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DMAW_ASPFU
ID   DMAW_ASPFU              Reviewed;         459 AA.
AC   Q50EL0; Q4WZ62;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Tryptophan dimethylallyltransferase {ECO:0000305};
DE            EC=2.5.1.34 {ECO:0000269|PubMed:15870460};
DE   AltName: Full=4-dimethylallyltryptophan synthase {ECO:0000303|PubMed:15870460};
DE   AltName: Full=All-trans-hexaprenyl-diphosphate synthase {ECO:0000305};
DE   AltName: Full=L-tryptophan dimethylallyl transferase {ECO:0000305};
DE            Short=DMATS {ECO:0000305};
GN   Name=dmaW {ECO:0000303|PubMed:22453123};
GN   Synonyms=fgaPT2 {ECO:0000303|PubMed:20526482}; ORFNames=AFUA_2G18040;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PATHWAY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, AND CATALYTIC ACTIVITY.
RC   STRAIN=B5233 / ATCC 13073;
RX   PubMed=15870460; DOI=10.1099/mic.0.27759-0;
RA   Unsoeld I.A., Li S.-M.;
RT   "Overproduction, purification and characterization of FgaPT2, a
RT   dimethylallyltryptophan synthase from Aspergillus fumigatus.";
RL   Microbiology 151:1499-1505(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
RN   [3]
RP   IDENTIFICATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15933009; DOI=10.1128/aem.71.6.3112-3118.2005;
RA   Coyle C.M., Panaccione D.G.;
RT   "An ergot alkaloid biosynthesis gene and clustered hypothetical genes from
RT   Aspergillus fumigatus.";
RL   Appl. Environ. Microbiol. 71:3112-3118(2005).
RN   [4]
RP   MUTAGENESIS OF LYS-187 AND LYS-259.
RX   PubMed=18677738; DOI=10.1002/cbic.200800237;
RA   Stec E., Steffan N., Kremer A., Zou H., Zheng X., Li S.M.;
RT   "Two lysine residues are responsible for the enzymatic activities of indole
RT   prenyltransferases from fungi.";
RL   ChemBioChem 9:2055-2058(2008).
RN   [5]
RP   FUNCTION.
RX   PubMed=19672909; DOI=10.1002/cbic.200900395;
RA   Liu X., Wang L., Steffan N., Yin W.B., Li S.M.;
RT   "Ergot alkaloid biosynthesis in Aspergillus fumigatus: FgaAT catalyses the
RT   acetylation of fumigaclavine B.";
RL   ChemBioChem 10:2325-2328(2009).
RN   [6]
RP   INDUCTION.
RX   PubMed=19028996; DOI=10.1128/ec.00265-08;
RA   Twumasi-Boateng K., Yu Y., Chen D., Gravelat F.N., Nierman W.C.,
RA   Sheppard D.C.;
RT   "Transcriptional profiling identifies a role for BrlA in the response to
RT   nitrogen depletion and for StuA in the regulation of secondary metabolite
RT   clusters in Aspergillus fumigatus.";
RL   Eukaryot. Cell 8:104-115(2009).
RN   [7]
RP   BIOTECHNOLOGY.
RX   PubMed=19523108; DOI=10.1111/j.1364-3703.2009.00548.x;
RA   Haarmann T., Rolke Y., Giesbert S., Tudzynski P.;
RT   "Ergot: from witchcraft to biotechnology.";
RL   Mol. Plant Pathol. 10:563-577(2009).
RN   [8]
RP   FUNCTION.
RX   PubMed=20039019; DOI=10.1007/s00203-009-0536-1;
RA   Wallwey C., Matuschek M., Li S.M.;
RT   "Ergot alkaloid biosynthesis in Aspergillus fumigatus: conversion of
RT   chanoclavine-I to chanoclavine-I aldehyde catalyzed by a short-chain
RT   alcohol dehydrogenase FgaDH.";
RL   Arch. Microbiol. 192:127-134(2010).
RN   [9]
RP   FUNCTION, AND NOMENCLATURE.
