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MLFA_ASPKW
ID   MLFA_ASPKW              Reviewed;        5101 AA.
AC   G7XQ31;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Malformin synthetase mlfA {ECO:0000303|PubMed:30560908};
DE            EC=6.3.2.- {ECO:0000269|PubMed:30560908};
DE   AltName: Full=Malformin biosynthesis cluster protein A {ECO:0000303|PubMed:30560908};
DE   AltName: Full=Nonribosomal peptide synthetase mlfA {ECO:0000303|PubMed:30560908};
GN   Name=mlfA {ECO:0000303|PubMed:30560908}; ORFNames=AKAW_07282;
OS   Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS   awamori var. kawachi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1033177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 4308;
RX   PubMed=22045919; DOI=10.1128/ec.05224-11;
RA   Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA   Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT   "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT   for brewing the Japanese distilled spirit shochu.";
RL   Eukaryot. Cell 10:1586-1587(2011).
RN   [2]
RP   BIOTECHNOLOGY.
RX   PubMed=19876076; DOI=10.1038/ja.2009.100;
RA   Kojima Y., Sunazuka T., Nagai K., Hirose T., Namatame M., Ishiyama A.,
RA   Otoguro K., Omura S.;
RT   "Solid-phase synthesis and biological activity of malformin C and its
RT   derivatives.";
RL   J. Antibiot. 62:681-686(2009).
RN   [3]
RP   BIOTECHNOLOGY.
RX   PubMed=26540166; DOI=10.1371/journal.pone.0140069;
RA   Wang J., Jiang Z., Lam W., Gullen E.A., Yu Z., Wei Y., Wang L., Zeiss C.,
RA   Beck A., Cheng E.C., Wu C., Cheng Y.C., Zhang Y.;
RT   "Study of malformin C, a fungal source cyclic pentapeptide, as an anti-
RT   cancer drug.";
RL   PLoS ONE 10:E0140069-E0140069(2015).
RN   [4]
RP   BIOTECHNOLOGY.
RX   PubMed=26645406; DOI=10.1007/s00280-015-2915-4;
RA   Liu Y., Wang M., Wang D., Li X., Wang W., Lou H., Yuan H.;
RT   "Malformin A1 promotes cell death through induction of apoptosis, necrosis
RT   and autophagy in prostate cancer cells.";
RL   Cancer Chemother. Pharmacol. 77:63-75(2016).
RN   [5]
RP   BIOTECHNOLOGY.
RX   PubMed=28713983; DOI=10.3892/ijo.2017.4070;
RA   Park S.Y., Oh H.H., Park Y.L., Yu H.M., Myung D.S., Cho S.B., Lee W.S.,
RA   Park D., Joo Y.E.;
RT   "Malformin A1 treatment alters invasive and oncogenic phenotypes of human
RT   colorectal cancer cells through stimulation of the p38 signaling pathway.";
RL   Int. J. Oncol. 51:959-966(2017).
RN   [6]
RP   IDENTIFICATION, FUNCTION, AND PATHWAY.
RX   PubMed=30560908; DOI=10.1038/s41598-018-36561-3;
RA   Theobald S., Vesth T.C., Rendsvig J.K., Nielsen K.F., Riley R.,
RA   de Abreu L.M., Salamov A., Frisvad J.C., Larsen T.O., Andersen M.R.,
RA   Hoof J.B.;
RT   "Uncovering secondary metabolite evolution and biosynthesis using gene
RT   cluster networks and genetic dereplication.";
RL   Sci. Rep. 8:17957-17957(2018).
CC   -!- FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster
CC       that mediates the biosynthesis of malformins, cyclic pentapeptides with
CC       a disulfide bond between 2 consecutive cysteins, that show potential
CC       anti-tumor as well as antimalarial and antitrypanosomal properties
CC       (PubMed:30560908). The nonribosomal peptide synthetase mlfA is
CC       responsible of the formation of the cyclic pentapeptide (Probable). The
CC       malformin biosynthesis clusters in malformin-producing fungi also
CC       contain enzymes involved in the formation of the disulfide bond between
CC       the two consecutive cysteins within malformins, in addition to
CC       additionnal tailoring enzymes such as methyltransferases or
CC       oxidoreductases. They are also composed of up to 4 major facilitator
CC       superfamily transporters, and transcription factors probably involved
CC       in the regulation of the expression of those clusters (Probable).
