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NPS2_COCH4
ID   NPS2_COCH4              Reviewed;        5386 AA.
AC   Q5D6D7; N4WT87;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2018, sequence version 2.
DT   23-FEB-2022, entry version 81.
DE   RecName: Full=Nonribosomal peptide synthetase 2 {ECO:0000303|PubMed:15755917};
DE            Short=NPRS 2 {ECO:0000303|PubMed:15755917};
DE            EC=6.3.2.- {ECO:0000305|PubMed:15755917};
DE   AltName: Full=Ferricrocin synthetase {ECO:0000303|PubMed:17601875};
DE   AltName: Full=Intracellular siderophore synthetase {ECO:0000303|PubMed:17601875};
GN   Name=NPS2 {ECO:0000303|PubMed:15755917};
OS   Cochliobolus heterostrophus (strain C4 / ATCC 48331 / race T) (Southern
OS   corn leaf blight fungus) (Bipolaris maydis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=665024;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DOMAIN.
RC   STRAIN=C4 / ATCC 48331 / race T;
RX   PubMed=15755917; DOI=10.1128/ec.4.3.545-555.2005;
RA   Lee B.N., Kroken S., Chou D.Y., Robbertse B., Yoder O.C., Turgeon B.G.;
RT   "Functional analysis of all nonribosomal peptide synthetases in
RT   Cochliobolus heterostrophus reveals a factor, NPS6, involved in virulence
RT   and resistance to oxidative stress.";
RL   Eukaryot. Cell 4:545-555(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C4 / ATCC 48331 / race T;
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C4 / ATCC 48331 / race T;
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
RN   [4]
RP   FUNCTION.
RX   PubMed=17056706; DOI=10.1105/tpc.106.045633;
RA   Oide S., Moeder W., Krasnoff S., Gibson D., Haas H., Yoshioka K.,
RA   Turgeon B.G.;
RT   "NPS6, encoding a nonribosomal peptide synthetase involved in siderophore-
RT   mediated iron metabolism, is a conserved virulence determinant of plant
RT   pathogenic ascomycetes.";
RL   Plant Cell 18:2836-2853(2006).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=17601875; DOI=10.1128/ec.00111-07;
RA   Oide S., Krasnoff S.B., Gibson D.M., Turgeon B.G.;
RT   "Intracellular siderophores are essential for ascomycete sexual development
RT   in heterothallic Cochliobolus heterostrophus and homothallic Gibberella
RT   zeae.";
RL   Eukaryot. Cell 6:1339-1353(2007).
RN   [6]
RP   INDUCTION.
RX   PubMed=23980626; DOI=10.1094/mpmi-02-13-0055-r;
RA   Zhang N., MohdZainudin N.A., Scher K., Condon B.J., Horwitz B.A.,
RA   Turgeon B.G.;
RT   "Iron, oxidative stress, and virulence: roles of iron-sensitive
RT   transcription factor Sre1 and the redox sensor ChAp1 in the maize pathogen
RT   Cochliobolus heterostrophus.";
RL   Mol. Plant Microbe Interact. 26:1473-1485(2013).
CC   -!- FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster
CC       that mediates the biosynthesis of hydroxamate-containing siderophores
CC       that play a critical role in virulence (PubMed:15755917,
CC       PubMed:17056706, PubMed:23980626). Cochliobolus heterostrophus produces
CC       extracellular coprogen-type siderophores including coprogen,
CC       neocoprogen I and neocoprogen II, as well as the intracellular
CC       siderophore ferricrocin (PubMed:17056706). The role of extracellular
CC       siderophores is to supply iron to the fungus during plant infection,
CC       and the intracellular ferricrocin is required for intracellular iron
CC       distribution and storage with a crucial role in ascus and ascospore
CC       development (PubMed:17056706, PubMed:17601875). SIDA2 catalyzes the
CC       conversion of L-ornithine to N(5)-hydroxyornithine, the first step in
CC       the biosynthesis of all hydroxamate-containing siderophores
CC       (PubMed:23980626). The assembly of extracellular coprogen-type
CC       siderophores is then performed by the nonribosomal peptide synthetase
CC       (NRPS) NPS6 whereas the intracellular siderophore ferricrocin is
CC       assembled by NPS2 (PubMed:17056706, PubMed:17601875).
