ID   MDN1_YEAST              Reviewed;        4910 AA.
AC   Q12019; D6VYA6; Q7LGX0;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 198.
DE   RecName: Full=Midasin;
DE   AltName: Full=Dynein-related AAA-ATPase REA1;
DE   AltName: Full=MIDAS-containing protein;
DE   AltName: Full=Ribosome export/assembly protein 1;
GN   Name=MDN1; Synonyms=REA1; OrderedLocusNames=YLR106C;
GN   ORFNames=L2901, L8004.13;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-115.
RC   STRAIN=ATCC 90840 / EAY235 / FY23;
RX   PubMed=9090053;
RX   DOI=10.1002/(sici)1097-0061(19970315)13:3<241::aid-yea61>3.0.co;2-#;
RA   Verhasselt P., Volckaert G.;
RT   "Sequence analysis of a 37.6 kbp cosmid clone from the right arm of
RT   Saccharomyces cerevisiae chromosome XII, carrying YAP3, HOG1, SNR6, tRNA-
RT   Arg3 and 23 new open reading frames, among which several homologies to
RT   proteins involved in cell division control and to mammalian growth factors
RT   and other animal proteins are found.";
RL   Yeast 13:241-250(1997).
RN   [4]
RP   SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=11583615; DOI=10.1016/s1097-2765(01)00342-2;
RA   Bassler J., Grandi P., Gadal O., Lessmann T., Petfalski E., Tollervey D.,
RA   Lechner J., Hurt E.;
RT   "Identification of a 60S preribosomal particle that is closely linked to
RT   nuclear export.";
RL   Mol. Cell 8:517-529(2001).
RN   [5]
RP   CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX   PubMed=12102729; DOI=10.1186/1471-2164-3-18;
RA   Garbarino J.E., Gibbons I.R.;
RT   "Expression and genomic analysis of midasin, a novel and highly conserved
RT   AAA protein distantly related to dynein.";
RL   BMC Genomics 3:18-18(2002).
RN   [6]
RP   IDENTIFICATION IN PRE-60S RIBOSOMES, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=12374754; DOI=10.1093/emboj/cdf547;
RA   Nissan T.A., Bassler J., Petfalski E., Tollervey D., Hurt E.;
RT   "60S pre-ribosome formation viewed from assembly in the nucleolus until
RT   export to the cytoplasm.";
RL   EMBO J. 21:5539-5547(2002).
RN   [7]
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   [8]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15528184; DOI=10.1074/jbc.m406876200;
RA   Galani K., Nissan T.A., Petfalski E., Tollervey D., Hurt E.;
RT   "Rea1, a dynein-related nuclear AAA-ATPase, is involved in late rRNA
RT   processing and nuclear export of 60 S subunits.";
RL   J. Biol. Chem. 279:55411-55418(2004).
RN   [9]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=15260980; DOI=10.1016/j.molcel.2004.06.033;
RA   Nissan T.A., Galani K., Maco B., Tollervey D., Aebi U., Hurt E.;
RT   "A pre-ribosome with a tadpole-like structure functions in ATP-dependent
RT   maturation of 60S subunits.";
RL   Mol. Cell 15:295-301(2004).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1026; SER-2971; SER-4353 AND
RP   THR-4388, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [11]
RP   FUNCTION, ASSOCIATION WITH THE PRE-60S PARTICLE, AND INTERACTION WITH RSA4.
RX   PubMed=19737519; DOI=10.1016/j.cell.2009.06.045;
RA   Ulbrich C., Diepholz M., Bassler J., Kressler D., Pertschy B., Galani K.,
RA   Bottcher B., Hurt E.;
RT   "Mechanochemical removal of ribosome biogenesis factors from nascent 60S
RT   ribosomal subunits.";
RL   Cell 138:911-922(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2971 AND SER-4555, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [13]
RP   FUNCTION, INTERACTION WITH RSA4 AND YTM1, AND SUBCELLULAR LOCATION.
