(data stored in ACNUC7421 zone)

SWISSPROT: AUHM_HUMAN

ID   AUHM_HUMAN              Reviewed;         339 AA.
AC   Q13825; B1ALV7; B1ALV8; Q8WUE4;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   30-AUG-2017, entry version 165.
DE   RecName: Full=Methylglutaconyl-CoA hydratase, mitochondrial;
DE            EC=4.2.1.18;
DE   AltName: Full=AU-specific RNA-binding enoyl-CoA hydratase;
DE            Short=AU-binding protein/enoyl-CoA hydratase;
DE   Flags: Precursor;
GN   Name=AUH;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 68-87;
RP   213-215; 235-241; 251-268 AND 278-286, FUNCTION, AND RNA-BINDING.
RC   TISSUE=Neuroblastoma;
RX   PubMed=7892223; DOI=10.1073/pnas.92.6.2051;
RA   Nakagawa J., Waldner H.P., Meyer-Monard S., Hofsteenge J., Jenoe P.,
RA   Moroni C.;
RT   "AUH, a gene encoding an AU-specific RNA binding protein with
RT   intrinsic enoyl-CoA hydratase activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:2051-2055(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA   Rogers J., Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   DISEASE, AND FUNCTION.
RX   PubMed=12434311; DOI=10.1086/344712;
RA   Ijlst L., Loupatty F.J., Ruiter J.P.N., Duran M., Lehnert W.,
RA   Wanders R.J.A.;
RT   "3-methylglutaconic aciduria type I is caused by mutations in AUH.";
RL   Am. J. Hum. Genet. 71:1463-1466(2002).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 75-339, HEXAMERIZATION,
RP   FUNCTION, AND MUTAGENESIS OF LYS-105; LYS-109 AND LYS-113.
RX   PubMed=11738050; DOI=10.1016/S0969-2126(01)00686-4;
RA   Kurimoto K., Fukai S., Nureki O., Muto Y., Yokoyama S.;
RT   "Crystal structure of human AUH protein, a single-stranded RNA binding
RT   homolog of enoyl-CoA hydratase.";
RL   Structure 9:1253-1263(2001).
RN   [10]
RP   VARIANT MGA1 VAL-240, AND FUNCTION.
RX   PubMed=12655555; DOI=10.1002/humu.10202;
RA   Ly T.B.N., Peters V., Gibson K.M., Liesert M., Buckel W., Wilcken B.,
RA   Carpenter K., Ensenauer R., Hoffmann G.F., Mack M., Zschocke J.;
RT   "Mutations in the AUH gene cause 3-methylglutaconic aciduria type I.";
RL   Hum. Mutat. 21:401-407(2003).
CC   -!- FUNCTION: Catalyzes the conversion of 3-methylglutaconyl-CoA to 3-
CC       hydroxy-3-methylglutaryl-CoA. Has very low enoyl-CoA hydratase
CC       activity. Was originally identified as RNA-binding protein that
CC       binds in vitro to clustered 5'-AUUUA-3' motifs.
CC       {ECO:0000269|PubMed:11738050, ECO:0000269|PubMed:12434311,
CC       ECO:0000269|PubMed:12655555, ECO:0000269|PubMed:7892223}.
CC   -!- CATALYTIC ACTIVITY: (S)-3-hydroxy-3-methylglutaryl-CoA = trans-3-
CC       methylglutaconyl-CoA + H(2)O.
CC   -!- PATHWAY: Amino-acid degradation; L-leucine degradation; (S)-3-
CC       hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 3/3.