CC       {ECO:0000269|PubMed:15755917, ECO:0000269|PubMed:17056706,
CC       ECO:0000269|PubMed:17601875}.
CC   -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:17601875}.
CC   -!- INDUCTION: Expression is repressed by the transcription repressor SRE1
CC       under iron replete conditions (PubMed:23980626).
CC       {ECO:0000269|PubMed:23980626}.
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 (By similarity). Each module is responsible for the recognition
CC       (via the A domain) and incorporation of a single amino acid into the
CC       growing peptide product (By similarity). Thus, an NRP synthetase is
CC       generally composed of one or more modules and can terminate in a
CC       thioesterase domain (TE) that releases the newly synthesized peptide
CC       from the enzyme (By similarity). Occasionally, methyltransferase
CC       domains (responsible for amino acid methylation) are present within the
CC       NRP synthetase (By similarity). NPS2 has the following architecture: A-
CC       T-C-A-T-C-A-T-C-A-T-C-T-C-T-C (PubMed:15755917).
CC       {ECO:0000250|UniProtKB:A0A144KPJ6, ECO:0000305|PubMed:15755917}.
CC   -!- DISRUPTION PHENOTYPE: Leads to defective intracellular siderophore
CC       (ferricrocin) biosynthesis and sexual development (PubMed:17601875).
CC       {ECO:0000269|PubMed:17601875}.
CC   -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAX09984.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY884187; AAX09984.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; KB733486; ENH99442.1; -; Genomic_DNA.
DR   RefSeq; XP_014073329.1; XM_014217854.1.
DR   SMR; Q5D6D7; -.
DR   EnsemblFungi; ENH99442; ENH99442; COCC4DRAFT_45281.
DR   GeneID; 25845193; -.
DR   HOGENOM; CLU_000092_2_0_1; -.
DR   OrthoDB; 4243at2759; -.
DR   PHI-base; PHI:4234; -.
DR   Proteomes; UP000012338; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1200.10; -; 6.
DR   Gene3D; 3.30.300.30; -; 4.
DR   Gene3D; 3.30.559.10; -; 6.
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; 6.
DR   Pfam; PF00550; PP-binding; 6.
DR   SMART; SM00823; PKS_PP; 6.
DR   SUPFAM; SSF47336; SSF47336; 6.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 3.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 6.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 5.
PE   2: Evidence at transcript level;
KW   Ligase; Multifunctional enzyme; Phosphopantetheine; Phosphoprotein.
FT   CHAIN           1..5386
FT                   /note="Nonribosomal peptide synthetase 2"
FT                   /id="PRO_0000444384"
FT   DOMAIN          544..617
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:15755917"
FT   DOMAIN          1611..1688
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:15755917"
FT   DOMAIN          2652..2725
FT                   /note="Carrier 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:15755917"
FT   DOMAIN          3728..3805
