CNX1_ARATH
ID CNX1_ARATH Reviewed; 670 AA.
AC Q39054;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Molybdopterin biosynthesis protein CNX1;
DE AltName: Full=Molybdenum cofactor biosynthesis enzyme CNX1;
DE Includes:
DE RecName: Full=Molybdopterin molybdenumtransferase;
DE Short=MPT Mo-transferase;
DE EC=2.10.1.1;
DE AltName: Full=Domain E;
DE Includes:
DE RecName: Full=Molybdopterin adenylyltransferase;
DE Short=MPT adenylyltransferase;
DE EC=2.7.7.75;
DE AltName: Full=Domain G;
GN Name=CNX1; OrderedLocusNames=At5g20990; ORFNames=F22D1.6, T10F18.20;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=8528286; DOI=10.1046/j.1365-313x.1995.08050751.x;
RA Stallmeyer B., Nerlich A., Schiemann J., Brinkmann H., Mendel R.R.;
RT "Molybdenum co-factor biosynthesis: the Arabidopsis thaliana cDNA cnx1
RT encodes a multifunctional two-domain protein homologous to a mammalian
RT neuroprotein, the insect protein Cinnamon and three Escherichia coli
RT proteins.";
RL Plant J. 8:751-762(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Brinkmann H., Schledzewski K., Nerlich A., Bollmann G., Stallmeyer B.,
RA Mendel R.R.;
RT "Sequence of the Arabidopsis thaliana gene cnx1 that is involved in the
RT last step of molybdenum cofactor biosynthesis.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP BINDING OF MPT TO DOMAIN G, AND SUBUNIT.
RX PubMed=9341109; DOI=10.1074/jbc.272.43.26811;
RA Schwarz G., Boxer D.H., Mendel R.R.;
RT "Molybdenum cofactor biosynthesis. The plant protein Cnx1 binds
RT molybdopterin with high affinity.";
RL J. Biol. Chem. 272:26811-26814(1997).
RN [6]
RP MUTAGENESIS OF ASP-515; VAL-557 AND ASN-597.
RX PubMed=10823911; DOI=10.1073/pnas.110568497;
RA Kuper J., Palmer T., Mendel R.R., Schwarz G.;
RT "Mutations in the molybdenum cofactor biosynthetic protein Cnx1G from
RT Arabidopsis thaliana define functions for molybdopterin binding, molybdenum
RT insertion, and molybdenum cofactor stabilization.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:6475-6480(2000).
RN [7]
RP FUNCTION OF DOMAIN G AS MPT ADENYLYLTRANSFERASE, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, COFACTOR, MUTAGENESIS, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=15504727; DOI=10.1074/jbc.m409862200;
RA Llamas A., Mendel R.R., Schwarz G.;
RT "Synthesis of adenylated molybdopterin: an essential step for molybdenum
RT insertion.";
RL J. Biol. Chem. 279:55241-55246(2004).
RN [8]
RP FUNCTION OF DOMAIN E AS MOLYBDENUM--MPT-AMP LIGASE, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND REACTION MECHANISM.
RX PubMed=16636046; DOI=10.1074/jbc.m601415200;
RA Llamas A., Otte T., Multhaup G., Mendel R.R., Schwarz G.;
RT "The Mechanism of nucleotide-assisted molybdenum insertion into
RT molybdopterin. A novel route toward metal cofactor assembly.";
RL J. Biol. Chem. 281:18343-18350(2006).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 462-623, AND SUBUNIT.
RX PubMed=11554796; DOI=10.1006/jmbi.2001.4952;
RA Schwarz G., Schrader N., Mendel R.R., Hecht H.-J., Schindelin H.;
RT "Crystal structures of human gephyrin and plant Cnx1 G domains: comparative
RT analysis and functional implications.";
RL J. Mol. Biol. 312:405-418(2001).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 462-628 OF MUTANTS ALA/ASP-542 AND
RP ALA-573, FUNCTION, MUTAGENESIS OF SER-475; ASP-485; ASP-515; THR-542;
RP ARG-547 AND SER-573, AND SUBUNIT.
