HMWC_DESVH
ID HMWC_DESVH Reviewed; 545 AA.
AC P24092;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=High-molecular-weight cytochrome c;
DE AltName: Full=Cytochrome CC3;
DE Flags: Precursor;
GN Name=hmcA; Synonyms=hmc; OrderedLocusNames=DVU_0536;
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1846136; DOI=10.1128/jb.173.1.220-228.1991;
RA Pollock W.B.R., Loutfi M., Bruschi M., Rapp-Giles B.J., Wall J.D.,
RA Voordouw G.;
RT "Cloning, sequencing, and expression of the gene encoding the high-
RT molecular-weight cytochrome c from Desulfovibrio vulgaris Hildenborough.";
RL J. Bacteriol. 173:220-228(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
RN [3]
RP EPR SPECTROSCOPY, AND REDOX POTENTIOMETRY OF HEMES.
RX PubMed=2163671; DOI=10.1021/bi00472a019;
RA Tan J.A., Cowan J.A.;
RT "Coordination and redox properties of a novel triheme cytochrome from
RT Desulfovibrio vulgaris (Hildenborough).";
RL Biochemistry 29:4886-4892(1990).
RN [4]
RP EPR SPECTROSCOPY, AND REDOX POTENTIOMETRY OF HEMES.
RX PubMed=1313289; DOI=10.1021/bi00127a033;
RA Bruschi M., Bertrand P., More C., Leroy G., Bonicel J., Haladjian J.,
RA Chottard G., Pollock W.B.R., Voordouw G.;
RT "Biochemical and spectroscopic characterization of the high molecular
RT weight cytochrome c from Desulfovibrio vulgaris Hildenborough expressed in
RT Desulfovibrio desulfuricans G200.";
RL Biochemistry 31:3281-3288(1992).
RN [5]
RP DOMAIN STRUCTURE.
RX PubMed=8335628; DOI=10.1128/jb.175.15.4699-4711.1993;
RA Rossi M., Pollock W.B.R., Reij M.W., Keon R.G., Fu R., Voordouw G.;
RT "The hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough
RT encodes a potential transmembrane redox protein complex.";
RL J. Bacteriol. 175:4699-4711(1993).
RN [6]
RP EPR SPECTROSCOPY, AND REDOX POTENTIOMETRY OF HEMES.
RX PubMed=7925451; DOI=10.1111/j.1432-1033.1994.00311.x;
RA Verhagen M.F.J.M., Pierik A.J., Wolbert R.B.G., Mallee L.F.,
RA Voorhorst W.G.B., Hagen W.R.;
RT "Axial coordination and reduction potentials of the sixteen hemes in high-
RT molecular-mass cytochrome c from Desulfovibrio vulgaris (Hildenborough).";
RL Eur. J. Biochem. 225:311-319(1994).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS).
RX PubMed=12356749; DOI=10.1074/jbc.m207465200;
RA Matias P.M., Coelho A.V., Valente F.M.A., Placido D., LeGall J.,
RA Xavier A.V., Pereira I.A.C., Carrondo M.A.;
RT "Sulfate respiration in Desulfovibrio vulgaris Hildenborough. Structure of
RT the 16-heme cytochrome c HmcA at 2.5-A resolution and a view of its role in
RT transmembrane electron transfer.";
RL J. Biol. Chem. 277:47907-47916(2002).
CC -!- FUNCTION: HMWC (high-molecular-weight cytochrome c), ORF2, ORF3, ORF4,
CC ORF5 and ORF6 in the HMC operon form a transmembrane protein complex
CC that allows electron flow from the periplasmic hydrogenase to the
CC cytoplasmic enzymes that catalyze reduction of sulfates.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Binds 16 heme c groups per subunit. High-spin heme 15 has single
CC axial histidine ligand and the other hemes are low-spin bis-histidinyl
CC coordinated.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS95018.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M63807; AAA23355.1; -; Genomic_DNA.
DR EMBL; AE017285; AAS95018.1; ALT_INIT; Genomic_DNA.
