(data stored in ACNUC11299 zone)

HOGENOM: YEASTIV_PE115

ID   YEASTIV_PE115                        STANDARD;      PRT;   1733 AA.
AC   YEASTIV_PE115; P04050; D6VRK8; Q12364; Q92315;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=DNA-directed RNA polymerase II subunit RPB1; Short=RNA
DE   polymerase II subunit 1; Short=RNA polymerase II subunit B1; EC=2.7.7
DE   6;AltName: Full=DNA-directed RNA polymerase III largest subunit;AltName:
DE   Full=RNA polymerase II subunit B220; (YEASTIV.PE115).
GN   Name=RPO21; Synonyms=RPB1, RPB220, SUA8; OrderedLocusNames=YDL140C;
OS   SACCHAROMYCES CEREVISIAE.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomyceta; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS YEASTIV.PE115.
CC       Saccharomyces cerevisiae chromosome IV EF2  sequence 1..1531919
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:RPB1_YEAST
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC       of DNA into RNA using the four ribonucleoside triphosphates as
CC       substrates. Largest and catalytic component of RNA polymerase II
CC       which synthesizes mRNA precursors and many functional non-coding
CC       RNAs. Forms the polymerase active center together with the second
CC       largest subunit. Pol II is the central component of the basal RNA
CC       polymerase II transcription machinery. During a transcription
CC       cycle, Pol II, general transcription factors and the Mediator
CC       complex assemble as the preinitiation complex (PIC) at the
CC       promoter. 11-15 base pairs of DNA surrounding the transcription
CC       start site are melted and the single stranded DNA template strand
CC       of the promoter is positioned deeply within the central active
CC       site cleft of Pol II to form the open complex. After synthesis of
CC       about 30 bases of RNA, Pol II releases its contacts with the core
CC       promoter and the rest of the transcription machinery (promoter
CC       clearance) and enters the stage of transcription elongation in
CC       which it moves on the template as the transcript elongates. Pol II
CC       appears to oscillate between inactive and active conformations at
CC       each step of nucleotide addition. Elongation is influenced by the
CC       phosphorylation status of the C-terminal domain (CTD) of Pol II
CC       largest subunit (RPB1), which serves as a platform for assembly of
CC       factors that regulate transcription initiation, elongation,
CC       termination and mRNA processing. Pol II is composed of mobile
CC       elements that move relative to each other. The core element with
CC       the central large cleft comprises RPB3, RBP10, RPB11, RPB12 and
CC       regions of RPB1 and RPB2 forming the active center. The clamp
CC       element (portions of RPB1, RPB2 and RPB3) is connected to the core
CC       through a set of flexible switches and moves to open and close the
CC       cleft. A bridging helix emanates from RPB1 and crosses the cleft
CC       near the catalytic site and is thought to promote translocation of
CC       Pol II by acting as a ratchet that moves the RNA-DNA hybrid
CC       through the active site by switching from straight to bent
CC       conformations at each step of nucleotide addition. In elongating
CC       Pol II, the lid loop (RPB1) appears to act as a wedge to drive
CC       apart the DNA and RNA strands at the upstream end of the
CC       transcription bubble and guide the RNA strand toward the RNA exit
CC       groove located near the base of the largely unstructured CTD
CC       domain of RPB1. The rudder loop (RPB1) interacts with single
CC       stranded DNA after separation from the RNA strand, likely
CC       preventing reassociation with the exiting RNA. The cleft is
CC       surrounded by jaws: an upper jaw formed by portions of RBP1, RPB2
CC       and RPB9, and a lower jaw, formed by RPB5 and portions of RBP1.
CC       The jaws are thought to grab the incoming DNA template, mainly by
CC       RPB5 direct contacts to DNA.
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1).
CC   -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex
CC       consisting of 12 subunits. Interacts with ASK10, ESS1, RTT103 and
CC       SHE2.
