TOM1_YEAST
ID TOM1_YEAST Reviewed; 3268 AA.
AC Q03280; D6VT81; Q7LIK7;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=E3 ubiquitin-protein ligase TOM1;
DE EC=2.3.2.26;
DE AltName: Full=HECT-type E3 ubiquitin transferase TOM1;
DE AltName: Full=Suppressor of snRNA protein 2;
DE AltName: Full=Temperature-dependent organization in mitotic nucleus protein 1;
GN Name=TOM1; Synonyms=SSR2; OrderedLocusNames=YDR457W; ORFNames=D8035.1;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 2156-3268, FUNCTION, AND MUTAGENESIS
RP OF CYS-3235.
RX PubMed=10395901; DOI=10.1016/s0378-1119(99)00197-3;
RA Utsugi T., Hirata A., Sekiguchi Y., Sasaki T., Toh-e A., Kikuchi Y.;
RT "Yeast tom1 mutant exhibits pleiotropic defects in nuclear division,
RT maintenance of nuclear structure and nucleocytoplasmic transport at high
RT temperatures.";
RL Gene 234:285-295(1999).
RN [4]
RP FUNCTION, INTERACTION WITH ADA3, AND MUTAGENESIS OF CYS-3235.
RX PubMed=9753545; DOI=10.1006/jmbi.1998.2036;
RA Saleh A., Collart M., Martens J.A., Genereaux J., Allard S., Cote J.,
RA Brandl C.J.;
RT "TOM1p, a yeast hect-domain protein which mediates transcriptional
RT regulation through the ADA/SAGA coactivator complexes.";
RL J. Mol. Biol. 282:933-946(1998).
RN [5]
RP FUNCTION.
RX PubMed=10660055; DOI=10.1007/pl00008662;
RA Sasaki T., Toh-e A., Kikuchi Y.;
RT "Extragenic suppressors that rescue defects in the heat stress response of
RT the budding yeast mutant tom1.";
RL Mol. Gen. Genet. 262:940-948(2000).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-3235.
RX PubMed=10873801; DOI=10.1016/s0960-9822(00)00527-3;
RA Duncan K., Umen J.G., Guthrie C.;
RT "A putative ubiquitin ligase required for efficient mRNA export
RT differentially affects hnRNP transport.";
RL Curr. Biol. 10:687-696(2000).
RN [7]
RP INTERACTION WITH KRR1.
RX PubMed=11027267; DOI=10.1128/mcb.20.21.7971-7979.2000;
RA Sasaki T., Toh-e A., Kikuchi Y.;
RT "Yeast Krr1p physically and functionally interacts with a novel essential
RT Kri1p, and both proteins are required for 40S ribosome biogenesis in the
RT nucleolus.";
RL Mol. Cell. Biol. 20:7971-7979(2000).
RN [8]
RP FUNCTION.
RX PubMed=11238398; DOI=10.1093/genetics/157.3.1107;
RA Tabb A.L., Utsugi T., Wooten-Kee C.R., Sasaki T., Edling S.A., Gump W.,
RA Kikuchi Y., Ellis S.R.;
RT "Genes encoding ribosomal proteins Rps0A/B of Saccharomyces cerevisiae
RT interact with TOM1 mutants defective in ribosome synthesis.";
RL Genetics 157:1107-1116(2001).
