位置:首页 > 蛋白库 > ARO1_NEOFI
ARO1_NEOFI
ID   ARO1_NEOFI              Reviewed;        1578 AA.
AC   A1D244;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Pentafunctional AROM polypeptide {ECO:0000255|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=3-dehydroquinate synthase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              Short=DHQS {ECO:0000255|HAMAP-Rule:MF_03143};
DE              EC=4.2.3.4 {ECO:0000255|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              EC=2.5.1.19 {ECO:0000255|HAMAP-Rule:MF_03143};
DE     AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              Short=EPSP synthase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              Short=EPSPS {ECO:0000255|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=Shikimate kinase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              Short=SK {ECO:0000255|HAMAP-Rule:MF_03143};
DE              EC=2.7.1.71 {ECO:0000255|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=Shikimate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              EC=1.1.1.25 {ECO:0000255|HAMAP-Rule:MF_03143};
GN   Name=aroM {ECO:0000255|HAMAP-Rule:MF_03143}; ORFNames=NFIA_011760;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic
CC       reactions in prechorismate polyaromatic amino acid biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-
CC         dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
CC         Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC         ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03143};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630,
CC         ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+);
CC         Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216;
CC         EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-
CC         carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702,
CC         ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03143};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 2 Zn(2+) ions per subunit.;
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       6/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the sugar phosphate
CC       cyclases superfamily. Dehydroquinate synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SIMILARITY: In the 4th section; belongs to the type-I 3-dehydroquinase
CC       family. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the shikimate
CC       dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS027688; EAW22487.1; -; Genomic_DNA.
DR   RefSeq; XP_001264384.1; XM_001264383.1.
DR   AlphaFoldDB; A1D244; -.
DR   SMR; A1D244; -.
DR   STRING; 36630.CADNFIAP00001438; -.
DR   PRIDE; A1D244; -.
DR   EnsemblFungi; EAW22487; EAW22487; NFIA_011760.
DR   GeneID; 4591045; -.
DR   KEGG; nfi:NFIA_011760; -.
DR   VEuPathDB; FungiDB:NFIA_011760; -.
DR   eggNOG; KOG0692; Eukaryota.
DR   HOGENOM; CLU_001201_1_2_1; -.
DR   OMA; YCYDDHR; -.
DR   OrthoDB; 39786at2759; -.
DR   UniPathway; UPA00053; UER00085.
DR   UniPathway; UPA00053; UER00086.
DR   UniPathway; UPA00053; UER00087.
DR   UniPathway; UPA00053; UER00088.
DR   UniPathway; UPA00053; UER00089.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00502; DHQase_I; 1.
DR   CDD; cd01556; EPSP_synthase; 1.
DR   CDD; cd00464; SK; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.65.10.10; -; 2.
DR   HAMAP; MF_00210; EPSP_synth; 1.
DR   HAMAP; MF_03143; Pentafunct_AroM; 1.
DR   HAMAP; MF_00109; Shikimate_kinase; 1.
DR   InterPro; IPR018508; 3-dehydroquinate_DH_AS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR   InterPro; IPR016037; DHQ_synth_AroB.
DR   InterPro; IPR030960; DHQS/DOIS.
DR   InterPro; IPR001381; DHquinase_I.
DR   InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR   InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
DR   InterPro; IPR006264; EPSP_synthase.
DR   InterPro; IPR023193; EPSP_synthase_CS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008289; Pentafunct_AroM.
DR   InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR   InterPro; IPR041121; SDH_C.
DR   InterPro; IPR031322; Shikimate/glucono_kinase.
DR   InterPro; IPR013708; Shikimate_DH-bd_N.
DR   InterPro; IPR010110; Shikimate_DH_AroM-type.
DR   InterPro; IPR000623; Shikimate_kinase/TSH1.
DR   InterPro; IPR023000; Shikimate_kinase_CS.
DR   Pfam; PF01761; DHQ_synthase; 1.
DR   Pfam; PF01487; DHquinase_I; 1.
DR   Pfam; PF00275; EPSP_synthase; 1.
DR   Pfam; PF18317; SDH_C; 1.
DR   Pfam; PF08501; Shikimate_dh_N; 1.
DR   Pfam; PF01202; SKI; 1.
DR   PIRSF; PIRSF000514; Pentafunct_AroM; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
DR   SUPFAM; SSF55205; SSF55205; 1.
DR   TIGRFAMs; TIGR01356; aroA; 1.
DR   TIGRFAMs; TIGR01357; aroB; 1.
DR   TIGRFAMs; TIGR01093; aroD; 1.
DR   TIGRFAMs; TIGR01809; Shik-DH-AROM; 1.
DR   PROSITE; PS01028; DEHYDROQUINASE_I; 1.
DR   PROSITE; PS00104; EPSP_SYNTHASE_1; 1.
DR   PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
DR   PROSITE; PS01128; SHIKIMATE_KINASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; ATP-binding;
KW   Cytoplasm; Kinase; Lyase; Metal-binding; Multifunctional enzyme; NADP;
KW   Nucleotide-binding; Oxidoreductase; Reference proteome; Transferase; Zinc.
