GLD2_CAEEL
ID GLD2_CAEEL Reviewed; 1113 AA.
AC O17087; Q86S49; Q86S50; Q86S51;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Poly(A) RNA polymerase gld-2;
DE EC=2.7.7.19 {ECO:0000269|PubMed:12239571};
DE AltName: Full=Defective in germ line development protein 2;
GN Name=gld-2; ORFNames=ZC308.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH GLD-3, DOMAIN,
RP AND MUTAGENESIS OF ASP-608 AND GLU-875.
RX PubMed=12239571; DOI=10.1038/nature01039;
RA Wang L., Eckmann C.R., Kadyk L.C., Wickens M., Kimble J.;
RT "A regulatory cytoplasmic poly(A) polymerase in Caenorhabditis elegans.";
RL Nature 419:312-316(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION.
RX PubMed=9550713; DOI=10.1242/dev.125.10.1803;
RA Kadyk L.C., Kimble J.;
RT "Genetic regulation of entry into meiosis in Caenorhabditis elegans.";
RL Development 125:1803-1813(1998).
RN [4]
RP FUNCTION.
RX PubMed=14660440; DOI=10.1242/dev.00916;
RA Hansen D., Wilson-Berry L., Dang T., Schedl T.;
RT "Control of the proliferation versus meiotic development decision in the C.
RT elegans germline through regulation of GLD-1 protein accumulation.";
RL Development 131:93-104(2004).
RN [5]
RP FUNCTION.
RX PubMed=15063172; DOI=10.1016/j.ydbio.2003.12.023;
RA Hansen D., Hubbard E.J.A., Schedl T.;
RT "Multi-pathway control of the proliferation versus meiotic development
RT decision in the Caenorhabditis elegans germline.";
RL Dev. Biol. 268:342-357(2004).
RN [6]
RP INTERACTION WITH GLD-3.
RX PubMed=15454534; DOI=10.1534/genetics.104.029264;
RA Eckmann C.R., Crittenden S.L., Suh N., Kimble J.;
RT "GLD-3 and control of the mitosis/meiosis decision in the germline of
RT Caenorhabditis elegans.";
RL Genetics 168:147-160(2004).
RN [7]
RP FUNCTION.
RX PubMed=15514056; DOI=10.1534/genetics.104.029355;
RA Maine E.M., Hansen D., Springer D., Vought V.E.;
RT "Caenorhabditis elegans atx-2 promotes germline proliferation and the
RT oocyte fate.";
RL Genetics 168:817-830(2004).
RN [8]
RP RNA EDITING.
RX PubMed=15317977; DOI=10.1261/rna.7570804;
RA Wang L., Kimble J., Wickens M.;
RT "Tissue-specific modification of gld-2 mRNA in C. elegans: likely C-to-U
RT editing.";
RL RNA 10:1444-1448(2004).
RN [9]
RP FUNCTION.
RX PubMed=15911573; DOI=10.1534/genetics.105.042135;
RA Vought V.E., Ohmachi M., Lee M.-H., Maine E.M.;
RT "EGO-1, a putative RNA-directed RNA polymerase, promotes germline
RT proliferation in parallel with GLP-1/notch signaling and regulates the
RT spatial organization of nuclear pore complexes and germline P granules in
RT Caenorhabditis elegans.";
RL Genetics 170:1121-1132(2005).
RN [10]
RP FUNCTION.
RX PubMed=17012378; DOI=10.1073/pnas.0607050103;
RA Suh N., Jedamzik B., Eckmann C.R., Wickens M., Kimble J.;
RT "The GLD-2 poly(A) polymerase activates gld-1 mRNA in the Caenorhabditis
RT elegans germ line.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15108-15112(2006).
CC -!- FUNCTION: Cytoplasmic poly(A) RNA polymerase that adds successive AMP
CC monomers to the 3'-end of specific RNAs, forming a poly(A) tail. Acts
CC as a regulator of mitosis/meiosis required for progression through
CC meiotic prophase during oogenesis and spermatogenesis and for promotion
CC of the entry into meiosis from the mitotic cell cycle. May act by
CC regulating and activating gld-1 mRNA activity in germline.