RN [9]
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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1890 AND SER-2418, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1890; SER-2376 AND SER-2418,
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1890; THR-2096; SER-2119;
RP SER-2376; SER-2406 AND SER-2418, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
CC -!- FUNCTION: Probable ubiquitin ligase protein involved in many cellular
CC processes, such as transcription regulation, maintenance of nuclear
CC structure, cell cycle, mRNA export and rRNA maturation. E3 ubiquitin
CC ligase proteins mediate ubiquitination and subsequent proteasomal
CC degradation of target proteins. Involved in transcription regulation by
CC interacting, and probably mediating, ubiquitination of some subunit of
CC the SAGA complex. Required for SPT7 ubiquitination. Participates in
CC mRNA export from the nucleus by regulating the transport of hnRNP
CC proteins. Required for the shuttling of hnRNP protein NAB2, probably by
CC mediating ubiquitination of a protein associated with NAB2. Also
CC required for full induction of the general stress and heat-shock
CC responses. Involved in 18S rRNA maturation by affecting several early
CC steps in the rRNA processing pathway. {ECO:0000269|PubMed:10395901,
CC ECO:0000269|PubMed:10660055, ECO:0000269|PubMed:10873801,
CC ECO:0000269|PubMed:11238398, ECO:0000269|PubMed:9753545}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with the ADA3/NGG1 subunit of the SAGA complex.
CC Interacts with KRR1. {ECO:0000269|PubMed:11027267,
CC ECO:0000269|PubMed:9753545}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10873801,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 350 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the UPL family. TOM1/PTR1 subfamily.
CC {ECO:0000305}.
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DR EMBL; U33050; AAB64910.1; -; Genomic_DNA.
DR EMBL; D63905; BAA21482.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12291.1; -; Genomic_DNA.
DR PIR; S69625; S69625.
DR RefSeq; NP_010745.3; NM_001180765.3.
DR SMR; Q03280; -.
DR BioGRID; 32511; 714.
DR DIP; DIP-5927N; -.
DR IntAct; Q03280; 6.
DR MINT; Q03280; -.
DR STRING; 4932.YDR457W; -.
DR iPTMnet; Q03280; -.
DR MaxQB; Q03280; -.
DR PaxDb; Q03280; -.
DR PRIDE; Q03280; -.
DR EnsemblFungi; YDR457W_mRNA; YDR457W; YDR457W.
DR GeneID; 852068; -.
DR KEGG; sce:YDR457W; -.
DR SGD; S000002865; TOM1.
DR VEuPathDB; FungiDB:YDR457W; -.
DR eggNOG; KOG0939; Eukaryota.
DR GeneTree; ENSGT00940000156319; -.
DR HOGENOM; CLU_000215_0_1_1; -.
DR InParanoid; Q03280; -.
DR OMA; HGLLFQI; -.
DR BioCyc; YEAST:G3O-29985-MON; -.
DR BRENDA; 2.3.2.26; 984.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q03280; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03280; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:SGD.
DR GO; GO:0000448; P:cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:SGD.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IMP:SGD.
DR GO; GO:0006997; P:nucleus organization; IMP:SGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IDA:SGD.
DR GO; GO:0008361; P:regulation of cell size; HMP:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR010309; E3_Ub_ligase_DUF908.
DR InterPro; IPR010314; E3_Ub_ligase_DUF913.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR025527; HUWE1/Rev1_UBM.
DR Pfam; PF06012; DUF908; 1.
DR Pfam; PF06025; DUF913; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF14377; UBM; 2.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS50237; HECT; 1.
PE 1: Evidence at protein level;
KW Cell cycle; mRNA transport; Nucleus; Phosphoprotein; Reference proteome;
KW rRNA processing; Transcription; Transcription regulation; Transferase;
KW Transport; Ubl conjugation pathway.
FT CHAIN 1..3268
FT /note="E3 ubiquitin-protein ligase TOM1"
FT /id="PRO_0000120348"
FT DOMAIN 2932..3268
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 1941..2023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2038..2083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2416..2443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1941..1962
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2006..2023
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2038..2052
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2423..2443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3235
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT MOD_RES 1890
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 2096
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 2119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 2376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 2406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 2418
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MUTAGEN 3235
FT /note="C->A: Loss of function. Induces a decrease in
FT transcription activation."
