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HMT1_YEAST
ID   HMT1_YEAST              Reviewed;         348 AA.
AC   P38074; D6VQ34;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 187.
DE   RecName: Full=Protein arginine N-methyltransferase 1 {ECO:0000303|PubMed:8647869};
DE            EC=2.1.1.- {ECO:0000269|PubMed:8647869, ECO:0000269|PubMed:8668183};
DE   AltName: Full=Major type I protein arginine N-methyltransferase {ECO:0000305|PubMed:8647869};
DE            Short=Type I PRMT {ECO:0000303|PubMed:22997150};
DE   AltName: Full=hnRNP arginine N-methyltransferase {ECO:0000303|PubMed:8668183};
GN   Name=HMT1 {ECO:0000303|PubMed:8668183};
GN   Synonyms=ODP1 {ECO:0000303|PubMed:7896706},
GN   RMT1 {ECO:0000303|PubMed:8647869};
GN   OrderedLocusNames=YBR034C {ECO:0000312|SGD:S000000238}; ORFNames=YBR0320;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091864; DOI=10.1002/yea.320100010;
RA   Smits P.H.M., de Haan M., Maat C., Grivell L.A.;
RT   "The complete sequence of a 33 kb fragment on the right arm of chromosome
RT   II from Saccharomyces cerevisiae reveals 16 open reading frames, including
RT   ten new open reading frames, five previously identified genes and a
RT   homologue of the SCO1 gene.";
RL   Yeast 10:S75-S80(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55.
RX   PubMed=7896706; DOI=10.1128/jb.177.7.1817-1823.1995;
RA   Loubbardi A., Karst F., Guilloton M., Marcireau C.;
RT   "Sterol uptake induced by an impairment of pyridoxal phosphate synthesis in
RT   Saccharomyces cerevisiae: cloning and sequencing of the PDX3 gene encoding
RT   pyridoxine (pyridoxamine) phosphate oxidase.";
RL   J. Bacteriol. 177:1817-1823(1995).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX   PubMed=8668183; DOI=10.1128/mcb.16.7.3668;
RA   Henry M.F., Silver P.A.;
RT   "A novel methyltransferase (Hmt1p) modifies poly(A)+-RNA-binding
RT   proteins.";
RL   Mol. Cell. Biol. 16:3668-3678(1996).
RN   [7]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=8647869; DOI=10.1074/jbc.271.21.12585;
RA   Gary J.D., Lin W.-J., Yang M.C., Herschmann H.R., Clarke S.;
RT   "The predominant protein-arginine methyltransferase from Saccharomyces
RT   cerevisiae.";
RL   J. Biol. Chem. 271:12585-12594(1996).
RN   [8]
RP   FUNCTION.
RX   PubMed=9499403; DOI=10.1101/gad.12.5.679;
RA   Shen E.C., Henry M.F., Weiss V.H., Valentini S.R., Silver P.A., Lee M.S.;
RT   "Arginine methylation facilitates the nuclear export of hnRNP proteins.";
RL   Genes Dev. 12:679-691(1998).
RN   [9]
RP   FUNCTION, AND MUTAGENESIS OF GLU-18 AND GLY-68.
RX   PubMed=10652296; DOI=10.1074/jbc.275.5.3128;
RA   McBride A.E., Weiss V.H., Kim H.K., Hogle J.M., Silver P.A.;
RT   "Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in
RT   vivo function. Cofactor binding and substrate interactions.";
RL   J. Biol. Chem. 275:3128-3136(2000).
RN   [10]
RP   FUNCTION.
RX   PubMed=11779864; DOI=10.1074/jbc.m110053200;
RA   Green D.M., Marfatia K.A., Crafton E.B., Zhang X., Cheng X., Corbett A.H.;
RT   "Nab2p is required for poly(A) RNA export in Saccharomyces cerevisiae and
RT   is regulated by arginine methylation via Hmt1p.";
RL   J. Biol. Chem. 277:7752-7760(2002).
RN   [11]
RP   FUNCTION.
RX   PubMed=12097318; DOI=10.1074/jbc.c200366200;
RA   Lacoste N., Utley R.T., Hunter J.M., Poirier G.G., Cote J.;
RT   "Disruptor of telomeric silencing-1 is a chromatin-specific histone H3
RT   methyltransferase.";
RL   J. Biol. Chem. 277:30421-30424(2002).
