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VLMS_LECSP
ID   VLMS_LECSP              Reviewed;        8903 AA.
AC   A0A024F910;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 1.
DT   23-FEB-2022, entry version 24.
DE   RecName: Full=Nonribosomal peptide synthetase vlms {ECO:0000303|PubMed:24848421};
DE            Short=NRPS vlmS {ECO:0000303|PubMed:24848421};
DE            EC=6.3.2.- {ECO:0000305|PubMed:24848421};
DE   AltName: Full=Verlamelin biosynthesis protein S {ECO:0000303|PubMed:24848421};
GN   Name=vlmS {ECO:0000303|PubMed:24848421};
OS   Lecanicillium sp.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Lecanicillium;
OC   unclassified Lecanicillium.
OX   NCBI_TaxID=1756136;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, DOMAIN,
RP   AND PATHWAY.
RC   STRAIN=HF627;
RX   PubMed=24848421; DOI=10.1007/s00253-014-5803-7;
RA   Ishidoh K., Kinoshita H., Nihira T.;
RT   "Identification of a gene cluster responsible for the biosynthesis of
RT   cyclic lipopeptide verlamelin.";
RL   Appl. Microbiol. Biotechnol. 98:7501-7510(2014).
CC   -!- FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster
CC       that mediates the biosynthesis of verlamelin, a lipopeptide that
CC       exhibits antifungal activity against plant pathogenic fungi
CC       (PubMed:24848421). Verlamelin is a cyclic hexadepsipeptide and is
CC       bridged by ester bonding between a 5-hydroxytetradecanoic acid moiety
CC       and a carboxyl group on the terminal Val of amide-bonded tetradecanoyl-
CC       hexapeptide D-allo-Thr-D-Ala-L-Pro-L-Gln-D-Tyr-L-Val (PubMed:24848421).
CC       VlmA and vlmB are altogether regarded as essential components in the
CC       biosynthesis of 5-hydroxytetradecanoic acid (PubMed:24848421). VlmA
CC       catalyzes the hydroxylation at position C5 of tetradecanoic acid
CC       produced in primary metabolism, while the precise function of vlmB
CC       still remains to be solved (PubMed:24848421). To be loaded onto the
CC       waiting NRPS, 5-hydroxytetradecanoic acid is activated in the form of
CC       acyladenylate by the AMP-dependent ligase vlmC (PubMed:24848421). VlmS
CC       seems to accept the fatty-acyl intermediate onto the initial module to
CC       further elongate amino acid residues by the downstream modules
CC       (PubMed:24848421). In addition, in the last module at its C-terminus,
CC       vlmS contains a surplus condensation (C) domain that may be involved in
CC       cyclization, the last step to form verlamelin (PubMed:24848421).
CC       {ECO:0000269|PubMed:24848421}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:24848421}.
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 (PubMed:24848421). Each module is responsible for the
CC       recognition (via the A domain) and incorporation of a single amino acid
CC       into the growing peptide product. Thus, an NRP synthetase is generally
CC       composed of one or more modules and can terminate in a thioesterase
CC       domain (TE) that releases the newly synthesized peptide from the
CC       enzyme. Occasionally, epimerase (E) domains (responsible for l- to d-
CC       amino acid conversion) are present within the NRP synthetase. VlmS has
CC       the following 7 module architecture: T-E-C-A-T-E-C-A-T-E-C-A-T-C-A-T-C-
CC       A-T-E-C-A-T-C (PubMed:24848421). The epimerase domain in the first
CC       module is probably non-functional (PubMed:24848421).
CC       {ECO:0000269|PubMed:24848421}.
CC   -!- DISRUPTION PHENOTYPE: Leads to complete loss of verlamelin production
CC       (PubMed:24848421). {ECO:0000269|PubMed:24848421}.
CC   -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR   EMBL; AB862312; BAO73252.1; -; Genomic_DNA.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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; -; 7.
DR   Gene3D; 3.30.300.30; -; 6.
DR   Gene3D; 3.30.559.10; -; 11.
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; 6.
DR   Pfam; PF00668; Condensation; 10.
DR   Pfam; PF00550; PP-binding; 7.
DR   SMART; SM00823; PKS_PP; 6.
