SUFS_ECOLI
ID SUFS_ECOLI Reviewed; 406 AA.
AC P77444;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Cysteine desulfurase;
DE EC=2.8.1.7 {ECO:0000305|PubMed:10329673};
DE AltName: Full=Cysteine sulfinate desulfinase;
DE Short=CSD;
DE EC=3.13.1.- {ECO:0000269|PubMed:10329673};
DE AltName: Full=Selenocysteine beta-lyase;
DE Short=SCL;
DE AltName: Full=Selenocysteine lyase;
DE EC=4.4.1.16 {ECO:0000269|PubMed:10329673};
DE AltName: Full=Selenocysteine reductase;
GN Name=sufS; Synonyms=csdB {ECO:0000303|PubMed:10329673}, ynhB;
GN OrderedLocusNames=b1680, JW1670;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND X-RAY CRYSTALLOGRAPHY (2.8
RP ANGSTROMS).
RC STRAIN=K12;
RX PubMed=10329673; DOI=10.1074/jbc.274.21.14768;
RA Mihara H., Maeda M., Fujii T., Kurihara T., Hata Y., Esaki N.;
RT "A nifS-like gene, csdB, encodes an Escherichia coli counterpart of
RT mammalian selenocysteine lyase. Gene cloning, purification,
RT characterization and preliminary X-ray crystallographic studies.";
RL J. Biol. Chem. 274:14768-14772(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP GENE NAME.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=10322040; DOI=10.1128/jb.181.10.3307-3309.1999;
RA Patzer S.I., Hantke K.;
RT "SufS is a NifS-like protein, and SufD is necessary for stability of the
RT 2Fe-2S FhuF protein in Escherichia coli.";
RL J. Bacteriol. 181:3307-3309(1999).
RN [6]
RP FUNCTION.
RX PubMed=10829016; DOI=10.1074/jbc.m000926200;
RA Lacourciere G.M., Mihara H., Kurihara T., Esaki N., Stadtman T.C.;
RT "Escherichia coli NifS-like proteins provide selenium in the pathway for
RT the biosynthesis of selenophosphate.";
RL J. Biol. Chem. 275:23769-23773(2000).
RN [7]
RP MUTAGENESIS OF CYS-364.
RX PubMed=10739946; DOI=10.1093/oxfordjournals.jbchem.a022641;
RA Mihara H., Kurihara T., Yoshimura T., Esaki N.;
RT "Kinetic and mutational studies of three NifS homologs from Escherichia
RT coli: mechanistic difference between L-cysteine desulfurase and L-
RT selenocysteine lyase reactions.";
RL J. Biochem. 127:559-567(2000).
RN [8]
RP FUNCTION IN FE-S CLUSTER SYSTEM.
RX PubMed=12089140; DOI=10.1074/jbc.c200365200;
RA Takahashi Y., Tokumoto U.;
RT "A third bacterial system for the assembly of iron-sulfur clusters with
RT homologs in archaea and plastids.";
RL J. Biol. Chem. 277:28380-28383(2002).
RN [9]
RP FUNCTION.
RX PubMed=11997471; DOI=10.1073/pnas.102176099;
RA Mihara H., Kato S., Lacourciere G.M., Stadtman T.C., Kennedy R.A.J.D.,
RA Kurihara T., Tokumoto U., Takahashi Y., Esaki N.;
RT "The iscS gene is essential for the biosynthesis of 2-selenouridine in tRNA
RT and the selenocysteine-containing formate dehydrogenase H.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:6679-6683(2002).
RN [10]
RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH SUFE AND SUFBCD
RP COMPLEX.
RC STRAIN=K12 / TG1;
RX PubMed=12876288; DOI=10.1074/jbc.m305953200;
RA Loiseau L., Ollagnier-de-Choudens S., Nachin L., Fontecave M., Barras F.;
RT "Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form
RT a new type of cysteine desulfurase.";
RL J. Biol. Chem. 278:38352-38359(2003).
RN [11]
RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH SUFE AND SUFBCD
RP COMPLEX.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12941942; DOI=10.1074/jbc.m308004200;
RA Outten F.W., Wood M.J., Munoz F.M., Storz G.;
RT "The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase
RT activity as part of a sulfur transfer pathway for Fe-S cluster assembly in
RT Escherichia coli.";
RL J. Biol. Chem. 278:45713-45719(2003).