RX   PubMed=20526482; DOI=10.1039/c003823g;
RA   Wallwey C., Matuschek M., Xie X.L., Li S.M.;
RT   "Ergot alkaloid biosynthesis in Aspergillus fumigatus: Conversion of
RT   chanoclavine-I aldehyde to festuclavine by the festuclavine synthase FgaFS
RT   in the presence of the old yellow enzyme FgaOx3.";
RL   Org. Biomol. Chem. 8:3500-3508(2010).
RN   [10]
RP   FUNCTION.
RX   PubMed=21409592; DOI=10.1007/s00294-011-0336-4;
RA   Goetz K.E., Coyle C.M., Cheng J.Z., O'Connor S.E., Panaccione D.G.;
RT   "Ergot cluster-encoded catalase is required for synthesis of chanoclavine-I
RT   in Aspergillus fumigatus.";
RL   Curr. Genet. 57:201-211(2011).
RN   [11]
RP   IDENTIFICATION, AND NOMENCLATURE.
RX   PubMed=22453123; DOI=10.3852/11-310;
RA   Robinson S.L., Panaccione D.G.;
RT   "Chemotypic and genotypic diversity in the ergot alkaloid pathway of
RT   Aspergillus fumigatus.";
RL   Mycologia 104:804-812(2012).
RN   [12]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=23435153; DOI=10.3390/toxins5020445;
RA   Ryan K.L., Moore C.T., Panaccione D.G.;
RT   "Partial reconstruction of the ergot alkaloid pathway by heterologous gene
RT   expression in Aspergillus nidulans.";
RL   Toxins 5:445-455(2013).
RN   [13]
RP   FUNCTION.
RX   PubMed=26972831; DOI=10.1007/s00294-016-0591-5;
RA   Bilovol Y., Panaccione D.G.;
RT   "Functional analysis of the gene controlling hydroxylation of festuclavine
RT   in the ergot alkaloid pathway of Neosartorya fumigata.";
RL   Curr. Genet. 62:853-860(2016).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH TRYPTOPHAN AND
RP   DIMETHYLALLYL S-THIOLODIPHOSPHATE, SUBUNIT, AND MUTAGENESIS OF GLU-89;
RP   ARG-100 AND LYS-174.
RX   PubMed=19706516; DOI=10.1073/pnas.0904897106;
RA   Metzger U., Schall C., Zocher G., Unsold I., Stec E., Li S.M., Heide L.,
RA   Stehle T.;
RT   "The structure of dimethylallyl tryptophan synthase reveals a common
RT   architecture of aromatic prenyltransferases in fungi and bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:14309-14314(2009).
CC   -!- FUNCTION: Tryptophan dimethylallyltransferase; part of the gene cluster
CC       that mediates the biosynthesis of fumiclavanine C, a fungal ergot
CC       alkaloid (PubMed:15933009, PubMed:23435153, PubMed:26972831). DmaW
CC       catalyzes the first step of ergot alkaloid biosynthesis by condensing
CC       dimethylallyl diphosphate (DMAP) and tryptophan to form 4-
CC       dimethylallyl-L-tryptophan (PubMed:15870460, PubMed:23435153). The
CC       second step is catalyzed by the methyltransferase easF that methylates
CC       4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-
CC       methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By
CC       similarity). The catalase easC and the FAD-dependent oxidoreductase
CC       easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is
CC       further oxidized by EasD in the presence of NAD(+), resulting in the
CC       formation of chanoclavine-I aldehyde (PubMed:20039019, PubMed:20526482,
CC       PubMed:21409592). EasA reduces chanoclavine-I aldehyde to
CC       dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form
CC       6,8-dimethyl-6,7-didehydroergoline (PubMed:20526482). EasG then
CC       catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form
CC       festuclavine (PubMed:20526482). Hydrolysis of festuclavine by easM then
CC       leads to the formation of fumigaclavine B which is in turn acetylated
CC       by easN to fumigaclavine A (PubMed:26972831). Finally, easL catalyzes
CC       the conversion of fumigaclavine A into fumigaclavine C by attaching a
CC       dimethylallyl moiety to C-2 of the indole nucleus (PubMed:19672909).