FT                   /note="Carrier 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:15755917"
FT   DOMAIN          4281..4357
FT                   /note="Carrier 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:15755917"
FT   DOMAIN          4840..4913
FT                   /note="Carrier 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:15755917"
FT   REGION          45..435
FT                   /note="Adenylation 1"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:15755917"
FT   REGION          652..1059
FT                   /note="Condensation 1"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:15755917"
FT   REGION          1089..1482
FT                   /note="Adenylation 2"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:15755917"
FT   REGION          1731..2141
FT                   /note="Condensation 2"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:15755917"
FT   REGION          2166..2551
FT                   /note="Adenylation 3"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:15755917"
FT   REGION          2763..3174
FT                   /note="Condensation 3"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:15755917"
FT   REGION          3202..3603
FT                   /note="Adenylation 4"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:15755917"
FT   REGION          3846..4250
FT                   /note="Condensation 4"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:15755917"
FT   REGION          4391..4802
FT                   /note="Condensation 5"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:15755917"
FT   REGION          4821..4842
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          4952..5257
FT                   /note="Condensation 6"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:15755917"
FT   MOD_RES         578
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1648
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         2686
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         3765
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         4318
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         4874
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   5386 AA;  600338 MW;  DFEBAC685156E13A CRC64;
     MSSATSPCEM AHKNRLNQTL SILNGQPLLL DGPDLLHQLV PRLHHDANAI DFLEHGSKRR
     KFSYTTLHSL SDAFAARITE ILGKLESASS IIPVFLPQSP ELYVVLLAIL KAGKAFCPLN
     LDTPTERLKF ILDDISADII ITFESYSEHI RTATNIHVVS ANRELSGCHD TFHHHSPHLS
     PDNLAYVLYT SGSTGLPKAV SVSHRAVTQS LLAHDPHIPA FSRFLQFAAP TFDVSIFEIF
     FPWFRGKTLV GCTRTQMLDD LPGTIASLDV DAAELTPTVV SSLLSGRSSV PGLKLLLTIG
     EMLTQPVIDE FGGDATKESI LWAMYGPTEA AIHCTIWPQF STSDSTNTIG HPLDTVSAFI
     LASSTGLHTS PIDILPIGQA GELAIGGPQV AKEYLHRPDL TRASFVEHPY YGRLYRTGDR
     ARINEQGLLE CLGRVVAGQV KLRGQRIELG EIEQAIMKTR GCRAVTAMVI QDNLVAFCSG
     RDGMSRGAVL TTCKHWLPAS MIPSDVFVID VMPQLPSGKV DRKSLEKAYL HSHPNGSSSS
