SPT6H_DROME
ID SPT6H_DROME Reviewed; 1831 AA.
AC Q9W420; Q960J2; Q9U8B5; Q9U8B6;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Transcription elongation factor SPT6;
GN Name=Spt6; ORFNames=CG12225;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Chiang P.-W.;
RT "Characterization of Drosophila SPT6 homolog.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 400-1831.
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=11040216; DOI=10.1101/gad.831900;
RA Kaplan C.D., Morris J.R., Wu C.-T., Winston F.;
RT "Spt5 and spt6 are associated with active transcription and have
RT characteristics of general elongation factors in D. melanogaster.";
RL Genes Dev. 14:2623-2634(2000).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=11040217; DOI=10.1101/gad.844200;
RA Andrulis E.D., Guzman E., Doering P., Werner J., Lis J.T.;
RT "High-resolution localization of Drosophila Spt5 and Spt6 at heat shock
RT genes in vivo: roles in promoter proximal pausing and transcription
RT elongation.";
RL Genes Dev. 14:2635-2649(2000).
RN [7]
RP SELF-ASSOCIATION, INTERACTION WITH SPT5 AND THE EXOSOME COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12490954; DOI=10.1038/nature01181;
RA Andrulis E.D., Werner J., Nazarian A., Erdjument-Bromage H., Tempst P.,
RA Lis J.T.;
RT "The RNA processing exosome is linked to elongating RNA polymerase II in
RT Drosophila.";
RL Nature 420:837-841(2002).
RN [8]
RP INTERACTION WITH SPT5; RNA POLYMERASE II AND THE FACT COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12934007; DOI=10.1126/science.1085712;
RA Saunders A., Werner J., Andrulis E.D., Nakayama T., Hirose S., Reinberg D.,
RA Lis J.T.;
RT "Tracking FACT and the RNA polymerase II elongation complex through
RT chromatin in vivo.";
RL Science 301:1094-1096(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-36; SER-37; SER-66;
RP SER-70; SER-75; SER-151; SER-156; SER-159; THR-171; SER-173; SER-1661;
RP SER-1664 AND SER-1815, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [11]
RP FUNCTION.
RX PubMed=19279664; DOI=10.1038/emboj.2009.56;
RA Ardehali M.B., Yao J., Adelman K., Fuda N.J., Petesch S.J., Webb W.W.,
RA Lis J.T.;
RT "Spt6 enhances the elongation rate of RNA polymerase II in vivo.";
RL EMBO J. 28:1067-1077(2009).
CC -!- FUNCTION: Transcription elongation factor which binds histone H3 and
CC enhances transcription elongation by RNA polymerase II (RNAPII).
CC Required for the transcriptional induction of heat shock response genes
CC and for maximal recruitment of two other elongation factors, Spt5 and
CC Paf1, to the induced Hsp70. Plays a critical role in normal fly
CC development throughout the lifecycle. {ECO:0000269|PubMed:19279664}.
CC -!- SUBUNIT: Self associates. Interacts with RNA polymerase II. Interacts
CC with the FACT complex, which is composed of dre4/Spt16 and Ssrp/Ssrp1.
CC Interacts with the exosome, a complex with 3'-5' exoribonuclease
CC activity which is composed of at least Csl4, Dis3, Mtr3, Rrp4, Rrp6,
CC Rrp40, Rrp42, Rrp46 and Ski6. Interacts with the DRB sensitivity-
CC inducing factor complex (the DSIF complex), which is composed of Spt4
CC and Spt5. {ECO:0000269|PubMed:12490954, ECO:0000269|PubMed:12934007}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11040216,
CC ECO:0000269|PubMed:11040217, ECO:0000269|PubMed:12490954,
CC ECO:0000269|PubMed:12934007}. Note=Recruited to sites of active
CC transcription where it colocalizes with the elongating form of RNA
CC polymerase II.
CC -!- SIMILARITY: Belongs to the SPT6 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF14115.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAK93454.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF104400; AAF14114.1; -; mRNA.
DR EMBL; AF104401; AAF14115.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE014298; AAF46140.1; -; Genomic_DNA.
DR EMBL; AY052030; AAK93454.1; ALT_INIT; mRNA.
DR RefSeq; NP_001284936.1; NM_001298007.1.
DR RefSeq; NP_651962.2; NM_143705.3.
DR AlphaFoldDB; Q9W420; -.
DR SMR; Q9W420; -.
DR BioGRID; 68765; 14.
DR IntAct; Q9W420; 14.
DR STRING; 7227.FBpp0070861; -.