RN   [12]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [13]
RP   FUNCTION.
RX   PubMed=12756332; DOI=10.1261/rna.5020803;
RA   Xu C., Henry P.A., Setya A., Henry M.F.;
RT   "In vivo analysis of nucleolar proteins modified by the yeast arginine
RT   methyltransferase Hmt1/Rmt1p.";
RL   RNA 9:746-759(2003).
RN   [14]
RP   FUNCTION.
RX   PubMed=15314027; DOI=10.1101/gad.1223204;
RA   Yu M.C., Bachand F., McBride A.E., Komili S., Casolari J.M., Silver P.A.;
RT   "Arginine methyltransferase affects interactions and recruitment of mRNA
RT   processing and export factors.";
RL   Genes Dev. 18:2024-2035(2004).
RN   [15]
RP   FUNCTION.
RX   PubMed=17158743; DOI=10.1101/gad.1495206;
RA   Yu M.C., Lamming D.W., Eskin J.A., Sinclair D.A., Silver P.A.;
RT   "The role of protein arginine methylation in the formation of silent
RT   chromatin.";
RL   Genes Dev. 20:3249-3254(2006).
RN   [16]
RP   FUNCTION.
RX   PubMed=20035717; DOI=10.1016/j.bbrc.2009.12.112;
RA   Lipson R.S., Webb K.J., Clarke S.G.;
RT   "Rmt1 catalyzes zinc-finger independent arginine methylation of ribosomal
RT   protein Rps2 in Saccharomyces cerevisiae.";
RL   Biochem. Biophys. Res. Commun. 391:1658-1662(2010).
RN   [17]
RP   FUNCTION.
RX   PubMed=20823272; DOI=10.1128/mcb.00359-10;
RA   Chen Y.C., Milliman E.J., Goulet I., Cote J., Jackson C.A.,
RA   Vollbracht J.A., Yu M.C.;
RT   "Protein arginine methylation facilitates cotranscriptional recruitment of
RT   pre-mRNA splicing factors.";
RL   Mol. Cell. Biol. 30:5245-5256(2010).
RN   [18]
RP   FUNCTION.
RX   PubMed=20053728; DOI=10.1093/nar/gkp1133;
RA   Wong C.M., Tang H.M., Kong K.Y., Wong G.W., Qiu H., Jin D.Y.,
RA   Hinnebusch A.G.;
RT   "Yeast arginine methyltransferase Hmt1p regulates transcription elongation
RT   and termination by methylating Npl3p.";
RL   Nucleic Acids Res. 38:2217-2228(2010).
RN   [19]
RP   FUNCTION, AND INTERACTION WITH BRE5; MTR4; SNF2; SUM1 AND SSD1.
RX   PubMed=22997150; DOI=10.1002/pmic.201200132;
RA   Jackson C.A., Yadav N., Min S., Li J., Milliman E.J., Qu J., Chen Y.C.,
RA   Yu M.C.;
RT   "Proteomic analysis of interactors for yeast protein arginine
RT   methyltransferase Hmt1 reveals novel substrate and insights into additional
RT   biological roles.";
RL   Proteomics 12:3304-3314(2012).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 24-348, FUNCTION, INTERACTION WITH
RP   NPL3, AND SUBUNIT.
RX   PubMed=11101900; DOI=10.1038/82028;
RA   Weiss V.H., McBride A.E., Soriano M.A., Filman D.J., Silver P.A.,
RA   Hogle J.M.;
RT   "The structure and oligomerization of the yeast arginine methyltransferase,
RT   Hmt1.";
RL   Nat. Struct. Biol. 7:1165-1171(2000).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-arginine N-
CC       methyltransferase that catalyzes both the mono- and asymmetric (type I)
CC       dimethylation of the guanidino nitrogens of arginine residues in a
CC       variety of RNA-binding proteins such as heterogeneous nuclear
CC       ribonucleoproteins (hnRNPs) and small nuclear ribonucleoproteins
CC       (snRNPs) (PubMed:8668183, PubMed:8647869). Methylates NAB2, NPL3, HRP1
CC       and YRA1, shuttling hnRNPs involved in mRNA processing and export,
CC       facilitating their export out of the nucleus (PubMed:8668183,
CC       PubMed:9499403, PubMed:10652296, PubMed:11779864, PubMed:15314027).