CC {ECO:0000269|PubMed:12239571, ECO:0000269|PubMed:14660440,
CC ECO:0000269|PubMed:15063172, ECO:0000269|PubMed:15514056,
CC ECO:0000269|PubMed:15911573, ECO:0000269|PubMed:17012378,
CC ECO:0000269|PubMed:9550713}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
CC Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173115; EC=2.7.7.19;
CC Evidence={ECO:0000269|PubMed:12239571};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11333;
CC Evidence={ECO:0000269|PubMed:12239571};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with gld-3. {ECO:0000269|PubMed:12239571,
CC ECO:0000269|PubMed:15454534}.
CC -!- INTERACTION:
CC O17087; Q95ZK7: gld-3; NbExp=2; IntAct=EBI-2420017, EBI-317828;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12239571}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=a;
CC IsoId=O17087-1; Sequence=Displayed;
CC Name=b;
CC IsoId=O17087-2; Sequence=VSP_034328;
CC Name=c;
CC IsoId=O17087-3; Sequence=VSP_034329;
CC Name=d;
CC IsoId=O17087-4; Sequence=VSP_034330;
CC -!- TISSUE SPECIFICITY: Germline-specific. {ECO:0000269|PubMed:12239571}.
CC -!- DEVELOPMENTAL STAGE: Abundant in embryos, fourth larval stages and
CC adults. {ECO:0000269|PubMed:12239571}.
CC -!- DOMAIN: In contrast to other poly(A) RNA polymerases, lacks any RNA-
CC binding domain. RNA-binding is mediated through its interaction with
CC gld-3. {ECO:0000269|PubMed:12239571}.
CC -!- RNA EDITING: Modified_positions=400 {ECO:0000269|PubMed:15317977};
CC Note=Partially edited. RNA editing takes place in most germline-
CC specific transcripts.;
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family. GLD2
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY125085; AAM94369.1; -; mRNA.
DR EMBL; FO081588; CCD72658.1; -; Genomic_DNA.
DR EMBL; FO081588; CCD72659.1; -; Genomic_DNA.
DR EMBL; FO081588; CCD72660.1; -; Genomic_DNA.
DR EMBL; FO081588; CCD72661.1; -; Genomic_DNA.
DR PIR; T32274; T32274.
DR PIR; T32275; T32275.
DR RefSeq; NP_001021844.1; NM_001026673.1. [O17087-2]
DR RefSeq; NP_001021845.1; NM_001026674.1.
DR RefSeq; NP_491841.2; NM_059440.2. [O17087-3]
DR RefSeq; NP_491842.2; NM_059441.4. [O17087-1]
DR PDB; 4ZRL; X-ray; 2.28 A; A=528-923.
DR PDB; 5JNB; X-ray; 2.49 A; A/B/C/D=546-923.
DR PDBsum; 4ZRL; -.
DR PDBsum; 5JNB; -.
DR AlphaFoldDB; O17087; -.
DR SMR; O17087; -.
DR BioGRID; 37791; 11.
DR ComplexPortal; CPX-1214; GLD-2-GLD-3 complex.
DR IntAct; O17087; 2.
DR STRING; 6239.ZC308.1a; -.
DR EPD; O17087; -.
DR PaxDb; O17087; -.
DR PeptideAtlas; O17087; -.
DR PRIDE; O17087; -.
DR DNASU; 172338; -.
DR EnsemblMetazoa; ZC308.1a.1; ZC308.1a.1; WBGene00001596. [O17087-1]
DR EnsemblMetazoa; ZC308.1a.2; ZC308.1a.2; WBGene00001596. [O17087-1]
DR EnsemblMetazoa; ZC308.1b.1; ZC308.1b.1; WBGene00001596. [O17087-2]
DR EnsemblMetazoa; ZC308.1c.1; ZC308.1c.1; WBGene00001596. [O17087-3]
DR GeneID; 172338; -.
DR KEGG; cel:CELE_ZC308.1; -.
DR UCSC; ZC308.1a; c. elegans. [O17087-1]
DR CTD; 172338; -.
DR WormBase; ZC308.1a; CE32766; WBGene00001596; gld-2. [O17087-1]
DR WormBase; ZC308.1b; CE15159; WBGene00001596; gld-2. [O17087-2]
DR WormBase; ZC308.1c; CE33255; WBGene00001596; gld-2. [O17087-3]
DR WormBase; ZC308.1d; CE33256; WBGene00001596; gld-2. [O17087-4]
DR eggNOG; KOG2277; Eukaryota.
