catalytic subunit PAN2 {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000305};
DE EC=3.1.13.4 {ECO:0000255|HAMAP-Rule:MF_03182};
DE AltName: Full=PAB1P-dependent poly(A)-specific ribonuclease {ECO:0000255|HAMAP-Rule:MF_03182};
DE AltName: Full=Poly(A)-nuclease deadenylation complex subunit 2 {ECO:0000255|HAMAP-Rule:MF_03182};
DE Short=PAN deadenylation complex subunit 2 {ECO:0000255|HAMAP-Rule:MF_03182};
GN Name=PAN2 {ECO:0000255|HAMAP-Rule:MF_03182}; OrderedLocusNames=YGL094C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RX PubMed=8550599; DOI=10.1074/jbc.271.1.432;
RA Boeck R., Tarun S.Z. Jr., Rieger M., Deardorff J.A., Mueller-Auer S.,
RA Sachs A.B.;
RT "The yeast Pan2 protein is required for poly(A)-binding protein-stimulated
RT poly(A)-nuclease activity.";
RL J. Biol. Chem. 271:432-438(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP PROTEIN SEQUENCE OF 489-504.
RX PubMed=1339314; DOI=10.1016/0092-8674(92)90246-9;
RA Sachs A.B., Deardorff J.A.;
RT "Translation initiation requires the PAB-dependent poly(A) ribonuclease in
RT yeast.";
RL Cell 70:961-973(1992).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=1358757; DOI=10.1101/gad.6.11.2088;
RA Lowell J.E., Rudner D.Z., Sachs A.B.;
RT "3'-UTR-dependent deadenylation by the yeast poly(A) nuclease.";
RL Genes Dev. 6:2088-2099(1992).
RN [7]
RP FUNCTION, INTERACTION WITH PAN3, AND ACTIVITY REGULATION.
RX PubMed=8816488; DOI=10.1128/mcb.16.10.5744;
RA Brown C.E., Tarun S.Z. Jr., Boeck R., Sachs A.B.;
RT "PAN3 encodes a subunit of the Pab1p-dependent poly(A) nuclease in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 16:5744-5753(1996).
RN [8]
RP FUNCTION.
RX PubMed=9774670; DOI=10.1128/mcb.18.11.6548;
RA Brown C.E., Sachs A.B.;
RT "Poly(A) tail length control in Saccharomyces cerevisiae occurs by message-
RT specific deadenylation.";
RL Mol. Cell. Biol. 18:6548-6559(1998).
RN [9]
RP FUNCTION.
RX PubMed=11239395; DOI=10.1016/s0092-8674(01)00225-2;
RA Tucker M., Valencia-Sanchez M.A., Staples R.R., Chen J., Denis C.L.,
RA Parker R.;
RT "The transcription factor associated Ccr4 and Caf1 proteins are components
RT of the major cytoplasmic mRNA deadenylase in Saccharomyces cerevisiae.";
RL Cell 104:377-386(2001).
RN [10]
RP FUNCTION.
RX PubMed=11953437; DOI=10.1074/jbc.m202473200;
RA Hammet A., Pike B.L., Heierhorst J.;
RT "Posttranscriptional regulation of the RAD5 DNA repair gene by the Dun1
RT kinase and the Pan2-Pan3 poly(A)-nuclease complex contributes to survival
RT of replication blocks.";
RL J. Biol. Chem. 277:22469-22474(2002).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [12]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [13]
RP ACTIVITY REGULATION.
RX PubMed=15121841; DOI=10.1128/mcb.24.10.4196-4206.2004;
RA Mangus D.A., Smith M.M., McSweeney J.M., Jacobson A.;
RT "Identification of factors regulating poly(A) tail synthesis and
RT maturation.";
RL Mol. Cell. Biol. 24:4196-4206(2004).
RN [14]
RP INTERACTION WITH PAN3.