DR PIR; A39193; A39193.
DR RefSeq; WP_014524248.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_009759.1; NC_002937.3.
DR PDB; 1GWS; X-ray; 2.42 A; A=1-545.
DR PDB; 1H29; X-ray; 2.51 A; A/B/C/D=32-545.
DR PDB; 2CVC; X-ray; 2.00 A; A=1-545.
DR PDBsum; 1GWS; -.
DR PDBsum; 1H29; -.
DR PDBsum; 2CVC; -.
DR AlphaFoldDB; P24092; -.
DR SMR; P24092; -.
DR STRING; 882.DVU_0536; -.
DR DrugBank; DB03317; Ferroheme C.
DR TCDB; 5.B.13.1.1; the one electron transmembrane transfer complex (hmcabcdef) family.
DR PaxDb; P24092; -.
DR EnsemblBacteria; AAS95018; AAS95018; DVU_0536.
DR KEGG; dvu:DVU_0536; -.
DR PATRIC; fig|882.5.peg.512; -.
DR eggNOG; COG0484; Bacteria.
DR HOGENOM; CLU_508744_0_0_7; -.
DR OMA; KLCFGCH; -.
DR EvolutionaryTrace; P24092; -.
DR Proteomes; UP000002194; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR002322; Cyt_c_III.
DR InterPro; IPR020942; Cyt_c_III_dom.
DR InterPro; IPR011346; Cyt_cc3.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR Pfam; PF02085; Cytochrom_CIII; 4.
DR PIRSF; PIRSF000026; Cytochrome_cc3; 1.
DR PRINTS; PR00609; CYTOCHROMEC3.
DR SUPFAM; SSF48695; SSF48695; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW Metal-binding; Periplasm; Reference proteome; Repeat; Signal; Transport.
FT SIGNAL 1..31
FT CHAIN 32..545
FT /note="High-molecular-weight cytochrome c"
FT /id="PRO_0000006593"
FT BINDING 66
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 BINDING 69
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 BINDING 80
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT BINDING 83
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT BINDING 84
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 BINDING 111
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 BINDING 114
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 117
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 118
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 BINDING 135
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT BINDING 138
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT BINDING 139
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 BINDING 159
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 BINDING 162
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 BINDING 178
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT BINDING 181
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT BINDING 182
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 BINDING 183
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 BINDING 202
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /note="covalent"
FT BINDING 205
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /note="covalent"
FT BINDING 206
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 BINDING 222
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 BINDING 225
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /note="covalent"
FT BINDING 228
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /note="covalent"
FT BINDING 229
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 BINDING 244
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /note="covalent"
FT BINDING 247
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /note="covalent"
FT BINDING 248
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 BINDING 298
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 BINDING 301
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="10"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 308
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /note="covalent"
FT BINDING 311
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /note="covalent"
FT BINDING 312
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 BINDING 313
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="9"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 319
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="9"
FT /note="covalent"
FT BINDING 322
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="9"
FT /note="covalent"
FT BINDING 323
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="9"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 341
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="12"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 349
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="10"
FT /note="covalent"
FT BINDING 352
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="10"
FT /note="covalent"
FT BINDING 353
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="10"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 362
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="11"
FT /note="covalent"
FT BINDING 365
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="11"
FT /note="covalent"
FT BINDING 366
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="11"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 378
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="12"
FT /note="covalent"
FT BINDING 381
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="12"
FT /note="covalent"
FT BINDING 382
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="12"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 449