CC   -!- INTERACTION:
CC       P27692:SPT5; NbExp=3; IntAct=EBI-15760, EBI-17937;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- PTM: The tandem 7 residues repeats in the C-terminal domain (CTD)
CC       can be highly phosphorylated. The phosphorylation activates Pol
CC       II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5'
CC       of the heptapepdtide repeat. The phosphorylated form of Pol II
CC       appears to carry, on average, one phosphate per repeat. The
CC       phosphorylation state is believed to result from the balanced
CC       action of site-specific CTD kinases and phosphataes, and a "CTD
CC       code" that specifies the position of Pol II within the
CC       transcription cycle has been proposed. Phosphorylation at 'Ser-5'
CC       occurs in promoter-proximal regions in early elongation.
CC       Phosphorylation at 'Ser-2' predominates in regions more distal to
CC       the promoter and triggers binding of the 3' RNA processing
CC       machinery. CTD kinases include KIN28 (as part of the TFKII
CC       complex, a subcomplex of the TFIIH holo complex), SSN3/SRB10 (as
CC       part of the SRB8-11 complex, a module of the Mediator complex),
CC       CTK1 (as part of CTD kinase), and probably BUR1 (as part of the
CC       BUR1-BUR2 kinase complex). Phosphatases include FCP1 and SSU72.
CC   -!- MISCELLANEOUS: Mutagenesis experiments demonstrate that the
CC       minimum viable CTD contains eight consensus Y-S-P-T-S-P-[A-S-N-G]
CC       heptapeptide repeats. Identical and simultaneous substitutions in
CC       a number of consecutive repeats are lethal: 'Ser-2' -> 'Ala-2' (14
CC       repeats), 'Ser-5' -> 'Ala-5' (15 repeats), '2-Ser-Pro-Thr-Ser-5'->
CC       '2-Ala-Pro-Thr-Ala-5' (10 repeats), 'Ser-2'-> 'Glu-2' (15
CC       repeats), 'Ser-5' -> 'Glu-5' (12 repeats), '2-Ser-Pro-3' -> '2-
CC       Pro-Ser-3' (15 repeats) and 'Tyr-1' -> 'Phe-1' (12 repeats).
CC   -!- MISCELLANEOUS: The binding of ribonucleoside triphosphate to the
CC       RNA polymerase II transcribing complex probably involves a two-
CC       step mechanism. The initial binding seems to occur at the entry
CC       (E) site and involves a magnesium ion temporarily coordinated by
CC       three conserved aspartate residues of the two largest RNA Pol II
CC       subunits. The ribonucleoside triphosphate is transferred by a
CC       rotation to the nucelotide addition (A) site for pairing with the
CC       template DNA. The catalytic A site involves three conserved
CC       aspartate residues of the RNA Pol II largest subunit which
CC       permanently coordinate a second magnesium ion.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC   -!- GENE_FAMILY: HOG000222975 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Saccharomyces_cerevisiae;YDL140C;YDL140C;YDL140C.
DR   EMBL; AY497704; - ;
DR   EMBL; FJ787035; - ;
DR   EMBL; FJ787036; - ;
DR   EMBL; FJ787037; - ;
DR   EMBL; FJ787038; - ;
DR   EMBL; FJ787039; - ;
DR   EMBL; FJ787040; - ;
DR   EMBL; FJ787041; - ;
DR   EMBL; FJ787042; - ;
DR   EMBL; FJ787043; - ;
DR   EMBL; U27182; - ;
DR   EMBL; X03128; - ;
DR   EMBL; X96876; - ;
DR   EMBL; Z74188; - ;
DR   UniProtKB/Swiss-Prot; P04050; D6VRK8; Q12364; Q92315; -.
DR   EMBL; X03128; CAA26904.1; -; Genomic_DNA.
DR   EMBL; X96876; CAA65619.1; -; Genomic_DNA.
DR   EMBL; Z74188; CAA98713.1; -; Genomic_DNA.
DR   EMBL; U27182; AAC49058.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11718.1; -; Genomic_DNA.