RX PubMed=12590921; DOI=10.1016/s0003-9861(02)00714-2;
RA Kuper J., Winking J., Hecht H.-J., Mendel R.R., Schwarz G.;
RT "The active site of the molybdenum cofactor biosynthetic protein domain
RT Cnx1G.";
RL Arch. Biochem. Biophys. 411:36-46(2003).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 462-623 OF WILD-TYPE AND MUTANT
RP ALA-583 IN COMPLEX WITH SUBSTRATE, FUNCTION, COFACTOR, ACTIVITY REGULATION,
RP AND SUBUNIT.
RX PubMed=15306815; DOI=10.1038/nature02681;
RA Kuper J., Llamas A., Hecht H.-J., Mendel R.R., Schwarz G.;
RT "Structure of the molybdopterin-bound Cnx1G domain links molybdenum and
RT copper metabolism.";
RL Nature 430:803-806(2004).
CC -!- FUNCTION: Catalyzes two steps in the biosynthesis of the molybdenum
CC cofactor. In the first step, molybdopterin is adenylated. Subsequently,
CC molybdate is inserted into adenylated molybdopterin and AMP is
CC released. {ECO:0000269|PubMed:12590921, ECO:0000269|PubMed:15306815,
CC ECO:0000269|PubMed:15504727, ECO:0000269|PubMed:16636046}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-
CC molybdopterin; Xref=Rhea:RHEA:35047, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36264, ChEBI:CHEBI:62727,
CC ChEBI:CHEBI:71302, ChEBI:CHEBI:456215; EC=2.10.1.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + molybdopterin = adenylyl-molybdopterin +
CC diphosphate; Xref=Rhea:RHEA:31331, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58698,
CC ChEBI:CHEBI:62727; EC=2.7.7.75;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15306815, ECO:0000269|PubMed:15504727};
CC -!- ACTIVITY REGULATION: Inhibited by copper and tungsten.
CC {ECO:0000269|PubMed:15306815}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=62 uM for ATP for domain G {ECO:0000269|PubMed:15504727,
CC ECO:0000269|PubMed:16636046};
CC KM=133 uM for Zn(2+) for domain E {ECO:0000269|PubMed:15504727,
CC ECO:0000269|PubMed:16636046};
CC KM=255 uM for Mg(2+) for domain E {ECO:0000269|PubMed:15504727,
CC ECO:0000269|PubMed:16636046};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC -!- SUBUNIT: The G domain: homotrimer or homohexamer. The E domain:
CC homodimer. {ECO:0000269|PubMed:11554796, ECO:0000269|PubMed:12590921,
CC ECO:0000269|PubMed:15306815, ECO:0000269|PubMed:9341109}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MoeA family.
CC {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; L47323; AAA97413.1; -; mRNA.
DR EMBL; AJ236870; CAB38312.1; -; Genomic_DNA.
DR EMBL; AC069325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF296834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92917.1; -; Genomic_DNA.
DR RefSeq; NP_197599.1; NM_122108.4.
DR PDB; 1EAV; X-ray; 2.60 A; A/B/C/D/E/F/G/H=462-623.
DR PDB; 1O8N; X-ray; 2.80 A; A/B/C=462-628.
DR PDB; 1O8O; X-ray; 2.70 A; A/B/C=462-628.
DR PDB; 1O8Q; X-ray; 2.60 A; A/B/C/D/E/F/G/H=462-628.
DR PDB; 1UUX; X-ray; 1.60 A; A=462-623.
DR PDB; 1UUY; X-ray; 1.45 A; A=462-624.
DR PDB; 5G2R; X-ray; 2.45 A; A=1-451.
DR PDB; 5G2S; X-ray; 2.84 A; A=1-451.