DR   SUPFAM; SSF47336; SSF47336; 7.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 6.
DR   PROSITE; PS00455; AMP_BINDING; 6.
DR   PROSITE; PS50075; CARRIER; 7.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE   3: Inferred from homology;
KW   Isomerase; Ligase; Phosphopantetheine; Phosphoprotein; Repeat; Virulence.
FT   CHAIN           1..8903
FT                   /note="Nonribosomal peptide synthetase vlms"
FT                   /id="PRO_0000438579"
FT   DOMAIN          11..84
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          1524..1600
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          3084..3160
FT                   /note="Carrier 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          4649..4725
FT                   /note="Carrier 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          5753..5829
FT                   /note="Carrier 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          6836..6912
FT                   /note="Carrier 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          8368..8444
FT                   /note="Carrier 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          13..81
FT                   /note="Thiolation (T) domain 1"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24848421"
FT   REGION          59..736
FT                   /note="Adenylation (A) domain 7"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24848421"
FT   REGION          572..953
FT                   /note="Condensation (C) domain 1"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24848421"
FT   REGION          989..1386
FT                   /note="Adenylation (A) domain 1"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24848421"
FT   REGION          1529..1597
FT                   /note="Thiolation (T) domain 2"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24848421"
FT   REGION          1613..2050
FT                   /note="Epimerase (E) domain 1"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24848421"
FT   REGION          2091..2523
FT                   /note="Condensation (C) domain 2"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24848421"
FT   REGION          2546..2943
FT                   /note="Adenylation (A) domain 2"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24848421"
FT   REGION          3089..3157
FT                   /note="Thiolation (T) domain 3"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24848421"
FT   REGION          3174..3614
FT                   /note="Epimerase (E) domain 2"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24848421"
