位置:首页 > 蛋白库 > SAHH_RAT
SAHH_RAT
ID   SAHH_RAT                Reviewed;         432 AA.
AC   P10760;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 197.
DE   RecName: Full=Adenosylhomocysteinase;
DE            Short=AdoHcyase {ECO:0000303|PubMed:11741948, ECO:0000303|PubMed:11927587};
DE            EC=3.3.1.1 {ECO:0000269|PubMed:11927587};
DE   AltName: Full=S-adenosyl-L-homocysteine hydrolase {ECO:0000303|PubMed:11741948};
GN   Name=Ahcy;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=3027698; DOI=10.1073/pnas.84.3.719;
RA   Ogawa H., Gomi T., Mueckler M.M., Fujioka M., Backlund P.S. Jr.,
RA   Aksamit R.R., Unson C.G., Cantoni G.L.;
RT   "Amino acid sequence of S-adenosyl-L-homocysteine hydrolase from rat liver
RT   as derived from the cDNA sequence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:719-723(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Fischer 344;
RX   PubMed=7744082; DOI=10.1111/j.1432-1033.1995.tb20500.x;
RA   Merta A., Aksamit R.R., Kasir J., Cantoni G.L.;
RT   "The gene and pseudogenes of rat S-adenosyl-L-homocysteine hydrolase.";
RL   Eur. J. Biochem. 229:575-582(1995).
RN   [3]
RP   PROTEIN SEQUENCE OF 76-94.
RX   PubMed=3759971; DOI=10.1016/s0021-9258(18)67034-6;
RA   Gomi T., Ogawa H., Fujioka M.;
RT   "S-adenosylhomocysteinase from rat liver. Amino acid sequences of the
RT   peptides containing active site cysteine residues modified by treatment
RT   with 5'-p-fluorosulfonylbenzoyladenosine.";
RL   J. Biol. Chem. 261:13422-13425(1986).
RN   [4]
RP   PROTEIN SEQUENCE OF 143-151 AND 268-285, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA   Lubec G., Afjehi-Sadat L., Diao W.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NAD, COFACTOR, AND
RP   SUBUNIT.
RC   TISSUE=Liver;
RX   PubMed=10387078; DOI=10.1021/bi990332k;
RA   Hu Y., Komoto J., Huang Y., Gomi T., Ogawa H., Takata Y., Fujioka M.,
RA   Takusagawa F.;
RT   "Crystal structure of S-adenosylhomocysteine hydrolase from rat liver.";
RL   Biochemistry 38:8323-8333(1999).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT GLU-245.
RX   PubMed=10913437; DOI=10.1074/jbc.m003725200;
RA   Komoto J., Huang Y., Gomi T., Ogawa H., Takata Y., Fujioka M.,
RA   Takusagawa F.;
RT   "Effects of site-directed mutagenesis on structure and function of
RT   recombinant rat liver S-adenosylhomocysteine hydrolase. Crystal structure
RT   of D244E mutant enzyme.";
RL   J. Biol. Chem. 275:32147-32156(2000).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH INHIBITOR, AND
RP   SUBUNIT.
RX   PubMed=11741948; DOI=10.1074/jbc.m109187200;
RA   Huang Y., Komoto J., Takata Y., Powell D.R., Gomi T., Ogawa H., Fujioka M.,
RA   Takusagawa F.;
RT   "Inhibition of S-adenosylhomocysteine hydrolase by acyclic sugar adenosine
RT   analogue D-eritadenine. Crystal structure of S-adenosylhomocysteine
RT   hydrolase complexed with D-eritadenine.";
RL   J. Biol. Chem. 277:7477-7482(2002).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), MUTAGENESIS OF ASP-131; LYS-186;
RP   ASP-190 AND ASN-191, FUNCTION, COFACTOR, PATHWAY, AND CATALYTIC ACTIVITY.
RX   PubMed=11927587; DOI=10.1074/jbc.m201116200;
RA   Takata Y., Yamada T., Huang Y., Komoto J., Gomi T., Ogawa H., Fujioka M.,
RA   Takusagawa F.;
RT   "Catalytic mechanism of S-adenosylhomocysteine hydrolase. Site-directed
RT   mutagenesis of Asp-130, Lys-185, Asp-189, and Asn-190.";
RL   J. Biol. Chem. 277:22670-22676(2002).