RX PubMed=15169912; DOI=10.1128/mcb.24.12.5521-5533.2004;
RA Mangus D.A., Evans M.C., Agrin N.S., Smith M.M., Gongidi P., Jacobson A.;
RT "Positive and negative regulation of poly(A) nuclease.";
RL Mol. Cell. Biol. 24:5521-5533(2004).
RN [15]
RP FUNCTION.
RX PubMed=15630021; DOI=10.1101/gad.1267005;
RA Dunn E.F., Hammell C.M., Hodge C.A., Cole C.N.;
RT "Yeast poly(A)-binding protein, Pab1, and PAN, a poly(A) nuclease complex
RT recruited by Pab1, connect mRNA biogenesis to export.";
RL Genes Dev. 19:90-103(2005).
RN [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15894541; DOI=10.1074/jbc.m504720200;
RA Dheur S., Nykamp K.R., Viphakone N., Swanson M.S., Minvielle-Sebastia L.;
RT "Yeast mRNA poly(A) tail length control can be reconstituted in vitro in
RT the absence of Pab1p-dependent poly(A) nuclease activity.";
RL J. Biol. Chem. 280:24532-24538(2005).
RN [17]
RP ACTIVITY REGULATION.
RX PubMed=16940550; DOI=10.1261/rna.241006;
RA Hilgers V., Teixeira D., Parker R.;
RT "Translation-independent inhibition of mRNA deadenylation during stress in
RT Saccharomyces cerevisiae.";
RL RNA 12:1835-1845(2006).
RN [18]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLU-912.
RX PubMed=24872509; DOI=10.15252/embj.201488373;
RA Wolf J., Valkov E., Allen M.D., Meineke B., Gordiyenko Y., McLaughlin S.H.,
RA Olsen T.M., Robinson C.V., Bycroft M., Stewart M., Passmore L.A.;
RT "Structural basis for Pan3 binding to Pan2 and its function in mRNA
RT recruitment and deadenylation.";
RL EMBO J. 33:1514-1526(2014).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 340-1115 IN COMPLEX WITH PAN3,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF ASP-1020.
RX PubMed=24880344; DOI=10.1038/nsmb.2834;
RA Schaefer I.B., Rode M., Bonneau F., Schuessler S., Conti E.;
RT "The structure of the Pan2-Pan3 core complex reveals cross-talk between
RT deadenylase and pseudokinase.";
RL Nat. Struct. Mol. Biol. 21:591-598(2014).
CC -!- FUNCTION: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation
CC complex, one of two cytoplasmic mRNA deadenylases involved in mRNA
CC turnover. PAN specifically shortens poly(A) tails of RNA and the
CC activity is stimulated by poly(A)-binding protein PAB1. PAN
CC deadenylation is followed by rapid degradation of the shortened mRNA
CC tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by
CC two alternative mechanisms, namely exosome-mediated 3'-5'
CC exonucleolytic degradation, or deadenlyation-dependent mRNA decaping by
CC DCP1-DCP2 and subsequent 5'-3' exonucleolytic degradation by XRN1. May
CC also be involved in post-transcriptional maturation of mRNA poly(A)
CC tails, trimming the tails from their synthesized length to the slightly
CC shorter, apparently messenger-specific length found on newly exported
CC mRNAs. PAN cooperates with protein kinase DUN1 in the regulation of
CC RAD5 mRNA levels and cell survival in response to replicational stress.