FT   REGION          3655..4093
FT                   /note="Condensation (C) domain 3"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24848421"
FT   REGION          4114..4512
FT                   /note="Adenylation (A) domain 3"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24848421"
FT   REGION          4654..4722
FT                   /note="Thiolation (T) domain 4"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24848421"
FT   REGION          4775..5191
FT                   /note="Condensation (C) domain 4"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24848421"
FT   REGION          5216..5614
FT                   /note="Adenylation (A) domain 4"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24848421"
FT   REGION          5758..5826
FT                   /note="Thiolation (T) domain 5"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24848421"
FT   REGION          5875
FT                   /note="Condensation (C) domain 5"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24848421"
FT   REGION          6311..6702
FT                   /note="Adenylation (A) domain 5"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24848421"
FT   REGION          6841..6909
FT                   /note="Thiolation (T) domain 6"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24848421"
FT   REGION          6923..7349
FT                   /note="Epimerase (E) domain 3"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24848421"
FT   REGION          7391..7823
FT                   /note="Condensation (C) domain 6"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24848421"
FT   REGION          7844..8240
FT                   /note="Adenylation (A) domain 6"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24848421"
FT   REGION          8369..8441
FT                   /note="Thiolation (T) domain 7"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24848421"
FT   REGION          8482..8897
FT                   /note="Condensation (C) domain 7"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:24848421"
FT   MOD_RES         45
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1561
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         3121
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         4686
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         5790
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         6873
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         8405
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   8903 AA;  977655 MW;  6142E7C18D693286 CRC64;
     MDAPDIQAPS GSCRTTLGKV AADIFEMNVE TLDWDMSFIQ MGGDSILAID FIVRCRDEGI