RN [12]
RP ACTIVITY REGULATION, AND INTERACTION WITH SUFE.
RX PubMed=14644425; DOI=10.1016/s0014-5793(03)01244-4;
RA Ollagnier-de-Choudens S., Lascoux D., Loiseau L., Barras F., Forest E.,
RA Fontecave M.;
RT "Mechanistic studies of the SufS-SufE cysteine desulfurase: evidence for
RT sulfur transfer from SufS to SufE.";
RL FEBS Lett. 555:263-267(2003).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=10684605; DOI=10.1021/bi991732a;
RA Fujii T., Maeda M., Mihara H., Kurihara T., Esaki N., Hata Y.;
RT "Structure of a NifS homologue: X-ray structure analysis of CsdB, an
RT Escherichia coli counterpart of mammalian selenocysteine lyase.";
RL Biochemistry 39:1263-1273(2000).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND MUTAGENESIS OF HIS-55; HIS-123
RP AND ARG-379.
RX PubMed=11983074; DOI=10.1093/oxfordjournals.jbchem.a003151;
RA Mihara H., Fujii T., Kato S., Kurihara T., Hata Y., Esaki N.;
RT "Structure of external aldimine of Escherichia coli CsdB, an IscS/NifS
RT homolog: implications for its specificity toward selenocysteine.";
RL J. Biochem. 131:679-685(2002).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH
RP L-CYSTEINE AND L-SELENOCYSTEINE, AND PYRIDOXAL PHOSPHATE AT LYS-226.
RX PubMed=11827487; DOI=10.1006/jmbi.2001.5308;
RA Lima C.D.;
RT "Analysis of the E. coli NifS CsdB protein at 2.0 A reveals the structural
RT basis for perselenide and persulfide intermediate formation.";
RL J. Mol. Biol. 315:1199-1208(2002).
CC -!- FUNCTION: Cysteine desulfurases mobilize the sulfur from L-cysteine to
CC yield L-alanine, an essential step in sulfur metabolism for
CC biosynthesis of a variety of sulfur-containing biomolecules. Component
CC of the suf operon, which is activated and required under specific
CC conditions such as oxidative stress and iron limitation. Acts as a
CC potent selenocysteine lyase in vitro, that mobilizes selenium from L-
CC selenocysteine. Selenocysteine lyase activity is however unsure in
CC vivo. Can also desulfinate L-cysteine sulfinate (3-sulfino-L-alanine).
CC {ECO:0000269|PubMed:10329673, ECO:0000269|PubMed:10829016,
CC ECO:0000269|PubMed:11997471, ECO:0000269|PubMed:12089140,
CC ECO:0000269|PubMed:12876288, ECO:0000269|PubMed:12941942}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-
CC alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:64428; EC=2.8.1.7;
CC Evidence={ECO:0000305|PubMed:10329673};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + L-selenocysteine = A + H(+) + hydrogenselenide + L-
CC alanine; Xref=Rhea:RHEA:11632, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:29317, ChEBI:CHEBI:57843,
CC ChEBI:CHEBI:57972; EC=4.4.1.16;
CC Evidence={ECO:0000269|PubMed:10329673};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-sulfino-L-alanine + H2O = H(+) + L-alanine + sulfite;
CC Xref=Rhea:RHEA:28278, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:57972, ChEBI:CHEBI:61085;
CC Evidence={ECO:0000269|PubMed:10329673};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:10329673};
CC -!- ACTIVITY REGULATION: Displays a strong preference for selenocysteine as
CC a substrate in vitro and is only very slightly active using cysteine.
CC The interactions with SufE and the SufBCD complex act synergistically
CC to enhance, up to 50-fold, its cysteine desulfurase activity.
CC {ECO:0000269|PubMed:12876288, ECO:0000269|PubMed:12941942,
CC ECO:0000269|PubMed:14644425}.
CC -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC -!- SUBUNIT: Homodimer (PubMed:10329673). Interacts with SufE and the
CC SufBCD complex composed of SufB, SufC and SufD. The interaction with
CC SufE is required to mediate the direct transfer of the sulfur atom from
CC the S-sulfanylcysteine. {ECO:0000269|PubMed:10329673,
CC ECO:0000269|PubMed:11827487, ECO:0000269|PubMed:12876288,
CC ECO:0000269|PubMed:12941942, ECO:0000269|PubMed:14644425}.