RX   PubMed=20542003; DOI=10.1016/j.molcel.2010.05.024;
RA   Bassler J., Kallas M., Pertschy B., Ulbrich C., Thoms M., Hurt E.;
RT   "The AAA-ATPase Rea1 drives removal of biogenesis factors during multiple
RT   stages of 60S ribosome assembly.";
RL   Mol. Cell 38:712-721(2010).
RN   [14]
RP   FUNCTION.
RX   PubMed=24240281; DOI=10.1038/nature12731;
RA   Matsuo Y., Granneman S., Thoms M., Manikas R.G., Tollervey D., Hurt E.;
RT   "Coupled GTPase and remodelling ATPase activities form a checkpoint for
RT   ribosome export.";
RL   Nature 505:112-116(2014).
RN   [15]
RP   STRUCTURE BY ELECTRON MICROSCOPY (9.50 ANGSTROMS), AND INTERACTION WITH
RP   RIX1.
RX   PubMed=26619264; DOI=10.1038/nsmb.3132;
RA   Barrio-Garcia C., Thoms M., Flemming D., Kater L., Berninghausen O.,
RA   Bassler J., Beckmann R., Hurt E.;
RT   "Architecture of the Rix1-Rea1 checkpoint machinery during pre-60S-ribosome
RT   remodeling.";
RL   Nat. Struct. Mol. Biol. 23:37-44(2016).
CC   -!- FUNCTION: Nuclear chaperone required for maturation and nuclear export
CC       of pre-60S ribosome subunits. Functions at successive maturation steps
CC       to remove ribosomal factors at critical transition points, first
CC       driving the exit of early pre-60S particles from the nucleolus and then
CC       driving late pre-60S particles from the nucleus (PubMed:15260980,
CC       PubMed:15528184, PubMed:19737519, PubMed:20542003). At an early stage
CC       in 60S maturation, mediates the dissociation of the NOP7 complex (YTM1-
CC       ERB1-NOP7) from early pre-60S particles, rendering them competent for
CC       export from the nucleolus to the nucleoplasm (PubMed:20542003).
CC       Subsequently recruited to the nucleoplasmic particles through
CC       interaction with the RIX1 complex. This binding is only possible if the
CC       5S RNP at the central protuberance has undergone the rotation to
CC       complete its maturation (PubMed:26619264). After remodeling, removes
CC       the ribosome biogenesis factor RSA4 in an ATP hydrolysis-driven step
CC       from pre-60S ribosomal subunits, rendering them competent for export
CC       from the nucleoplasm to the cytoplasm (PubMed:19737519,
CC       PubMed:20542003). Activates the GTPase activity of NOG2, which
CC       disengages from the pre-60S particle upon GTP hydrolysis, thus freeing
CC       its binding site for the nuclear export factor NMD3 (PubMed:24240281).
CC       {ECO:0000269|PubMed:15260980, ECO:0000269|PubMed:15528184,
CC       ECO:0000269|PubMed:19737519, ECO:0000269|PubMed:20542003,
CC       ECO:0000269|PubMed:24240281, ECO:0000269|PubMed:26619264}.
CC   -!- SUBUNIT: Associates with pre-60S ribosomes in the nucleoplasm
CC       (PubMed:11583615, PubMed:12374754, PubMed:15260980, PubMed:19737519).
CC       Interacts (via its hexameric AAA ATPase ring) with the RIX1 complex
CC       (via RIX1); this interaction is crucial for recruitment of MDN1 to the
CC       pre-ribosomal particle (PubMed:15260980, PubMed:26619264). Interacts
CC       (via VWFA/MIDAS domain) with YTM1 (via UBL domain) (PubMed:20542003).