DR   PIR; S67686; RNBY2L.
DR   RefSeq; NP_010141.1; NM_001180200.1.
DR   PDB; 1I3Q; X-ray; 3.10 A; A=1-1733.
DR   PDB; 1I50; X-ray; 2.80 A; A=1-1733.
DR   PDB; 1I6H; X-ray; 3.30 A; A=1-1733.
DR   PDB; 1K83; X-ray; 2.80 A; A=1-1733.
DR   PDB; 1NIK; X-ray; 4.10 A; A=1-1733.
DR   PDB; 1NT9; X-ray; 4.20 A; A=1-1733.
DR   PDB; 1PQV; X-ray; 3.80 A; A=1-1733.
DR   PDB; 1R5U; X-ray; 4.50 A; A=1-1733.
DR   PDB; 1R9S; X-ray; 4.25 A; A=1-1733.
DR   PDB; 1R9T; X-ray; 3.50 A; A=1-1733.
DR   PDB; 1SFO; X-ray; 3.61 A; A=1-1733.
DR   PDB; 1TWA; X-ray; 3.20 A; A=1-1733.
DR   PDB; 1TWC; X-ray; 3.00 A; A=1-1733.
DR   PDB; 1TWF; X-ray; 2.30 A; A=1-1733.
DR   PDB; 1TWG; X-ray; 3.30 A; A=1-1733.
DR   PDB; 1TWH; X-ray; 3.40 A; A=1-1733.
DR   PDB; 1WCM; X-ray; 3.80 A; A=1-1733.
DR   PDB; 1Y1V; X-ray; 3.80 A; A=1-1733.
DR   PDB; 1Y1W; X-ray; 4.00 A; A=1-1733.
DR   PDB; 1Y1Y; X-ray; 4.00 A; A=1-1733.
DR   PDB; 1Y77; X-ray; 4.50 A; A=1-1733.
DR   PDB; 2B63; X-ray; 3.80 A; A=1-1733.
DR   PDB; 2B8K; X-ray; 4.15 A; A=1-1733.
DR   PDB; 2E2H; X-ray; 3.95 A; A=1-1733.
DR   PDB; 2E2I; X-ray; 3.41 A; A=1-1733.
DR   PDB; 2E2J; X-ray; 3.50 A; A=1-1733.
DR   PDB; 2JA5; X-ray; 3.80 A; A=1-1733.
DR   PDB; 2JA6; X-ray; 4.00 A; A=1-1733.
DR   PDB; 2JA7; X-ray; 3.80 A; A/M=1-1733.
DR   PDB; 2JA8; X-ray; 3.80 A; A=1-1733.
DR   PDB; 2L0I; NMR; -; B=1556-1569.
DR   PDB; 2NVQ; X-ray; 2.90 A; A=1-1733.
DR   PDB; 2NVT; X-ray; 3.36 A; A=1-1733.
DR   PDB; 2NVX; X-ray; 3.60 A; A=1-1733.
DR   PDB; 2NVY; X-ray; 3.40 A; A=1-1733.
DR   PDB; 2NVZ; X-ray; 4.30 A; A=1-1733.
DR   PDB; 2R7Z; X-ray; 3.80 A; A=1-1733.
DR   PDB; 2R92; X-ray; 3.80 A; A=1-1733.
DR   PDB; 2R93; X-ray; 4.00 A; A=1-1733.
DR   PDB; 2VUM; X-ray; 3.40 A; A=1-1733.
DR   PDB; 2YU9; X-ray; 3.40 A; A=1-1733.
DR   PDB; 3CQZ; X-ray; 2.80 A; A=1-1733.
DR   PDB; 3FKI; X-ray; 3.88 A; A=1-1733.
DR   PDB; 3GTG; X-ray; 3.78 A; A=1-1733.
DR   PDB; 3GTJ; X-ray; 3.42 A; A=1-1733.
DR   PDB; 3GTK; X-ray; 3.80 A; A=1-1733.