CC -!- INTERACTION:
CC P77444; P76194: sufE; NbExp=3; IntAct=EBI-1124981, EBI-1124973;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Suf operon is under both the Fe-dependent Fur repressor and
CC the oxidative stress dependent OxyR activator.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. Csd subfamily. {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; AB055108; BAB21542.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74750.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15457.1; -; Genomic_DNA.
DR PIR; H64925; H64925.
DR RefSeq; NP_416195.1; NC_000913.3.
DR RefSeq; WP_000577988.1; NZ_SSZK01000001.1.
DR PDB; 1C0N; X-ray; 2.80 A; A=1-406.
DR PDB; 1I29; X-ray; 2.80 A; A=1-406.
DR PDB; 1JF9; X-ray; 2.00 A; A=1-406.
DR PDB; 1KMJ; X-ray; 2.00 A; A=1-406.
DR PDB; 1KMK; X-ray; 2.20 A; A=1-406.
DR PDB; 5DB5; X-ray; 2.75 A; A/B=1-406.
DR PDB; 6MR2; X-ray; 2.40 A; A=1-406.
DR PDB; 6MR6; X-ray; 2.02 A; A=1-406.
DR PDB; 6MRE; X-ray; 2.50 A; A=1-406.
DR PDB; 6MRH; X-ray; 2.02 A; A=1-406.
DR PDB; 6MRI; X-ray; 2.62 A; A=1-406.
DR PDB; 6O10; X-ray; 2.00 A; A=1-406.
DR PDB; 6O11; X-ray; 1.84 A; A=1-406.
DR PDB; 6O12; X-ray; 2.05 A; A=1-406.
DR PDB; 6O13; X-ray; 2.20 A; A=1-406.
DR PDB; 6UY5; X-ray; 1.50 A; A/B=1-406.
DR PDBsum; 1C0N; -.
DR PDBsum; 1I29; -.
DR PDBsum; 1JF9; -.
DR PDBsum; 1KMJ; -.
DR PDBsum; 1KMK; -.
DR PDBsum; 5DB5; -.
DR PDBsum; 6MR2; -.
DR PDBsum; 6MR6; -.
DR PDBsum; 6MRE; -.
DR PDBsum; 6MRH; -.
DR PDBsum; 6MRI; -.
DR PDBsum; 6O10; -.
DR PDBsum; 6O11; -.
DR PDBsum; 6O12; -.
DR PDBsum; 6O13; -.
DR PDBsum; 6UY5; -.
DR AlphaFoldDB; P77444; -.
DR SMR; P77444; -.
DR BioGRID; 4260281; 100.
DR BioGRID; 850545; 4.
DR ComplexPortal; CPX-2124; sufS cysteine desulfurase complex.
DR DIP; DIP-9324N; -.
DR IntAct; P77444; 14.
DR STRING; 511145.b1680; -.
DR DrugBank; DB04217; L-2-amino-3-butynoic acid.
DR DrugBank; DB02761; S-Mercaptocysteine.
DR DrugBank; DB03049; S-Selanyl Cysteine.
DR DrugBank; DB02345; Selenocysteine.
DR jPOST; P77444; -.
DR PaxDb; P77444; -.
DR PRIDE; P77444; -.
DR EnsemblBacteria; AAC74750; AAC74750; b1680.
DR EnsemblBacteria; BAA15457; BAA15457; BAA15457.
DR GeneID; 946185; -.
DR KEGG; ecj:JW1670; -.
DR KEGG; eco:b1680; -.
DR PATRIC; fig|1411691.4.peg.578; -.
DR EchoBASE; EB3720; -.
DR eggNOG; COG0520; Bacteria.
DR HOGENOM; CLU_003433_2_5_6; -.
DR InParanoid; P77444; -.
DR OMA; HKLCGPT; -.
DR PhylomeDB; P77444; -.
DR BioCyc; EcoCyc:G6906-MON; -.
DR BioCyc; MetaCyc:G6906-MON; -.
DR BRENDA; 2.8.1.7; 2026.
DR BRENDA; 4.4.1.16; 2026.
DR UniPathway; UPA00266; -.
DR EvolutionaryTrace; P77444; -.
DR PRO; PR:P77444; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990221; C:L-cysteine desulfurase complex; IPI:ComplexPortal.
DR GO; GO:0031071; F:cysteine desulfurase activity; IDA:EcoCyc.