DR GeneTree; ENSGT00970000196213; -.
DR HOGENOM; CLU_009389_0_0_1; -.
DR InParanoid; O17087; -.
DR OMA; MEDWELD; -.
DR OrthoDB; 803033at2759; -.
DR BRENDA; 2.7.7.19; 1045.
DR PRO; PR:O17087; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001596; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; O17087; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IDA:WormBase.
DR GO; GO:0032991; C:protein-containing complex; IDA:WormBase.
DR GO; GO:0030880; C:RNA polymerase complex; EXP:ComplexPortal.
DR GO; GO:0031379; C:RNA-directed RNA polymerase complex; IPI:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IDA:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006378; P:mRNA polyadenylation; EXP:ComplexPortal.
DR GO; GO:0006397; P:mRNA processing; EXP:ComplexPortal.
DR GO; GO:0006997; P:nucleus organization; IMP:WormBase.
DR GO; GO:0060903; P:positive regulation of meiosis I; IGI:UniProtKB.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; EXP:ComplexPortal.
DR GO; GO:0051302; P:regulation of cell division; IMP:WormBase.
DR GO; GO:0031123; P:RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0043631; P:RNA polyadenylation; IDA:WormBase.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR045100; TUTase_dom.
DR Pfam; PF03828; PAP_assoc; 1.
DR Pfam; PF19088; TUTase; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm;
KW Developmental protein; Magnesium; Manganese; Meiosis; Metal-binding;
KW mRNA processing; Nucleotide-binding; Reference proteome; RNA editing;
KW Transferase.
FT CHAIN 1..1113
FT /note="Poly(A) RNA polymerase gld-2"
FT /id="PRO_0000341556"
FT DOMAIN 780..816
FT /note="PAP-associated"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..234
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..1072
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 606
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 608
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT VAR_SEQ 1..482
FT /note="MVMAQQQKNAERNDEHTRRNRSPSVDSVSRVQQQSGGFAFYNQQSNHQYQQS
FT HPRRTSFSRDGNTGYYNNHSGNKRQTYNNQRGGRSYNHRGNSNYQQNGEYSGNQGCVPK
FT YHQRNQNYPQLQPKYSYFQPHQRPIFNSTQGYGTYSVRRSSPPSPSALSSSTANSTSNR
FT APTQPPILLRHAEPASDKNHQGSDHEQNHDPKIHLYRSAGTAPGGYTQCPSPYKQPPPQ
FT PPSTPSSSDKRIEQQQAEDWPTRFQHPPPQFRRGQDPMPASIELQHKTANQTMPVDIVQ
FT TNQQKTVSSYERAAQFRASASELPTDSVDAKHPCFANERMQSALIGISPQLKTQQQSPG
FT IPIQNEAEASAVMKAMRSFQFHNWPQMSHGSYYPMPYHLENQMRPMKSGDQLPLNQQNH
FT NLSGFPAFVGKSSLVGSSLNTRNSSEADPEEMPRIMEKLDDEVTGADHDKTIDENRRRI
FT HKSQEPRIGTEEKALNE -> MPSSIICDVSHEGEASGGPSPSSRISNGFSHTVCDLHH