FT   CHAIN           1..1578
FT                   /note="Pentafunctional AROM polypeptide"
FT                   /id="PRO_0000406726"
FT   REGION          1..384
FT                   /note="3-dehydroquinate synthase"
FT   REGION          397..842
FT                   /note="EPSP synthase"
FT   REGION          864..1055
FT                   /note="Shikimate kinase"
FT   REGION          1056..1276
FT                   /note="3-dehydroquinase"
FT   REGION          1289..1578
FT                   /note="Shikimate dehydrogenase"
FT   ACT_SITE        260
FT                   /note="Proton acceptor; for 3-dehydroquinate synthase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   ACT_SITE        275
FT                   /note="Proton acceptor; for 3-dehydroquinate synthase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   ACT_SITE        824
FT                   /note="For EPSP synthase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   ACT_SITE        1179
FT                   /note="Proton acceptor; for 3-dehydroquinate dehydratase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   ACT_SITE        1207
FT                   /note="Schiff-base intermediate with substrate; for 3-
FT                   dehydroquinate dehydratase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         44..46
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         81..84
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         114..116
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         119
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         130
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         139..140
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         146
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         152
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         161
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         162
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         179..182
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         190
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         194..197
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         250
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         264..268
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         271
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         271
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         287
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         287
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         356
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         871..878
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
SQ   SEQUENCE   1578 AA;  171374 MW;  E559B4F835C69978 CRC64;
     MTGPTKISIL GQESIVADFG LWRNYVAKDL ISGCPSTTYV LITDTNIGSI YTPGFQKSFE
     EAAASVSPSP RLLIYNAPPG EVSKSRQTKA DIEDWMLSQS PPCGRDTVVI ALGGGVIGDL
     TGFVAATYMR GVRFVQVPTT LLAMVDSSIG GKTAIDTPLG KNLIGAIWQP SRIYIDLEFL
     ETLPVREFIN GMAEVIKTAA ISSEEEFTAL EDNAETILSA VRREVKPGQR RFEGIEEILK
     ARILASARHK AFVVSADERE GGLRNLLNWG HSIGHAIEAI LTPQILHGEC VAIGMVKEAE
     LARHLGILKG VAVARIVKCI AAYGLPTSLK DSRIRKLTAG KHCSVDQILF NMALDKKNDG
     PKKKIVLLSA IGRTYEPRAS VVPNEDIGVV LAPSIEVYPG VSPASEVVCA PPGSKSISNR
     ALVLAALGSG TVRIKNLLHS DDTEVMLNAL ERLGAATFSW EEEGEVLVVN GKGGALQAHP
     SPLYLGNAGT ASRFLTTVAT LATASSVDSS VLTGNNRMKQ RPIGDLVDAL TANGAQIEYV
     ENKGSLPLKI AASGGFTGGQ INLAAKVSSQ YVSSLLMCAP YAKEPVTLKL VGGKPISQPY
     IDMTTAMMRS FGIDVKKSTT EEHTYHIPQG RYINPAEYVV ESDASSATYP LAIAAVTGTT
     CTIPNIGSKS LQGDARFAVD VLRPMGCTVE QTDTSTTVTG PADGVLRPLP NVDMEPMTDA
     FLGASVLAAI ARGKDSNHTT RIYGIANQRV KECNRIKAMH DELAKFGVVC REHDDGLEID
     GIDRSTLRQP AGGVFCYDDH RVAFSFSVLS LVAPKPTLIL EKECVGKTWP GWWDTLRQKF
     AVKLEGKELK EAESPVLTRA EKASASVFII GMRGAGKTTS GNWVASTLKR PFIDLDDELE
     RIEGMTIPDI IKQRGWQGFR DAELSLLQRT MKERPTGHVF ACGGGVVEIP EARKLLIDWH
     KTKGNVLLIM RDIKQVMAFL NIDKTRPAYV EDMLGVWLRR KPWFQECSNI QYYSQHASAG
     LPRASEDFAR FIKFVTGLED SLSTIKKKQH SFFVSLTLPD VRGADQILEQ ACVGSDAVEL
     RVDLLEDPDS ANGIPTVDFV ADQISYLRSR ITLPVIFTIR TKGQGGRFPD DAHAEAMQLY
     RLAVRSGCEF VDLEIAFPDE MLRAVTEMKG YSKIITSHHD PKGELSWANM SWMKYYNRAL
     EYGDVIKLVG VARNLDDNTA LRKFKNWAEE AHDVPLIAIN MGGNGQLSRI LNGFMTPVSH
     PALPFRAAPG QLSATDIRKG LSLMGEIKKK RFALFGSPIS ESRSPALHNT LFAEMGLPHE
     YTRLETANVE DVKDFIRAPD FGGASVTIPL KLDIMPLLDE ITAEAEIIGA VNTVVPVSDG
     EGKPQRLVGH NTDWQGMVQC LRNAGAYGAD GNASGLVVGG GGTSRAAIYA LHHMGFSPIY
     IVGRNPAKLE SMVATFPTGY NIRIVEGNEK LEHVPHVAIG TIPADRPIDP GMREILCHMF
     ERAQEADADA ARTIEGSPRV LLEMAYKPRV TALMQLAVDA GWTTVPGLEA LIGQGVHQFQ
     HWTGIRPLYE RARAIVLG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024