HAO_NITEU
ID HAO_NITEU Reviewed; 570 AA.
AC Q50925;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Hydroxylamine oxidoreductase;
DE Short=HAO;
DE EC=1.7.2.6 {ECO:0000269|PubMed:497235, ECO:0000269|PubMed:6289867};
DE EC=1.7.2.9 {ECO:0000269|PubMed:497235};
DE Flags: Precursor;
GN Name=hao1; OrderedLocusNames=NE2044;
GN and
GN Name=hao2; OrderedLocusNames=NE0962;
GN and
GN Name=hao3; OrderedLocusNames=NE2339;
OS Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS 14298).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=228410;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=8288544; DOI=10.1128/jb.176.2.504-510.1994;
RA Sayavedra-Soto L.A., Hommes N.G., Arp D.J.;
RT "Characterization of the gene encoding hydroxylamine oxidoreductase in
RT Nitrosomonas europaea.";
RL J. Bacteriol. 176:504-510(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003;
RA Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT chemolithoautotroph Nitrosomonas europaea.";
RL J. Bacteriol. 185:2759-2773(2003).
RN [3]
RP CATALYTIC ACTIVITY.
RX PubMed=497235; DOI=10.1016/0005-2744(79)90220-1;
RA Hooper A.B., Terry K.R.;
RT "Hydroxylamine oxidoreductase of Nitrosomonas. Production of nitric oxide
RT from hydroxylamine.";
RL Biochim. Biophys. Acta 571:12-20(1979).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND EPR SPECTROSCOPY.
RX PubMed=6289867; DOI=10.1021/bi00260a010;
RA Lipscomb J.D., Hooper A.B.;
RT "Resolution of multiple heme centers of hydroxylamine oxidoreductase from
RT Nitrosomonas. 1. Electron paramagnetic resonance spectroscopy.";
RL Biochemistry 21:3965-3972(1982).
RN [5] {ECO:0007744|PDB:1FGJ}
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 25-570 IN COMPLEX WITH HEMES C.
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=9095195; DOI=10.1038/nsb0497-276;
RA Igarashi N., Moriyama H., Fujiwara T., Fukumori Y., Tanaka N.;
RT "The 2.8 A structure of hydroxylamine oxidoreductase from a nitrifying
RT chemoautotrophic bacterium, Nitrosomonas europaea.";
RL Nat. Struct. Biol. 4:276-284(1997).
CC -!- FUNCTION: Catalyzes the oxidation of hydroxylamine to nitrite. The
CC electrons released in the reaction are partitioned to ammonium
CC monooxygenase and to the respiratory chain. The immediate acceptor of
CC electrons from HAO is cytochrome c-554. {ECO:0000269|PubMed:6289867}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(III)-[cytochrome c] + H2O + hydroxylamine = 4 Fe(II)-
CC [cytochrome c] + 5 H(+) + nitrite; Xref=Rhea:RHEA:45032, Rhea:RHEA-
CC COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15429, ChEBI:CHEBI:16301,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.7.2.6;
CC Evidence={ECO:0000269|PubMed:497235, ECO:0000269|PubMed:6289867};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 Fe(III)-[cytochrome c] + hydroxylamine = 3 Fe(II)-
CC [cytochrome c] + 3 H(+) + nitric oxide; Xref=Rhea:RHEA:45036,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15429, ChEBI:CHEBI:16480, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=1.7.2.9; Evidence={ECO:0000269|PubMed:497235};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000269|PubMed:6289867, ECO:0000269|PubMed:9095195};
CC Note=Binds 8 heme c groups per subunit. One specific heme c group is
CC called heme P460. {ECO:0000269|PubMed:6289867,
CC ECO:0000269|PubMed:9095195};
CC -!- SUBUNIT: Homotrimer.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Binds 8 heme groups per subunit.
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DR EMBL; U04053; AAC43216.1; -; Unassigned_DNA.
DR EMBL; AL954747; CAD84873.1; -; Genomic_DNA.
DR EMBL; AL954747; CAD85955.1; -; Genomic_DNA.
DR EMBL; AL954747; CAD86251.1; -; Genomic_DNA.
DR PIR; A36954; A36954.
DR RefSeq; WP_011111571.1; NC_004757.1.
DR PDB; 1FGJ; X-ray; 2.80 A; A/B=25-570.
DR PDB; 4FAS; X-ray; 2.10 A; A/B/C=25-570.
DR PDB; 4N4N; X-ray; 2.20 A; A/C/E=25-570.
DR PDB; 4N4O; X-ray; 2.47 A; A/C/E=25-570.
DR PDB; 6M0P; X-ray; 2.78 A; A/C/E=1-570.
DR PDB; 6M0Q; X-ray; 1.99 A; A/C/E/G/I/K=1-570.
DR PDBsum; 1FGJ; -.
DR PDBsum; 4FAS; -.