DR GO; GO:0008826; F:cysteine sulfinate desulfinase activity; IEA:RHEA.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR GO; GO:0009000; F:selenocysteine lyase activity; IDA:EcoCyc.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:EcoCyc.
DR GO; GO:0019448; P:L-cysteine catabolic process; IDA:ComplexPortal.
DR GO; GO:0006790; P:sulfur compound metabolic process; IDA:EcoCyc.
DR GO; GO:0031162; P:sulfur incorporation into metallo-sulfur cluster; IDA:EcoCyc.
DR CDD; cd06453; SufS_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_01831; SufS_aminotrans_5; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR010970; Cys_dSase_SufS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01979; sufS; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase; Lyase;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..406
FT /note="Cysteine desulfurase"
FT /id="PRO_0000150329"
FT ACT_SITE 364
FT /note="Cysteine persulfide intermediate"
FT MOD_RES 226
FT /note="N6-(pyridoxal phosphate)lysine"
FT MUTAGEN 55
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:11983074"
FT MUTAGEN 123
FT /note="H->A: Loss of function; possibly due to
FT destabilization of PLP in the active site."
FT /evidence="ECO:0000269|PubMed:11983074"
FT MUTAGEN 364
FT /note="C->A: Abolishes activity towards L-cysteine but not
FT towards selenocysteine."
FT /evidence="ECO:0000269|PubMed:10739946"
FT MUTAGEN 379
FT /note="R->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:11983074"
FT HELIX 5..9
FT /evidence="ECO:0007829|PDB:6UY5"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:6UY5"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:6UY5"
FT HELIX 37..49
FT /evidence="ECO:0007829|PDB:6UY5"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:6O11"
FT HELIX 60..79
FT /evidence="ECO:0007829|PDB:6UY5"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:6UY5"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:6UY5"
FT HELIX 94..109
FT /evidence="ECO:0007829|PDB:6UY5"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:6UY5"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:6UY5"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:6UY5"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:6UY5"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:6UY5"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:6UY5"
FT STRAND 165..173
FT /evidence="ECO:0007829|PDB:6UY5"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:6UY5"
FT HELIX 183..192
FT /evidence="ECO:0007829|PDB:6UY5"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:6UY5"
FT TURN 202..207
FT /evidence="ECO:0007829|PDB:6UY5"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:6UY5"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:6UY5"
FT TURN 225..228
FT /evidence="ECO:0007829|PDB:6UY5"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:6UY5"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:6UY5"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:6MRH"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:6UY5"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:6UY5"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:6UY5"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:6UY5"
FT HELIX 281..297
FT /evidence="ECO:0007829|PDB:6UY5"
FT HELIX 299..317
FT /evidence="ECO:0007829|PDB:6UY5"
FT STRAND 323..327
FT /evidence="ECO:0007829|PDB:6UY5"
FT STRAND 333..339
FT /evidence="ECO:0007829|PDB:6UY5"
FT HELIX 344..353
FT /evidence="ECO:0007829|PDB:6UY5"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:6UY5"
FT HELIX 366..371
FT /evidence="ECO:0007829|PDB:6UY5"
FT STRAND 377..381
FT /evidence="ECO:0007829|PDB:6UY5"
FT HELIX 388..405
FT /evidence="ECO:0007829|PDB:6UY5"
SQ SEQUENCE 406 AA; 44434 MW; 9374C43C3AD9D8E3 CRC64;
MIFSVDKVRA DFPVLSREVN GLPLAYLDSA ASAQKPSQVI DAEAEFYRHG YAAVHRGIHT
LSAQATEKME NVRKRASLFI NARSAEELVF VRGTTEGINL VANSWGNSNV RAGDNIIISQ
MEHHANIVPW QMLCARVGAE LRVIPLNPDG TLQLETLPTL FDEKTRLLAI THVSNVLGTE
NPLAEMITLA HQHGAKVLVD GAQAVMHHPV DVQALDCDFY VFSGHKLYGP TGIGILYVKE
ALLQEMPPWE GGGSMIATVS LSEGTTWTKA PWRFEAGTPN TGGIIGLGAA LEYVSALGLN
NIAEYEQNLM HYALSQLESV PDLTLYGPQN RLGVIAFNLG KHHAYDVGSF LDNYGIAVRT
GHHCAMPLMA YYNVPAMCRA SLAMYNTHEE VDRLVTGLQR IHRLLG
