CY1_YEAST
ID CY1_YEAST Reviewed; 309 AA.
AC P07143; D6W2C8;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Cytochrome c1, heme protein, mitochondrial;
DE EC=7.1.1.8 {ECO:0000269|PubMed:11279090};
DE AltName: Full=Complex III subunit 4;
DE AltName: Full=Complex III subunit IV;
DE AltName: Full=Cytochrome b-c1 complex subunit 4;
DE AltName: Full=Ubiquinol-cytochrome c oxidoreductase cytochrome c1 subunit;
DE Short=Cytochrome c-1;
DE Flags: Precursor;
GN Name=CYT1; Synonyms=CTC1; OrderedLocusNames=YOR065W; ORFNames=YOR29-16;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND POST-TRANSLATIONAL CLEAVAGE.
RX PubMed=6092058; DOI=10.1002/j.1460-2075.1984.tb02103.x;
RA Sadler I., Suda K., Schatz G., Kaudewitz F., Haid A.;
RT "Sequencing of the nuclear gene for the yeast cytochrome c1 precursor
RT reveals an unusually complex amino-terminal presequence.";
RL EMBO J. 3:2137-2143(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9133743;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<379::aid-yea85>3.0.co;2-g;
RA Valens M., Bohn C., Daignan-Fornier B., Dang V.-D., Bolotin-Fukuhara M.;
RT "The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the
RT presence of two tRNAs and 24 new open reading frames.";
RL Yeast 13:379-390(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP POST-TRANSLATIONAL CLEAVAGE, AND TOPOLOGY.
RX PubMed=9430684; DOI=10.1074/jbc.273.3.1469;
RA Arnold I., Foelsch H., Neupert W., Stuart R.A.;
RT "Two distinct and independent mitochondrial targeting signals function in
RT the sorting of an inner membrane protein, cytochrome c1.";
RL J. Biol. Chem. 273:1469-1476(1998).
RN [6]
RP FORMATION OF CYTOCHROME BC1-CYTOCHROME C OXIDASE SUPERCOMPLEX.
RX PubMed=10775262; DOI=10.1093/emboj/19.8.1777;
RA Schaegger H., Pfeiffer K.;
RT "Supercomplexes in the respiratory chains of yeast and mammalian
RT mitochondria.";
RL EMBO J. 19:1777-1783(2000).
RN [7]
RP FORMATION OF CYTOCHROME BC1-CYTOCHROME C OXIDASE SUPERCOMPLEX.
RX PubMed=10764779; DOI=10.1074/jbc.m001901200;
RA Cruciat C.M., Brunner S., Baumann F., Neupert W., Stuart R.A.;
RT "The cytochrome bc1 and cytochrome c oxidase complexes associate to form a
RT single supracomplex in yeast mitochondria.";
RL J. Biol. Chem. 275:18093-18098(2000).
RN [8]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF ARG-166.
RX PubMed=11279090; DOI=10.1074/jbc.m100550200;
RA Ahmad Z., Sherman F.;
RT "Role of Arg-166 in yeast cytochrome C1.";
RL J. Biol. Chem. 276:18450-18456(2001).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10] {ECO:0007744|PDB:1EZV}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH HEME.
RX PubMed=10873857; DOI=10.1016/s0969-2126(00)00152-0;
RA Hunte C., Koepke J., Lange C., Rossmanith T., Michel H.;
RT "Structure at 2.3 A resolution of the cytochrome bc1 complex from the yeast
RT Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment.";
RL Structure 8:669-684(2000).
RN [11] {ECO:0007744|PDB:1KYO}
RP X-RAY CRYSTALLOGRAPHY (2.97 ANGSTROMS) IN COMPLEX WITH HEME, AND
RP MUTAGENESIS OF LYS-288; LYS-289 AND LYS-296.
RX PubMed=11880631; DOI=10.1073/pnas.052704699;
RA Lange C., Hunte C.;
RT "Crystal structure of the yeast cytochrome bc1 complex with its bound
RT substrate cytochrome c.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2800-2805(2002).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).
RX PubMed=18390544; DOI=10.1074/jbc.m710126200;
RA Solmaz S.R., Hunte C.;
RT "Structure of complex III with bound cytochrome c in reduced state and
RT definition of a minimal core interface for electron transfer.";
RL J. Biol. Chem. 283:17542-17549(2008).
RN [13]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.23 ANGSTROMS).
RX PubMed=30598556; DOI=10.1038/s41594-018-0169-7;
RA Rathore S., Berndtsson J., Marin-Buera L., Conrad J., Carroni M.,
RA Brzezinski P., Ott M.;
RT "Cryo-EM structure of the yeast respiratory supercomplex.";
RL Nat. Struct. Mol. Biol. 26:50-57(2019).
RN [14]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.35 ANGSTROMS) IN COMPLEX WITH HEME.
