ADAL_ARATH
ID ADAL_ARATH Reviewed; 355 AA.
AC Q8LPL7; Q9M0Z1;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=N6-mAMP deaminase {ECO:0000303|PubMed:29884623};
DE Short=AtMAPDA {ECO:0000303|PubMed:29884623};
DE EC=3.5.4.- {ECO:0000269|PubMed:29884623};
DE AltName: Full=Adenosine deaminase-like protein {ECO:0000305};
GN Name=MAPDA {ECO:0000303|PubMed:29884623};
GN Synonyms=ADAL {ECO:0000303|PubMed:29884623};
GN OrderedLocusNames=At4g04880 {ECO:0000312|Araport:AT4G04880};
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 [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 [2]
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 [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, MUTAGENESIS OF VAL-57, AND DISRUPTION PHENOTYPE.
RX PubMed=29884623; DOI=10.1105/tpc.18.00236;
RA Chen M., Urs M.J., Sanchez-Gonzalez I., Olayioye M.A., Herde M.,
RA Witte C.P.;
RT "m6A RNA degradation products are catabolized by an evolutionarily
RT conserved N6-methyl-AMP deaminase in plant and mammalian cells.";
RL Plant Cell 30:1511-1522(2018).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) IN COMPLEX WITH N(6)-METHYL-AMP AND
RP ZINC ION, FUNCTION, SUBUNIT, AND MUTAGENESIS OF HIS-15; ASN-17; HIS-65;
RP THR-97; THR-98; LYS-100; GLU-220; ASP-295 AND ASP-296.
RX PubMed=30721978; DOI=10.1093/nar/gkz070;
RA Jia Q., Xie W.;
RT "Alternative conformation induced by substrate binding for Arabidopsis
RT thaliana N6-methyl-AMP deaminase.";
RL Nucleic Acids Res. 47:3233-3243(2019).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH N(6)-METHYL-AMP AND
RP ZINC ION, FUNCTION, AND MUTAGENESIS OF ASP-295.
RX PubMed=31318636; DOI=10.1080/15476286.2019.1642712;
RA Wu B., Zhang D., Nie H., Shen S., Li Y., Li S.;
RT "Structure of Arabidopsis thaliana N6-methyl-AMP deaminase ADAL with bound
RT GMP and IMP and implications for N6-methyl-AMP recognition and
RT processing.";
RL RNA Biol. 2019:1-9(2019).
CC -!- FUNCTION: Catalyzes the hydrolysis of the free cytosolic methylated
CC adenosine nucleotide N(6)-methyl-AMP (N6-mAMP) to produce inositol
CC monophosphate (IMP) and methylamine (PubMed:29884623, PubMed:30721978,
CC PubMed:31318636). Is required for the catabolism of cytosolic N6-mAMP,
CC which is derived from the degradation of mRNA containing N6-methylated
CC adenine (m6A) (PubMed:29884623). Does not possess deaminase activity
CC toward adenosine, AMP, N6-methyladenosine, or N6-mATP in vitro
CC (PubMed:29884623). {ECO:0000269|PubMed:29884623,
CC ECO:0000269|PubMed:30721978, ECO:0000269|PubMed:31318636}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O + N(6)-methyl-AMP = IMP + methylamine;
CC Xref=Rhea:RHEA:16001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:59338, ChEBI:CHEBI:144842;
CC Evidence={ECO:0000269|PubMed:29884623};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16002;
CC Evidence={ECO:0000269|PubMed:29884623};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:29884623, ECO:0000269|PubMed:30721978,
CC ECO:0000269|PubMed:31318636};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:30721978,
CC ECO:0000269|PubMed:31318636};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.17 uM for N(6)-methyl-AMP {ECO:0000269|PubMed:29884623};
CC Note=kcat is 0.21 sec(-1) with N(6)-methyl-AMP as substrate.
CC {ECO:0000269|PubMed:29884623};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:30721978}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:29884623}.
CC -!- DISRUPTION PHENOTYPE: Slight reduction of root growth
CC (PubMed:29884623). 10-fold increase of the ratio N(6)-methyl-AMP/AMP in
CC leaf cells (PubMed:29884623). {ECO:0000269|PubMed:29884623}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB80853.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL161501; CAB80853.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82436.1; -; Genomic_DNA.