CC   -!- SUBUNIT: Homohexamer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q13825-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q13825-2; Sequence=VSP_008336;
CC         Note=No experimental confirmation available.;
CC   -!- DISEASE: 3-methylglutaconic aciduria 1 (MGA1) [MIM:250950]: An
CC       inborn error of leucine metabolism. It leads to an autosomal
CC       recessive syndrome with variable clinical phenotype, ranging from
CC       delayed speech development to severe psychomotor retardation,
CC       coma, failure to thrive, metabolic acidosis and dystonia. MGA1 can
CC       be distinguished from other forms of MGA by the pattern of
CC       metabolite excretion: 3-methylglutaconic acid levels are higher
CC       than those detected in other forms, whereas methylglutaric acid
CC       levels are usually only slightly elevated and there is a high
CC       level of 3-hydroxyisovaleric acid excretion (not present in other
CC       MGA forms). {ECO:0000269|PubMed:12655555}. Note=The disease is
CC       caused by mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000305}.
DR   EMBL; X79888; CAA56260.1; -; mRNA.
DR   EMBL; AL158071; CAH72265.1; -; Genomic_DNA.
DR   EMBL; AL353645; CAH72265.1; JOINED; Genomic_DNA.
DR   EMBL; AL513353; CAH72265.1; JOINED; Genomic_DNA.
DR   EMBL; AL158071; CAH72266.1; -; Genomic_DNA.
DR   EMBL; AL353645; CAH72266.1; JOINED; Genomic_DNA.
DR   EMBL; AL513353; CAH72266.1; JOINED; Genomic_DNA.
DR   EMBL; AL513353; CAH72310.1; -; Genomic_DNA.
DR   EMBL; AL158071; CAH72310.1; JOINED; Genomic_DNA.
DR   EMBL; AL353645; CAH72310.1; JOINED; Genomic_DNA.
DR   EMBL; AL513353; CAH72311.1; -; Genomic_DNA.
DR   EMBL; AL158071; CAH72311.1; JOINED; Genomic_DNA.
DR   EMBL; AL353645; CAH72311.1; JOINED; Genomic_DNA.
DR   EMBL; AL353645; CAH73894.1; -; Genomic_DNA.
DR   EMBL; AL158071; CAH73894.1; JOINED; Genomic_DNA.
DR   EMBL; AL513353; CAH73894.1; JOINED; Genomic_DNA.
DR   EMBL; AL353645; CAH73895.1; -; Genomic_DNA.
DR   EMBL; AL158071; CAH73895.1; JOINED; Genomic_DNA.
DR   EMBL; AL513353; CAH73895.1; JOINED; Genomic_DNA.
DR   EMBL; CH471089; EAW62794.1; -; Genomic_DNA.
DR   EMBL; CH471089; EAW62795.1; -; Genomic_DNA.
DR   EMBL; BC020722; AAH20722.1; -; mRNA.
DR   CCDS; CCDS6689.1; -. [Q13825-1]
DR   CCDS; CCDS78409.1; -. [Q13825-2]
DR   PIR; I37195; I37195.
DR   RefSeq; NP_001293119.1; NM_001306190.1. [Q13825-2]
DR   RefSeq; NP_001689.1; NM_001698.2. [Q13825-1]
DR   UniGene; Hs.175905; -.
DR   PDB; 1HZD; X-ray; 2.20 A; A/B/C/D/E/F=68-339.
DR   PDB; 2ZQQ; X-ray; 2.20 A; A/B/C/D/E/F=68-339.
DR   PDB; 2ZQR; X-ray; 2.50 A; A/B/C/D/E/F=68-339.
DR   PDBsum; 1HZD; -.
DR   PDBsum; 2ZQQ; -.
DR   PDBsum; 2ZQR; -.
DR   ProteinModelPortal; Q13825; -.
DR   SMR; Q13825; -.
DR   BioGrid; 107030; 9.
DR   STRING; 9606.ENSP00000364883; -.
DR   iPTMnet; Q13825; -.
DR   PhosphoSitePlus; Q13825; -.
DR   BioMuta; AUH; -.
DR   DMDM; 37076898; -.
DR   EPD; Q13825; -.
DR   MaxQB; Q13825; -.
DR   PaxDb; Q13825; -.
DR   PeptideAtlas; Q13825; -.
DR   PRIDE; Q13825; -.