FT /evidence="ECO:0000269|PubMed:10395901,
FT ECO:0000269|PubMed:10873801, ECO:0000269|PubMed:9753545"
SQ SEQUENCE 3268 AA; 374185 MW; 8F71F3493D70A6C9 CRC64;
MVLFTRCEKA RKEKLAAGYK PLVDYLIDCD TPTFLERIEA IQEWDRSRDD LYVWIPILDR
MDGLLLKVAE KYKYKQDPKK ECEVKLVEME AHDVDYCLKM LKFTRRLLLN TENRFVYSSG
DVLMYLLNCP NFTIKLAVMR ILAILGERFV IAREKIVAHN IFGDHNLRKK TLKLALSLSS
SVMDEDGEHF SLVDLYFDKK KVPQKWRKLR FTHYTSNDFK KSSQQKNNIN ETQTSIKKVT
MTTQELCEHS LQQIFDKGMA LLPAESWFDF SIKASVAKAF SDDSGENIDL RNIIIETKLN
AIAFVNTIFS PPQVSSKLFE LDPYAFNSLT DLISLSETKI PKELRTDALF TLECISLKHV
WCSDIIRNLG GNISHGLLFQ ILRYIAKTLR EATDEIDEEY NVRFFYLISN LADVKPLHES
LFAAGLIPTL LEIVSIRNCP YKRTLASATH LLETFIDNSE TTTEFIENDG FTMLITSVAN
EIDFTLAHPE TWQPPKYSVV YYSISFRELA YIRSLLKLVL KLLSTDSGDR IRNLIDSPIL
VSLKKILENK LVFGLTLITY TLDVVQKVIN SEPTIYPVLV EAGLIPYVID NFPKLIGPSA
ELLSLLPDVV SAICLNPEGL KQVKEKGLIN NLFDFLLDAD HARILTGGDR STEYGTDIDE
LARHYPDLKA NIVEALCNVI RKMPSTFRNE REFLFTSPKD QKYFFHRKNE EILTDKEEHE
PAYWELLDKG TMLDTFTSVL FGMSLGNGSF SQVPQHLEAR DFLAIIFMEN PPYEYFTSVA
ISNVTEVLQY LDEKYEDYAF MDVMKVLNDQ LENLNDFLNS PNDRSFFLER DGENSVRSCH
SKLCRLAAIL NIVTNVYIDL TTLSCKRIMQ IYSYFDKRGF SLIKNLKLLF QKCALEEMYI
RQHMPDSVIT ETMPLPIVDV SGDGPPLQIY IDDPKKGDQK GKITSVKTRN TLQMRTILYT
LQSNTAILFR CFLRLSHSRN MDLEHKDLTT EVHIFENVVE NVIEMLKATE LEGHLPYILV
LLNFNTFVFT IPKASPNSTE ILQTIPAYIF YQKGGYLLYL HIIRDLFTRM TKIKDLSSLD
NINYIDESNG ILTLSCLINA LTFYNKSMQT ETMENVQSIG KYYVSIDDDY NIMKALTVPI
KVMALAMILD LDKSDSLFKT QSRNVPYSVF KQLLSMLKNI FTNVNIYTKE LYELHWDLIF
PPIKKISLFE QVGIPGDVAA NYLTDTGDDL PADNSIGLFS PEQWEKYKKL IGEDKSIYYP
QPMQAQYYKG CSSKELDELR DTFFNDGLPS RIFTVLPFYP KLVNAFAKTL LQIFTKYDEP
TEVFAGRILD RILETDLDDP ATLSSLIHLF GIFLNEKYIY QKASHLMQRF IEYLEKSLKP
EHVNTPWFSK ALYVYEIILA KSELPHLEEL SKDVLLRYPL LSMAKVFRIP DPMKQKLFDI
LIRVSDISNF YSALATSRIL IFYSRDELYA NNIARSGILS RLLKVIGSFQ KLDKINFLES
SFLLLTRRCF ETTENVDALI RAEINRSFTA RPLGGGDDAV RELTTILEEK AHVVMRSPSQ