RX PubMed=30598554; DOI=10.1038/s41594-018-0172-z;
RA Hartley A.M., Lukoyanova N., Zhang Y., Cabrera-Orefice A., Arnold S.,
RA Meunier B., Pinotsis N., Marechal A.;
RT "Structure of yeast cytochrome c oxidase in a supercomplex with cytochrome
RT bc1.";
RL Nat. Struct. Mol. Biol. 26:78-83(2019).
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a
CC multisubunit transmembrane complex that is part of the mitochondrial
CC electron transport chain which drives oxidative phosphorylation. The
CC respiratory chain contains 3 multisubunit complexes succinate
CC dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase
CC (complex IV, CIV), that cooperate to transfer electrons derived from
CC NADH and succinate to molecular oxygen, creating an electrochemical
CC gradient over the inner membrane that drives transmembrane transport
CC and the ATP synthase. The cytochrome b-c1 complex catalyzes electron
CC transfer from ubiquinol to cytochrome c, linking this redox reaction to
CC translocation of protons across the mitochondrial inner membrane, with
CC protons being carried across the membrane as hydrogens on the quinol.
CC In the process called Q cycle, 2 protons are consumed from the matrix,
CC 4 protons are released into the intermembrane space and 2 electrons are
CC passed to cytochrome c (Probable). Cytochrome c1 is a catalytic core
CC subunit containing a c-type heme. It transfers electrons from the [2Fe-
CC 2S] iron-sulfur cluster of the Rieske protein to cytochrome c
CC (PubMed:18390544). {ECO:0000269|PubMed:18390544,
CC ECO:0000305|PubMed:11880631}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2
CC Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:132124; EC=7.1.1.8;
CC Evidence={ECO:0000269|PubMed:11279090};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554};
CC Note=Binds 1 heme c group covalently per subunit.
CC {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554};
CC -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC composed of 10 subunits. The complex is composed of 3 respiratory
CC subunits cytochrome b (COB), cytochrome c1 (CYT1) and Rieske protein
CC (RIP1), 2 core protein subunits COR1 and QCR2, and 5 low-molecular
CC weight protein subunits QCR6, QCR7, QCR8, QCR9 and QCR10
CC (PubMed:10873857, PubMed:11880631, PubMed:18390544, PubMed:30598554).
CC The complex exists as an obligatory dimer and forms supercomplexes
CC (SCs) in the inner mitochondrial membrane with a monomer or a dimer of
CC cytochrome c oxidase (complex IV, CIV), resulting in 2 different
CC assemblies (supercomplexes III(2)IV and III(2)IV(2)) (PubMed:10775262,
CC PubMed:10764779, PubMed:30598556, PubMed:30598554). CYT1 interacts with
CC COX5A at the CIII-CIV interface (PubMed:30598554).
CC {ECO:0000269|PubMed:10764779, ECO:0000269|PubMed:10775262,
CC ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631,
CC ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554,
CC ECO:0000269|PubMed:30598556}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Single-pass
CC membrane protein {ECO:0000269|PubMed:18390544,
CC ECO:0000269|PubMed:30598554}.
CC -!- MISCELLANEOUS: Present with 39900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cytochrome c family. {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; X00791; CAA25375.1; -; Genomic_DNA.
DR EMBL; Z74973; CAA99258.1; -; Genomic_DNA.
DR EMBL; Z70678; CAA94550.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10844.1; -; Genomic_DNA.
DR PIR; A22737; CCBY1H.
DR RefSeq; NP_014708.1; NM_001183484.1.
DR PDB; 1EZV; X-ray; 2.30 A; D=62-306.
DR PDB; 1KB9; X-ray; 2.30 A; D=62-307.
DR PDB; 1KYO; X-ray; 2.97 A; D/O=62-309.
DR PDB; 1P84; X-ray; 2.50 A; D=62-307.
DR PDB; 2IBZ; X-ray; 2.30 A; D=62-309.
DR PDB; 3CX5; X-ray; 1.90 A; D/O=62-309.
DR PDB; 3CXH; X-ray; 2.50 A; D/O=62-309.
DR PDB; 4PD4; X-ray; 3.04 A; D=62-309.
DR PDB; 6GIQ; EM; 3.23 A; D/O=1-309.
DR PDB; 6HU9; EM; 3.35 A; D/O=62-309.
DR PDB; 6T0B; EM; 2.80 A; D/O=62-309.
DR PDB; 6T15; EM; 3.29 A; D/O=62-309.
DR PDB; 6YMX; EM; 3.17 A; D/O=62-309.
DR PDBsum; 1EZV; -.
DR PDBsum; 1KB9; -.
DR PDBsum; 1KYO; -.
DR PDBsum; 1P84; -.
DR PDBsum; 2IBZ; -.
DR PDBsum; 3CX5; -.
DR PDBsum; 3CXH; -.
DR PDBsum; 4PD4; -.
DR PDBsum; 6GIQ; -.
DR PDBsum; 6HU9; -.