CC       Interacts (via VWFA/MIDAS domain) with RSA4 (via UBL domain)
CC       (PubMed:19737519, PubMed:20542003). {ECO:0000269|PubMed:11583615,
CC       ECO:0000269|PubMed:12374754, ECO:0000269|PubMed:15260980,
CC       ECO:0000269|PubMed:19737519, ECO:0000269|PubMed:20542003,
CC       ECO:0000269|PubMed:26619264}.
CC   -!- INTERACTION:
CC       Q12019; P25382: RSA4; NbExp=5; IntAct=EBI-10633, EBI-21980;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11583615,
CC       ECO:0000269|PubMed:12102729, ECO:0000269|PubMed:15528184}. Nucleus,
CC       nucleolus {ECO:0000269|PubMed:20542003}. Nucleus, nucleoplasm
CC       {ECO:0000269|PubMed:15528184}.
CC   -!- DOMAIN: The protein has several distinct domains, an N-terminal
CC       extension (35 kDa), followed by an ATPase domain containing a hexameric
CC       ring of six tandem AAA protomers (between 28 and 40 kDa each), a linker
CC       domain (260 kDa), an Asp/Glu-rich domain (approximately 70 kDa) and a
CC       C-terminal VWFA domain (30 kDa) that possesses a MIDAS (metal ion-
CC       dependent adhesion site). The ring-like ATPase head domain associates
CC       with the RIX1 complex on the pre-ribosome, while the flexible tail
CC       protrudes from the molecule. {ECO:0000305|PubMed:26619264}.
CC   -!- MISCELLANEOUS: Present with 538 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the midasin family. {ECO:0000305}.
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DR   EMBL; U53876; AAB67548.1; -; Genomic_DNA.
DR   EMBL; Z73278; CAA97671.1; -; Genomic_DNA.
DR   EMBL; X89514; CAA61684.1; -; Genomic_DNA.
DR   EMBL; Z73279; CAA97673.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09422.1; -; Genomic_DNA.
DR   PIR; S64942; S64942.
DR   RefSeq; NP_013207.1; NM_001181993.1.
DR   PDB; 5JCS; EM; 9.50 A; s=1-4910.
DR   PDB; 6HYD; EM; 3.90 A; A=2356-4041.
DR   PDB; 6HYP; EM; 4.40 A; A=238-4910.
DR   PDB; 6I26; EM; 4.30 A; A=238-4910.
DR   PDB; 6I27; EM; 7.80 A; A=238-4910.
DR   PDB; 6YLF; EM; 4.20 A; AP1=1-4910.
DR   PDB; 6YLH; EM; 3.10 A; v=1-4910.
DR   PDBsum; 5JCS; -.
DR   PDBsum; 6HYD; -.
DR   PDBsum; 6HYP; -.
DR   PDBsum; 6I26; -.
DR   PDBsum; 6I27; -.
DR   PDBsum; 6YLF; -.
DR   PDBsum; 6YLH; -.
DR   EMDB; EMD-0308; -.
DR   EMDB; EMD-0309; -.
DR   EMDB; EMD-0328; -.
DR   EMDB; EMD-0329; -.
DR   EMDB; EMD-10837; -.
DR   EMDB; EMD-10839; -.
DR   SMR; Q12019; -.
DR   BioGRID; 31379; 180.
DR   DIP; DIP-6285N; -.
DR   IntAct; Q12019; 43.
DR   MINT; Q12019; -.
DR   STRING; 4932.YLR106C; -.
DR   iPTMnet; Q12019; -.
DR   MaxQB; Q12019; -.
DR   PaxDb; 4932-YLR106C; -.
DR   PeptideAtlas; Q12019; -.
DR   EnsemblFungi; YLR106C_mRNA; YLR106C; YLR106C.
DR   GeneID; 850796; -.
DR   KEGG; sce:YLR106C; -.
DR   AGR; SGD:S000004096; -.
DR   SGD; S000004096; MDN1.
DR   VEuPathDB; FungiDB:YLR106C; -.
DR   eggNOG; KOG1808; Eukaryota.