CC       {ECO:0000269|PubMed:30560908, ECO:0000305|PubMed:30560908}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:30560908}.
CC   -!- DOMAIN: NRP synthetases are composed of discrete domains (adenylation
CC       (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation
CC       (C) domains) which when grouped together are referred to as a single
CC       module. Each module is responsible for the recognition (via the A
CC       domain) and incorporation of a single amino acid into the growing
CC       peptide product. Thus, an NRP synthetase is generally composed of one
CC       or more modules and can terminate in a thioesterase domain (TE) that
CC       releases the newly synthesized peptide from the enzyme. Occasionally,
CC       epimerase (E) domains (responsible for L- to D- amino acid conversion)
CC       are present within the NRP synthetase. MlfA has the following
CC       architecture: A-T-C-A-T-C-A-T-C-C-A-T-C, with the functions of the five
CC       condensation domains during malformin biosynthesis being DL-joining
CC       (epimerizing subtype), LL-joining, epimerization, DL-joining and
CC       cyclizing domain, respectively. {ECO:0000305|PubMed:30560908}.
CC   -!- BIOTECHNOLOGY: Malformins show anti-tumor properties against human
CC       colorectal and prostate cancer cells by the inhibition of proliferation
CC       and induction of apoptosis through the activation of the p38 signaling
CC       pathway (PubMed:26540166, PubMed:26645406, PubMed:28713983). Malformin
CC       C has also been shown to exhibit potent antimalarial and
CC       antitrypanosomal properties (PubMed:19876076).
CC       {ECO:0000269|PubMed:19876076, ECO:0000269|PubMed:26540166,
CC       ECO:0000269|PubMed:26645406, ECO:0000269|PubMed:28713983}.
CC   -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR   EMBL; DF126466; GAA89168.1; -; Genomic_DNA.
DR   SMR; G7XQ31; -.
DR   STRING; 40384.G7XQ31; -.
DR   VEuPathDB; FungiDB:AKAW_07282; -.
DR   eggNOG; KOG1178; Eukaryota.
DR   InParanoid; G7XQ31; -.
DR   Proteomes; UP000006812; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   Gene3D; 1.10.1200.10; -; 4.
DR   Gene3D; 3.30.300.30; -; 4.
DR   Gene3D; 3.30.559.10; -; 5.
DR   Gene3D; 3.40.50.12780; -; 4.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR036736; ACP-like_sf.
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   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   Pfam; PF00501; AMP-binding; 4.
DR   Pfam; PF00668; Condensation; 5.
DR   Pfam; PF00550; PP-binding; 4.
DR   SMART; SM00823; PKS_PP; 3.
DR   SUPFAM; SSF47336; SSF47336; 4.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 4.
DR   PROSITE; PS00455; AMP_BINDING; 2.
DR   PROSITE; PS50075; CARRIER; 4.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   1: Evidence at protein level;
KW   Ligase; Phosphopantetheine; Phosphoprotein.