     LAISPKDPIG HSVWSVVSHH TTQNIGLETN LTSIGIDSLK SIRIASALRR KGYSLGAIEV
     LSAATLADLI EVCRESKPVD FSSQDKETKP GAFIDTKNLQ LNGWRHNVAL ILPCTPLQEA
     MLAETRSKPT AYCNWIEVEL SVAYTYEQIQ DALLFLAQEN EILRTGFCID SQHTTVFSQV
     IWKELSLSQI QKVASFSNQY SMQSDHDFLR PFGVQIKTHC KLPRLLFQIH HALYDGWSLD
     LLLRDLDHCL RGKQDLKRPS FREVVRYLDD DRRLNKTQNS TNYWKSLLGD YIPTTLPNYH
     GKLVHNASIH RFFGQSSVSR HNLFECAHHS AINPQVYFQA ATAFVLSLYT GSSDVVLGNV
     TSGRTIPVAG IEDIIGPCIA SLPFRIDFAD TYCVRDVLKR TQSTNRDSLR YSQLPLREIA
     RAVNVKPGAR LFETLFVWQQ SMVEDEDDNA SLIAKVVDSA DELEFRITLE FEPVGDNILF
     RSTFDAATVS EHQIQYLFRQ IDEVVEMFMV DADRHVSAIN QCFTTPSLSI ANPTPLEQRF
     DHGPSHAVEK WAATDPHRTA IIFGHEVNGS IKVKDTMTYS MLNSRANQLA RLLAEHGVTN
     DQLVCIIMEK SVNLYTCILA VLKLGCGYLP LVPDTPIDRV KTILNDAQIA VCMSELSLSA
     TLRSHLSVDI IDFDLAALSD YCDRNLEIPY NGQHLAYAVF TSGSTGTPKG VLVTQDNLMS
     NLHYLSTIYP FSADSRLLQA CSQAFDVSVF EIFFTWYVGI CLCSATKEHL FRDFEAAIDQ
     LKVTHLSLTP TVAALVDPKN VPKVEFLVTA GEAVTEHVRR KWAGRGLYQG YGPSETTNIC
     TVRVAVTPDD LINNIGSPFA NTSAFVLDPE SQDILPRGAV GELCFGGSQV FRGYLNRPEL
     NAQKIIQHPT YGRIYRSGDM GILLPDDSIL STGRTDDQVK IRGQRVELGE VTSVILDHGA
     VWDCVTLALE QSTNSKTLVS FWVPREDSSS RVESLEPSKF TTTISELFDL LSRRVPSYMV
     PSHLIPISCL PMTPQAKIDK RFLQRLFSSC EEHTLNNATN SNSITETEEG ELLSQWERDV
     SQLLIRMLAT SSDKLKRTSS FFNLGIDSVS AIRFCSELRK AGLGDYSVSE VLKHPSIASL
     ASLKKLQSST TTTTTTMDKT LSVDASHIFT TNQLERIRST VDMNGVRATK ILPCTPLQEA
     MISSGLSSPG QAYCNVMVFD VKGDLQQLQR CWKTVIQRHE IFRTSFVATD NPLYSFAQVI
     VEGYGMGWHE DSIDSGLQLR VSKILFDLME ANKPPVYFSL NREEDSAKLL FCCHHALYDG
     IAMSTLLAEV QELYHGRQLL PPVSYDVYLK RMLEQNLDEA DKYWSALLEG FEPTSFPSLT
     GKRVREYEAF TSSSRRLSMS LDSVRNSCQN SSVSLLSVVH AAWAKLLHFY THESDICFGN
     IVSGRSFPGE HLERLVAPCF NTLPVRVDFD FGKSNRALVD LMHNQSIESL AYQLSPLRRI
     QKTTLKDGGR LFDSLVILQQ PNVPLDSSIW RLEQDSGDMD IPVVCEVVQD QSEDALRLLM
     HYNNSLISET EASIVMETFD AALSSLIKFP DALSADTDMF PSNLWANYNT NFKRLESDSK
     FLHSGFERTA LLHPDRIALD FWHSQGKKTT WSFEQLNREA NQIAHALIRA GAWPDQVIPI
     HISKSPIYYA SILGVLKSGA AFAPVHPDLP EARKQLMFKD LKPKIILCDD GSLLPEDLPD
     VTVLITQSMS SDDVSNPIIE DLKDTNLAYC LFTSGSTGVP KAVSMEHCAP IQTIESSRTI
     IPWNPQSRLL QYAAVTFDMC YYDCFLSWTF GFALCAAEQS DLLNDLSGVI KTLEADLLDL
     TPSVAETLKR ADVPNVKWLY CIGEAMSSSV VKEWEGACVN SYGPTEAAFC TTITPLSKDE
     STSIIGKPFP TTSFAVFSEG SQTPLPALSI GELYIGGAQL ARGYWGRANL TNDRFVSRCG
     QRFYKSGDMV RMLSDGNFEF MGRLDDQVKI RGLRVELGEI NSILAELDPD LLSVTTQILL
     KGESSKEQLV SFMVLRQSIQ ESDIPTLQRK LKKLASARLP SYMVPQFFLV VDEIPKSMAG
     KIDKKALKHQ WSKTESEVRN ILAHISKTPT ENISPLTSIY QLGLDSISAV QIASALRSQG
     YTIKATDVLK HTTCNDLAEH LDQISTSEAP ESSPFDFHGF ESRHRMQILR DHGIQDGNVA
     AVRPCTPLQN GMVSQFLAKE GAVYMNYLRL QLEPKVDLEK LKAAWSSTME RHSLLRTGFA
     HVNDPLFPFA MIEYTQVSVT LPWSAIREQK KSQSSNAWLQ RIRAQSLKEL YVPPWALRFV
     ERNDQSFLDL AIFHALFDAQ SLQNIFTDVT AFYKGLSLPP VPSLNEVVSH VIQSYKQDNS
     SGKEFWVELG KTANPSRFPN LAPLKCDPKP PIVCTRRSAK SLIDLENGCR QANTTMPAVG