DR   TopDownProteomics; Q13825-1; -. [Q13825-1]
DR   TopDownProteomics; Q13825-2; -. [Q13825-2]
DR   DNASU; 549; -.
DR   Ensembl; ENST00000303617; ENSP00000307334; ENSG00000148090. [Q13825-2]
DR   Ensembl; ENST00000375731; ENSP00000364883; ENSG00000148090. [Q13825-1]
DR   GeneID; 549; -.
DR   KEGG; hsa:549; -.
DR   UCSC; uc004arf.5; human. [Q13825-1]
DR   CTD; 549; -.
DR   DisGeNET; 549; -.
DR   GeneCards; AUH; -.
DR   HGNC; HGNC:890; AUH.
DR   HPA; HPA004171; -.
DR   MalaCards; AUH; -.
DR   MIM; 250950; phenotype.
DR   MIM; 600529; gene.
DR   neXtProt; NX_Q13825; -.
DR   OpenTargets; ENSG00000148090; -.
DR   Orphanet; 67046; 3-methylglutaconic aciduria type 1.
DR   PharmGKB; PA25181; -.
DR   eggNOG; KOG1679; Eukaryota.
DR   eggNOG; COG1024; LUCA.
DR   GeneTree; ENSGT00890000139344; -.
DR   HOGENOM; HOG000027939; -.
DR   HOVERGEN; HBG106714; -.
DR   InParanoid; Q13825; -.
DR   KO; K05607; -.
DR   OMA; KGRAMEM; -.
DR   OrthoDB; EOG091G0Q9K; -.
DR   PhylomeDB; Q13825; -.
DR   TreeFam; TF314276; -.
DR   BioCyc; MetaCyc:HS07490-MONOMER; -.
DR   BRENDA; 4.2.1.18; 2681.
DR   Reactome; R-HSA-70895; Branched-chain amino acid catabolism.
DR   SABIO-RK; Q13825; -.
DR   UniPathway; UPA00363; UER00862.
DR   EvolutionaryTrace; Q13825; -.
DR   GenomeRNAi; 549; -.
DR   PRO; PR:Q13825; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   Bgee; ENSG00000148090; -.
DR   CleanEx; HS_AUH; -.
DR   Genevisible; Q13825; HS.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IDA:UniProtKB.
DR   GO; GO:0004490; F:methylglutaconyl-CoA hydratase activity; EXP:Reactome.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR   GO; GO:0009083; P:branched-chain amino acid catabolic process; TAS:Reactome.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR   GO; GO:0006552; P:leucine catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.12.10; -; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom.
DR   InterPro; IPR014748; Crontonase_C.
DR   InterPro; IPR001753; Crotonase_core_superfam.
DR   InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q13825.
DR   SWISS-2DPAGE; Q13825.
KW   3D-structure; Acetylation; Alternative splicing;
KW   Branched-chain amino acid catabolism; Complete proteome;
KW   Direct protein sequencing; Disease mutation; Lyase; Mitochondrion;
KW   Reference proteome; RNA-binding; Transit peptide.
FT   TRANSIT       1     67       Mitochondrion.
FT                                {ECO:0000269|PubMed:7892223}.
FT   CHAIN        68    339       Methylglutaconyl-CoA hydratase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000007415.
FT   REGION      105    119       RNA-binding.
FT   MOD_RES     100    100       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q9JLZ3}.
FT   MOD_RES     100    100       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q9JLZ3}.
FT   MOD_RES     109    109       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q9JLZ3}.
FT   MOD_RES     113    113       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q9JLZ3}.
FT   MOD_RES     113    113       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q9JLZ3}.
FT   MOD_RES     144    144       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q9JLZ3}.
FT   MOD_RES     144    144       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q9JLZ3}.
FT   MOD_RES     148    148       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q9JLZ3}.
FT   MOD_RES     160    160       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q9JLZ3}.
FT   MOD_RES     204    204       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q9JLZ3}.
FT   MOD_RES     204    204       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q9JLZ3}.
FT   MOD_RES     211    211       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q9JLZ3}.