DR   PDB; 3GTL; X-ray; 3.38 A; A=1-1733.
DR   PDB; 3GTM; X-ray; 3.80 A; A=1-1733.
DR   PDB; 3GTO; X-ray; 4.00 A; A=1-1733.
DR   PDB; 3GTP; X-ray; 3.90 A; A=1-1733.
DR   PDB; 3GTQ; X-ray; 3.80 A; A=1-1733.
DR   PDB; 3H3V; X-ray; 4.00 A; B=1-1733.
DR   PDB; 3HOU; X-ray; 3.20 A; A/M=1-1733.
DR   PDB; 3HOV; X-ray; 3.50 A; A=1-1733.
DR   PDB; 3HOW; X-ray; 3.60 A; A=1-1733.
DR   PDB; 3HOX; X-ray; 3.65 A; A=1-1733.
DR   PDB; 3HOY; X-ray; 3.40 A; A=1-1733.
DR   PDB; 3HOZ; X-ray; 3.65 A; A=1-1733.
DR   PDB; 3I4M; X-ray; 3.70 A; A=1-1733.
DR   PDB; 3I4N; X-ray; 3.90 A; A=1-1733.
DR   PDB; 3K1F; X-ray; 4.30 A; A=1-1733.
DR   PDB; 3K7A; X-ray; 3.80 A; A=1-1733.
DR   PDB; 3M3Y; X-ray; 3.18 A; A=1-1733.
DR   PDB; 3M4O; X-ray; 3.57 A; A=1-1733.
DR   PDB; 3PO2; X-ray; 3.30 A; A=1-1733.
DR   PDB; 3PO3; X-ray; 3.30 A; A=1-1733.
DR   PDB; 3QT1; X-ray; 4.30 A; A=1-1733.
DR   PDBsum; 1I3Q; -.
DR   PDBsum; 1I50; -.
DR   PDBsum; 1I6H; -.
DR   PDBsum; 1K83; -.
DR   PDBsum; 1NIK; -.
DR   PDBsum; 1NT9; -.
DR   PDBsum; 1PQV; -.
DR   PDBsum; 1R5U; -.
DR   PDBsum; 1R9S; -.
DR   PDBsum; 1R9T; -.
DR   PDBsum; 1SFO; -.
DR   PDBsum; 1TWA; -.
DR   PDBsum; 1TWC; -.
DR   PDBsum; 1TWF; -.
DR   PDBsum; 1TWG; -.
DR   PDBsum; 1TWH; -.
DR   PDBsum; 1WCM; -.
DR   PDBsum; 1Y1V; -.
DR   PDBsum; 1Y1W; -.
DR   PDBsum; 1Y1Y; -.
DR   PDBsum; 1Y77; -.
DR   PDBsum; 2B63; -.
DR   PDBsum; 2B8K; -.
DR   PDBsum; 2E2H; -.
DR   PDBsum; 2E2I; -.
DR   PDBsum; 2E2J; -.
DR   PDBsum; 2JA5; -.
DR   PDBsum; 2JA6; -.
DR   PDBsum; 2JA7; -.
DR   PDBsum; 2JA8; -.
DR   PDBsum; 2L0I; -.
DR   PDBsum; 2NVQ; -.
DR   PDBsum; 2NVT; -.
DR   PDBsum; 2NVX; -.
DR   PDBsum; 2NVY; -.
DR   PDBsum; 2NVZ; -.
DR   PDBsum; 2R7Z; -.
DR   PDBsum; 2R92; -.
DR   PDBsum; 2R93; -.
DR   PDBsum; 2VUM; -.
DR   PDBsum; 2YU9; -.
DR   PDBsum; 3CQZ; -.
DR   PDBsum; 3FKI; -.
DR   PDBsum; 3GTG; -.
DR   PDBsum; 3GTJ; -.
DR   PDBsum; 3GTK; -.
DR   PDBsum; 3GTL; -.
DR   PDBsum; 3GTM; -.