CC {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:11239395,
CC ECO:0000269|PubMed:11953437, ECO:0000269|PubMed:1358757,
CC ECO:0000269|PubMed:15630021, ECO:0000269|PubMed:15894541,
CC ECO:0000269|PubMed:24880344, ECO:0000269|PubMed:8550599,
CC ECO:0000269|PubMed:8816488, ECO:0000269|PubMed:9774670}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03182,
CC ECO:0000269|PubMed:1358757, ECO:0000269|PubMed:24880344};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03182,
CC ECO:0000269|PubMed:24880344};
CC Note=Binds 2 metal cations per subunit in the catalytic exonuclease
CC domain. {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:24880344};
CC -!- ACTIVITY REGULATION: Positively regulated by the regulatory subunit
CC PAN3. Negatively regulated by PAB1-binding protein PBP1. Inhibited
CC under stress conditions. Inhibition of deadenylation under stress
CC increases mRNA stability, which may be a mechanism to retain the
CC majority of the cytoplasmic pool of mRNAs for later reuse and recovery
CC from stress. {ECO:0000255|HAMAP-Rule:MF_03182,
CC ECO:0000269|PubMed:15121841, ECO:0000269|PubMed:16940550,
CC ECO:0000269|PubMed:8816488}.
CC -!- SUBUNIT: Forms a heterotrimer with an asymmetric homodimer of the
CC regulatory subunit PAN3 to form the poly(A)-nuclease (PAN)
CC deadenylation complex. {ECO:0000255|HAMAP-Rule:MF_03182,
CC ECO:0000269|PubMed:15169912, ECO:0000269|PubMed:24872509,
CC ECO:0000269|PubMed:24880344, ECO:0000269|PubMed:8816488}.
CC -!- INTERACTION:
CC P53010; P36102: PAN3; NbExp=9; IntAct=EBI-12887, EBI-12895;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03182,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15894541}.
CC -!- DOMAIN: Contains a pseudo-UCH domain. This ubiquitin C-terminal
CC hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain
CC is predicted to be catalytically inactive because it lacks the active
CC site catalytic triad characteristic of thiol proteases, with residues
CC at the equivalent structural positions that are incompatible with
CC catalysis, and it cannot bind ubiquitin. It functions as a structural
CC scaffold for intra- and intermolecular interactions in the complex.
CC {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:24880344}.
CC -!- DOMAIN: The linker, or PAN3 interaction domain (PID), between the WD40
CC repeats and the pseudo-UCH domain mediates interaction with PAN3.
CC {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:24872509}.
CC -!- MISCELLANEOUS: Present with 1510 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. PAN2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03182}.
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DR EMBL; U39204; AAC49152.1; -; Genomic_DNA.
DR EMBL; Z72616; CAA96800.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08012.1; -; Genomic_DNA.
DR PIR; S64101; S64101.
DR RefSeq; NP_011421.1; NM_001180959.1.
DR PDB; 4Q8G; X-ray; 2.10 A; A/B=416-870.
DR PDB; 4Q8H; X-ray; 3.10 A; A=460-1115.
DR PDB; 4XR7; X-ray; 3.80 A; A/D/G/J=340-1115.
DR PDB; 6R5K; EM; 4.80 A; A=1-1115.
DR PDB; 6R9I; X-ray; 3.00 A; A=461-1115.
DR PDB; 6R9J; X-ray; 3.33 A; A=461-1115.
DR PDB; 6R9M; X-ray; 3.33 A; A=461-1115.
DR PDB; 6R9O; X-ray; 3.32 A; A=461-1115.
DR PDB; 6R9P; X-ray; 2.98 A; A=461-1115.
DR PDB; 6R9Q; X-ray; 3.08 A; A=461-1115.
DR PDBsum; 4Q8G; -.
DR PDBsum; 4Q8H; -.
DR PDBsum; 4XR7; -.
DR PDBsum; 6R5K; -.
DR PDBsum; 6R9I; -.
DR PDBsum; 6R9J; -.
DR PDBsum; 6R9M; -.
DR PDBsum; 6R9O; -.
DR PDBsum; 6R9P; -.
DR PDBsum; 6R9Q; -.
DR AlphaFoldDB; P53010; -.
DR SMR; P53010; -.
DR BioGRID; 33157; 134.
DR ComplexPortal; CPX-3294; PAN deadenylation complex.
DR DIP; DIP-2466N; -.
DR IntAct; P53010; 6.
DR MINT; P53010; -.