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="13"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 470
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="11"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 477
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="13"
FT /note="covalent"
FT BINDING 480
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="13"
FT /note="covalent"
FT BINDING 481
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="13"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 482
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="14"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 493
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="14"
FT /note="covalent"
FT BINDING 496
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="14"
FT /note="covalent"
FT BINDING 497
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="14"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 516
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="16"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 519
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="15"
FT /note="covalent"
FT BINDING 522
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="15"
FT /note="covalent"
FT BINDING 523
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="15"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 536
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="16"
FT /note="covalent"
FT BINDING 539
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="16"
FT /note="covalent"
FT BINDING 540
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="16"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:2CVC"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:2CVC"
FT HELIX 50..54
FT /evidence="ECO:0007829|PDB:2CVC"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:2CVC"
FT HELIX 66..75
FT /evidence="ECO:0007829|PDB:2CVC"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2CVC"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:2CVC"
FT HELIX 103..123
FT /evidence="ECO:0007829|PDB:2CVC"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:2CVC"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:2CVC"
FT HELIX 156..163
FT /evidence="ECO:0007829|PDB:2CVC"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:2CVC"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:2CVC"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:2CVC"
FT TURN 187..190
FT /evidence="ECO:0007829|PDB:2CVC"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:2CVC"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:2CVC"
FT HELIX 217..234
FT /evidence="ECO:0007829|PDB:2CVC"
FT HELIX 244..248
FT /evidence="ECO:0007829|PDB:2CVC"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:2CVC"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:2CVC"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:2CVC"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:2CVC"
FT HELIX 298..304
FT /evidence="ECO:0007829|PDB:2CVC"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:2CVC"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:2CVC"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:2CVC"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:2CVC"
FT HELIX 336..341
FT /evidence="ECO:0007829|PDB:2CVC"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:1GWS"
FT HELIX 349..356
FT /evidence="ECO:0007829|PDB:2CVC"
FT HELIX 360..366
FT /evidence="ECO:0007829|PDB:2CVC"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:2CVC"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:2CVC"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:1H29"
FT HELIX 390..393
FT /evidence="ECO:0007829|PDB:2CVC"
FT TURN 394..400
FT /evidence="ECO:0007829|PDB:2CVC"
FT HELIX 403..416
FT /evidence="ECO:0007829|PDB:2CVC"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:2CVC"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:2CVC"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:2CVC"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:2CVC"
FT HELIX 449..460
FT /evidence="ECO:0007829|PDB:2CVC"
FT HELIX 464..469
FT /evidence="ECO:0007829|PDB:2CVC"
FT TURN 473..475
FT /evidence="ECO:0007829|PDB:2CVC"
FT HELIX 476..479
FT /evidence="ECO:0007829|PDB:2CVC"
FT HELIX 493..495
FT /evidence="ECO:0007829|PDB:2CVC"
FT HELIX 511..526
FT /evidence="ECO:0007829|PDB:2CVC"
FT STRAND 538..540
FT /evidence="ECO:0007829|PDB:2CVC"
SQ SEQUENCE 545 AA; 58901 MW; 70A620FCC60D070B CRC64;
MRNGRTLLRW AGVLAATAII GVGGFWSQGT TKALPEGPGE KRADLIEIGA MERFGKLDLP
KVAFRHDQHT TAVTGMGKDC AACHKSKDGK MSLKFMRLDD NSAAELKEIY HANCIGCHTD
LAKAGKKTGP QDGECRSCHN PKPSAASSWK EIGFDKSLHY RHVASKAIKP VGDPQKNCGA
CHHVYDEASK KLVWGKNKED SCRACHGEKP VDKRPALDTA AHTACISCHM DVAKTKAETG
PVNCAGCHAP EAQAKFKVVR EVPRLDRGQP DAALILPVPG KDAPREMKGT MKPVAFDHKA
HEAKANDCRT CHHVRIDTCT ACHTVNGTAD SKFVQLEKAM HQPDSMRSCV GCHNTRVQQP
TCAGCHGFIK PTKSDAQCGV CHVAAPGFDA KQVEAGALLN LKAEQRSQVA ASMLSARPQP
KGTFDLNDIP EKVVIGSIAK EYQPSEFPHR KIVKTLIAGI GEDKLAATFH IEKGTLCQGC
HHNSPASLTP PKCASCHGKP FDADRGDRPG LKAAYHQQCM GCHDRMKIEK PANTACVDCH
KERAK