DR PDB; 6ETD; X-ray; 1.72 A; A=1-452.
DR PDB; 6ETF; X-ray; 1.78 A; A=1-452.
DR PDB; 6ETH; X-ray; 1.64 A; A=1-452.
DR PDB; 6GAX; X-ray; 1.77 A; A=1-452.
DR PDB; 6GB0; X-ray; 1.81 A; A=1-452.
DR PDB; 6GB4; X-ray; 1.65 A; A=1-450.
DR PDB; 6GB9; X-ray; 1.67 A; A=1-450.
DR PDB; 6GBC; X-ray; 1.59 A; A=1-450.
DR PDB; 6GBF; X-ray; 1.71 A; A=1-450.
DR PDB; 6Q32; X-ray; 1.39 A; A=1-452.
DR PDB; 6RMS; Other; 1.74 A; A=16-442.
DR PDBsum; 1EAV; -.
DR PDBsum; 1O8N; -.
DR PDBsum; 1O8O; -.
DR PDBsum; 1O8Q; -.
DR PDBsum; 1UUX; -.
DR PDBsum; 1UUY; -.
DR PDBsum; 5G2R; -.
DR PDBsum; 5G2S; -.
DR PDBsum; 6ETD; -.
DR PDBsum; 6ETF; -.
DR PDBsum; 6ETH; -.
DR PDBsum; 6GAX; -.
DR PDBsum; 6GB0; -.
DR PDBsum; 6GB4; -.
DR PDBsum; 6GB9; -.
DR PDBsum; 6GBC; -.
DR PDBsum; 6GBF; -.
DR PDBsum; 6Q32; -.
DR PDBsum; 6RMS; -.
DR AlphaFoldDB; Q39054; -.
DR SASBDB; Q39054; -.
DR SMR; Q39054; -.
DR BioGRID; 17499; 3.
DR STRING; 3702.AT5G20990.1; -.
DR iPTMnet; Q39054; -.
DR PaxDb; Q39054; -.
DR PRIDE; Q39054; -.
DR ProteomicsDB; 220540; -.
DR EnsemblPlants; AT5G20990.1; AT5G20990.1; AT5G20990.
DR GeneID; 832224; -.
DR Gramene; AT5G20990.1; AT5G20990.1; AT5G20990.
DR KEGG; ath:AT5G20990; -.
DR Araport; AT5G20990; -.
DR TAIR; locus:2147157; AT5G20990.
DR eggNOG; KOG2371; Eukaryota.
DR HOGENOM; CLU_010186_6_1_1; -.
DR InParanoid; Q39054; -.
DR OMA; HRAIVRW; -.
DR OrthoDB; 1114121at2759; -.
DR PhylomeDB; Q39054; -.
DR BRENDA; 2.10.1.1; 399.
DR BRENDA; 2.7.7.75; 399.
DR UniPathway; UPA00344; -.
DR EvolutionaryTrace; Q39054; -.
DR PRO; PR:Q39054; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q39054; baseline and differential.
DR Genevisible; Q39054; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030151; F:molybdenum ion binding; IDA:TAIR.
DR GO; GO:0061598; F:molybdopterin adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0061599; F:molybdopterin molybdotransferase activity; IBA:GO_Central.
DR GO; GO:0008940; F:nitrate reductase activity; IMP:CAFA.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IMP:TAIR.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IBA:GO_Central.
DR GO; GO:0018315; P:molybdenum incorporation into molybdenum-molybdopterin complex; IBA:GO_Central.
DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IBA:GO_Central.
DR GO; GO:0010038; P:response to metal ion; IMP:CAFA.
DR CDD; cd00887; MoeA; 1.
DR CDD; cd00886; MogA_MoaB; 1.
DR Gene3D; 2.40.340.10; -; 1.
DR Gene3D; 3.40.980.10; -; 2.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR008284; MoCF_biosynth_CS.