CC       Methylation of NPL3 weakens its interaction with THO2, a component of
CC       the TREX (transcription/export) complex important for transcriptional
CC       elongation and recruitment of mRNA export factors (PubMed:15314027,
CC       PubMed:20053728). Methylates the hnRNP HRB1, but does not influence its
CC       subcellular location (PubMed:9499403). Methylates the nucleolar
CC       proteins GAR1, NOP1 and NSR1 (PubMed:12756332). Methylates the snRNP
CC       SNP1 and modulates the cotranscriptional recruitment of splicing
CC       factors (PubMed:20823272). Dimethylates free histone H4 (HHF1/HHF2) at
CC       'Arg-4' (H4R3me2a) and plays a role in preservation and establishment
CC       of silent chromatin domains (PubMed:12097318, PubMed:17158743).
CC       Mono- and dimethylates ribosomal protein S2 (RPS2) at 'Arg-11'
CC       (PubMed:20035717). Methylates the catalytic subunit of the SWI/SNF
CC       chromatin-remodeling complex SNF2 (PubMed:22997150).
CC       {ECO:0000269|PubMed:10652296, ECO:0000269|PubMed:11101900,
CC       ECO:0000269|PubMed:11779864, ECO:0000269|PubMed:12097318,
CC       ECO:0000269|PubMed:12756332, ECO:0000269|PubMed:15314027,
CC       ECO:0000269|PubMed:17158743, ECO:0000269|PubMed:20035717,
CC       ECO:0000269|PubMed:20053728, ECO:0000269|PubMed:20823272,
CC       ECO:0000269|PubMed:22997150, ECO:0000269|PubMed:8647869,
CC       ECO:0000269|PubMed:8668183, ECO:0000269|PubMed:9499403}.
CC   -!- SUBUNIT: Homodimer. The dimers can then associate to form a ring-shaped
CC       homohexamer. Interacts with NPL3, BRE5, MTR4, SNF2, SUM1, AND SSD1.
CC       {ECO:0000269|PubMed:11101900, ECO:0000269|PubMed:22997150}.
CC   -!- INTERACTION:
CC       P38074; P53741: BRE5; NbExp=2; IntAct=EBI-8394, EBI-28528;
CC       P38074; P22204: DBF2; NbExp=4; IntAct=EBI-8394, EBI-5569;
CC       P38074; P38074: HMT1; NbExp=3; IntAct=EBI-8394, EBI-8394;
CC       P38074; P47047: MTR4; NbExp=2; IntAct=EBI-8394, EBI-11592;
CC       P38074; P32505: NAB2; NbExp=2; IntAct=EBI-8394, EBI-11770;
CC       P38074; Q01560: NPL3; NbExp=9; IntAct=EBI-8394, EBI-12114;
CC       P38074; P23595: PPH22; NbExp=3; IntAct=EBI-8394, EBI-12752;
CC       P38074; P22082: SNF2; NbExp=3; IntAct=EBI-8394, EBI-17526;
CC       P38074; P24276: SSD1; NbExp=2; IntAct=EBI-8394, EBI-18153;
CC       P38074; P46676: SUM1; NbExp=2; IntAct=EBI-8394, EBI-18547;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8668183}.
CC   -!- MISCELLANEOUS: Present with 37600 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Protein arginine N-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01015}.
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DR   EMBL; X76078; CAA53689.1; -; Genomic_DNA.
DR   EMBL; Z35903; CAA84976.1; -; Genomic_DNA.
DR   EMBL; X76992; CAA54296.1; -; Genomic_DNA.
DR   EMBL; AY557869; AAS56195.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07154.1; -; Genomic_DNA.
DR   PIR; S45890; S45890.
DR   RefSeq; NP_009590.1; NM_001178382.1.
DR   PDB; 1G6Q; X-ray; 2.90 A; 1/2/3/4/5/6=21-348.
DR   PDBsum; 1G6Q; -.
DR   AlphaFoldDB; P38074; -.
DR   SMR; P38074; -.
DR   BioGRID; 32735; 445.
DR   DIP; DIP-2608N; -.
DR   IntAct; P38074; 264.
DR   MINT; P38074; -.
DR   STRING; 4932.YBR034C; -.
DR   iPTMnet; P38074; -.
DR   MaxQB; P38074; -.
DR   PaxDb; P38074; -.
DR   PRIDE; P38074; -.
DR   EnsemblFungi; YBR034C_mRNA; YBR034C; YBR034C.