     WVDMMDLLTV DTLAELADSI DEQNGVTADV ANSSDLNEHE THQENGENIN ATLPVADRPL
     RFASMEIAHV KDASLVSSAL ESLITRHSAL RSVWSVSSTG EYTLTTKPTA MAYESQPFFL
     AEASEPTKMN DAFELLKNAL RSDGAPPLGC LFISNNATTA SSIIVLAADA NLVDSLSMRI
     LRTEFREFIL GHALDAPPGF QFSNWVAAKC QSTTARPRTL QQPQRAMERA IATKLSSSTS
     SADSSSNEAT ITTFQITHST TKKLFAAQTH AALRTIPAEI INAALVYVLG AHYKKNVDHL
     MIKTAYSVRE QQNLPLDAVG CYEAEIEWEA PALSSHESAV FAVRRVCDAF ATPSRNSYDT
     STETLYIDCT RLQDTEDDEL SSFSDTILGH GHHVSVATVA GQVHVSMQLG NEKISRESIT
     NEFKLCLEKM LDELAQSPEM ATLRDYPLIH WSYSDLDDLV ADLKSQIVTI KGIESIGPSS
     AVQESFFISQ AINPDSYINH VKVRMASADD SVPHQLDTEK LVYAWGNIVK RHAVLRTAFV
     ESRDRPGKYD QLVFNPIAVL PRVTVFSCTP EASNTPSFQT GKFEVPMRLC VYEISTSELQ
     LELDISHALV DGHSAKILLH DLRASYLQDT YFSELAPLPY TDFAFHQQTV LDAGETSDGV
     AYWTSYMNKA GESHLPLITT NPNLKNLETA HRTISLPAGK LRAICGQLSI TPANLFHIAW
     ALALRRIILT DTITFSYIVS GRNGSLENSE ATVGPFINTL PFSLALAPET SVTEVLDLSK
     RDWQEGASFH NVPISELAVS KTRSLKRLGN TLLSIEREGS SSHPFADGSD LSLSARTSAT
     DFDLTANIRF DEERIEFSVE YWASRIAWPV AKAQMSAFED AVSFLLDGVN MSIRDFPTHG
     IQDKMAFLEW NTAPARLESC VHDLVLEKMA AQPTALAISA WDGEMTYGQL DHASYRVACE
     LVEFGITPDT MVGMCMEKSK LGVVAMLGIL RAGGAVVPLG VQHPIARIKG IVADAQIPLI
     LVDEAHKERL AELEPAAKLF AVDSFVKNDK SSPSTASSPK PCTSVGPDHV AWVIYTSGST
     GAPKGVMLEH GALSTSILYH GRRLDIQSYD RLLQFAAFTF DAAIQEIITA FAFGASTCIP
     SEQERMDQLP AFISREKITI TTLTSTVAAL LHPQDVPTVR TMILMGEAVQ AKVVDQWIDH
     ATVINAYGPS ECCIHSTCRP VQSSLTALNI GTAIAGATWI ANPKNVGQLV PLGAPGELLL
     EGPLLARGYL NDPIKTAKAF VADPAFVAEL NLSPGRRFYR TGDLAQQNPD GTITYLGRID
     TQIKIRGQRV EIGEIEYHIG KQSGVHDAAV LYIREGPLAD RLVAAVNLGE STPNADQFQG
     SAIQCVTGDE KDKATLQLRE IQYALSQQVM HYMVPSVWIP LYAMPMNNSG KTDRRALTLW
     VQALSQSEID EITAAEADDD IDESSMSTVE QELRQIWSKV LDVPLRSVTY SANFFSLGGD
     SITAMQVVSA CRARGIIVTV RKVLDCQTIP QLALAAESQA TSANEEVVTE APFPLSPIQK
     MYFETVAADG LRADGETSFN QGVLLHVTRR VELAELTEAL NKTVAKHAML RARFFRTQNQ
     EFQQKIERDV TGSYRLRAHA DVANAESLHG IVAESQATLD LERGPIFAAD LIERQDRQVL
     HLVAHHLVID LVSWRILVQD LEEVIINKAL PNPRSMAFPT WIERQHNYLD KLMDRKTEVL
     PVTVPATSWS YWGLVPGEEV YANRTSYQVK CDSNVVDLLS GHANAALKTE PVEVLLAALV
     FSFQQAFPDR DVPAIFTEGH GRETIDAVSD PSDTIGWFTT MAPVYLPQRA SENAIIEVVK
     QVKDQRRRIP GRGMPYFGSR FSTTRCKSQF ASHSPAEIIF NYAGRFQQLE REDALFRFDS
     EDDMNTTSKI GGRVKLLSAL DVAATVEGNE LLITVNFSNQ SQHQDSIRSW VDAYGKCIES
     TVKELAAVSA PIATATDFPL AHLSDADMKT IETDSDYLAV IGCSSTAELD DILPCSPIQQ
     GILLTQLQSP STYCIHQTCR IRSTTTSPMD IERLIAAWKE IVSRHSILRT VLLEPLPGQE
     QFMQMVLKEP RIGIKRVNDI SDDIAAEWLE SQPTLDLSEL TRPPHLLTLL TTAKGEVYCR
     FDISHALVDA SSVSLIMQDL LSAYDGNLGP NVGSDYSSYV AYLEEQDSQD ELEYWTSVLR