CC   -!- FUNCTION: Catalyzes the hydrolysis of S-adenosyl-L-homocysteine to form
CC       adenosine and homocysteine (PubMed:11927587). Binds copper ions (By
CC       similarity). {ECO:0000250|UniProtKB:P50247,
CC       ECO:0000269|PubMed:11927587}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine;
CC         Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.3.1.1;
CC         Evidence={ECO:0000269|PubMed:11927587};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21709;
CC         Evidence={ECO:0000269|PubMed:11927587};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000269|PubMed:10387078, ECO:0000269|PubMed:10913437,
CC         ECO:0000269|PubMed:11741948, ECO:0000269|PubMed:11927587,
CC         ECO:0007744|PDB:1B3R, ECO:0007744|PDB:1D4F, ECO:0007744|PDB:1K0U,
CC         ECO:0007744|PDB:1KY4, ECO:0007744|PDB:1KY5, ECO:0007744|PDB:1XWF,
CC         ECO:0007744|PDB:2H5L};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000269|PubMed:10387078,
CC       ECO:0000269|PubMed:10913437, ECO:0000269|PubMed:11741948,
CC       ECO:0000269|PubMed:11927587, ECO:0007744|PDB:1B3R,
CC       ECO:0007744|PDB:1D4F, ECO:0007744|PDB:1K0U, ECO:0007744|PDB:1KY4,
CC       ECO:0007744|PDB:1KY5, ECO:0007744|PDB:1XWF, ECO:0007744|PDB:2H5L};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC       homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC       {ECO:0000305|PubMed:11927587}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10387078,
CC       ECO:0000269|PubMed:11741948}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P23526}.
CC       Melanosome {ECO:0000250|UniProtKB:P23526}.
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC       {ECO:0000305}.
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; M15185; AAA40705.1; -; mRNA.
DR   EMBL; U14937; AAA92043.1; -; Genomic_DNA.
DR   PIR; A26583; A26583.
DR   RefSeq; NP_058897.1; NM_017201.1.
DR   PDB; 1B3R; X-ray; 2.80 A; A/B/C/D=2-432.
DR   PDB; 1D4F; X-ray; 2.80 A; A/B/C/D=2-432.
DR   PDB; 1K0U; X-ray; 3.00 A; A/B/C/D/E/F/G/H=2-432.
DR   PDB; 1KY4; X-ray; 2.80 A; A/B/C/D=2-432.
DR   PDB; 1KY5; X-ray; 2.80 A; A/B/C/D=2-432.
DR   PDB; 1XWF; X-ray; 2.80 A; A/B/C/D=2-432.
DR   PDB; 2H5L; X-ray; 2.80 A; A/B/C/D/E/F/G/H=2-432.
DR   PDBsum; 1B3R; -.
DR   PDBsum; 1D4F; -.
DR   PDBsum; 1K0U; -.
DR   PDBsum; 1KY4; -.
DR   PDBsum; 1KY5; -.
DR   PDBsum; 1XWF; -.
DR   PDBsum; 2H5L; -.
DR   AlphaFoldDB; P10760; -.
DR   SMR; P10760; -.
DR   BioGRID; 248089; 1.
DR   IntAct; P10760; 1.
DR   STRING; 10116.ENSRNOP00000024310; -.
DR   BindingDB; P10760; -.
DR   ChEMBL; CHEMBL3118; -.
DR   iPTMnet; P10760; -.
DR   PhosphoSitePlus; P10760; -.
DR   World-2DPAGE; 0004:P10760; -.
DR   jPOST; P10760; -.
DR   PaxDb; P10760; -.
DR   PRIDE; P10760; -.
DR   Ensembl; ENSRNOT00000024310; ENSRNOP00000024310; ENSRNOG00000017777.
DR   GeneID; 29443; -.
DR   KEGG; rno:29443; -.
DR   UCSC; RGD:69260; rat.
DR   CTD; 191; -.
DR   RGD; 69260; Ahcy.
DR   eggNOG; KOG1370; Eukaryota.
DR   GeneTree; ENSGT00950000182981; -.
DR   HOGENOM; CLU_025194_2_1_1; -.
DR   InParanoid; P10760; -.
DR   OMA; NKYGCRE; -.
DR   OrthoDB; 371693at2759; -.
DR   PhylomeDB; P10760; -.
DR   TreeFam; TF300415; -.
DR   BioCyc; MetaCyc:MON-8582; -.
DR   BRENDA; 3.3.1.1; 5301.
DR   Reactome; R-RNO-156581; Methylation.
DR   Reactome; R-RNO-1614635; Sulfur amino acid metabolism.
DR   SABIO-RK; P10760; -.
DR   UniPathway; UPA00314; UER00076.
DR   EvolutionaryTrace; P10760; -.
DR   PRO; PR:P10760; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000017777; Expressed in liver and 19 other tissues.
DR   Genevisible; P10760; RN.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0043005; C:neuron projection; IDA:RGD.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; IDA:UniProtKB.