DR   GeneTree; ENSGT00550000074802; -.
DR   HOGENOM; CLU_000050_0_2_1; -.
DR   InParanoid; Q12019; -.
DR   OMA; ILEQWHR; -.
DR   OrthoDB; 1221059at2759; -.
DR   BioCyc; YEAST:G3O-32254-MONOMER; -.
DR   BioGRID-ORCS; 850796; 0 hits in 10 CRISPR screens.
DR   PRO; PR:Q12019; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q12019; Protein.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR   GO; GO:0110136; P:protein-RNA complex remodeling; IDA:SGD.
DR   GO; GO:2000200; P:regulation of ribosomal subunit export from nucleus; IMP:SGD.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD.
DR   GO; GO:0000055; P:ribosomal large subunit export from nucleus; IBA:GO_Central.
DR   GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR   CDD; cd00009; AAA; 2.
DR   CDD; cd01460; vWA_midasin; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 6.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR040848; AAA_lid_7.
DR   InterPro; IPR011704; ATPase_dyneun-rel_AAA.
DR   InterPro; IPR048617; MDN1_AAA_lid_4.
DR   InterPro; IPR012099; Midasin.
DR   InterPro; IPR041190; Midasin_AAA_lid_5.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR48103:SF2; MIDASIN; 1.
DR   PANTHER; PTHR48103; MIDASIN-RELATED; 1.
DR   Pfam; PF07728; AAA_5; 8.
DR   Pfam; PF17865; AAA_lid_5; 1.
DR   Pfam; PF17867; AAA_lid_7; 3.
DR   Pfam; PF21108; MDN1_4th; 1.
DR   PIRSF; PIRSF010340; Midasin; 1.
DR   SMART; SM00382; AAA; 6.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 6.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Chaperone; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..4910
FT                   /note="Midasin"
FT                   /id="PRO_0000096337"
FT   DOMAIN          4704..4899
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   REGION          305..528
FT                   /note="AAA-ATPase protomer 1"
FT                   /evidence="ECO:0000255"
FT   REGION          636..975
FT                   /note="AAA-ATPase protomer 2"
FT                   /evidence="ECO:0000255"
FT   REGION          695..803
FT                   /note="Interaction with RIX1"
FT                   /evidence="ECO:0000269|PubMed:26619264"
FT   REGION          1054..1280
FT                   /note="AAA-ATPase protomer 3"
FT                   /evidence="ECO:0000255"
FT   REGION          1345..1624
FT                   /note="AAA-ATPase protomer 4"
FT                   /evidence="ECO:0000255"
FT   REGION          1732..1985
FT                   /note="AAA-ATPase protomer 5"
FT                   /evidence="ECO:0000255"
FT   REGION          2036..2286