FT NFPIVKNRRKYHNSISTQSSSSTTTSLERISTSTCTSTSSSASDAIISRAEKDVQTFLV
FT SDESTTGDHEEEEEDDEDGDDESDHNDYDYEDDGERSEHDHEQTDNDDDEDEIEPFVSS
FT WCFAMGTQRSVMSSVGEKAPKSNVKSMEDWELDVVERAHRESHLAELYADLSWRFYTHP
FT PTSFCLARVFLRHGLTGNEGVSSWK (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_034328"
FT VAR_SEQ 1..334
FT /note="MVMAQQQKNAERNDEHTRRNRSPSVDSVSRVQQQSGGFAFYNQQSNHQYQQS
FT HPRRTSFSRDGNTGYYNNHSGNKRQTYNNQRGGRSYNHRGNSNYQQNGEYSGNQGCVPK
FT YHQRNQNYPQLQPKYSYFQPHQRPIFNSTQGYGTYSVRRSSPPSPSALSSSTANSTSNR
FT APTQPPILLRHAEPASDKNHQGSDHEQNHDPKIHLYRSAGTAPGGYTQCPSPYKQPPPQ
FT PPSTPSSSDKRIEQQQAEDWPTRFQHPPPQFRRGQDPMPASIELQHKTANQTMPVDIVQ
FT TNQQKTVSSYERAAQFRASASELPTDSVDAKHPCFANERMQSALIG -> MPLSTGSID
FT SGFFGCTTNDSLKKGDIEDPQKTTPLSMTDEEETFSTSSSGFSQSSAPPLGDAILSSSN
FT STSSYLTLNSGAYPRKHRTRVRRSNRKLKRLPQNMSMRFESSSLFSNTLTESLETASCC
FT VSVAGSSRSSLSSSSNSANASYDDMVIRLYFYFKSLLIAINHQKMICESIAYLVKDFDA
FT RWGNSGVRKKACDPKGCLAPIYTSSRNTDGGLDKKLVKPANFPMCWAVPQPAIFYQLMA
FT IDVVEYIKFLER (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_034329"
FT VAR_SEQ 1..334
FT /note="MVMAQQQKNAERNDEHTRRNRSPSVDSVSRVQQQSGGFAFYNQQSNHQYQQS
FT HPRRTSFSRDGNTGYYNNHSGNKRQTYNNQRGGRSYNHRGNSNYQQNGEYSGNQGCVPK
FT YHQRNQNYPQLQPKYSYFQPHQRPIFNSTQGYGTYSVRRSSPPSPSALSSSTANSTSNR
FT APTQPPILLRHAEPASDKNHQGSDHEQNHDPKIHLYRSAGTAPGGYTQCPSPYKQPPPQ
FT PPSTPSSSDKRIEQQQAEDWPTRFQHPPPQFRRGQDPMPASIELQHKTANQTMPVDIVQ
FT TNQQKTVSSYERAAQFRASASELPTDSVDAKHPCFANERMQSALIG -> MCWAVPQPA
FT IFYQLMAIDVVEYIKFLER (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_034330"
FT VARIANT 400
FT /note="P -> L (in RNA edited version)"
FT MUTAGEN 608
FT /note="D->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:12239571"
FT MUTAGEN 875
FT /note="E->K: In h292; induces defects in entry into meiosis
FT and abolishes interaction with gld-3."
FT /evidence="ECO:0000269|PubMed:12239571"
FT HELIX 548..560
FT /evidence="ECO:0007829|PDB:4ZRL"
FT HELIX 564..581
FT /evidence="ECO:0007829|PDB:4ZRL"
FT TURN 582..584
FT /evidence="ECO:0007829|PDB:4ZRL"
FT STRAND 589..593
FT /evidence="ECO:0007829|PDB:4ZRL"
FT HELIX 594..596
FT /evidence="ECO:0007829|PDB:4ZRL"
FT STRAND 605..612
FT /evidence="ECO:0007829|PDB:4ZRL"
FT TURN 620..622
FT /evidence="ECO:0007829|PDB:4ZRL"
FT HELIX 623..635
FT /evidence="ECO:0007829|PDB:4ZRL"
FT STRAND 641..647
FT /evidence="ECO:0007829|PDB:4ZRL"
FT STRAND 649..651
FT /evidence="ECO:0007829|PDB:4ZRL"
FT STRAND 653..658
FT /evidence="ECO:0007829|PDB:4ZRL"
FT HELIX 660..662
FT /evidence="ECO:0007829|PDB:4ZRL"
FT STRAND 666..672