DR   GO; GO:0098604; F:adenosylselenohomocysteinase activity; TAS:Reactome.
DR   GO; GO:0030554; F:adenyl nucleotide binding; IDA:RGD.
DR   GO; GO:0005507; F:copper ion binding; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; IDA:RGD.
DR   GO; GO:0051287; F:NAD binding; IDA:RGD.
DR   GO; GO:0043621; F:protein self-association; ISO:RGD.
DR   GO; GO:0002439; P:chronic inflammatory response to antigenic stimulus; IMP:RGD.
DR   GO; GO:0042745; P:circadian sleep/wake cycle; IDA:RGD.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0007584; P:response to nutrient; IDA:RGD.
DR   GO; GO:0019510; P:S-adenosylhomocysteine catabolic process; IDA:RGD.
DR   GO; GO:0033353; P:S-adenosylmethionine cycle; IBA:GO_Central.
DR   CDD; cd00401; SAHH; 1.
DR   Gene3D; 3.40.50.1480; -; 2.
DR   HAMAP; MF_00563; AdoHcyase; 1.
DR   InterPro; IPR042172; Adenosylhomocyst_ase-like_sf.
DR   InterPro; IPR000043; Adenosylhomocysteinase-like.
DR   InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS.
DR   PANTHER; PTHR23420; PTHR23420; 1.
DR   Pfam; PF05221; AdoHcyase; 1.
DR   Pfam; PF00670; AdoHcyase_NAD; 1.
DR   PIRSF; PIRSF001109; Ad_hcy_hydrolase; 1.
DR   SMART; SM00996; AdoHcyase; 1.
DR   SMART; SM00997; AdoHcyase_NAD; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00936; ahcY; 1.
DR   PROSITE; PS00738; ADOHCYASE_1; 1.
DR   PROSITE; PS00739; ADOHCYASE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Copper; Cytoplasm; Direct protein sequencing; Hydrolase;
KW   Hydroxylation; NAD; One-carbon metabolism; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..432
FT                   /note="Adenosylhomocysteinase"
FT                   /id="PRO_0000116905"
FT   BINDING         57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:11741948"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:11927587"
FT   BINDING         156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:11741948"
FT   BINDING         157..159
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:10913437,
FT                   ECO:0000269|PubMed:11741948, ECO:0000269|PubMed:11927587,
FT                   ECO:0007744|PDB:1D4F, ECO:0007744|PDB:1K0U,
FT                   ECO:0007744|PDB:1KY5, ECO:0007744|PDB:2H5L"
FT   BINDING         186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:11741948,
FT                   ECO:0000269|PubMed:11927587"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:11741948,
FT                   ECO:0000269|PubMed:11927587"
FT   BINDING         222..227
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:10387078"
FT   BINDING         243
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:10387078"
FT   BINDING         248
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:10913437,
FT                   ECO:0000269|PubMed:11741948, ECO:0000269|PubMed:11927587,
FT                   ECO:0007744|PDB:1D4F, ECO:0007744|PDB:1K0U,
FT                   ECO:0007744|PDB:1KY4, ECO:0007744|PDB:1XWF,
FT                   ECO:0007744|PDB:2H5L"
FT   BINDING         299..301
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:10387078,
FT                   ECO:0000269|PubMed:10913437, ECO:0000269|PubMed:11741948,
FT                   ECO:0000269|PubMed:11927587, ECO:0007744|PDB:1B3R,
FT                   ECO:0007744|PDB:1D4F, ECO:0007744|PDB:1K0U,
FT                   ECO:0007744|PDB:1KY4, ECO:0007744|PDB:1KY5,
FT                   ECO:0007744|PDB:1XWF, ECO:0007744|PDB:2H5L"
FT   BINDING         346
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:10387078,
FT                   ECO:0000269|PubMed:10913437, ECO:0000269|PubMed:11741948,
FT                   ECO:0000269|PubMed:11927587, ECO:0007744|PDB:1B3R,
FT                   ECO:0007744|PDB:1D4F, ECO:0007744|PDB:1K0U,
FT                   ECO:0007744|PDB:1KY4, ECO:0007744|PDB:1KY5,
FT                   ECO:0007744|PDB:1XWF, ECO:0007744|PDB:2H5L"
FT   BINDING         353
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:10387078,
FT                   ECO:0000269|PubMed:10913437, ECO:0000269|PubMed:11741948,
FT                   ECO:0007744|PDB:1B3R, ECO:0007744|PDB:1D4F,
FT                   ECO:0007744|PDB:1K0U, ECO:0007744|PDB:1XWF,
FT                   ECO:0007744|PDB:2H5L"
FT   BINDING         426..430
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:10387078"
FT   BINDING         426
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:10387078,
FT                   ECO:0000269|PubMed:11741948, ECO:0000269|PubMed:11927587,
FT                   ECO:0007744|PDB:1B3R, ECO:0007744|PDB:1K0U,
FT                   ECO:0007744|PDB:1KY4, ECO:0007744|PDB:1KY5,
FT                   ECO:0007744|PDB:1XWF, ECO:0007744|PDB:2H5L"
FT   BINDING         430
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:10387078,
FT                   ECO:0000269|PubMed:10913437, ECO:0000269|PubMed:11741948,
FT                   ECO:0000269|PubMed:11927587, ECO:0007744|PDB:1B3R,
FT                   ECO:0007744|PDB:1D4F, ECO:0007744|PDB:1K0U,
FT                   ECO:0007744|PDB:1KY4, ECO:0007744|PDB:1KY5,
FT                   ECO:0007744|PDB:1XWF, ECO:0007744|PDB:2H5L"
FT   MOD_RES         183
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P23526"
FT   MOD_RES         186
FT                   /note="N6-(2-hydroxyisobutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P23526"
FT   MOD_RES         193
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P50247"
FT   MUTAGEN         131
FT                   /note="D->N: Strongly reduces S-adenosyl-L-homocysteine