DR   PDBsum; 3GTO; -.
DR   PDBsum; 3GTP; -.
DR   PDBsum; 3GTQ; -.
DR   PDBsum; 3H3V; -.
DR   PDBsum; 3HOU; -.
DR   PDBsum; 3HOV; -.
DR   PDBsum; 3HOW; -.
DR   PDBsum; 3HOX; -.
DR   PDBsum; 3HOY; -.
DR   PDBsum; 3HOZ; -.
DR   PDBsum; 3I4M; -.
DR   PDBsum; 3I4N; -.
DR   PDBsum; 3K1F; -.
DR   PDBsum; 3K7A; -.
DR   PDBsum; 3M3Y; -.
DR   PDBsum; 3M4O; -.
DR   PDBsum; 3PO2; -.
DR   PDBsum; 3PO3; -.
DR   PDBsum; 3QT1; -.
DR   ProteinModelPortal; P04050; -.
DR   SMR; P04050; 12-882, 1008-1447.
DR   DIP; DIP-611N; -.
DR   IntAct; P04050; 28.
DR   MINT; MINT-432838; -.
DR   STRING; P04050; -.
DR   PeptideAtlas; P04050; -.
DR   EnsemblFungi; YDL140C; YDL140C; YDL140C.
DR   GeneID; 851415; -.
DR   KEGG; sce:YDL140C; -.
DR   NMPDR; fig|4932.3.peg.878; -.
DR   CYGD; YDL140c; -.
DR   SGD; S000002299; RPO21.
DR   eggNOG; fuNOG04507; -.
DR   OMA; SPTSPHY; -.
DR   OrthoDB; EOG4J14H5; -.
DR   PhylomeDB; P04050; -.
DR   NextBio; 968606; -.
DR   ArrayExpress; P04050; -.
DR   Genevestigator; P04050; -.
DR   GermOnline; YDL140C; Saccharomyces cerevisiae.
DR   GO; GO:0005665; C:DNA-directed RNA polymerase II, core complex; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; IMP:SGD.
DR   InterPro; IPR000722; RNA_pol_asu.
DR   InterPro; IPR000684; RNA_pol_II_repeat_euk.
DR   InterPro; IPR006592; RNA_pol_N.
DR   InterPro; IPR007080; RNA_pol_Rpb1_1.
DR   InterPro; IPR007066; RNA_pol_Rpb1_3.
DR   InterPro; IPR007083; RNA_pol_Rpb1_4.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR007075; RNA_pol_Rpb1_6.
DR   InterPro; IPR007073; RNA_pol_Rpb1_7.
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR   Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR   Pfam; PF04992; RNA_pol_Rpb1_6; 1.
DR   Pfam; PF04990; RNA_pol_Rpb1_7; 1.
DR   Pfam; PF05001; RNA_pol_Rpb1_R; 16.
DR   SMART; SM00663; RPOLA_N; 1.
DR   PROSITE; PS00115; RNA_POL_II_REPEAT; 22.
DR   HOGENOMDNA; YEASTIV.PE115; -.
KW   YDL140C-B100026476820036002503210000011; YDL140C-B1; RPB1_YEAST;
KW   C5I8K1_YEAST; C5I8K2_YEAST; C5I8K4_YEAST; C5I8K5_YEAST; Q6JEC5_YEAST;
KW   FJ787035; FJ787036; FJ787037; FJ787038; FJ787039; FJ787040; FJ787041;
KW   FJ787043; U27182; X03128; X96876; Z74188;
KW   3D-structure; Complete proteome; DNA-binding;
KW   DNA-directed RNA polymerase; Isopeptide bond; Magnesium;
KW   Metal-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transferase;
KW   Ubl conjugation; Zinc.