FT /evidence="ECO:0007829|PDB:4ZRL"
FT HELIX 675..686
FT /evidence="ECO:0007829|PDB:4ZRL"
FT TURN 687..689
FT /evidence="ECO:0007829|PDB:4ZRL"
FT HELIX 693..706
FT /evidence="ECO:0007829|PDB:4ZRL"
FT STRAND 712..716
FT /evidence="ECO:0007829|PDB:4ZRL"
FT HELIX 719..732
FT /evidence="ECO:0007829|PDB:4ZRL"
FT STRAND 733..735
FT /evidence="ECO:0007829|PDB:4ZRL"
FT HELIX 741..744
FT /evidence="ECO:0007829|PDB:4ZRL"
FT TURN 746..748
FT /evidence="ECO:0007829|PDB:4ZRL"
FT STRAND 749..753
FT /evidence="ECO:0007829|PDB:4ZRL"
FT HELIX 755..757
FT /evidence="ECO:0007829|PDB:4ZRL"
FT TURN 773..775
FT /evidence="ECO:0007829|PDB:5JNB"
FT HELIX 776..778
FT /evidence="ECO:0007829|PDB:5JNB"
FT HELIX 781..791
FT /evidence="ECO:0007829|PDB:4ZRL"
FT HELIX 795..797
FT /evidence="ECO:0007829|PDB:4ZRL"
FT TURN 798..800
FT /evidence="ECO:0007829|PDB:5JNB"
FT STRAND 801..804
FT /evidence="ECO:0007829|PDB:5JNB"
FT TURN 805..808
FT /evidence="ECO:0007829|PDB:5JNB"
FT STRAND 809..812
FT /evidence="ECO:0007829|PDB:5JNB"
FT TURN 861..865
FT /evidence="ECO:0007829|PDB:4ZRL"
FT HELIX 869..871
FT /evidence="ECO:0007829|PDB:4ZRL"
FT HELIX 886..909
FT /evidence="ECO:0007829|PDB:4ZRL"
FT HELIX 912..916
FT /evidence="ECO:0007829|PDB:4ZRL"
SQ SEQUENCE 1113 AA; 124612 MW; EDDB685EFE422F4B CRC64;
MVMAQQQKNA ERNDEHTRRN RSPSVDSVSR VQQQSGGFAF YNQQSNHQYQ QSHPRRTSFS
RDGNTGYYNN HSGNKRQTYN NQRGGRSYNH RGNSNYQQNG EYSGNQGCVP KYHQRNQNYP
QLQPKYSYFQ PHQRPIFNST QGYGTYSVRR SSPPSPSALS SSTANSTSNR APTQPPILLR
HAEPASDKNH QGSDHEQNHD PKIHLYRSAG TAPGGYTQCP SPYKQPPPQP PSTPSSSDKR
IEQQQAEDWP TRFQHPPPQF RRGQDPMPAS IELQHKTANQ TMPVDIVQTN QQKTVSSYER
AAQFRASASE LPTDSVDAKH PCFANERMQS ALIGISPQLK TQQQSPGIPI QNEAEASAVM
KAMRSFQFHN WPQMSHGSYY PMPYHLENQM RPMKSGDQLP LNQQNHNLSG FPAFVGKSSL
VGSSLNTRNS SEADPEEMPR IMEKLDDEVT GADHDKTIDE NRRRIHKSQE PRIGTEEKAL
NELPRKANRR NSSCSSISSV SESSSPSALD ESTLTKILPT DNFRGGRGFA SPSPPTSLLS
EPLSRMDVLS EKIWDYHNKV SQTDEMLQRK LHLRDMLYTA ISPVFPLSGL YVVGSSLNGF
GNNSSDMDLC LMITNKDLDQ KNDAVVVLNL ILSTLQYEKF VESQKLILAK VPILRINFAA
PFDDITVDLN ANNSVAIRNT HLLCYYSSYD WRVRPLVSVV KEWAKRKGIN DANKSSFTSY
SLVLMVIHFL QCGPTKVLPN LQQSYPNRFS NKVDVRTLNV TMALEEVADD IDQSLSEKTT
LGELLIGFLD YYANEFNYDR DAISIRQGRR VERAALAVRP KIHSNSEGDK ETPPPSSSAS
TSSIHNGGTP GIPMHHSISN PHFWRSQWRC VCIEEPFTNS NTAHSIYDEM VFEAIKKAFR
EAHGELQHNH DLDKLMECEP IKASTTNTGA AVFAATYEGE RPLAQQPNTI ACASLRVLNS
IPVSSGPGHY HYQQQSNQNL SRPQRPGSNQ GYQMNNNRGF NGNNQQQHQN RRSFNNQSSS
NPGNGSTGPR SSRSNENVRD SSRQQNSQKG SSGVSVSKEN VASTTGVPVD KKQQNSNRKD
DGNRTKRSPM VQSPEPAKTK SEKTPMASSN VSQ