FT                   /note="AAA-ATPase protomer 6"
FT                   /evidence="ECO:0000255"
FT   REGION          2372..4075
FT                   /note="Linker"
FT                   /evidence="ECO:0000305|PubMed:26619264"
FT   REGION          4045..4600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4099..4152
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4153..4205
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4206..4248
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4255..4276
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4277..4302
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4303..4351
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4352..4382
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4395..4430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4431..4449
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4456..4497
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4498..4517
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4518..4556
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4557..4598
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         315..322
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         653..660
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         1083..1090
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         1368..1375
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         1747..1754
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2054..2061
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1026
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         2971
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         4353
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         4388
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         4555
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   4910 AA;  559308 MW;  E4E873BEDF6E1E5B CRC64;
     MSQDRILLDL DVVNQRLILF NSAFPSDAIE APFHFSNKES TSENLDNLAG TILHSRSITG
     HVFLYKHIFL EIVARWIKDS KKKDYVLVIE KLASIITIFP VAMPLIEDYL DKENDHFITI
     LQNPSTQKDS DMFKILLAYY RLLYHNKEVF ARFIQPDILY QLVDLLTKEQ ENQVVIFLAL
     KVLSLYLDMG EKTLNDMLDT YIKSRDSLLG HFEGDSGIDY SFLELNEAKR CANFSKLPSV
     PECFTIEKKS SYFIIEPQDL STKVASICGV IVPKVHTIHD KVFYPLTFVP THKTVSSLRQ
     LGRKIQNSTP IMLIGKAGSG KTFLINELSK YMGCHDSIVK IHLGEQTDAK LLIGTYTSGD
     KPGTFEWRAG VLATAVKEGR WVLIEDIDKA PTDVLSILLS LLEKRELTIP SRGETVKAAN
     GFQLISTVRI NEDHQKDSSN KIYNLNMIGM RIWNVIELEE PSEEDLTHIL AQKFPILTNL
     IPKLIDSYKN VKSIYMNTKF ISLNKGAHTR VVSVRDLIKL CERLDILFKN NGINKPDQLI