DR EMBL; AY099563; AAM20415.1; -; mRNA.
DR EMBL; BT001246; AAN65133.1; -; mRNA.
DR PIR; D85061; D85061.
DR RefSeq; NP_192397.2; NM_116726.4.
DR PDB; 6IJM; X-ray; 2.02 A; A=1-355.
DR PDB; 6IJN; X-ray; 1.66 A; A=1-355.
DR PDB; 6IJP; X-ray; 1.85 A; A=1-355.
DR PDB; 6IV5; X-ray; 1.75 A; A=1-355.
DR PDB; 6J23; X-ray; 1.90 A; A=1-355.
DR PDB; 6J4T; X-ray; 1.82 A; A=1-355.
DR PDBsum; 6IJM; -.
DR PDBsum; 6IJN; -.
DR PDBsum; 6IJP; -.
DR PDBsum; 6IV5; -.
DR PDBsum; 6J23; -.
DR PDBsum; 6J4T; -.
DR AlphaFoldDB; Q8LPL7; -.
DR SMR; Q8LPL7; -.
DR STRING; 3702.AT4G04880.1; -.
DR PaxDb; Q8LPL7; -.
DR PRIDE; Q8LPL7; -.
DR ProteomicsDB; 181029; -.
DR EnsemblPlants; AT4G04880.1; AT4G04880.1; AT4G04880.
DR GeneID; 825826; -.
DR Gramene; AT4G04880.1; AT4G04880.1; AT4G04880.
DR KEGG; ath:AT4G04880; -.
DR Araport; AT4G04880; -.
DR TAIR; locus:2138967; AT4G04880.
DR eggNOG; KOG1097; Eukaryota.
DR HOGENOM; CLU_039228_3_0_1; -.
DR InParanoid; Q8LPL7; -.
DR OMA; RPQFKPY; -.
DR PhylomeDB; Q8LPL7; -.
DR PRO; PR:Q8LPL7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8LPL7; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0019239; F:deaminase activity; IMP:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0062154; F:N6-mAMP deaminase activity; IDA:TAIR.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006401; P:RNA catabolic process; IMP:TAIR.
DR InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11409; PTHR11409; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Metal-binding; Nucleotide metabolism;
KW Reference proteome; Zinc.
FT CHAIN 1..355
FT /note="N6-mAMP deaminase"
FT /id="PRO_0000448573"
FT ACT_SITE 220
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P03958"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:30721978,
FT ECO:0000269|PubMed:31318636, ECO:0007744|PDB:6IJM,
FT ECO:0007744|PDB:6IV5"
FT BINDING 15
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000269|PubMed:30721978,
FT ECO:0007744|PDB:6IJN"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:30721978,
FT ECO:0000269|PubMed:31318636, ECO:0007744|PDB:6IJM,
FT ECO:0007744|PDB:6IV5"
FT BINDING 17
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000269|PubMed:30721978,
FT ECO:0000269|PubMed:31318636, ECO:0007744|PDB:6IJN,
FT ECO:0007744|PDB:6J4T"
FT BINDING 65
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000269|PubMed:30721978,
FT ECO:0000269|PubMed:31318636, ECO:0007744|PDB:6IJN,
FT ECO:0007744|PDB:6J4T"
FT BINDING 97..100
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000269|PubMed:30721978,
FT ECO:0000269|PubMed:31318636, ECO:0007744|PDB:6IJN,
FT ECO:0007744|PDB:6J4T"
FT BINDING 160
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000269|PubMed:30721978,
FT ECO:0000269|PubMed:31318636, ECO:0007744|PDB:6IJN,
FT ECO:0007744|PDB:6J4T"
FT BINDING 190
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000269|PubMed:30721978,
FT ECO:0000269|PubMed:31318636, ECO:0007744|PDB:6IJN,
FT ECO:0007744|PDB:6J4T"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:30721978,
FT ECO:0000269|PubMed:31318636, ECO:0007744|PDB:6IJM,
FT ECO:0007744|PDB:6IV5"
FT BINDING 220
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000269|PubMed:30721978,
FT ECO:0000269|PubMed:31318636, ECO:0007744|PDB:6IJP,
FT ECO:0007744|PDB:6J4T"
FT BINDING 295
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000269|PubMed:30721978,
FT ECO:0007744|PDB:6IJP"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:30721978,
FT ECO:0000269|PubMed:31318636, ECO:0007744|PDB:6IJM,
FT ECO:0007744|PDB:6IV5"
FT BINDING 296
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000269|PubMed:30721978,
FT ECO:0007744|PDB:6IJP"
FT SITE 240
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P03958"
FT MUTAGEN 15
FT /note="H->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:30721978"
FT MUTAGEN 17
FT /note="N->A: Reduces catalytic efficiency 2-fold."