DR PDBsum; 6T0B; -.
DR PDBsum; 6T15; -.
DR PDBsum; 6YMX; -.
DR AlphaFoldDB; P07143; -.
DR SMR; P07143; -.
DR BioGRID; 34464; 502.
DR ComplexPortal; CPX-567; Mitochondrial respiratory chain complex III.
DR DIP; DIP-4166N; -.
DR IntAct; P07143; 15.
DR MINT; P07143; -.
DR STRING; 4932.YOR065W; -.
DR TCDB; 3.D.3.3.1; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
DR MaxQB; P07143; -.
DR PaxDb; P07143; -.
DR PRIDE; P07143; -.
DR EnsemblFungi; YOR065W_mRNA; YOR065W; YOR065W.
DR GeneID; 854231; -.
DR KEGG; sce:YOR065W; -.
DR SGD; S000005591; CYT1.
DR VEuPathDB; FungiDB:YOR065W; -.
DR eggNOG; KOG3052; Eukaryota.
DR GeneTree; ENSGT00390000012445; -.
DR HOGENOM; CLU_040334_1_1_1; -.
DR InParanoid; P07143; -.
DR OMA; VWVKKFK; -.
DR BioCyc; MetaCyc:MON3O-103; -.
DR BioCyc; YEAST:MON3O-103; -.
DR Reactome; R-SCE-611105; Respiratory electron transport.
DR EvolutionaryTrace; P07143; -.
DR PRO; PR:P07143; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P07143; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IMP:SGD.
DR GO; GO:0045333; P:cellular respiration; IDA:ComplexPortal.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IDA:ComplexPortal.
DR Gene3D; 1.10.760.10; -; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR002326; Cyt_c1.
DR InterPro; IPR021157; Cyt_c1_TM_anchor_C.
DR PANTHER; PTHR10266; PTHR10266; 1.
DR Pfam; PF02167; Cytochrom_C1; 1.
DR PRINTS; PR00603; CYTOCHROMEC1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR SUPFAM; SSF81496; SSF81496; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Respiratory chain; Transit peptide; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..61
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:6092058,
FT ECO:0000269|PubMed:9430684"
FT CHAIN 62..309
FT /note="Cytochrome c1, heme protein, mitochondrial"
FT /id="PRO_0000006566"
FT TOPO_DOM 62..262
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0000269|PubMed:9430684"
FT TRANSMEM 263..296
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554"
FT TOPO_DOM 297..309
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0000269|PubMed:9430684"
FT DOMAIN 88..241
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT REGION 131..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 101
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:10873857,
FT ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV,
FT ECO:0007744|PDB:1KYO"
FT BINDING 104
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:10873857,
FT ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV,
FT ECO:0007744|PDB:1KYO"
FT BINDING 105
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:11880631,
FT ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554,
FT ECO:0007744|PDB:1KYO"
FT BINDING 225
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:10873857,
FT ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV,
FT ECO:0007744|PDB:1KYO"
FT MUTAGEN 166
FT /note="R->G: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:11279090"
FT MUTAGEN 272
FT /note="K->A: Loss of RIP1 from the bc1 complex."
FT MUTAGEN 288
FT /note="K->L: Loss of CYT1 and COB from the bc1 complex;
FT when associated with L-289 and L-296."
FT /evidence="ECO:0000269|PubMed:11880631"
FT MUTAGEN 289
FT /note="K->L: Loss of CYT1 and COB from the bc1 complex;
FT when associated with L-288 and L-296."
FT /evidence="ECO:0000269|PubMed:11880631"
FT MUTAGEN 296
FT /note="K->L: Loss of CYT1 and COB from the bc1 complex;
FT when associated with L-288 and L-289."
FT /evidence="ECO:0000269|PubMed:11880631"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:6GIQ"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:3CX5"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 122..129
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:4PD4"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:6T0B"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:4PD4"
FT HELIX 162..167
FT /evidence="ECO:0007829|PDB:3CX5"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:6T0B"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:4PD4"
FT HELIX 187..196
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:1P84"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 244..259
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 263..296
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:3CX5"
SQ SEQUENCE 309 AA; 34055 MW; 6CB7A0813AA06AF5 CRC64;
MFSNLSKRWA QRTLSKSFYS TATGAASKSG KLTQKLVTAG VAAAGITAST LLYADSLTAE
AMTAAEHGLH APAYAWSHNG PFETFDHASI RRGYQVYREV CAACHSLDRV AWRTLVGVSH
TNEEVRNMAE EFEYDDEPDE QGNPKKRPGK LSDYIPGPYP NEQAARAANQ GALPPDLSLI
VKARHGGCDY IFSLLTGYPD EPPAGVALPP GSNYNPYFPG GSIAMARVLF DDMVEYEDGT
PATTSQMAKD VTTFLNWCAE PEHDERKRLG LKTVIILSSL YLLSIWVKKF KWAGIKTRKF
VFNPPKPRK