DR iPTMnet; Q9W420; -.
DR PaxDb; Q9W420; -.
DR PRIDE; Q9W420; -.
DR DNASU; 44000; -.
DR EnsemblMetazoa; FBtr0070896; FBpp0070861; FBgn0028982.
DR EnsemblMetazoa; FBtr0340027; FBpp0309041; FBgn0028982.
DR GeneID; 44000; -.
DR KEGG; dme:Dmel_CG12225; -.
DR CTD; 44000; -.
DR FlyBase; FBgn0028982; Spt6.
DR VEuPathDB; VectorBase:FBgn0028982; -.
DR eggNOG; KOG1856; Eukaryota.
DR GeneTree; ENSGT00510000047446; -.
DR HOGENOM; CLU_001680_4_0_1; -.
DR InParanoid; Q9W420; -.
DR OMA; LCNGFKT; -.
DR OrthoDB; 56990at2759; -.
DR PhylomeDB; Q9W420; -.
DR Reactome; R-DME-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-DME-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DME-75955; RNA Polymerase II Transcription Elongation.
DR SignaLink; Q9W420; -.
DR BioGRID-ORCS; 44000; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 44000; -.
DR PRO; PR:Q9W420; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0028982; Expressed in cleaving embryo and 26 other tissues.
DR ExpressionAtlas; Q9W420; baseline and differential.
DR Genevisible; Q9W420; DM.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:FlyBase.
DR GO; GO:0000791; C:euchromatin; IDA:FlyBase.
DR GO; GO:0035363; C:histone locus body; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005705; C:polytene chromosome interband; IDA:UniProtKB.
DR GO; GO:0005703; C:polytene chromosome puff; IDA:UniProtKB.
DR GO; GO:0008023; C:transcription elongation factor complex; IPI:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IDA:UniProtKB.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0034728; P:nucleosome organization; IBA:GO_Central.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0006963; P:positive regulation of antibacterial peptide biosynthetic process; IMP:FlyBase.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:FlyBase.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEP:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR CDD; cd09928; SH2_Cterm_SPT6_like; 1.
DR CDD; cd09918; SH2_Nterm_SPT6_like; 1.
DR Gene3D; 1.10.10.2740; -; 1.
DR Gene3D; 1.10.10.650; -; 1.
DR Gene3D; 1.10.3500.10; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.420.140; -; 1.
DR Gene3D; 3.30.505.10; -; 2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR028083; Spt6_acidic_N_dom.
DR InterPro; IPR042066; Spt6_death-like.
DR InterPro; IPR032706; Spt6_HHH.
DR InterPro; IPR028088; Spt6_HTH_DNA-bd_dom.
DR InterPro; IPR035420; Spt6_SH2.
DR InterPro; IPR035018; Spt6_SH2_C.
DR InterPro; IPR035019; Spt6_SH2_N.
DR InterPro; IPR028231; Spt6_YqgF.
DR InterPro; IPR023323; Tex-like_dom_sf.
DR InterPro; IPR023319; Tex-like_HTH_dom_sf.
DR InterPro; IPR017072; TF_Spt6.
DR InterPro; IPR006641; YqgF/RNaseH-like_dom.
DR InterPro; IPR037027; YqgF/RNaseH-like_dom_sf.
DR PANTHER; PTHR10145; PTHR10145; 1.
DR Pfam; PF14635; HHH_7; 1.
DR Pfam; PF14641; HTH_44; 1.
DR Pfam; PF00575; S1; 1.
DR Pfam; PF14633; SH2_2; 1.
DR Pfam; PF14632; SPT6_acidic; 1.
DR Pfam; PF14639; YqgF; 1.
DR PIRSF; PIRSF036947; Spt6; 1.
DR SMART; SM00316; S1; 1.
DR SMART; SM00732; YqgFc; 1.
DR SUPFAM; SSF47781; SSF47781; 2.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF55550; SSF55550; 2.
DR PROSITE; PS50126; S1; 1.
