FBRL2_ARATH
ID FBRL2_ARATH Reviewed; 320 AA.
AC Q94AH9; Q9SZZ1;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=rRNA 2'-O-methyltransferase fibrillarin 2;
DE Short=AtFib2 {ECO:0000303|PubMed:10829025};
DE EC=2.1.1.- {ECO:0000305|PubMed:10829025};
DE AltName: Full=Fibrillarin-like protein 2;
DE AltName: Full=Histone-glutamine methyltransferase;
GN Name=FIB2 {ECO:0000303|PubMed:10829025};
GN Synonyms=FLP {ECO:0000303|PubMed:10806224},
GN MED36_1 {ECO:0000303|PubMed:22021418}, MED36A;
GN OrderedLocusNames=At4g25630 {ECO:0000312|Araport:AT4G25630};
GN ORFNames=L73G19.10 {ECO:0000312|EMBL:CAB43694.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=10829025; DOI=10.1074/jbc.m002996200;
RA Barneche F., Steinmetz F., Echeverria M.;
RT "Fibrillarin genes encode both a conserved nucleolar protein and a novel
RT small nucleolar RNA involved in ribosomal RNA methylation in Arabidopsis
RT thaliana.";
RL J. Biol. Chem. 275:27212-27220(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=10806224; DOI=10.1104/pp.123.1.51;
RA Pih K.T., Yi M.J., Liang Y.S., Shin B.J., Cho M.J., Hwang I., Son D.;
RT "Molecular cloning and targeting of a fibrillarin homolog from
RT Arabidopsis.";
RL Plant Physiol. 123:51-58(2000).
RN [7]
RP INTERACTION WITH PRMT11 AND PRMT12.
RX PubMed=17666011; DOI=10.1042/bj20070786;
RA Yan D., Zhang Y., Niu L., Yuan Y., Cao X.;
RT "Identification and characterization of two closely related histone H4
RT arginine 3 methyltransferases in Arabidopsis thaliana.";
RL Biochem. J. 408:113-121(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17560376; DOI=10.1016/j.molcel.2007.05.007;
RA Baeckstroem S., Elfving N., Nilsson R., Wingsle G., Bjoerklund S.;
RT "Purification of a plant mediator from Arabidopsis thaliana identifies PFT1
RT as the Med25 subunit.";
RL Mol. Cell 26:717-729(2007).
RN [9]
RP INTERACTION WITH GROUNDNUT ROSETTE VIRUS LONG-DISTANCE MOVEMENT PROTEIN.
RX PubMed=17576925; DOI=10.1073/pnas.0704632104;
RA Kim S.H., Macfarlane S., Kalinina N.O., Rakitina D.V., Ryabov E.V.,
RA Gillespie T., Haupt S., Brown J.W., Taliansky M.;
RT "Interaction of a plant virus-encoded protein with the major nucleolar
RT protein fibrillarin is required for systemic virus infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:11115-11120(2007).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=18322146; DOI=10.1104/pp.107.111799;
RA Degenhardt R.F., Bonham-Smith P.C.;
RT "Arabidopsis ribosomal proteins RPL23aA and RPL23aB are differentially
RT targeted to the nucleolus and are disparately required for normal
RT development.";
RL Plant Physiol. 147:128-142(2008).
RN [11]
RP FUNCTION, INTERACTION WITH RNA, AND MUTAGENESIS OF 180-GLY--PHE-187.
RX PubMed=21785141; DOI=10.1093/nar/gkr594;
RA Rakitina D.V., Taliansky M., Brown J.W., Kalinina N.O.;
RT "Two RNA-binding sites in plant fibrillarin provide interactions with
RT various RNA substrates.";
RL Nucleic Acids Res. 39:8869-8880(2011).
RN [12]
RP NOMENCLATURE.
RX PubMed=22021418; DOI=10.1104/pp.111.188300;
RA Mathur S., Vyas S., Kapoor S., Tyagi A.K.;
RT "The Mediator complex in plants: structure, phylogeny, and expression
RT profiling of representative genes in a dicot (Arabidopsis) and a monocot
RT (rice) during reproduction and abiotic stress.";
RL Plant Physiol. 157:1609-1627(2011).
RN [13]
RP INTERACTION WITH HORDEIVIRUS TGB1 MOVEMENT PROTEIN.
RX PubMed=22349738; DOI=10.1016/j.biochi.2012.02.005;
RA Semashko M.A., Gonzalez I., Shaw J., Leonova O.G., Popenko V.I.,
RA Taliansky M.E., Canto T., Kalinina N.O.;
RT "The extreme N-terminal domain of a hordeivirus TGB1 movement protein
RT mediates its localization to the nucleolus and interaction with
RT fibrillarin.";
RL Biochimie 94:1180-1188(2012).
RN [14]
RP FUNCTION.