FT                   hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:11927587"
FT   MUTAGEN         186
FT                   /note="K->N: Strongly reduces S-adenosyl-L-homocysteine
FT                   hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:11927587"
FT   MUTAGEN         190
FT                   /note="D->N: Strongly reduces S-adenosyl-L-homocysteine
FT                   hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:11927587"
FT   MUTAGEN         191
FT                   /note="N->S: Strongly reduces S-adenosyl-L-homocysteine
FT                   hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:11927587"
FT   MUTAGEN         245
FT                   /note="D->E: Changes active site geometry and alters
FT                   affinity for NAD."
FT   STRAND          8..10
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   TURN            12..14
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   HELIX           15..25
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   HELIX           26..28
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   HELIX           30..39
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   TURN            40..42
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   TURN            44..47
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   STRAND          49..54
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   HELIX           58..69
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   STRAND          73..77
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   TURN            81..83
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   HELIX           86..94
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   STRAND          99..101
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   HELIX           107..116
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   STRAND          118..120
FT                   /evidence="ECO:0007829|PDB:1D4F"
FT   STRAND          127..133
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   HELIX           134..142
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   HELIX           144..147
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   STRAND          152..155
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   HELIX           158..169
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   STRAND          177..179
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   HELIX           180..182
FT                   /evidence="ECO:0007829|PDB:1XWF"
FT   HELIX           184..190
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   HELIX           192..207
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   STRAND          215..219
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   HELIX           223..234
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   STRAND          238..242
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   HELIX           246..253
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   TURN            254..256
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   STRAND          258..260
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   HELIX           262..265
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   TURN            266..268
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   STRAND          270..274
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   STRAND          277..279
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   HELIX           284..287
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   STRAND          294..298
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   TURN            302..304
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   HELIX           308..314
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   STRAND          315..322
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   STRAND          325..330
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   STRAND          335..339
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   HELIX           340..342
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   HELIX           345..349
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   HELIX           355..374
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   TURN            376..378
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   STRAND          381..385
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   HELIX           388..398
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   TURN            399..402
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   HELIX           411..417
FT                   /evidence="ECO:0007829|PDB:1B3R"
FT   STRAND          421..423
FT                   /evidence="ECO:0007829|PDB:1B3R"
SQ   SEQUENCE   432 AA;  47538 MW;  93CA5BED07B4FCDE CRC64;
     MADKLPYKVA DIGLAAWGRK ALDIAENEMP GLMRMREMYS ASKPLKGARI AGCLHMTVET
     AVLIETLVAL GAEVRWSSCN IFSTQDHAAA AIAKAGIPVF AWKGETDEEY LWCIEQTLHF
     KDGPLNMILD DGGDLTNLIH TKHPQLLSGI RGISEETTTG VHNLYKMMAN GILKVPAINV
     NDSVTKSKFD NLYGCRESLI DGIKRATDVM IAGKVAVVAG YGDVGKGCAQ ALRGFGARVI
     ITEIDPINAL QAAMEGYEVT TMDEACKEGN IFVTTTGCVD IILGRHFEQM KDDAIVCNIG
     HFDVEIDVKW LNENAVEKVN IKPQVDRYLL KNGHRIILLA EGRLVNLGCA MGHPSFVMSN
     SFTNQVMAQI ELWTHPDKYP VGVHFLPKKL DEAVAEAHLG KLNVKLTKLT EKQAQYLGMP
     INGPFKPDHY RY
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024