FT   CHAIN           1..5101
FT                   /note="Malformin synthetase mlfA"
FT                   /id="PRO_0000446432"
FT   DOMAIN          757..830
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          1854..1931
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          3032..3108
FT                   /note="Carrier 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          4579..4655
FT                   /note="Carrier 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          225..616
FT                   /note="Adenylation 1"
FT                   /evidence="ECO:0000255"
FT   REGION          868..1299
FT                   /note="Condensation 1"
FT                   /evidence="ECO:0000255"
FT   REGION          1327..1716
FT                   /note="Adenylation 2"
FT                   /evidence="ECO:0000255"
FT   REGION          1932..1961
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1994..2020
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2066..2481
FT                   /note="Condensation 2"
FT                   /evidence="ECO:0000255"
FT   REGION          2504..2896
FT                   /note="Adenylation 3"
FT                   /evidence="ECO:0000255"
FT   REGION          3125..3590
FT                   /note="Condensation 3"
FT                   /evidence="ECO:0000255"
FT   REGION          3611..4030
FT                   /note="Condensation 4"
FT                   /evidence="ECO:0000255"
FT   REGION          4055..4445
FT                   /note="Adenylation 4"
FT                   /evidence="ECO:0000255"
FT   REGION          4712..5097
FT                   /note="Condensation 5"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1932..1955
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1994..2016
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         791
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1891
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         3069
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         4616
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   5101 AA;  561810 MW;  976EEA82BA3D97F1 CRC64;
     MSRFSCIFPT LTDGYVPNPD HTRAAGRRTY RIDLSGWKAP GSETESLILA AWGLVLSSYV
     GTDEVAFYVV PTTGPDTTAL AELKVEGDMP RQSLTYAAHQ LLHPGLVGAG QVSGETANTI
     ITFANDIESL FVTQTEESFL SLHVYRDEQG HISLSLTYYL SLLTDAQAAN VGTAMAQALA
     EVGTCDNDKL VKDLSLMSPA HLEHIWRFNA DVPGIWEECF HDVIERHAAN RPHSLAVDAW
     DTELTYTDLV REARLLAAYL QRRGVGPGSV VPISFERSGA ALVAMLAVSK AGGAFVSVPP
     NLPAGRVDAI LEVIEAPFVV TWTKYESFWA ERLPTLPIDN YPKPAADATV EALGKPEDLF
     YVIFTSGSTG RPKGCMLSHT NWLNGALRNA PSWKYGPESR VLQMLSHTFD MSLLEICTSL
     GSGSCVCVPR PEEIETSISD AINRWQVNHV IMTPSLARAL RPDDVPGLKT MCLGGEAFPK
     EIVTMWSERI NLWQFYGPSE CSINSSSWPI TRPDADPLNI GPPNSAACWV VDVHDYNKLV