FT   MOD_RES     211    211       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q9JLZ3}.
FT   MOD_RES     329    329       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q9JLZ3}.
FT   VAR_SEQ     140    168       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_008336.
FT   VARIANT     240    240       A -> V (in MGA1; dbSNP:rs769894315).
FT                                {ECO:0000269|PubMed:12655555}.
FT                                /FTId=VAR_016911.
FT   MUTAGEN     105    105       K->N: Abolishes RNA-binding; when
FT                                associated with E-109 and Q-113.
FT                                {ECO:0000269|PubMed:11738050}.
FT   MUTAGEN     109    109       K->E: Abolishes RNA-binding; when
FT                                associated with N-105 and Q-113.
FT                                {ECO:0000269|PubMed:11738050}.
FT   MUTAGEN     113    113       K->Q: Abolishes RNA-binding; when
FT                                associated with N-105 and E-109.
FT                                {ECO:0000269|PubMed:11738050}.
FT   STRAND       76     81       {ECO:0000244|PDB:1HZD}.
FT   HELIX        84     86       {ECO:0000244|PDB:1HZD}.
FT   STRAND       89     94       {ECO:0000244|PDB:1HZD}.
FT   HELIX        97     99       {ECO:0000244|PDB:1HZD}.
FT   HELIX       107    120       {ECO:0000244|PDB:1HZD}.
FT   STRAND      125    133       {ECO:0000244|PDB:1HZD}.
FT   STRAND      135    138       {ECO:0000244|PDB:1HZD}.
FT   HELIX       143    146       {ECO:0000244|PDB:1HZD}.
FT   HELIX       151    169       {ECO:0000244|PDB:1HZD}.
FT   STRAND      175    184       {ECO:0000244|PDB:1HZD}.
FT   HELIX       186    193       {ECO:0000244|PDB:1HZD}.
FT   STRAND      194    200       {ECO:0000244|PDB:1HZD}.
FT   STRAND      204    206       {ECO:0000244|PDB:1HZD}.
FT   HELIX       209    212       {ECO:0000244|PDB:1HZD}.
FT   HELIX       220    228       {ECO:0000244|PDB:1HZD}.
FT   HELIX       230    239       {ECO:0000244|PDB:1HZD}.
FT   STRAND      242    244       {ECO:0000244|PDB:1HZD}.
FT   HELIX       245    250       {ECO:0000244|PDB:1HZD}.
FT   STRAND      255    258       {ECO:0000244|PDB:1HZD}.
FT   HELIX       266    276       {ECO:0000244|PDB:1HZD}.
FT   TURN        277    280       {ECO:0000244|PDB:1HZD}.
FT   HELIX       283    297       {ECO:0000244|PDB:1HZD}.
FT   HELIX       301    313       {ECO:0000244|PDB:1HZD}.
FT   TURN        314    317       {ECO:0000244|PDB:1HZD}.
FT   HELIX       319    328       {ECO:0000244|PDB:1HZD}.
FT   TURN        329    331       {ECO:0000244|PDB:1HZD}.
SQ   SEQUENCE   339 AA;  35609 MW;  E04FEB95933FB30B CRC64;
     MAAAVAAAPG ALGSLHAGGA RLVAACSAWL CPGLRLPGSL AGRRAGPAIW AQGWVPAAGG
     PAPKRGYSSE MKTEDELRVR HLEEENRGIV VLGINRAYGK NSLSKNLIKM LSKAVDALKS
     DKKVRTIIIR SEVPGIFCAG ADLKERAKMS SSEVGPFVSK IRAVINDIAN LPVPTIAAID
     GLALGGGLEL ALACDIRVAA SSAKMGLVET KLAIIPGGGG TQRLPRAIGM SLAKELIFSA
     RVLDGKEAKA VGLISHVLEQ NQEGDAAYRK ALDLAREFLP QGPVAMRVAK LAINQGMEVD
     LVTGLAIEEA CYAQTIPTKD RLEGLLAFKE KRPPRYKGE
//

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