RX PubMed=29163603; DOI=10.3389/fpls.2017.01878;
RA Rodriguez-Corona U., Pereira-Santana A., Sobol M., Rodriguez-Zapata L.C.,
RA Hozak P., Castano E.;
RT "Novel ribonuclease activity differs between fibrillarins from Arabidopsis
RT thaliana.";
RL Front. Plant Sci. 8:1878-1878(2017).
RN [15]
RP FUNCTION, AND INTERACTION WITH MED19A AND THE LNCRNA ELENA1 (AT4G16355).
RX PubMed=30307032; DOI=10.1111/nph.15530;
RA Seo J.S., Diloknawarit P., Park B.S., Chua N.H.;
RT "ELF18-INDUCED LONG NONCODING RNA 1 evicts fibrillarin from mediator
RT subunit to enhance PATHOGENESIS-RELATED GENE 1 (PR1) expression.";
RL New Phytol. 221:2067-2079(2019).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that has
CC the ability to methylate both RNAs and proteins (Probable). Involved in
CC pre-rRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine
CC to catalyze the site-specific 2'-hydroxyl methylation of ribose
CC moieties in pre-ribosomal RNA (Probable). Site specificity is provided
CC by a guide RNA that base pairs with the substrate (Probable).
CC Methylation occurs at a characteristic distance from the sequence
CC involved in base pairing with the guide RNA (Probable). Also acts as a
CC protein methyltransferase by mediating methylation of 'Gln-105' of
CC histone H2A (H2AQ105me), a modification that impairs binding of the
CC FACT complex and is specifically present at 35S ribosomal DNA locus (By
CC similarity). Acts as negative regulator of expression of immune
CC responsive genes, including pathogenesis-related gene 1 (PR1), and of
CC resistance against bacterial pathogen (PubMed:30307032). Binds to
CC MED19A, a positive regulator of PR1 expression, to repress the
CC activator activity of MED19A (PubMed:30307032). In response to the
CC bacterial pathogen-associated molecular pattern (PAMP) elf18,
CC associates with the long non-coding RNA (lncRNA) ELENA1 (At4g16355),
CC and releases its repression of MED19A (PubMed:30307032). Possesses
CC ribonuclease activity toward rRNA in vitro (PubMed:29163603). Binds
CC phosphoinositides, phospholipids and phosphatidic acid in vitro
CC (PubMed:29163603). {ECO:0000250|UniProtKB:P15646,
CC ECO:0000269|PubMed:29163603, ECO:0000269|PubMed:30307032,
CC ECO:0000305|PubMed:10829025}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleotide in rRNA + S-adenosyl-L-methionine = a 2'-O-
CC methylribonucleotide in rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:48628, Rhea:RHEA-COMP:12164, Rhea:RHEA-COMP:12165,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90675, ChEBI:CHEBI:90676;
CC Evidence={ECO:0000305|PubMed:10829025};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48629;
CC Evidence={ECO:0000305|PubMed:10829025};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutaminyl-[histone H2A] + S-adenosyl-L-methionine = H(+) +
CC N(5)-methyl-L-glutaminyl-[histone H2A] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:50904, Rhea:RHEA-COMP:12837, Rhea:RHEA-COMP:12839,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30011, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61891;
CC Evidence={ECO:0000250|UniProtKB:P15646};
CC -!- SUBUNIT: Component of box C/D small nucleolar ribonucleoprotein
CC (snoRNP) particles (By similarity). Interacts with groundnut rosette
CC virus long-distance movement protein; this interaction is required for
CC virus long-distance movement protein transiting through host Cajal body
CC and nucleolus, relocalization of fibrillarin to the cytoplasm, and in
CC presence of viral RNA, leads to the formation of stable RNPs
CC (PubMed:17576925). Interacts (via GAR domain) with the hordeivirus TGB1
CC movement protein (via the first 82 amino acid residues)
CC (PubMed:22349738). Interacts with PRMT11 and PRMT12 (PubMed:17666011).
CC Interacts with MED19A (PubMed:30307032). {ECO:0000250|UniProtKB:P15646,
CC ECO:0000269|PubMed:17576925, ECO:0000269|PubMed:17666011,
CC ECO:0000269|PubMed:22349738, ECO:0000269|PubMed:30307032}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:18322146}.
CC Note=Localizes to the fibrillar region of the nucleolus. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and flowers (PubMed:10829025,
CC PubMed:10806224). Expressed in leaves and stems (PubMed:10806224).
CC Expression levels decrease during aging (PubMed:10806224).
CC {ECO:0000269|PubMed:10806224, ECO:0000269|PubMed:10829025}.
CC -!- INDUCTION: Repressed by abscisic acid (ABA).
CC {ECO:0000269|PubMed:10806224}.