     PVGAIGELLV SGPIVGMGYL KNPVKTAEAF LEEVGFVAKD DPQFGGFRFY RTGDLVRWNS
     DGTITFCGRA DTQVKLNGQR LELAEVEYQL GLEAGVQYAI AMAPQAGLCK NNLIAILTVK
     GTSTGTQDTA ADEIPLLDRR DPIVQETVKK LRSQLQHALP RYMVPTIWAF VGRMPMSASG
     KIDRVKLRDW VQRMSQETFD AITGRSLEAE EHAFGLSRLE QKIQLAWAEA LGLSAAEVGL
     QQPFVALGGD SIKALDAVAR CRARQIKISM VHILSCEGVR EAASLAEVQE TPAQQVAEMA
     VDYSNLWTRL SNDYDLDKLG VTQVEEVEDV FPCTTMQEGM FLGQIRRPGA YHMRFFHRVQ
     LKGGCLPTVE RIQQAWASLV ERHPSLRTVF VDDLSPEAIY HSIVLRSVPM EVRMREVPRD
     LSAEAALAIF TEELVPFRAN APLHRMLLLT CRGRVPYLML EISHVIMDGY ALSVFRREFI
     RACSSSAPLP RGPDYRMFAN YHRTRQTDDS ARYWTDYLAD CVPCHIPTHA VSAPSDGPPE
     WPRTLQRRDF GFENSAAFLQ RCKERQVTLA CAIRAAWALV LRAYTQSEDV CFGYVSSGRN
     VPVPEVETIF GLCLSMQVCR ARLSEASTIA SLARKIQEDY VASLPFQHYP LAEAQRGLKQ
     THGQGLFNTA ISMEWVPPSA EDEDALLDLE EIREQDDPTE YDIAISVDVH EGHIKLGFLY
     WPDLTDFEIN HLAEALHGAM NCFASHPDEA LNTLSLLQAS DVCSALSDGP TLLPLEAVRG
     NVVSMIDRWV TRQPEGAAID GWDGSMSYKE LHEQSSWVAR NLLHQGVRLG DRVLVCADRS
     SRTVATILGI VRAGCVLVLS NPTDPEKRLQ WLAKKCNASL VVADPTYEER LATADAHVLS
     TTSVCAPAAW DYEFPALDEH DLISILFKSG STGTPKGILM EHGALATSVF LGHGRTLRFS
     RHTRMLHFAS LTFDAALAEI FTTLAHGGCI CVPCEEDRLS DVPGCISRFA VNTAMLTPSV
     GRLLDPGALP TLQTLIMVGE PMSRLDVERF APVLDLYNGA GPTETSIMVT IAGPMKPTDE
     PVNLGYAVAG VRLWVTEAEN PNRLAPLGAV GELIVEGRLV TSGYLDDQAR TQEAFLPTLP
     WLPSQHALYR TGDLVRYVDD GSLRYMGRKD TQVKLRGQRI ELQEVEYHLR KSLQQAQIVV
     EMVVPAGKMR AQASLVAFVS GLTAADVESS SACNLEGTIP ISQIVLPKSA FQALEEVLPR
     HMIPSVYYAL DTIPLSVNGK ADRRRLREMG SLLLASSAAH KNNIEGMSKS VKWTPTLELE
     RTLLGLWAAT LGLEAETIHG DDSFFELGGD SVSAMKLVAT ARDKYKLSLS VPQMFRYPTV
     CQLAAEVGEP AGQSASSASS TTEEGFTFST PDDSSTNDGV DDDFLQLATA QLAQLAQEKG
     KKVDIAALLK QLQGGSSSNK TPSVSSSSSS SSSSKRKKNA AKAESLAEAA APIPVQFSLL
     DGGADALDKV RAQAVEHCKI THDDIEDIYP ATALQEGMMA LTARTPGVYT TTLTGDLSEQ
     VDIARLQYAW GKAAEAHPIL RTRIILTDNN TAVQVVQRAK GLPWDTYSLR EDNVLPDLTS
     NMTSGSPLLR LAVVHRQSQP RMLLVAIHHA LYDGWSMPLL KQAVEDAYHG RDLRPQPFTP
     FIKHLIAGKP AAQDFWTTHL DNFVGGVFPK LPSIYHQIQP TERRTRSMTL PTAAPKAQYT
     MATKIQAAWA VTVSRYVEAN DIVFGTVSTG RSAPVPAIDR MVGPTVTTVP VRISLGGQAD
     RVLSLLQRVQ EDSWNKLDHE HLGLQHIRRL GESAAAACNF QTLLVIQPRE QPDTKYRSTL
     LSGLQDVAEL EGVDTYPLML VCEPDGASLN LTAVFDRAVL DGATLDRMLA HWELVLTQMW
     NEPNMAVIDI DAVSCSDKET LMRWNTGETI TEGCAHNAVC EWSRRTPHAP AVCAWDGEWT
     YKELERYSSL IASQISAHGL SSGDFVALYH EKSRWTAAGI LAVFKAGAIL ITLDPAHPTD
     RIKDILDQAR PRLILTSQSL LDVARNLDTP VLSVQFAASQ PLPEEWSSLP TICPTLAAYA
     PFTSGSTGRP KGIPLDHRGL AASTASIARS CLLRPASRVL HFASFAFDAS MMEHLIAWHA
     GGCLCIPDET ARQTDLAKCI RDFNVTWAFL TPSCLRLITP DDVPSLQALG LGGESMTSED
     ITIWSPRLRQ IVQLYGPAEC CIVAALTEVT KPSENRLIGR PNACRCWVVD PQNPDRLAPI