FT /evidence="ECO:0000269|PubMed:30721978"
FT MUTAGEN 57
FT /note="V->F: Reduces catalytic efficiency 20-fold."
FT /evidence="ECO:0000269|PubMed:29884623"
FT MUTAGEN 65
FT /note="H->A: Reduces catalytic efficiency 2-fold."
FT /evidence="ECO:0000269|PubMed:30721978"
FT MUTAGEN 97
FT /note="T->A: Reduces catalytic efficiency 3-fold."
FT /evidence="ECO:0000269|PubMed:30721978"
FT MUTAGEN 98
FT /note="T->A: Reduces catalytic efficiency 2-fold."
FT /evidence="ECO:0000269|PubMed:30721978"
FT MUTAGEN 100
FT /note="K->A: Reduces catalytic efficiency 3-fold."
FT /evidence="ECO:0000269|PubMed:30721978"
FT MUTAGEN 220
FT /note="E->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:30721978"
FT MUTAGEN 295
FT /note="D->A,N: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:30721978,
FT ECO:0000269|PubMed:31318636"
FT MUTAGEN 296
FT /note="D->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:30721978"
FT HELIX 1..6
FT /evidence="ECO:0007829|PDB:6IJN"
FT STRAND 9..15
FT /evidence="ECO:0007829|PDB:6IJN"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:6IJN"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:6IJN"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:6IJN"
FT HELIX 54..68
FT /evidence="ECO:0007829|PDB:6IJN"
FT HELIX 71..87
FT /evidence="ECO:0007829|PDB:6IJN"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:6IJN"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:6IJN"
FT HELIX 109..121
FT /evidence="ECO:0007829|PDB:6IJN"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:6IJN"
FT STRAND 150..160
FT /evidence="ECO:0007829|PDB:6IJN"
FT HELIX 165..177
FT /evidence="ECO:0007829|PDB:6IJN"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:6IJN"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:6IJN"
FT HELIX 197..209
FT /evidence="ECO:0007829|PDB:6IJN"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:6IJN"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:6IJN"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:6IJN"
FT HELIX 246..255
FT /evidence="ECO:0007829|PDB:6IJN"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:6IJN"
FT HELIX 263..268
FT /evidence="ECO:0007829|PDB:6IJN"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:6IJN"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:6IJN"
FT HELIX 279..285
FT /evidence="ECO:0007829|PDB:6IJN"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:6IJN"
FT TURN 297..301
FT /evidence="ECO:0007829|PDB:6IJN"
FT HELIX 304..315
FT /evidence="ECO:0007829|PDB:6IJN"
FT HELIX 319..328
FT /evidence="ECO:0007829|PDB:6IJN"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:6IJN"
FT HELIX 337..350
FT /evidence="ECO:0007829|PDB:6IJN"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:6IJN"
SQ SEQUENCE 355 AA; 39949 MW; FF042073AC6FE508 CRC64;
MEWIQSLPKI ELHAHLNGSI RDSTLLELAR VLGEKGVIVF ADVEHVIQKN DRSLVEVFKL
FDLIHKLTTD HKTVTRITRE VVEDFALENV VYLELRTTPK RSDSIGMSKR SYMEAVIQGL
RSVSEVDIDF VTASDSQKLH NAGDGIGRKK IYVRLLLSID RRETTESAME TVKLALEMRD
VGVVGIDLSG NPLVGEWSTF LPALQYAKDN DLHITLHCGE VPNPKEIQAM LDFKPHRIGH
ACFFKDEDWT KLKSFRIPVE ICLTSNIVTK SISSIDIHHF ADLYNAKHPL ILCTDDFGVF
STSLSNEYAL AVRSLGLSKS ETFALARAAI DATFAEDEVK QQLRFIFDSA SPEHV