SQ   SEQUENCE   1733 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MVGQQYSSAP LRTVKEVQFG LFSPEEVRAI SVAKIRFPET MDETQTRAKI GGLNDPRLGS
     IDRNLKCQTC QEGMNECPGH FGHIDLAKPV FHVGFIAKIK KVCECVCMHC GKLLLDEHNE
     LMRQALAIKD SKKRFAAIWT LCKTKMVCET DVPSEDDPTQ LVSRGGCGNT QPTIRKDGLK
     LVGSWKKDRA TGDADEPELR VLSTEEILNI FKHISVKDFT SLGFNEVFSR PEWMILTCLP
     VPPPPVRPSI SFNESQRGED DLTFKLADIL KANISLETLE HNGAPHHAIE EAESLLQFHV
     ATYMDNDIAG QPQALQKSGR PVKSIRARLK GKEGRIRGNL MGKRVDFSAR TVISGDPNLE
     LDQVGVPKSI AKTLTYPEVV TPYNIDRLTQ LVRNGPNEHP GAKYVIRDSG DRIDLRYSKR
     AGDIQLQYGW KVERHIMDND PVLFNRQPSL HKMSMMAHRV KVIPYSTFRL NLSVTSPYNA
     DFDGDEMNLH VPQSEETRAE LSQLCAVPLQ IVSPQSNKPC MGIVQDTLCG IRKLTLRDTF
     IELDQVLNML YWVPDWDGVI PTPAIIKPKP LWSGKQILSV AIPNGIHLQR FDEGTTLLSP
     KDNGMLIIDG QIIFGVVEKK TVGSSNGGLI HVVTREKGPQ VCAKLFGNIQ KVVNFWLLHN
     GFSTGIGDTI ADGPTMREIT ETIAEAKKKV LDVTKEAQAN LLTAKHGMTL RESFEDNVVR
     FLNEARDKAG RLAEVNLKDL NNVKQMVMAG SKGSFINIAQ MSACVGQQSV EGKRIAFGFV
     DRTLPHFSKD DYSPESKGFV ENSYLRGLTP QEFFFHAMGG REGLIDTAVK TAETGYIQRR
     LVKALEDIMV HYDNTTRNSL GNVIQFIYGE DGMDAAHIEK QSLDTIGGSD AAFEKRYRVD
     LLNTDHTLDP SLLESGSEIL GDLKLQVLLD EEYKQLVKDR KFLREVFVDG EANWPLPVNI
     RRIIQNAQQT FHIDHTKPSD LTIKDIVLGV KDLQENLLVL RGKNEIIQNA QRDAVTLFCC
     LLRSRLATRR VLQEYRLTKQ AFDWVLSNIE AQFLRSVVHP GEMVGVLAAQ SIGEPATQMT
     LNTFHFAGVA SKKVTSGVPR LKEILNVAKN MKTPSLTVYL EPGHAADQEQ AKLIRSAIEH
     TTLKSVTIAS EIYYDPDPRS TVIPEDEEII QLHFSLLDEE AEQSFDQQSP WLLRLELDRA
     AMNDKDLTMG QVGERIKQTF KNDLFVIWSE DNDEKLIIRC RVVRPKSLDA ETEAEEDHML
     KKIENTMLEN ITLRGVENIE RVVMMKYDRK VPSPTGEYVK EPEWVLETDG VNLSEVMTVP
     GIDPTRIYTN SFIDIMEVLG IEAGRAALYK EVYNVIASDG SYVNYRHMAL LVDVMTTQGG
     LTSVTRHGFN RSNTGALMRC SFEETVEILF EAGASAELDD CRGVSENVIL GQMAPIGTGA
     FDVMIDEESL VKYMPEQKIT EIEDGQDGGV TPYSNESGLV NADLDVKDEL MFSPLVDSGS
     NDAMAGGFTA YGGADYGEAT SPFGAYGEAP TSPGFGVSSP GFSPTSPTYS PTSPAYSPTS
     PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS
     PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPA YSPTSPSYSP TSPSYSPTSP
     SYSPTSPSYS PTSPNYSPTS PSYSPTSPGY SPGSPAYSPK QDEQKHNENE NSR
//

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