DR STRING; 4932.YGL094C; -.
DR iPTMnet; P53010; -.
DR MaxQB; P53010; -.
DR PaxDb; P53010; -.
DR PRIDE; P53010; -.
DR EnsemblFungi; YGL094C_mRNA; YGL094C; YGL094C.
DR GeneID; 852786; -.
DR KEGG; sce:YGL094C; -.
DR SGD; S000003062; PAN2.
DR VEuPathDB; FungiDB:YGL094C; -.
DR eggNOG; KOG1275; Eukaryota.
DR GeneTree; ENSGT00390000013978; -.
DR HOGENOM; CLU_002369_1_0_1; -.
DR InParanoid; P53010; -.
DR OMA; TQELLWT; -.
DR BioCyc; YEAST:G3O-30594-MON; -.
DR PRO; PR:P53010; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53010; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0031251; C:PAN complex; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IDA:SGD.
DR GO; GO:0006301; P:postreplication repair; IGI:SGD.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_03182; PAN2; 1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR030843; PAN2.
DR InterPro; IPR028881; PAN2_UCH_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF00929; RNase_T; 1.
DR Pfam; PF13423; UCH_1; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Exonuclease; Hydrolase;
KW Metal-binding; mRNA processing; Nuclease; Reference proteome; Repeat;
KW WD repeat.
FT CHAIN 1..1115
FT /note="PAN2-PAN3 deadenylation complex catalytic subunit
FT PAN2"
FT /id="PRO_0000058222"
FT REPEAT 27..66
FT /note="WD 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 112..153
FT /note="WD 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 155..194
FT /note="WD 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 197..236
FT /note="WD 4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 295..334
FT /note="WD 5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT DOMAIN 474..855
FT /note="USP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182,
FT ECO:0000305|PubMed:24880344"
FT DOMAIN 907..1079
FT /note="Exonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REGION 337..473
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182,
FT ECO:0000305|PubMed:24880344"
FT BINDING 660
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24880344,
FT ECO:0007744|PDB:4Q8G"
FT BINDING 662
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24880344,
FT ECO:0007744|PDB:4Q8G"
FT BINDING 713
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24880344,
FT ECO:0007744|PDB:4Q8G"
FT BINDING 716
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24880344,
FT ECO:0007744|PDB:4Q8G"
FT BINDING 910
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-
FT Rule:MF_03182, ECO:0000305|PubMed:24880344"
FT BINDING 912
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-
FT Rule:MF_03182, ECO:0000305|PubMed:24880344"
FT BINDING 1020
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-
FT Rule:MF_03182"
FT BINDING 1071
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-
FT Rule:MF_03182, ECO:0000305|PubMed:24880344"
FT MUTAGEN 912
FT /note="E->A: Abolishes nuclease activity."
FT /evidence="ECO:0000269|PubMed:24872509"
FT MUTAGEN 1020
FT /note="D->A: Abolishes nuclease activity."