     QSSVYDSIFS EAADCFAGAI GEFKALEPII QAIGESLDIA SSRISLFLTQ HVPTLENLDD
     SIKIGRAVLL KEKLNIQKKS MNSTLFAFTN HSLRLMEQIS VCIQMTEPVL LVGETGTGKT
     TVVQQLAKML AKKLTVINVS QQTETGDLLG GYKPVNSKTV AVPIQENFET LFNATFSLKK
     NEKFHKMLHR CFNKNQWKNV VKLWNEAYKM AQSILKITNT ENENENAKKK KRRLNTHEKK
     LLLDKWADFN DSVKKFEAQS SSIENSFVFN FVEGSLVKTI RAGEWLLLDE VNLATADTLE
     SISDLLTEPD SRSILLSEKG DAEPIKAHPD FRIFACMNPA TDVGKRDLPM GIRSRFTEIY
     VHSPERDITD LLSIIDKYIG KYSVSDEWVG NDIAELYLEA KKLSDNNTIV DGSNQKPHFS
     IRTLTRTLLY VTDIIHIYGL RRSLYDGFCM SFLTLLDQKS EAILKPVIEK FTLGRLKNVK
     SIMSQTPPSP GPDYVQFKHY WMKKGPNTIQ EQAHYIITPF VEKNMMNLVR ATSGKRFPVL
     IQGPTSSGKT SMIKYLADIT GHKFVRINNH EHTDLQEYLG TYVTDDTGKL SFKEGVLVEA
     LRKGYWIVLD ELNLAPTDVL EALNRLLDDN RELFIPETQE VVHPHPDFLL FATQNPPGIY
     GGRKILSRAF RNRFLELHFD DIPQDELEII LRERCQIAPS YAKKIVEVYR QLSIERSASR
     LFEQKNSFAT LRDLFRWALR DAVGYEQLAA SGYMLLAERC RTPQEKVTVK KTLEKVMKVK
     LDMDQYYASL EDKSLEAIGS VTWTKGMRRL SVLVSSCLKN KEPVLLVGET GCGKTTICQL
     LAQFMGRELI TLNAHQNTET GDILGAQRPV RNRSEIQYKL IKSLKTALNI ANDQDVDLKE
     LLQLYSKSDN KNIAEDVQLE IQKLRDSLNV LFEWSDGPLI QAMRTGNFFL LDEISLADDS
     VLERLNSVLE PERSLLLAEQ GSSDSLVTAS ENFQFFATMN PGGDYGKKEL SPALRNRFTE
     IWVPSMEDFN DVNMIVSSRL LEDLKDLANP IVKFSEWFGK KLGGGNATSG VISLRDILAW
     VEFINKVFPK IQNKSTALIQ GASMVFIDAL GTNNTAYLAE NENDLKSLRT ECIIQLLKLC
     GDDLELQQIE TNEIIVTQDE LQVGMFKIPR FPDAQSSSFN LTAPTTASNL VRVVRAMQVH
     KPILLEGSPG VGKTSLITAL ANITGNKLTR INLSEQTDLV DLFGADAPGE RSGEFLWHDA
     PFLRAMKKGE WVLLDEMNLA SQSVLEGLNA CLDHRGEAYI PELDISFSCH PNFLVFAAQN
     PQYQGGGRKG LPKSFVNRFS VVFIDMLTSD DLLLIAKHLY PSIEPDIIAK MIKLMSTLED
     QVCKRKLWGN SGSPWEFNLR DTLRWLKLLN QYSICEDVDV FDFVDIIVKQ RFRTISDKNK
     AQLLIEDIFG KFSTKENFFK LTEDYVQINN EVALRNPHYR YPITQNLFPL ECNVAVYESV
     LKAINNNWPL VLVGPSNSGK TETIRFLASI LGPRVDVFSM NSDIDSMDIL GGYEQVDLTR
     QISYITEELT NIVREIISMN MKLSPNATAI MEGLNLLKYL LNNIVTPEKF QDFRNRFNRF
     FSHLEGHPLL KTMSMNIEKM TEIITKEASV KFEWFDGMLV KAVEKGHWLI LDNANLCSPS
     VLDRLNSLLE IDGSLLINEC SQEDGQPRVL KPHPNFRLFL TMDPKYGELS RAMRNRGVEI
     YIDELHSRST AFDRLTLGFE LGENIDFVSI DDGIKKIKLN EPDMSIPLKH YVPSYLSRPC
     IFAQVHDILL LSDEEPIEES LAAVIPISHL GEVGKWANNV LNCTEYSEKK IAERLYVFIT
     FLTDMGVLEK INNLYKPANL KFQKALGLHD KQLTEETVSL TLNEYVLPTV SKYSDKIKSP
     ESLYLLSSLR LLLNSLNALK LINEKSTHGK IDELTYIELS AAAFNGRHLK NIPRIPIFCI
     LYNILTVMSE NLKTESLFCG SNQYQYYWDL LVIVIAALET AVTKDEARLR VYKELIDSWI
     ASVKSKSDIE ITPFLNINLE FTDVLQLSRG HSITLLWDIF RKNYPTTSNS WLAFEKLINL
     SEKFDKVRLL QFSESYNSIK DLMDVFRLLN DDVLNNKLSE FNLLLSKLED GINELELISN
     KFLNKRKHYF ADEFDNLIRY TFSVDTAELI KELAPASSLA TQKLTKLITN KYNYPPIFDV