FIDVLCETAR FHEFDDQGAL VDYSLKRFLG EKDKNTQASS TEKSDIYERT GIMHLLLSQL
MAASEKDWLS EPANSSDLPE NKKAQLDPSR NPVCAYMIFL LKLLVELVSS YNQCKFEFLT
FSRRNTYAER PRPRTTAINF FLYRLLDKPV GTDHDKHEAK RREVIGMLAR SVIIGFLATV
QDDRTTKTDV KLADPHMNFI RKFAIEAIIK AIRNATSSSK LLESNHLKLD MWFRIITSMV
YVQAPYLRQL LDSNKVEADQ YQLCKLVIDL GLPSVITEAM ASIDLNYPFS KKIFNVAVEA
LNTISSTRNN FSEHFKIEDH DEVEDEVDES DKEEIPDMFK NSALGMYDVE DIEEDDDDDT
SLIGDDDAMA FVDSDNGFEV VFSDEDDDMG EEDADDARSD SEENELSSEM QSSTADGTDV
DYEVDDADGL IINIDQPSGD DEEMADYDAN ISHSSHSENE DDASMDVIEV YDDELSSGYD
VDLSDYDVDE SDWDSGLSSL SISDEDSESS EDEPINSTRM GDSRRRWLIA EGVELTDDSQ
GESEEDDRGV FRGIEHIFSN ENEPLFRVHD EMRHRNHHRS INRTHFHSAM SAPSLSLLNR
GRRNQSNLIN PLGPTGLEQV ENDISDQVTV AGSGSRPRSH HLHFSEVLVS GSFFDEPVLD
GIILKSTVSR WKDIFDMFYD SKTYANCIIP TVINRLYKVS LALQKDLENK REQEKLKNKN
LLFNEAKVES HNSSDAISVE QDDIQESNVT HDDHEPVYVT IQGSEVDIGG TDIDPEFMNA
LPDDIRADVF AQHVRERRAE ARLNSDHNVH SREIDSDFLE AIPEDIREGI LDTEAEEQRM
FGRIGSSADV IRADDDVSNN DEEVENGLDH GNSNDRNNAD PEKKKPARIY FAPLIDRAGI
ASLMKSVFIS KPYIQREIYH ELFYRLCSSK QNRNDLMNTF LFILSEGIID QHSLEKVYNI
ISSRAMGHAK TTTVRQLPSD CTPLTVANQT IEILQSLIDA DSRLKYFLIA EHDNLIVNKA
NNKSRKEALP DKKLRWPLWH LFSLLDRKLI TDESVLMDLL TRILQVCTKT LAVLSTSSNG
KENLSKKFHL PSFDEDDLMK ILSIIMLDSC TTRVFQQTLN IIYNLSKLQG CMSIFTKHLV
SLAISIMSKL KSALDGLSRE VGTITTGMEI NSELLQKFTL PSSDQAKLLK ILTTVDFLYT
HKRKEEERNV KDLQSLYDKM NGGPVWSSLS ECLSQFEKSQ AINTSATILL PLIESLMVVC
RRSDLSQNRN TAVKYEDAKL LDFSKTRVEN LFFPFTDAHK KLLNQMIRSN PKLMSGPFAL
LVKNPKVLDF DNKRYFFNAK LKSDNQERPK LPITVRREQV FLDSYRALFF KTNDEIKNSK
LEITFKGESG VDAGGVTREW YQVLSRQMFN PDYALFLPVP SDKTTFHPNR TSGINPEHLS
FFKFIGMIIG KAIRDQCFLD CHFSREVYKN ILGRPVSLKD MESLDPDYYK SLVWILENDI
TDIIEETFSV ETDDYGEHKV INLIEGGKDI IVTEANKQDY VKKVVEYKLQ TSVKEQMDNF
LVGFYALISK DLITIFDEQE LELLISGLPD IDVDDWKNNT TYVNYTATCK EVSYFWRAVR
SFDAEERAKL LQFVTGTSKV PLNGFKELSG VNGVCKFSIH RDFGSSERLP SSHTCFNQLN
LPPYESYETL RGSLLLAINE GHEGFGLA