DR InterPro; IPR038987; MoeA-like.
DR InterPro; IPR005111; MoeA_C_domain_IV.
DR InterPro; IPR036688; MoeA_C_domain_IV_sf.
DR InterPro; IPR005110; MoeA_linker/N.
DR InterPro; IPR036135; MoeA_linker/N_sf.
DR PANTHER; PTHR10192; PTHR10192; 2.
DR Pfam; PF00994; MoCF_biosynth; 2.
DR Pfam; PF03454; MoeA_C; 1.
DR Pfam; PF03453; MoeA_N; 1.
DR SMART; SM00852; MoCF_biosynth; 2.
DR SUPFAM; SSF53218; SSF53218; 2.
DR SUPFAM; SSF63867; SSF63867; 1.
DR SUPFAM; SSF63882; SSF63882; 1.
DR TIGRFAMs; TIGR00177; molyb_syn; 2.
DR PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
DR PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Magnesium; Metal-binding; Molybdenum;
KW Molybdenum cofactor biosynthesis; Multifunctional enzyme;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..670
FT /note="Molybdopterin biosynthesis protein CNX1"
FT /id="PRO_0000170963"
FT REGION 19..439
FT /note="MPT Mo-transferase"
FT REGION 466..620
FT /note="MPT adenylyltransferase"
FT REGION 624..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 485
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT BINDING 486
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT BINDING 541
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT BINDING 542..543
FT /ligand="substrate"
FT BINDING 573
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15306815"
FT BINDING 600
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT BINDING 600
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15306815"
FT BINDING 607
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15306815"
FT MUTAGEN 475
FT /note="S->D: Reduced molybdopterin binding. Loss of
FT adenylation activity."
FT /evidence="ECO:0000269|PubMed:12590921"
FT MUTAGEN 485
FT /note="D->S: Reduced molybdopterin binding. Loss of
FT adenylation activity."
FT /evidence="ECO:0000269|PubMed:12590921"
FT MUTAGEN 515
FT /note="D->H,N: Almost normal molybdopterin binding. Loss
FT adenylation activity."
FT /evidence="ECO:0000269|PubMed:10823911,
FT ECO:0000269|PubMed:12590921"
FT MUTAGEN 542
FT /note="T->A: Strongly reduced molybdopterin binding.
FT Reduced activity."
FT /evidence="ECO:0000269|PubMed:12590921"
FT MUTAGEN 542
FT /note="T->D,N: Loss of molybdopterin binding. Loss of
FT activity."
FT /evidence="ECO:0000269|PubMed:12590921"
FT MUTAGEN 542
FT /note="T->S: Reduced molybdopterin binding. No effect on
FT activity."
FT /evidence="ECO:0000269|PubMed:12590921"
FT MUTAGEN 542
FT /note="T->V: Strongly reduced molybdopterin binding. No
FT effect on activity."
FT /evidence="ECO:0000269|PubMed:12590921"
FT MUTAGEN 547
FT /note="R->E: No effect on molybdopterin binding. Clear
FT reduction in adenylation activity."
FT /evidence="ECO:0000269|PubMed:12590921"
FT MUTAGEN 557
FT /note="V->G: Impaired folding. Loss of activity."
FT /evidence="ECO:0000269|PubMed:10823911"
FT MUTAGEN 573
FT /note="S->A: Loss of molybdopterin binding. Loss of
FT activity."
FT /evidence="ECO:0000269|PubMed:12590921"
FT MUTAGEN 583
FT /note="S->A: No effect on activity."
FT /evidence="ECO:0000269|PubMed:15504727"
FT MUTAGEN 597
FT /note="N->L: Loss of molybdopterin binding. Loss of
FT activity."