CC -!- DOMAIN: The N-terminal DMA/Gly-rich region (also called GAR domain) is
CC rich in Gly and Arg and functions in nucleolar targeting (By
CC similarity). The central (138-179) and C-terminal (225-281) part of the
CC protein exhibit cooperative RNA-binding activities. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9FEF8}.
CC -!- PTM: Methylated by PRMT11 and PRMT12.
CC -!- MISCELLANEOUS: Baeckstroem et al identified FIB2 in a Mediator complex
CC pull-down assay and suggested that FIB2 could be a plant specific
CC component of the Mediator complex (PubMed:17560376). However, no
CC experimental evidence has been brought so far to confirm this
CC hypothesis (Probable). {ECO:0000269|PubMed:17560376, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Fibrillarin
CC family. {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; AF233444; AAG10104.1; -; mRNA.
DR EMBL; AF267171; AAG10153.1; -; Genomic_DNA.
DR EMBL; AL050400; CAB43694.1; -; Genomic_DNA.
DR EMBL; AL161563; CAB81373.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85085.1; -; Genomic_DNA.
DR EMBL; AY046027; AAK76701.1; -; mRNA.
DR EMBL; AY142647; AAN13105.1; -; mRNA.
DR EMBL; AY084608; AAM61172.1; -; mRNA.
DR PIR; T09555; T09555.
DR RefSeq; NP_567724.1; NM_118695.4.
DR AlphaFoldDB; Q94AH9; -.
DR SMR; Q94AH9; -.
DR BioGRID; 13955; 87.
DR DIP; DIP-39086N; -.
DR IntAct; Q94AH9; 7.
DR STRING; 3702.AT4G25630.1; -.
DR SwissPalm; Q94AH9; -.
DR PaxDb; Q94AH9; -.
DR PRIDE; Q94AH9; -.
DR ProteomicsDB; 238247; -.
DR EnsemblPlants; AT4G25630.1; AT4G25630.1; AT4G25630.
DR GeneID; 828668; -.
DR Gramene; AT4G25630.1; AT4G25630.1; AT4G25630.
DR KEGG; ath:AT4G25630; -.
DR Araport; AT4G25630; -.
DR TAIR; locus:2131386; AT4G25630.
DR eggNOG; KOG1596; Eukaryota.
DR HOGENOM; CLU_059055_1_0_1; -.
DR InParanoid; Q94AH9; -.
DR OMA; INMATHR; -.
DR OrthoDB; 1411035at2759; -.
DR PhylomeDB; Q94AH9; -.
DR PRO; PR:Q94AH9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94AH9; baseline and differential.
DR Genevisible; Q94AH9; AT.
DR GO; GO:0031428; C:box C/D RNP complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:1990259; F:histone-glutamine methyltransferase activity; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0004540; F:ribonuclease activity; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IDA:TAIR.
DR GO; GO:0008649; F:rRNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0030515; F:snoRNA binding; ISS:TAIR.
DR GO; GO:0000494; P:box C/D RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:1990258; P:histone glutamine methylation; IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00351; RNA_methyltransf_FlpA; 1.
DR InterPro; IPR000692; Fibrillarin.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01269; Fibrillarin; 1.
DR PIRSF; PIRSF006540; Nop17p; 1.
DR PRINTS; PR00052; FIBRILLARIN.
DR SMART; SM01206; Fibrillarin; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Methylation; Methyltransferase; Nucleus; Plant defense; Reference proteome;
KW Ribonucleoprotein; RNA-binding; rRNA processing; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..320
FT /note="rRNA 2'-O-methyltransferase fibrillarin 2"
FT /id="PRO_0000148519"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 167..168
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9Y9U3"
FT BINDING 186..187
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT BINDING 211..212
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT BINDING 231..234
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P22087"
FT MUTAGEN 180..187
FT /note="GCVYAVEF->AAAAAAAA: No effect on RNA binding."
FT /evidence="ECO:0000269|PubMed:21785141"
FT CONFLICT 181
FT /note="C -> S (in Ref. 4; AAK76701)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 33653 MW; 0E3DF1733F52CFDC CRC64;
MRPPLTGSGG GFSGGRGRGG YSGGRGDGGF SGGRGGGGRG GGRGFSDRGG RGRGRGPPRG
GARGGRGPAG RGGMKGGSKV IVEPHRHAGV FIAKGKEDAL VTKNLVPGEA VYNEKRISVQ
NEDGTKTEYR VWNPFRSKLA AAILGGVDNI WIKPGAKVLY LGAASGTTVS HVSDLVGPEG
CVYAVEFSHR SGRDLVNMAK KRTNVIPIIE DARHPAKYRM LVGMVDVIFS DVAQPDQARI
LALNASYFLK SGGHFVISIK ANCIDSTVPA EAVFQTEVKK LQQEQFKPAE QVTLEPFERD
HACVVGGYRM PKKPKAATAA
