4CLL6_ARATH
ID 4CLL6_ARATH Reviewed; 566 AA.
AC Q84P24; O49414; Q8GYV8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=4-coumarate--CoA ligase-like 6 {ECO:0000303|PubMed:12805634};
DE EC=6.2.1.- {ECO:0000305|PubMed:18267944};
DE AltName: Full=4-coumarate--CoA ligase {ECO:0000303|PubMed:24838974};
DE EC=6.2.1.12 {ECO:0000269|PubMed:24838974};
DE AltName: Full=4-coumarate--CoA ligase isoform 7;
DE Short=At4CL7;
DE AltName: Full=4-hydroxybenzoate--CoA ligase {ECO:0000303|PubMed:24838974};
DE EC=6.2.1.27 {ECO:0000269|PubMed:24838974};
GN Name=4CLL6 {ECO:0000303|PubMed:12805634};
GN OrderedLocusNames=At4g19010 {ECO:0000312|Araport:AT4G19010};
GN ORFNames=F13C5.180 {ECO:0000312|EMBL:CAA16758.1};
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 [MRNA], AND GENE FAMILY ORGANIZATION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=12805634; DOI=10.1104/pp.103.020552;
RA Shockey J.M., Fulda M.S., Browse J.;
RT "Arabidopsis contains a large superfamily of acyl-activating enzymes.
RT Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme
RT a synthetases.";
RL Plant Physiol. 132:1065-1076(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lawrence P.K.;
RT "Functional classification of Arabidopsis thaliana 4-coumarate CoA ligase
RT genes.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
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 [7]
RP GENE FAMILY ORGANIZATION.
RX PubMed=12819348; DOI=10.1073/pnas.1430550100;
RA Schneider K., Hoevel K., Witzel K., Hamberger B., Schomburg D.,
RA Kombrink E., Stuible H.-P.;
RT "The substrate specificity-determining amino acid code of 4-coumarate:CoA
RT ligase.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8601-8606(2003).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=18267944; DOI=10.1093/jxb/erm325;
RA Kienow L., Schneider K., Bartsch M., Stuible H.-P., Weng H., Miersch O.,
RA Wasternack C., Kombrink E.;
RT "Jasmonates meet fatty acids: functional analysis of a new acyl-coenzyme A
RT synthetase family from Arabidopsis thaliana.";
RL J. Exp. Bot. 59:403-419(2008).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24838974; DOI=10.1105/tpc.114.125807;
RA Block A., Widhalm J.R., Fatihi A., Cahoon R.E., Wamboldt Y., Elowsky C.,
RA Mackenzie S.A., Cahoon E.B., Chapple C., Dudareva N., Basset G.J.;
RT "The Origin and Biosynthesis of the Benzenoid Moiety of Ubiquinone
RT (Coenzyme Q) in Arabidopsis.";
RL Plant Cell 26:1938-1948(2014).
CC -!- FUNCTION: Contributes to jasmonic acid biosynthesis by initiating the
CC beta-oxidative chain shortening of its precursors (PubMed:18267944).
CC CoA ligase that can use preferentially p-coumarate, ferulate and
CC caffeate as substrates and can use, with a lower efficiency, t-
CC cinnamate and 4-hydroxybenzoate as substrates (PubMed:24838974).
CC Involved in the biosynthesis of ubiquinone from phenylalanine by
CC activating the propyl side chain of 4-coumarate, and possibly trans-
CC cinnamate and 4-hydroxybenzoate, for subsequent beta-oxidative
CC shortening and the formation of the benzenoid moiety of ubiquinone
CC (PubMed:24838974). {ECO:0000269|PubMed:18267944,
CC ECO:0000269|PubMed:24838974}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + tetradecanoate = AMP + diphosphate +
CC tetradecanoyl-CoA; Xref=Rhea:RHEA:33619, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57385, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:18267944};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33620;
CC Evidence={ECO:0000269|PubMed:18267944};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexanoate = AMP + diphosphate + hexanoyl-CoA;
CC Xref=Rhea:RHEA:43740, ChEBI:CHEBI:17120, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:18267944};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43741;
CC Evidence={ECO:0000269|PubMed:18267944};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + heptanoate = AMP + diphosphate + heptanoyl-CoA;
CC Xref=Rhea:RHEA:44088, ChEBI:CHEBI:30616, ChEBI:CHEBI:32362,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:78811,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:18267944};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44089;
CC Evidence={ECO:0000269|PubMed:18267944};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-caffeate + ATP + CoA = (E)-caffeoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:36299, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57770,
CC ChEBI:CHEBI:87136, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:24838974};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36300;
CC Evidence={ECO:0000269|PubMed:24838974};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-ferulate + ATP + CoA = (E)-feruloyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:36251, ChEBI:CHEBI:29749,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:87305, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:24838974};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36252;
CC Evidence={ECO:0000269|PubMed:24838974};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:19641, ChEBI:CHEBI:12876,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:85008, ChEBI:CHEBI:456215; EC=6.2.1.12;
CC Evidence={ECO:0000269|PubMed:24838974};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19642;
CC Evidence={ECO:0000269|PubMed:24838974};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybenzoate + ATP + CoA = 4-hydroxybenzoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:23116, ChEBI:CHEBI:17879,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57356, ChEBI:CHEBI:456215; EC=6.2.1.27;
CC Evidence={ECO:0000269|PubMed:24838974};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23117;
CC Evidence={ECO:0000269|PubMed:24838974};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=47.5 uM for tetradecanoic acid {ECO:0000269|PubMed:18267944};
CC KM=112 uM for trans-cinnamate {ECO:0000269|PubMed:24838974};
CC KM=125 uM for p-coumarate {ECO:0000269|PubMed:24838974};
CC KM=113 uM for ferulate {ECO:0000269|PubMed:24838974};
CC KM=85 uM for caffeate {ECO:0000269|PubMed:24838974};
CC KM=67 uM for 4-hydroxybenzoate {ECO:0000269|PubMed:24838974};
CC Note=kcat is 0.43 sec(-1) with tetradecanoic acid as substrate
CC (PubMed:18267944). kcat is 0.7 sec(-1) with trans-cinnamate as
CC substrate (PubMed:24838974). kcat is 2.1 sec(-1) with p-coumarate as
CC substrate (PubMed:24838974). kcat is 3.6 sec(-1) with ferulate as
CC substrate (PubMed:24838974). kcat is 2.4 sec(-1) with caffeate as
CC substrate (PubMed:24838974). kcat is 0.01 sec(-1) with 4-
CC hydroxybenzoate as substrate (PubMed:24838974).