FT /evidence="ECO:0000269|PubMed:10823911"
FT CONFLICT 113
FT /note="D -> V (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="S -> A (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="S -> L (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:6Q32"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:6Q32"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 77..88
FT /evidence="ECO:0007829|PDB:6Q32"
FT TURN 89..94
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:6Q32"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:6ETH"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:6Q32"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:6Q32"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:6Q32"
FT HELIX 219..229
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 234..240
FT /evidence="ECO:0007829|PDB:6Q32"
FT HELIX 244..256
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 260..271
FT /evidence="ECO:0007829|PDB:6Q32"
FT HELIX 276..283
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:6Q32"
FT TURN 295..298
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 316..322
FT /evidence="ECO:0007829|PDB:6Q32"
FT HELIX 326..344
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 354..361
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 371..381
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 389..394
FT /evidence="ECO:0007829|PDB:6Q32"
FT HELIX 403..406
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:6ETH"
FT STRAND 427..432
FT /evidence="ECO:0007829|PDB:6Q32"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:6Q32"
FT STRAND 466..474
FT /evidence="ECO:0007829|PDB:1UUY"
FT HELIX 476..479
FT /evidence="ECO:0007829|PDB:1UUY"
FT HELIX 487..497
FT /evidence="ECO:0007829|PDB:1UUY"
FT TURN 498..503
FT /evidence="ECO:0007829|PDB:1UUY"
FT STRAND 504..513
FT /evidence="ECO:0007829|PDB:1UUY"
FT HELIX 517..529
FT /evidence="ECO:0007829|PDB:1UUY"
FT STRAND 534..540
FT /evidence="ECO:0007829|PDB:1UUY"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:1UUY"
FT HELIX 550..557
FT /evidence="ECO:0007829|PDB:1UUY"
FT STRAND 559..561
FT /evidence="ECO:0007829|PDB:1UUY"
FT HELIX 563..576
FT /evidence="ECO:0007829|PDB:1UUY"
FT HELIX 578..582
FT /evidence="ECO:0007829|PDB:1UUY"
FT STRAND 587..590
FT /evidence="ECO:0007829|PDB:1UUY"
FT STRAND 593..598
FT /evidence="ECO:0007829|PDB:1UUY"
FT HELIX 604..623
FT /evidence="ECO:0007829|PDB:1UUY"
SQ SEQUENCE 670 AA; 71279 MW; 4405722BB9C5EF02 CRC64;
MEGQGCCGGG GGKTEMIPTE EALRIVFGVS KRLPPVIVSL YEALGKVLAE DIRAPDPLPP
YPASVKDGYA VVASDGPGEY PVITESRAGN DGLGVTVTPG TVAYVTTGGP IPDGADAVVQ
VEDTKVIGDV STESKRVKIL IQTKKGTDIR RVGCDIEKDA TVLTTGERIG ASEIGLLATA
GVTMVKVYPM PIVAILSTGD ELVEPTAGTL GRGQIRDSNR AMLVAAVMQQ QCKVVDLGIV
RDDRKELEKV LDEAVSSGVD IILTSGGVSM GDRDFVKPLL EEKGKVYFSK VLMKPGKPLT
FAEIRAKPTE SMLGKTVLAF GLPGNPVSCL VCFNIFVVPT IRQLAGWTSP HPLRVRLRLQ
EPIKSDPIRP EFHRAIIKWK DNDGSGTPGF VAESTGHQMS SRLLSMRSAN ALLELPATGN
VLSAGSSVSA IIVSDISAFS IDKKASLSEP GSIRKEKKYD EVPGPEYKVA ILTVSDTVSA
GAGPDRSGPR AVSVVDSSSE KLGGAKVVAT AVVPDEVERI KDILQKWSDV DEMDLILTLG
GTGFTPRDVT PEATKKVIER ETPGLLFVMM QESLKITPFA MLSRSAAGIR GSTLIINMPG
NPNAVAECME ALLPALKHAL KQIKGDKREK HPKHIPHAEA TLPTDTWDQS YKSAYETGEK
KEEAGCSCTH