     NAEPCILSPQ DPIHDNRADS TIKRVVAHID DLSPLYKFRD TYGVSLASIC QLSWALVLAM
     RTNSENISFG NLSSGRDVPI QNVQALVGPM INMLICRLSL DWDANASDVA RNLQRQVSES
     FEHQRSSLAS IQHALGLSRN QPLFNSTLSY KRADSDAAAS PATGIYLEGL AWDDPTEYDL
     HTNIETSKTG MEIHMQYSTA VFSDNAATKM IEGLTRAIQA VCVGGETPLS QLQLLSVSEE
     NKLRQWNAVA TPRLERCVHE LVLEKMSSHA DATAISAWDG SMTYQELNNA SIQLAHHLVA
     QGVRPEVKIG LCLDKSRLGV VAMLATLRAG GAVVPLGVQS PVARIETIVN DSEMKIVLVD
     RNNQERLNTL ASTVQLLAVD QFAQTMSTPT DILLKEPCSS VQPDNTAWII YTSGSTGIPK
     GVVLEHGSIA TSMRAHGPAI GIQPQDRVSQ FAAYTFDVSI AETMTTLAYG ACICIPSEDD
     RINRLTGFLS EHKVTIATLT STVASLVQSI DTPTIKTLVL TGEAVQPNVV DQWKQHNTTV
     INAYGPSESS IWATSKIVED SKDALNIGLP LSGAFWVVNR NNIGQLVPVG SPGELLIEGP
     LLARGYLNDQ IKTAASFVVD PAFIHDLGFT TGRRMYRTGD LVQQNDDGTM VYLGRQDSQV
     KIRGQRVEIG EIEYHVGKQE GVQDAAVLHM KDGPLADRLV AIVIPRNDDL KTTRGQNDAQ
     ITQIPQQFKE DTKRHLQGVK QKLSQLVMQY MVPNVWIPLV AMPVNMSGKM DRLALNRWIQ
     SLSKDELAFM TGTEETQDPD QDKLFTTAIE RQLRQVWSDV LGVSVHAVTY TSNFFSLGGD
     SITAMQVVSM SRSHGILVTV RTVLECQTIP ELALQAKMVD GDNSQLTRVP EGPFALSPIQ
     QMYFANISGD GIRADGNYRF NQAVSLYIST HISQEQLKHA LDAVVSKHAM LRARYSQGPA
     GWQQWIEKDV SGGFRCQSYD AVDLDAMRQI IETSQTSLDI EHGPVFAADL IERQDNDRQV
     LHLVAHHLSI DLVSWRIVIQ DLEQLLTNGK LPNPTTLSFP VWLERQQDSL DTFIAKMDTP
     ESALSQLLPT SVPVIDWNYW GLSPGQEVYG SLTSLETRCD SATTSLLLDQ ANSALKTEPV
     EILLAALLSS FQQVFTDRQS PAVFTEGHGR EAFDTKSELD LSETVGWFTT MTPVYIPQSA
     ATNSIQMLQK IKDQRRRVPG RGMPYFGSRY LTSAGEEKFA DHATPEILFN YFGRFQQFER
     DDALFQINND DDSASSQFGD LIKLFAALDV TVAVEASELH IKTRFSRQSQ HQASIQRWVQ
     AYGNAIKSLV EELMVTAATS TATDFPLARL TDTNWEFMQK QYLVAMNLQS TAEIEDILPC
     SPMQQGILLT QLQSPTTYCI HQISRFQPSK SGSVSVERLI SSWKHVVSRH SILRTILVEP
     LPGQERFVQI VLKQPHLDII KLREITDSEH AAIATLEAQP LLNARKITSP PHRITMLQST
     AGEVYCRFDI SHALIDGSSM AILIRDLMSA YSEDVSSDSI ASGSKYSSYV AYLEDTDHQK
     ADLQYWTSLL ADSEPCILPS EASAPESEPA QLGHVSKTIS DLDALHGFRD THNVSIASIC
     QLAWALVLST WTGSSDISFG NLSSGRDVPI EGVQDLVGPM INMLICHVPL DWNASVADVA
     RKIQSQSAEA FEHQRSSLAA IQHELGLSRD KPLFNTTLSY KRITPPPSSS GSTSITFEAL
     VQEDPTEHDL HVNIDSTPTG LQFDIQFSTA VFSSAAAETL TESLVRTVGI LSQSAHLSLG
     NVNLMSTKDI QQLCEWNSKM PSRTELCVHD LISERLNTQP ESMAISAWDG DMSYLELDAV
     SHTLASHLIT LGLDFQRSEP MIGLCMDKSK WAVVAMLAIL RAGGTVVPLG VQHPVSRIDN
     IVQDTSAIVV IVDRGQEQRL ASLGTSTHLL AIESFFEASP PVASQSTPLT ADTTPDSAAW
     VIYTSGSTGK PKGVVLEHGA LVTNILAHGR AMNIQPGDRV LQFAAYTFDI SIAEVLTTLI
     FGACVCVPSE SERMEQLACF ISRQEVTTAI LTSTVAALVD PQQTPTLQTL VLTGEAVQPK
     VVSQWIGQAT VMNCYGPSES WICTTHKIES AATASVVGPP IAGGFWVVNP GSVDQLVPIG
     APGELLIEGP LLAREYLNNA DKTAASFIND LAFTKELGLG SRRMYRTGDL VKYNSNGALV