     LWTEKNAKLT SFTSTIFSSQ FLEDVVRKSN NLKSFSGNQI KQSISDAELL LSSTIKCSPN
     LLKSQMEYYK NMLLSWLRKV IDIHVGGDCL KLTLKELCSL IEEKTASETR VTFAEYIFPA
     LDLAESSKSL EELGEAWITF GTGLLLLFVP DSPYDPAIHD YVLYDLFLKT KTFSQNLMKS
     WRNVRKVISG DEEIFTEKLI NTISDDDAPQ SPRVYRTGMS IDSLFDEWMA FLSSTMSSRQ
     IKELVSSYKC NSDQSDRRLE MLQQNSAHFL NRLESGYSKF ADLNDILAGY IYSINFGFDL
     LKLQKSKDRA SFQISPLWSM DPINISCAEN VLSAYHELSR FFKKGDMEDT SIEKVLMYFL
     TLFKFHKRDT NLLEIFEAAL YTLYSRWSVR RFRQEQEENE KSNMFKFNDN SDDYEADFRK
     LFPDYEDTAL VTNEKDISSP ENLDDIYFKL ADTYISVFDK DHDANFSSEL KSGAIITTIL
     SEDLKNTRIE ELKSGSLSAV INTLDAETQS FKNTEVFGNI DFYHDFSIPE FQKAGDIIET
     VLKSVLKLLK QWPEHATLKE LYRVSQEFLN YPIKTPLARQ LQKIEQIYTY LAEWEKYASS
     EVSLNNTVKL ITDLIVSWRK LELRTWKGLF NSEDAKTRKS IGKWWFYLYE SIVISNFVSE
     KKETAPNATL LVSSLNLFFS KSTLGEFNAR LDLVKAFYKH IQLIGLRSSK IAGLLHNTIK
     FYYQFKPLID ERITNGKKSL EKEIDDIILL ASWKDVNVDA LKQSSRKSHN NLYKIVRKYR
     DLLNGDAKTI IEAGLLYSNE NKLKLPTLKQ HFYEDPNLEA SKNLVKEIST WSMRAAPLRN
     IDTVASNMDS YLEKISSQEF PNFADLASDF YAEAERLRKE TPNVYTKENK KRLAYLKTQK
     SKLLGDALKE LRRIGLKVNF REDIQKVQSS TTTILANIAP FNNEYLNSSD AFFFKILDLL
     PKLRSAASNP SDDIPVAAIE RGMALAQSLM FSLITVRHPL SEFTNDYCKI NGMMLDLEHF
     TCLKGDIVHS SLKANVDNVR LFEKWLPSLL DYAAQTLSVI SKYSATSEQQ KILLDAKSTL
     SSFFVHFNSS RIFDSSFIES YSRFELFINE LLKKLENAKE TGNAFVFDII IEWIKANKGG
     PIKKEQKRGP SVEDVEQAFR RTFTSIILSF QKVIGDGIES ISETDDNWLS ASFKKVMVNV
     KLLRSSVVSK NIETALSLLK DFDFTTTESI YVKSVISFTL PVITRYYNAM TVVLERSRIY
     YTNTSRGMYI LSTILHSLAK NGFCSPQPPS EEVDDKNLQE GTGLGDGEGA QNNNKDVEQD
     EDLTEDAQNE NKEQQDKDER DDENEDDAVE MEGDMAGELE DLSNGEENDD EDTDSEEEEL
     DEEIDDLNED DPNAIDDKMW DDKASDNSKE KDTDQNLDGK NQEEDVQAAE NDEQQRDNKE
     GGDEDPNAPE DGDEEIENDE NAEEENDVGE QEDEVKDEEG EDLEANVPEI ETLDLPEDMN
     LDSEHEESDE DVDMSDGMPD DLNKEEVGNE DEEVKQESGI ESDNENDEPG PEEDAGETET
     ALDEEEGAEE DVDMTNDEGK EDEENGPEEQ AMSDEEELKQ DAAMEENKEK GGEQNTEGLD
     GVEEKADTED IDQEAAVQQD SGSKGAGADA TDTQEQDDVG GSGTTQNTYE EDQEDVTKNN
     EESREEATAA LKQLGDSMKE YHRRRQDIKE AQTNGEEDEN LEKNNERPDE FEHVEGANTE
     TDTQALGSAT QDQLQTIDED MAIDDDREEQ EVDQKELVED ADDEKMDIDE EEMLSDIDAH
     DANNDVDSKK SGFIGKRKSE EDFENELSNE HFSADQEDDS EIQSLIENIE DNPPDASASL
     TPERSLEESR ELWHKSEIST ADLVSRLGEQ LRLILEPTLA TKLKGDYKTG KRLNMKRIIP
     YIASQFRKDK IWLRRTKPSK RQYQIMIALD DSKSMSESKC VKLAFDSLCL VSKTLTQLEA
     GGLSIVKFGE NIKEVHSFDQ QFSNESGARA FQWFGFQETK TDVKKLVAES TKIFERARAM
     VHNDQWQLEI VISDGICEDH ETIQKLVRRA RENKIMLVFV IIDGITSNES ILDMSQVNYI
     PDQYGNPQLK ITKYLDTFPF EFYVVVHDIS ELPEMLSLIL RQYFTDLASS
//