FT /evidence="ECO:0000269|PubMed:24880344"
FT TURN 460..465
FT /evidence="ECO:0007829|PDB:4Q8H"
FT STRAND 470..474
FT /evidence="ECO:0007829|PDB:6R9P"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:4Q8G"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:4Q8G"
FT HELIX 497..499
FT /evidence="ECO:0007829|PDB:4Q8G"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:4Q8G"
FT TURN 512..515
FT /evidence="ECO:0007829|PDB:4Q8G"
FT HELIX 516..524
FT /evidence="ECO:0007829|PDB:4Q8G"
FT HELIX 527..536
FT /evidence="ECO:0007829|PDB:4Q8G"
FT HELIX 546..559
FT /evidence="ECO:0007829|PDB:4Q8G"
FT STRAND 560..562
FT /evidence="ECO:0007829|PDB:4Q8G"
FT HELIX 568..576
FT /evidence="ECO:0007829|PDB:4Q8G"
FT HELIX 587..589
FT /evidence="ECO:0007829|PDB:6R9I"
FT HELIX 590..595
FT /evidence="ECO:0007829|PDB:6R9P"
FT TURN 598..600
FT /evidence="ECO:0007829|PDB:6R9P"
FT TURN 603..605
FT /evidence="ECO:0007829|PDB:4Q8H"
FT STRAND 610..613
FT /evidence="ECO:0007829|PDB:4Q8H"
FT HELIX 618..636
FT /evidence="ECO:0007829|PDB:4Q8G"
FT STRAND 637..639
FT /evidence="ECO:0007829|PDB:4Q8G"
FT HELIX 643..648
FT /evidence="ECO:0007829|PDB:4Q8G"
FT STRAND 650..657
FT /evidence="ECO:0007829|PDB:4Q8G"
FT STRAND 659..661
FT /evidence="ECO:0007829|PDB:4Q8G"
FT STRAND 666..675
FT /evidence="ECO:0007829|PDB:4Q8G"
FT TURN 684..686
FT /evidence="ECO:0007829|PDB:6R9Q"
FT HELIX 696..703
FT /evidence="ECO:0007829|PDB:4Q8G"
FT STRAND 704..712
FT /evidence="ECO:0007829|PDB:4Q8G"
FT TURN 714..716
FT /evidence="ECO:0007829|PDB:4Q8G"
FT STRAND 719..728
FT /evidence="ECO:0007829|PDB:4Q8G"
FT STRAND 733..739
FT /evidence="ECO:0007829|PDB:4Q8G"
FT HELIX 743..751
FT /evidence="ECO:0007829|PDB:4Q8G"
FT STRAND 752..754
FT /evidence="ECO:0007829|PDB:6R9P"
FT STRAND 758..765
FT /evidence="ECO:0007829|PDB:4Q8G"
FT STRAND 768..774
FT /evidence="ECO:0007829|PDB:4Q8G"
FT HELIX 775..777
FT /evidence="ECO:0007829|PDB:4Q8G"
FT STRAND 782..797
FT /evidence="ECO:0007829|PDB:4Q8G"
FT STRAND 803..813
FT /evidence="ECO:0007829|PDB:4Q8G"
FT TURN 814..817
FT /evidence="ECO:0007829|PDB:4Q8G"
FT STRAND 818..825
FT /evidence="ECO:0007829|PDB:4Q8G"
FT STRAND 828..832
FT /evidence="ECO:0007829|PDB:4Q8G"
FT HELIX 834..838
FT /evidence="ECO:0007829|PDB:4Q8G"
FT STRAND 845..854
FT /evidence="ECO:0007829|PDB:4Q8G"
FT HELIX 857..859
FT /evidence="ECO:0007829|PDB:4Q8G"
FT HELIX 865..867
FT /evidence="ECO:0007829|PDB:6R9I"
FT HELIX 873..875
FT /evidence="ECO:0007829|PDB:6R9P"
FT HELIX 897..899