     YIGRIDTQIK IRGQRVEIGE IENQIVDLLP GAREAVVDLI TPAEVEGASP MLVAVVEYRQ
     DEPRTDATGL SLYDPSQLTD ATLEALDQLQ TDIAKALPAY MIPATFLLAS KLPINASGKL
     DRRTLRLALQ DMTREELGNS TGNTSTKQAP RTTMEKKLRD LFAATLQLTP DNFGINDSFF
     RLGGDSVAAM KMTAAARALD LPLSVVDIFR FPILADLAEA TELKCSQQQE DSRSLVPFSL
     WPELQQDHAS SSDSYKTQLL AEAAQLCGVS ASQIEDVYPC SPLQAGLMAI TSQRPEAYIM
     RRAFKLRASF PIEQLKIAYE RLTEAVSILR TRIIPSTCVD ALQVVVQEKP FWHGEVGMSL
     EQYIAKDRSA SMAYGRALSR TAIVSNEDGQ FFVWTMHHSV YDGWSLTKMM GMLTQLMTGQ
     ALATTVPSSR FINYLVQQDT DQVAKFWQSH FQGANWTRFP ALPSPRYQAK SSGQLRSQFQ
     LPLNPSILET DSTVLRAAWA LLVASKIGAD EAVINVVLSG RMAPVEDIMN MLTPTVTTVP
     VRVSATKNQS INKFLKTIHD TAIDMVPFEH TGLQNIRTMV PTLGSDFDPG HTFVVQPAGE
     SESAATMWNM DLEREATPLD AFDAYALTVE CTVDSQRTGE VTVDIRYDSF VIPDDDAQKL
     LNQFTHIAQE LAQQAATTKP LAQLQMLSEE DRFLLSKWNA HVPPRLEYTL HDAVTETMTS
     QPDAPAIYSW DGDMTYGEVN AASHRLASHL ANQGVGPEVM VGLCMDKSKW AIVSMLAILR
     AGGAVVPLGI SHPLARIDNI IQDTAAPLVL VDSTHQHRLQ DLTAPTPLLA VDKFFEEYEA
     ANYDSSAKLP STVQPHHPAW VIYTSGSTGT PKGIVLEHRA LATSILSHGK EFGIQAHDRV
     LQFAAYTFDV AIQDVIATLA SGACLCVLSE YDRINRLTEF LSESNVSFAI LTPTVAALIE
     PKDVPTVKTL VLGGEALPAK VVDQWAEHAL IINGYGPSEC CIHSTCAKIP LGSDARNIGR
     GVTANTWVVD PTDIGQLVPI GSPGELLIEG PLLARGYLND PTKTAKSFIR DPAFLSTLNL
     PNGRRMYRTG DLVQQNRDGS LIYIGRRDTQ VKIRGQRVEI GEIESRIVDL LPEAREAVVN
     LVRPAGEAAD LVTLVAVIEC DYAAGASHDT ESELELFKPS SYSDALNRAL VKLDDDLGQA
     LPSYMVPSAY LLVPKLPLNP SGKLDRRAIQ DQLQLLPRAK INSLSGLTNR KQAPTTAMEK
     RLQNLFCQTL MLTPEEVGVN DSFFRIGGDS IAAMKLTAVA RHQNLPVSAA DIFRWPRLGD
     LAQELEQRHE LKTATLNDPA PLSLWPELSQ AGTQSKSQLL ANIASQCGVS VEAIEDVYPC
     SALQAGLMAI TTQRPEAYVV QRVFKLQPSL SSQHFKAAWN QLAQSLPILR TRIVPSIHTD
     ALQVVTRDAP VWQETQASVQ DYLENDRTVP IAYGTPLSRV AIVQDQQSRY FVWTIHHSAY
     DGWSMGKMME VLSQVLEGTT PSVLVPVSRF IGYLSQQDKS QTSTFWQKHF EGASCTVFPE
     LPSRQHVVNP NKTLKSRIQI SQSPGVTPFT ALRAAWALVV ASATGSDDAL INVVLSGRLA
     SVDGIMDLVA PTITTVPFHV PISQDLSVKE FLANVDERAS DMIPYEHTGL QHIRRMVPGL
     GPEFSPGHVF VVQPAAESES TVAALPQMEL IKSDFESEDA FHAQALTVEC TVGQDLSDVE
     VQMRYDGNVL STESATHLLD QFSHVVEQLA LNGDKSLSQL ELLTANDRQR LIEWNSTVPP
     RVERCIHQLV EEQMSLRPSE LAIKAWDGDM TYAELDTSSR QLAQRLTQMG VGPDVMVGIC
     MDKSKMGVVA ILAILRAGGA VVPLGVTHPL TRIEGIVKDT KSPLILVDSA QKQRLASLTA
     QLLVVDSTLT NTLTASAQNI SVQSKNVAWV VYTSGSTGTP KGVVLEHGAL ATSVLGHGAA
     YNVRSDDRIL QFAAYTFDAA IQEIITTLAF GACICVPSEQ DRVNRLTDFF IETGITMATL
     TSTVAGLVRP NMTPAVRTII LVGEAVQANV VDQWIQKATV INGYGPSECS IASTCGEIRH
     SSYALNIGTA IAGATWIVGS TNKLVPIGTP GELLLEGPLL ARGYLNDAVK TAASFTTNAA
     FVEELGLSSA NRRMYRTGDL VKQNIDGSIT YLGRMDGQIK IRGQRVEIGE IEHHLQKHSV