PE 1: Evidence at protein level;
KW Chaperone; Coiled coil; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..1831
FT /note="Transcription elongation factor SPT6"
FT /id="PRO_0000072170"
FT DOMAIN 1217..1286
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 1329..1440
FT /note="SH2"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1531..1587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1602..1716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1730..1831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 7..59
FT /evidence="ECO:0000255"
FT COILED 467..494
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1547..1587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1602..1684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1735..1762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1785..1820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 171
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1661
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1664
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1815
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 1194
FT /note="L -> I (in Ref. 1; AAF14114/AAF14115)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1831 AA; 208599 MW; 005FC78C83EF744D CRC64;
MAEFLDSEAE ESEEEEELDV NERKRLKKLK AAVSDSSEEE EDDEERLREE LKDLIDDNPI
EEDDGSGYDS DGVGSGKKRK KHEDDDLDDR LEDDDYDLIE ENLGVKVERR KRFKRLRRIH
DNESDGEEQH VDEGLVREQI AEQLFDENDE SIGHRSERSH READDYDDVD TESDADDFIV
DDNGRPIAEK KKKRRPIFTD ASLQEGQDIF GVDFDYDDFS KYEEDDYEDD SEGDEYDEDL
GVGDDTRVKK KKALKKKVVK KTIFDIYEPS ELKRGHFTDM DNEIRKTDIP ERMQLREVPV
TPVPEGSDEL DLEAEWIYKY AFCKHTVSEQ EKPESREKMR KPPTTVNKIK QTLEFIRNQQ
LEVPFIAFYR KEYVKPELNI DDLWKVYYYD GIWCQLNERK RKLKVLFEKM RQFQLDTLCA
DTDQPVPDDV RLILDSDFER LADVQSMEEL KDVHMYFLLN YSHELPRMQA EQRRKAIQER
REAKARRQAA AAENGDDAAE AIVVPEPEDD DDPELIDYQL KQASNSSPYA VFRKAGICGF
AKHFGLTPEQ YAENLRDNYQ RNEITQESIG PTELAKQYLS PRFMTTDEVI HAAKYVVARQ
LAQEPLLRKT MREVYFDRAR INIRPTKNGM VLIDENSPVY SMKYVAKKPV SDLFGDQFIK
LMMAEEEKLL EITFLEEFEG NACANGTPGD YVEESKALYQ LDQFAKHVQE WNKLRAECVQ
LALQKWVIPD LIKELRSTLH EEAQQFVLRS CTGKLYKWLK VAPYKPQLPP DFGYEEWSTL
RGIRVLGLAY DPDHSVAAFC AVTTVEGDIS DYLRLPNILK RKNSYNLEEK AQKLADLRKL
SDFIKMKKPH IVVIGAESRD AQNIQADIKE ILHELETSEQ FPPIEVEIID NELAKIYANS
KKGESDFKEY PPLLKQAASL ARKMQDPLVE YSQLCDADDE ILCLRYHPLQ ERVPREQLLE
QLSLQFINRT SEVGLDINLM VQNSRTINLL QYICGLGPRK GQALLKLLKQ SNQRLENRTQ
LVTVCHLGPR VFINCSGFIK IDTSSLGDST EAYVEVLDGS RVHPETYEWA RKMAIDAMEY
DDEETNPAGA LEEILESPER LKDLDLDAFA VELERQGFGS KSITLYDIRN ELSCLYKDYR
TPYTKPSAEE LFDMLTKETP DSFYVGKCVT AMVTGFTYRR PQGDQLDSAN PVRLDSNESW
QCPFCHKDDF PELSEVWNHF DANACPGQPS GVRVRLENGL PGFIHIKNLS DRQVRNPEER
VRVSQMIHVR IIKIDIDRFS VECSSRTADL KDVNNEWRPR RDNYYDYVTE EQDNRKVSDA
KARALKRKIY ARRVIAHPSF FNKSYAEVVA MLAEADQGEV ALRPSSKSKD HLTATWKVAD
DIFQHIDVRE EGKENDFSLG RSLWIGTEEF EDLDEIIARH IMPMALAARE LIQYKYYKPN
MVTGDENERD VMEKLLREEK ANDPKKIHYF FTASRAMPGK FLLSYLPKTK VRHEYVTVMP
EGYRFRGQIF DTVNSLLRWF KEHWLDPTAT PASASASNLT PLHLMRPPPT ISSSSQTSLG
PQAPYSVTGS VTGGTPRSGI SSAVGGGGSS AYSITQSITG YGTSGSSAPG AGVSSSHYGS
SSTPSFGAIN TPYTPSGQTP FMTPYTPHAS QTPRYGHNVP SPSSQSSSSQ RHHYGSSSGT
GSTPRYHDMG GGGGGGVGGG GGSNAYSMQP HHQQRAKENL DWQLANDAWA RRRPQQHQSH
QSYHAQQQHH HSQQQPHMGM SMNMGITMSL GRGTGGGGGG GYGSTPVNDY STGGGHNRGM
SSKASVRSTP RTNASPHSMN LGDATPLYDE N