     GAVGELLIEG ITVGRGYIND PDRTTPAFIR PPKWLQTLYP DDQEPKRLYR TGDLVRYAGV
     DGKLAFIGRR DGQLKLHGQR IELADVEAHL RSLIPGMQKM VVEMVHSADN QNPFLAAFLE
     EISTSQKPKE REIGLLHPSQ SQCALDVKAI DSALSRTVPQ YMIPSMYLHI SRLPLSASGK
     LDRRHLREMV AELPRQSLNE YAAGSGLGVP DRPVTSQEHE MQAIWARVLS LDPNTFGVND
     DFFRIGGDSI SGMQVSTKCN AAGIHITSAD LFRHRTIEQL ICHLNTIRTT DSASVLLPTE
     PVNEWVALAP IQHLFFEVAP EGPNHFNQSL LLRTSRRVSV EELAGGLDVL IGRHSMLRAR
     FCRKDSGQWF QQVKSLDSEP ASAFYRLAAH NHITRESLPT LFTAAQMALS IEDGPLLTVD
     LVELEDGSQL VYLAAHHLII DLVSWRILHG DLEEYLQTGS LSSATGSVPF LTWTQLQAEY
     SAEHLTPARA LPGFQEANDD FDFMRYWGIS SESNTFGQTS TSRFALDRTV TDILFGSANK
     VMDTRPVEIL EAALWYSCNQ ALPDHPGPSI YVEGHGREPW TDSIDVSGTV GWFTIMSPLV
     STPWHHLSRK SMRDFVDVLS YIKDQRRRIP ANGWAYFTSR YLNDEGRVAY GRTKPVMEVL
     FNYMGQYQEM KREDAILQLA GDDIQSGTGA SDIAGNVPRF SLIDVTAFTA NGCLTFEFTF
     PQLIQQDARL EQCIKECEHT LVAAASSLSA EGPRKTLTDF PLMSALTYDQ LSQCLNHTLP
     SMGLRAQDVW NIYPCSPVQR GMLLAQLRDR QAYQQRFKFQ VMSRGPTEQL SLEKVKDAWT
     EVINRHDILR TLLLPVSDHS HFDQVVMVPG SLQHLVRGDA MDANPTEGLP HTINITSDST
     GAIICEWNVS HALVDAMSIA FIQREVNQAL EGSLGQHQNL PQYVEYIKWL TLQDNTEAQA
     YWQNHLNGVE PCLFPKLTSS PDKVNPEATI SAIRATWSRD VRMDELCHKH AITLTNLFHI
     VWAIVLGAYV GTDEVCFGYT ALGRDVPVHR VETLVGPLVN VLATTVRHQE DETILNALLT
     HQAHLTNSLQ HQHYALADVY ASLGLVGSQL FNTIVSLQDT SHFDAPDEQR TRLEMLPAND
     VSEYDVALNI GVDKSTIQLV CSYQTVSLSA EQADALLRTA FHVLDEILRD PTQRFCELEV
     ISPKCKEHLV KWNAGMLAPT HEYIHEKIQG QCRIHNSRQA VCAWDGMFTY AEVDDLSSRL
     AARLIRMGVT SEDIIPIYSP KSRWMVIAIL GVLKAGAAFT LLEISHPMAR LRVICNQIKA
     PMLIAPASHA VPAANLAPIL VVLDNITSLA EERPVSLPAV DIPPAREALA YLIFTSGSTG
     NPKGVMVTHQ NLCSNASIIT TSVNMTSDSR VLQFASHAFD GCLWEILGAL LAGACLIIPS
     ESENKEDLTG CIERMGVTWA FLTPSVARIL KPETLPSLCN LVLGGEPIAA SDLEMWRGHV
     QVVCAYGPTE TTILASTTSP STFPRDGKDI GTPTSSSLWI VDTRNYQTLV PLGATGELLI
     EGPNVSQGYL GDPEKTNNAF PDAPRWLSQL RKSPTRLYRT GDLVRFDTST GTIRFVGRKD
     NQIKFHGQRI ELGEIEYHAQ FAFSSASTVI VDLITPEQPR QPYIVAFVHQ LDAANETTDT
     NDTLLLPSSE VFRADALAAQ NKMHKRLPHY MVPAVFLPLH RLPLSVTGKA DRKRLRQCAL
     ALSSPELSAY RATASTKRMP STAAERKMQE LVATVLGRDP TEIGMDDSFF YLGGDSVQAM
     RLVAEGRQQG LTLSLRAIFD SPCLGDLSDQ AKSLIEDNQR ASTASRGNLR YDCDRIDKIV
     VTNSLNKADV VDVLPTTSFQ RHWLDAQLKS YIVVDIPGPI DPARLLRAMH RVVEAHPILR
     VSFVPYETTT VQVILRTAVA ITNVDLSTAT VEELCRRDVD AQMAPGVPYL RVIIATQDKA
     GHKLIMRLSH AQYDAVSLSL LMNDLSHAYA NDTHPLPSSH FPRFNDYITY QQAQRADPTA
     TTFWRHLLQD VPLTHLNLQP AESSASNGTP ITLSRDIDIA VFPSLPSDIT IATMVKAAWS
     LALAQKTNSL AVIFGQVVHG RAIALPGVEG IVGPCANITP VVARLGLETT GLELMQALQD
     QHHSAMSYES VDLDDALAYA NDSQAGRKGL QTIVQHQNNV MVDDMELSLG EVKCGVDFRA
     VDHLPKEVWV YSSVDEKRPG MLEVKIMSST LVLGEEFAEE LMGLLVEKIV GLLRHPESVC
     V
 
 
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