     MASWLSLLSS YTGESSVTCG VVLSGRSSDA TAHANFPCIN TVPLAFTVAN DTTKMLESIT
     VLNAGIQEHQ FKPLKEIQAL MGFPNESLFD SIFAYQKLAN NKDTSDLWTV VDENATIEYP
     VSIELEPKEE RLEYRLTYFP HIIPREQASL ILAQLDHLME SLIFHSQIPL AKTDYSQHLY
     SITPAKEDEL PSDMKLLHEL VEKTAQEHPQ RIAFEFVSKE SSGKRPVRKW TYRELDQEGN
     KIAQLLAAHN VKQNSLVGVC FDKCPEASFA MLGILKAGCA FVAIDPGAPA ARQTFIIEDS
     DAQAVLSMSS QSAQFNAIAK VPVLNLDEVE WCSLSGQKLL QNSVIDPQDR SYCLYTSGTT
     GTPKGCELTH ENAVQALLAF QRLFAGHWDV DSRWLQFASF HFDVSVLEQY WSWSVGICVV
     SAPRDLIFED LAGSIRDLNI THIDLTPSLA QILHPDDVPS LCKGVFITGG ESLKQEILDV
     WGPKGVIYNG YGPTEATIGC TMYPRVPANG KPSNIGPQFD NVGSLVLRPG SDVPVLRGGV
     GELCVSGKLV GKGYLNRPDL TTERFPYLNR FSQRVYRTGD VVRILHDGTF HFLGRADDQV
     KLRGQRLEVA EINSVIKQSD SDISDVATLV LKHPKQQKEQ LVSFVVCGKA LKAQPEVLLG
     EVGGIASAKQ ACNDKLPPYM LPTHFVPLTS MPLNVNNKAD GKALKKMYES LSSTDLQKLS
     ATSLSRDEQW SKQEEKLRDV MLEALGADHE SMSKNTSFYE LGMDSISVIG VTQSLKQSGF
     TKVTTSMILQ CPTIRRLAKS LAANSAMSNV RGSILAAQQS INAVNHRHRR KIAKRLSVKP
     SMIESLAPCT PLQQGMIARS MENGNGLYFN TFRFRLNMDV DEGKLRHAWE TMYNSTQILR
     TVFVNTEEGY LQAVLGGIPF NGFIQTSTQD DDLISHMAQL HKDWLSLNDV DFRQPFQVHL
     VSAQKQKQLI VHIFHGLYDG NSIGLLLQGV WNSYERRDSM PDAPSFHTAL AHGPLRIPDD
     AKSFWKDLIL ARTSSLPTLF DNSSQDAVVI ARTMRAPANF DLIRRQLNVT AQAVVQACWF
     SVLHRHVKGD VATGIIVSGR SIEFEGADRV IGPMFNTIPY HHRAQRSESW SSIIERVHDF
     NIQAHPFQHT PLRDIMKWCK RSPSNPLFDN LFVYQVPQDN QEWAKNDLWT LLDDEAIADY
     PLAFEVEHRG GTELKLTLVT QGHVANDQIA AKLLDMFEEA LDQAINDPSA VLELPADVDG
     AVENNTAIRS KLDDNNDISD FEWSDNAIAI REEIANLTAN EMESISETTS IFELGLDSID
     AIKLSSKLKK RGMELSVSGI MRGLTIEKMA QNMSMKNTQT TEAAPHFDLD AHKTKLAKCL
     YHQGFSADDI EEILPLTPLQ EAMVAEMIAS EYTRYFNHDV LKLSPDTDIS KFQKAWTTVV
     MGSPILRTGF VEVDNPDIDL SFAQIIHRQP HDFYSHMSFG SRPDFASIFK DLRNDAIQRP
     LSTPLFHLTF IDTPDQSYLV LSIAHALYDG WSLSLLHSDV HRAYQNEFEA RPSYQPSLAE
     IIKTSGPDAA GFWQDYLSGA NGNTFPRRTL EPDEKSSTVH RHQENSKIAL ELIQSFARKN
     NVSLQTVGQT VFALVTASFT RSLDVTFGSV LSGRDEEETS QLMFPTMNTV AIRTILHGKS
     IELLRYVQDN FANIKQWQHY PLRKAMSQAR LDGRLFDSLF IYQKRLEQQQ NEGERLYTSV
     GGHSDVEYAV CVEMEVVKEA LIWRCAVKDD VFDLEETRQL LKRMDDVLIH LMERAEAPVI
     DMTAEGTSVC GLPAFEEAEM HTGSGHVESG EDDGQDTPST ETTNRIRKIL AAVSKTPEEE
     MTNDMTIFHM GLDSISAIKV SSLLRKQGVV LSVGEMLQAG SVEKMAKLAD ARATEPSKDD
     AIDSASLGEI LKELNEAEVF KRAGVDVDNV VQMLPVTAGQ LYMLSMWLNT NGSNFYPEFS
     YEFEADVAFE DLKKAWQALV TTNPILRTCF VSVGNHQVSY VQLVLRDIDI AITNVTEYGE
     EEIRNCIRKA TTQQPWARLL VSRNSHSWTL RLKIHHALYD GISLPLLMQQ FEDLCNGSVL
     NASRNDILAD FISSTSSLSS SPQRRQFWET HLLSRTAPTQ LKQPSHTPTT RLEIFRPSLT
     PIQTLDTTAR HHGISPHALF LAIYAKLHSR LPHSTTTDDN IVLGIYLANR SLSCTPELPG
     AAIPTLNLVP LRVSTPQSRS VVESAKQVQA HLRHLNDATL ATTSLVEIER WTGVKIDVFV
     NFLVDIDDQG ARPKHAHQRV KISPTLRQQY YCSSFSRTSS VVQPEFMDFQ ALRNEHVNGV
     YLHAIDIEAT VREGYLDVGI FAPGDMISLE QGEQLMDGLK GEVEGL
 
 
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