CC {ECO:0000269|PubMed:18267944, ECO:0000269|PubMed:24838974};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:24838974}.
CC -!- TISSUE SPECIFICITY: Expressed at very low level in leaves.
CC {ECO:0000269|PubMed:18267944}.
CC -!- DOMAIN: Both substrate-binding domains (SBD1 and SBD2) are involved in
CC the substrate recognition, and are sufficient to confer the substrate
CC specificity. {ECO:0000250|UniProtKB:Q42524}.
CC -!- DISRUPTION PHENOTYPE: Cannot use 4-coumarate for ubiquinone
CC biosynthesis. {ECO:0000269|PubMed:24838974}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AY250834; AAP03017.1; -; mRNA.
DR EMBL; AY376733; AAQ86592.1; -; mRNA.
DR EMBL; AL021711; CAA16758.1; -; Genomic_DNA.
DR EMBL; AL161549; CAB78903.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84125.1; -; Genomic_DNA.
DR EMBL; AK117362; BAC42032.1; -; mRNA.
DR EMBL; BT005912; AAO64847.1; -; mRNA.
DR PIR; F85214; F85214.
DR PIR; T05038; T05038.
DR RefSeq; NP_193636.1; NM_118019.3.
DR AlphaFoldDB; Q84P24; -.
DR SMR; Q84P24; -.
DR STRING; 3702.AT4G19010.1; -.
DR SwissLipids; SLP:000001790; -.
DR iPTMnet; Q84P24; -.
DR PaxDb; Q84P24; -.
DR PRIDE; Q84P24; -.
DR ProteomicsDB; 245165; -.
DR EnsemblPlants; AT4G19010.1; AT4G19010.1; AT4G19010.
DR GeneID; 827639; -.
DR Gramene; AT4G19010.1; AT4G19010.1; AT4G19010.
DR KEGG; ath:AT4G19010; -.
DR Araport; AT4G19010; -.
DR TAIR; locus:2117209; AT4G19010.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_2_1; -.
DR InParanoid; Q84P24; -.
DR OMA; RVAAYKY; -.
DR OrthoDB; 683933at2759; -.
DR PhylomeDB; Q84P24; -.
DR BioCyc; ARA:AT4G19010-MON; -.
DR SABIO-RK; Q84P24; -.
DR PRO; PR:Q84P24; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q84P24; baseline and differential.
DR Genevisible; Q84P24; AT.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0106286; F:(E)-caffeate-CoA ligase activity; IEA:RHEA.
DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0018859; F:4-hydroxybenzoate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016405; F:CoA-ligase activity; IDA:TAIR.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IMP:TAIR.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Nucleotide-binding; Peroxisome; Reference proteome;
KW Ubiquinone biosynthesis.
FT CHAIN 1..566
FT /note="4-coumarate--CoA ligase-like 6"
FT /id="PRO_0000299179"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..356
FT /note="SBD1"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT REGION 357..421
FT /note="SBD2"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT MOTIF 564..566
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 212..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 334..336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 356..357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 442
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 457
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 548
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT CONFLICT 89
FT /note="I -> T (in Ref. 5; BAC42032 and 6; AAO64847)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="S -> P (in Ref. 1; AAP03017)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 566 AA; 61957 MW; A4EE22717B17E349 CRC64;
MAATHLHIPP NPKTQTSHQN PPFWFSSKTG IYTSKFPSLH LPVDPNLDAV SALFSHKHHG
DTALIDSLTG FSISHTELQI MVQSMAAGIY HVLGVRQGDV VSLVLPNSVY FPMIFLSLIS
LGAIVTTMNP SSSLGEIKKQ VSECSVGLAF TSTENVEKLS SLGVSVISVS ESYDFDSIRI
ENPKFYSIMK ESFGFVPKPL IKQDDVAAIM YSSGTTGASK GVLLTHRNLI ASMELFVRFE
ASQYEYPGSS NVYLAALPLC HIYGLSLFVM GLLSLGSTIV VMKRFDASDV VNVIERFKIT
HFPVVPPMLM ALTKKAKGVC GEVFKSLKQV SSGAAPLSRK FIEDFLQTLP HVDLIQGYGM
TESTAVGTRG FNSEKLSRYS SVGLLAPNMQ AKVVDWSSGS FLPPGNRGEL WIQGPGVMKG
YLNNPKATQM SIVEDSWLRT GDIAYFDEDG YLFIVDRIKE IIKYKGFQIA PADLEAVLVS
HPLIIDAAVT AAPNEECGEI PVAFVVRRQE TTLSEEDVIS YVASQVAPYR KVRKVVMVNS
IPKSPTGKIL RKELKRILTN SVSSRL