     VGDAVVLYMK QGPLSGRLIA IVVTNDTNST SQTAEIQHLP TGQRESANLE LTDVQQSLSN
     QLMQYMIPSV WIALASIPVN ISGKTDRLTL TRWLQSLSDD EVEALTGTEE TEVDESSATN
     TERQLRQIWS QVLDVPIEKI TFSSTFFSLG GDSITAMQVV SACRSCGLLV SVQKVLNCQT
     IPELAATLEV MDIVNDVDQI PEGFFELSPI QRMYFDDMAA MGLRADGENR FNQAVTLRIT
     RPTTSEELIQ ATDILVAKHP MLRARFIQNQ QSWQQHIEKE VAGSYRFELH EVADAQAMQS
     IITQSQASLN LEHGPVFAID LIDLPTKKVL HLVAHHLVID LVSWRVLAQN LEDLLTSGTE
     PNPTSLSFPS WIQKQFQFLP SSEETSESVL PVQIPASNWE YWGLVPGSER FGNRSKIEVK
     CDTSTTSLLT GDANYAFNTE PVEVLLAALA ISFQKTFTDR SMPAVFVEGH GRETMDDKVD
     LSDTVGWFTT MTPVHVPMDK NESDLDVLRR TKDQRRRIPG RGLPYFASRF LGPNPDKFDN
     HGPAEILFNY FGRFQQLERE NSVFQIEQDG ESAPQLGNSV KLFAALDLSI AIEGDQLSIT
     VHYSNKSKHQ STIRQWAESY GRTIKTLVEA LVIAPPTSTA TDFALARLSD SDMVAIEKDC
     VSNVGSTRNI EDILPCSPIQ QGILLSQLQS PTTYSIYQTC RIKPSKHDSL VDAHRFLGAW
     KQLVAHHSIL RTVLLEPLPG HEKFMQIVLR EPEINVLTKS GVADAEAVEW INSRPGLDLT
     DRHHPPHRLT LLTTTSGQVY CRFDISHALV DASSLALIIR DLMSAYEGKL GSSSNGSNYS
     AYIAYLDDNN QQDDLNYWTS LLNNAEPCLV PPKEPTHTAT QATIGHASQK VSDLDVLHKF
     RDTYGISIAS ICQLSWALVL ATWTGSQNVS FGNLSSGRDA PIPGAQDLVG PMINMLVCHL
     QLDWDSKVSD AARKIQTQSS EAFEHQRVSL ASIHHALGLS KDQPLFNSVM SYKRLATGES
     TPREIILEGL TAEDPSEYDV NVHINASSTS LDFNIQFSTT VLSQAAANKL TASLVQAVHA
     ITQNANRSLG QLKLVLTNDE AQICKWNSFM PAGLQNRVHD HVLEQMARKP EAQAIFASDG
     QMSYGELDVS SRQLAHHLVS QGVGPDVVVG VCMDKSRWAV VAMLSILRAG GAVAPLGVQH
     PVARIDTIVK DASAPVILVD AEQEQRLDTL SNNFQLINVK SFFDTVQNTV STSEPCTTVQ
     SHHIAWVLYT SGSTGVPKGV MLEHGSLATS IMLHSRRFAM QSTERLLQFA AFTFDAAVFD
     IFAPLSHGGC TCIPSEHDRM NNLEAFAIGA KVTWGFFTPT VAALMQPSDI PSMRTLILGG
     EVVTAKGVDH WVKAGVKVIN VYGPTECSIY STYKHIQDTQ NLRNIGTTVA AGLWVVNPVS
     GEQLVPIGAP GELLIEGPLL ARGYLNDSAK TAASFVTDPK FVKELGLSPG RRMYRTGDLV
     QQNSDGTLTY LDRIGTQVKI HGQRLEIGEI ESQLHDLLPE SRYVCVCKKG TSLVAVIEST
     TPNRDTPGTS AHYIVAPGPE QEKTFEYLNS TLREKLPSYM IPSAFLVINE FPLNDNGKFD
     RRRIGNLLNS IPSDKWLEYT AKSQTYYAPI SATEAVFCEL WSQCIQQLDK PVSRTDNFFD
     LGGDSVTAMQ LVQQLAKRGM RLATIDIFNN PVLHAMAACV SDVSDDNQEY KRFSLISTEE
     KSTALELVAA DDTVDKQIRV IDVLPTTEFQ TLMVRQIMSA ARRQLNQFAF DADEACDVSV
     LTSAISDLVA TIESLRAGFV KLPGQKYLQV VYAVWEPEIR VFYTEKSPRA FYEESSEQDL
     FPEPTLSRPL FDVAIIIDKI TQKHRVVFRI SHALYDGATL HRVWTALEAL TTGQAPGYFA
     PIGAYLQSLQ AQTTSETEDY WQQLVDGATI SCVGTSSEPK VSRLGHVSGP PITLPESKQS
     HFNLAVAVKA AWALVFGHHA NTHDIVFADV MTGRNTVDSS VADVVSCCAR AVPCRITYEP
     DWTVEKLLDL TKQQQVNSMR HEGLELQQIA QRYMGWPQDD HEEAPDMRVS MTNYVKTSIR
     DLLLGATQYR RATAGFQNAY ASADFSVDSV EESDGSLSVS IAYAADRISE QLAATLLHRT
     RVTLEKMMEN PRSTVGHLLK QLD
 
 
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