CC       {ECO:0000250|UniProtKB:B6D5I7, ECO:0000269|PubMed:15870460,
CC       ECO:0000269|PubMed:15933009, ECO:0000269|PubMed:19672909,
CC       ECO:0000269|PubMed:20039019, ECO:0000269|PubMed:20526482,
CC       ECO:0000269|PubMed:21409592, ECO:0000269|PubMed:23435153,
CC       ECO:0000269|PubMed:26972831}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dimethylallyl diphosphate + L-tryptophan = 4-(3-methylbut-2-
CC         enyl)-L-tryptophan + diphosphate; Xref=Rhea:RHEA:14173,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:57912,
CC         ChEBI:CHEBI:58209; EC=2.5.1.34;
CC         Evidence={ECO:0000269|PubMed:15870460};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4 uM for dimethylallyl diphosphate {ECO:0000269|PubMed:15870460};
CC         KM=8 uM for L-tryptophan {ECO:0000269|PubMed:15870460};
CC         Vmax=0.198 umol/min/mg enzyme {ECO:0000269|PubMed:15870460};
CC   -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC       {ECO:0000269|PubMed:15870460, ECO:0000269|PubMed:23435153}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15870460,
CC       ECO:0000269|PubMed:19706516}.
CC   -!- INDUCTION: The expression of the ergot alkaloid synthesis cluster which
CC       leads to the synthesis of fumigaclavines is positively regulated by the
CC       brlA and stuA transcription factors (PubMed:19028996).
CC       {ECO:0000269|PubMed:19028996}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the production of ergot alkaloids
CC       including festuclavine, fumigaclavine A, fumigaclavine B and
CC       fumigaclavine C (PubMed:15933009). {ECO:0000269|PubMed:15933009}.
CC   -!- BIOTECHNOLOGY: Ergot alkaloids are known for their toxic effects on
CC       humans who consume contaminated grains or livestock that graze on
CC       grasses harboring ergot alkaloid-producing fungi (PubMed:19523108). Due
CC       to their strong affinity for monoamine neurotransmitter receptors they
CC       may also have clinical uses such as treatment of migraines, Parkinson's
CC       disease and cerebrovascular insufficiency (PubMed:19523108).
CC       {ECO:0000305|PubMed:19523108}.
CC   -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL94103.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY775787; AAX08549.1; -; mRNA.
DR   EMBL; AAHF01000001; EAL94103.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_756141.2; XM_751048.2.
DR   PDB; 3I4X; X-ray; 2.10 A; A/B=1-459.
DR   PDB; 3I4Z; X-ray; 1.76 A; A/B=1-459.
DR   PDBsum; 3I4X; -.
DR   PDBsum; 3I4Z; -.
DR   AlphaFoldDB; Q50EL0; -.
DR   SMR; Q50EL0; -.
DR   STRING; 746128.CADAFUBP00003306; -.
DR   ChEMBL; CHEMBL4523316; -.
DR   PRIDE; Q50EL0; -.
DR   GeneID; 3512716; -.
DR   KEGG; afm:AFUA_2G18040; -.
DR   eggNOG; ENOG502S2XP; Eukaryota.
DR   HOGENOM; CLU_037431_0_0_1; -.
DR   InParanoid; Q50EL0; -.
DR   OrthoDB; 1531660at2759; -.
DR   BioCyc; MetaCyc:MON-15369; -.
DR   BRENDA; 2.5.1.34; 508.
DR   SABIO-RK; Q50EL0; -.
DR   UniPathway; UPA00327; -.
DR   EvolutionaryTrace; Q50EL0; -.
DR   Proteomes; UP000002530; Chromosome 2.
DR   GO; GO:0004659; F:prenyltransferase activity; IEA:UniProt.
DR   GO; GO:0050364; F:tryptophan dimethylallyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:1900809; P:fumigaclavine C biosynthetic process; IDA:GO_Central.
DR   CDD; cd13929; PT-DMATS_CymD; 1.
DR   InterPro; IPR033964; Aro_prenylTrfase.
DR   InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR   InterPro; IPR012148; DMATS-type_fun.
DR   InterPro; IPR017796; Trp_dimethylallylTrfase.
DR   PANTHER; PTHR40627; PTHR40627; 1.
DR   Pfam; PF11991; Trp_DMAT; 1.
DR   PIRSF; PIRSF000509; Trp_DMAT; 1.