DR PDBsum; 4N4N; -.
DR PDBsum; 4N4O; -.
DR PDBsum; 6M0P; -.
DR PDBsum; 6M0Q; -.
DR AlphaFoldDB; Q50925; -.
DR SMR; Q50925; -.
DR STRING; 228410.NE0962; -.
DR EnsemblBacteria; CAD84873; CAD84873; NE0962.
DR EnsemblBacteria; CAD85955; CAD85955; NE2044.
DR EnsemblBacteria; CAD86251; CAD86251; NE2339.
DR KEGG; neu:NE0962; -.
DR KEGG; neu:NE2044; -.
DR KEGG; neu:NE2339; -.
DR eggNOG; COG3303; Bacteria.
DR HOGENOM; CLU_022756_0_0_4; -.
DR OMA; FLEHRMR; -.
DR OrthoDB; 738283at2; -.
DR BioCyc; MetaCyc:HAONITRO-MON; -.
DR BRENDA; 1.7.2.6; 3654.
DR EvolutionaryTrace; Q50925; -.
DR Proteomes; UP000001416; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0047991; F:hydroxylamine oxidase activity; IDA:CACAO.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:CACAO.
DR GO; GO:0019331; P:anaerobic respiration, using ammonium as electron donor; IDA:CACAO.
DR InterPro; IPR012138; HAO.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR PIRSF; PIRSF000242; HAO; 1.
DR SUPFAM; SSF48695; SSF48695; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Oxidoreductase; Periplasm; Reference proteome; Signal.
FT SIGNAL 1..24
FT CHAIN 25..570
FT /note="Hydroxylamine oxidoreductase"
FT /evidence="ECO:0000269|PubMed:8288544"
FT /id="PRO_0000006604"
FT BINDING 103
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 106
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 107
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 123
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 169
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 172
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 173
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 184
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 196
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 199
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 200
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 228
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 253
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 256
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 257
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 263
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 266
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 267
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 270
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 283
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 286
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 287
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 303
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 334
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 337
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 338
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 347
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 384
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 387
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 388
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT BINDING 483
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:9095195,
FT ECO:0007744|PDB:1FGJ"
FT CONFLICT 243
FT /note="A -> T (in Ref. 1; AAC43216)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="A -> G (in Ref. 1; AAC43216)"
FT /evidence="ECO:0000305"
FT HELIX 31..36
FT /evidence="ECO:0007829|PDB:6M0Q"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 112..120
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 140..154
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 169..173
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 193..199
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 201..208
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:6M0Q"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 231..236
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 239..243
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 247..255
FT /evidence="ECO:0007829|PDB:6M0Q"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:6M0Q"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:6M0Q"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:6M0Q"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:6M0Q"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:6M0P"
FT HELIX 294..300
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 302..310
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:6M0Q"
FT TURN 323..327
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 334..338
FT /evidence="ECO:0007829|PDB:6M0Q"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:6M0Q"
FT TURN 362..365
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 366..369
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 371..384
FT /evidence="ECO:0007829|PDB:6M0Q"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 390..424
FT /evidence="ECO:0007829|PDB:6M0Q"
FT TURN 428..432
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 448..451
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 461..471
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 473..482
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:6M0Q"
FT TURN 489..491
FT /evidence="ECO:0007829|PDB:6M0Q"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:6M0Q"
FT HELIX 495..526
FT /evidence="ECO:0007829|PDB:6M0Q"
SQ SEQUENCE 570 AA; 64259 MW; C76AB9019512105E CRC64;
MRIGEWMRGL LLCAGLMMCG VVHADISTVP DETYDALKLD RGKATPKETY EALVKRYKDP
AHGAGKGTMG DYWEPIAISI YMDPNTFYKP PVSPKEVAER KDCVECHSDE TPVWVRAWKR
STHANLDKIR NLKSDDPLYY KKGKLEEVEN NLRSMGKLGE KETLKEVGCI DCHVDVNKKD
KADHTKDIRM PTADTCGTCH LREFAERESE RDTMVWPNGQ WPAGRPSHAL DYTANIETTV
WAAMPQREVA EGCTMCHTNQ NKCDNCHTRH EFSAAESRKP EACATCHSGV DHNNWEAYTM
SKHGKLAEMN RDKWNWEVRL KDAFSKGGQN APTCAACHME YEGEYTHNIT RKTRWANYPF
VPGIAENITS DWSEARLDSW VLTCTQCHSE RFARSYLDLM DKGTLEGLAK YQEANAIVHK
MYEDGTLTGQ KTNRPNPPEP EKPGFGIFTQ LFWSKGNNPA SLELKVLEMA ENNLAKMHVG
LAHVNPGGWT YTEGWGPMNR AYVEIQDEYT KMQELSALQA RVNKLEGKQT SLLDLKGTGE
KISLGGLGGG MLLAGALALI GWRKRKQTRA