FT /evidence="ECO:0007829|PDB:6R9Q"
FT STRAND 906..915
FT /evidence="ECO:0007829|PDB:6R9P"
FT STRAND 937..945
FT /evidence="ECO:0007829|PDB:6R9P"
FT STRAND 948..952
FT /evidence="ECO:0007829|PDB:6R9P"
FT STRAND 956..962
FT /evidence="ECO:0007829|PDB:6R9P"
FT HELIX 973..976
FT /evidence="ECO:0007829|PDB:6R9I"
FT STRAND 983..986
FT /evidence="ECO:0007829|PDB:6R9P"
FT STRAND 988..990
FT /evidence="ECO:0007829|PDB:6R9P"
FT HELIX 995..1008
FT /evidence="ECO:0007829|PDB:6R9P"
FT STRAND 1011..1016
FT /evidence="ECO:0007829|PDB:6R9P"
FT HELIX 1017..1023
FT /evidence="ECO:0007829|PDB:6R9P"
FT HELIX 1030..1032
FT /evidence="ECO:0007829|PDB:6R9P"
FT STRAND 1033..1035
FT /evidence="ECO:0007829|PDB:6R9P"
FT HELIX 1036..1039
FT /evidence="ECO:0007829|PDB:6R9P"
FT STRAND 1043..1045
FT /evidence="ECO:0007829|PDB:6R9I"
FT HELIX 1050..1055
FT /evidence="ECO:0007829|PDB:6R9P"
FT STRAND 1056..1058
FT /evidence="ECO:0007829|PDB:6R9J"
FT STRAND 1063..1065
FT /evidence="ECO:0007829|PDB:6R9J"
FT HELIX 1068..1087
FT /evidence="ECO:0007829|PDB:6R9P"
FT TURN 1088..1090
FT /evidence="ECO:0007829|PDB:6R9O"
FT HELIX 1091..1101
FT /evidence="ECO:0007829|PDB:6R9P"
FT TURN 1102..1107
FT /evidence="ECO:0007829|PDB:6R9P"
SQ SEQUENCE 1115 AA; 127039 MW; 4F91B737F761AE5A CRC64;
MNNWQHFFNN PVDLSEHLKK PYFRFDNRDK EITAISFDEK ANLIWSGDSY GCISSYDPTF
QLYTRYRGHI GGNSVKDILS HRDGILSISE DSLHFANRRG VTKLNLTSID IAAFSELNTM
CYSPHSLKNN IYCGGDNTNW GIASIDLNRG CLDSLLNYSS KVKLMCSNNK VLSIGRQTGT
VDLLDPTSNR TIKSFNAHSA SISAMDLRDN TLVTVGKSKR FYNLYADPFV NVYDLRTMRQ
LPPVSFSKGT TMGSGGADFV QLHPLLPTVM IVASSSGSFD FIDLSNPTLR TQYVHPCQSI
KKLCLSPNGD VLGILEADNH LDTWRRSSNN MGMFTNTPEM LAYPDYFNDI TSDGPISVDD
ETYPLSSVGM PYYLDKLLSA WPPVVFKSEG TIPQLTGKSP LPSSGKLKSN LAVISSQNEK
LSTQEFPLLR YDRTKYGMRN AIPDYVCLRD IRKQITSGLE TSDIQTYTSI NKYEVPPAYS
RLPLTSGRFG TDNFDFTPFN NTEYSGLDPD VDNHYTNAII QLYRFIPEMF NFVVGCLKDE
NFETTLLTDL GYLFDMMERS HGKICSSSNF QASLKSLTDK RQLENGEPQE HLEEYLESLC
IRESIEDFNS SESIKRNMPQ KFNRFLLSQL IKEEAQTVNH NITLNQCFGL ETEIRTECSC
DHYDTTVKLL PSLSISGINK TVIKQLNKKS NGQNILPYIE YAMKNVTQKN SICPTCGKTE
TITQECTVKN LPSVLSLELS LLDTEFSNIR SSKNWLTSEF YGSIIKNKAV LRSTASELKG
TSHIFKYELN GYVAKITDNN NETRLVTYVK KYNPKENCFK WLMFNDYLVV EITEEEALKM
TYPWKTPEII IYCDAEELRK PFFSVDTYSI NYDILFRDYF ANGIRDTARR EYKLLTHDEA
PKSGTLVAID AEFVSLQSEL CEIDHQGIRS IIRPKRTALA RISIIRGEEG ELYGVPFVDD
YVVNTNHIED YLTRYSGILP GDLDPEKSTK RLVRRNVVYR KVWLLMQLGC VFVGHGLNND
FKHININVPR NQIRDTAIYF LQGKRYLSLR YLAYVLLGMN IQEGNHDSIE DAHTALILYK
KYLHLKEKAI FEKVLNSVYE EGRAHNFKVP ETSKG