DR   SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR   TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
DR   TIGRFAMs; TIGR03430; trp_dimet_allyl; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alkaloid metabolism; Reference proteome; Transferase.
FT   CHAIN           1..459
FT                   /note="Tryptophan dimethylallyltransferase"
FT                   /id="PRO_0000228687"
FT   BINDING         80..81
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000269|PubMed:19706516"
FT   BINDING         89
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000269|PubMed:19706516"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:19706516"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:19706516"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:19706516"
FT   BINDING         191
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000269|PubMed:19706516"
FT   BINDING         244
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000269|PubMed:19706516"
FT   BINDING         257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:19706516"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:19706516"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:19706516"
FT   BINDING         343
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:19706516"
FT   BINDING         345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:19706516"
FT   BINDING         409
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:19706516"
FT   BINDING         413
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:19706516"
FT   VARIANT         443
FT                   /note="S -> A (in strain: B5233 / ATCC 13073)"
FT   MUTAGEN         89
FT                   /note="E->A: Abolishes tryptophan dimethylallyltransferase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:19706516"
FT   MUTAGEN         100
FT                   /note="R->D,Q: Nearly abolishes tryptophan
FT                   dimethylallyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:19706516"
FT   MUTAGEN         174
FT                   /note="K->E: Nearly abolishess tryptophan
FT                   dimethylallyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:19706516"
FT   MUTAGEN         174
FT                   /note="K->Q: Impairs tryptophan dimethylallyltransferase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:19706516"
FT   MUTAGEN         187
FT                   /note="K->E: Nearly abolishes tryptophan
FT                   dimethylallyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:18677738"
FT   MUTAGEN         259
FT                   /note="K->E: Nearly abolishes tryptophan
FT                   dimethylallyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:18677738"
FT   HELIX           6..8
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   HELIX           10..18
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   HELIX           24..43
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   HELIX           48..61
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   HELIX           63..65
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   STRAND          72..74
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   STRAND          87..93
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   TURN            94..97
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   STRAND          98..103
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   HELIX           122..129
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   HELIX           130..132
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   HELIX           139..148
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   HELIX           152..160
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   HELIX           162..164
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   TURN            165..167
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   STRAND          173..180
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   STRAND          183..190
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   HELIX           193..199
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   HELIX           203..217
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   HELIX           219..221
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   HELIX           222..234
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   STRAND          240..251
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   TURN            253..255
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   STRAND          258..264
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   STRAND          266..268
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   HELIX           269..276
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   TURN            277..281
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   HELIX           285..301
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   STRAND          327..333
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   STRAND          341..346
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   HELIX           353..366
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   HELIX           370..383
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   HELIX           389..391
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   STRAND          394..404
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   STRAND          407..414
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   HELIX           420..424
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   HELIX           448..450
FT                   /evidence="ECO:0007829|PDB:3I4Z"
FT   STRAND          451..454
FT                   /evidence="ECO:0007829|PDB:3I4Z"
SQ   SEQUENCE   459 AA;  52463 MW;  ED7AAB193E9A46C8 CRC64;
     MKAANASSAE AYRVLSRAFR FDNEDQKLWW HSTAPMFAKM LETANYTTPC QYQYLITYKE
     CVIPSLGCYP TNSAPRWLSI LTRYGTPFEL SLNCSNSIVR YTFEPINQHT GTDKDPFNTH
     AIWESLQHLL PLEKSIDLEW FRHFKHDLTL NSEESAFLAH NDRLVGGTIR TQNKLALDLK
     DGRFALKTYI YPALKAVVTG KTIHELVFGS VRRLAVREPR ILPPLNMLEE YIRSRGSKST
     ASPRLVSCDL TSPAKSRIKI YLLEQMVSLE AMEDLWTLGG RRRDASTLEG LSLVRELWDL
     IQLSPGLKSY PAPYLPLGVI PDERLPLMAN FTLHQNDPVP EPQVYFTTFG MNDMAVADAL
     TTFFERRGWS EMARTYETTL KSYYPHADHD KLNYLHAYIS FSYRDRTPYL SVYLQSFETG
     DWAVANLSES KVKCQDAACQ PTSLPPDLSK TGVYYSGLH
 
 
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