DR   GeneID; 852322; -.
DR   KEGG; sce:YBR034C; -.
DR   SGD; S000000238; HMT1.
DR   VEuPathDB; FungiDB:YBR034C; -.
DR   eggNOG; KOG1499; Eukaryota.
DR   GeneTree; ENSGT00940000175369; -.
DR   HOGENOM; CLU_017375_1_1_1; -.
DR   InParanoid; P38074; -.
DR   OMA; RNDFVHA; -.
DR   BioCyc; YEAST:G3O-29011-MON; -.
DR   Reactome; R-SCE-3214858; RMTs methylate histone arginines.
DR   Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
DR   EvolutionaryTrace; P38074; -.
DR   PRO; PR:P38074; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38074; protein.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IDA:SGD.
DR   GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IDA:SGD.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IMP:SGD.
DR   GO; GO:0006406; P:mRNA export from nucleus; IMP:SGD.
DR   GO; GO:0060567; P:negative regulation of DNA-templated transcription, termination; IMP:SGD.
DR   GO; GO:0018216; P:peptidyl-arginine methylation; IDA:SGD.
DR   GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR025799; Arg_MeTrfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR11006; PTHR11006; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51678; SAM_MT_PRMT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Methyltransferase; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..348
FT                   /note="Protein arginine N-methyltransferase 1"
FT                   /id="PRO_0000212341"
FT   DOMAIN          20..322
FT                   /note="SAM-dependent MTase PRMT-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT   ACT_SITE        132
FT                   /evidence="ECO:0000250|UniProtKB:Q63009"
FT   ACT_SITE        141
FT                   /evidence="ECO:0000250|UniProtKB:Q63009"
FT   BINDING         33
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q63009"
FT   BINDING         42
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q63009"
FT   BINDING         66
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q63009"
FT   BINDING         88
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q63009"
FT   BINDING         117
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q63009"
FT   MUTAGEN         18
FT                   /note="E->V: Cold-sensitive; reduces catalytic activity
FT                   more than 20-fold at 14 degrees Celsius."
FT                   /evidence="ECO:0000269|PubMed:10652296"
FT   MUTAGEN         68
FT                   /note="G->A: Reduces catalytic activity between 5- to 25-
FT                   fold."
FT                   /evidence="ECO:0000269|PubMed:10652296"
FT   MUTAGEN         68
FT                   /note="G->R: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:10652296"
FT   HELIX           30..37
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   HELIX           40..57
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   STRAND          61..65
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   HELIX           71..78
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   STRAND          82..90
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   HELIX           92..102
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   TURN            106..108
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   STRAND          109..114
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   TURN            116..118
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   STRAND          122..124
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   STRAND          126..131
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   HELIX           144..154
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   STRAND          155..163
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   STRAND          165..173
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   HELIX           176..185
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   HELIX           197..201
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   STRAND          206..208
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   HELIX           212..214
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   STRAND          220..226
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   TURN            227..229
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   HELIX           232..235
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   STRAND          236..245
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   STRAND          250..261
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   STRAND          272..274
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   STRAND          286..296
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   STRAND          302..312
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   STRAND          315..328
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   HELIX           334..337
FT                   /evidence="ECO:0007829|PDB:1G6Q"
FT   STRAND          339..347
FT                   /evidence="ECO:0007829|PDB:1G6Q"
SQ   SEQUENCE   348 AA;  39786 MW;  383AF61033FB4AC2 CRC64;
     MSKTAVKDSA TEKTKLSESE QHYFNSYDHY GIHEEMLQDT VRTLSYRNAI IQNKDLFKDK
     IVLDVGCGTG ILSMFAAKHG AKHVIGVDMS SIIEMAKELV ELNGFSDKIT LLRGKLEDVH
     LPFPKVDIII SEWMGYFLLY ESMMDTVLYA RDHYLVEGGL IFPDKCSIHL AGLEDSQYKD
     EKLNYWQDVY GFDYSPFVPL VLHEPIVDTV ERNNVNTTSD KLIEFDLNTV KISDLAFKSN
     FKLTAKRQDM INGIVTWFDI VFPAPKGKRP VEFSTGPHAP YTHWKQTIFY FPDDLDAETG
     DTIEGELVCS PNEKNNRDLN IKISYKFESN GIDGNSRSRK NEGSYLMH
 
 
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