AGO_METJA
ID AGO_METJA Reviewed; 713 AA.
AC Q58717;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Protein argonaute {ECO:0000303|PubMed:24442234};
DE Short=MjAgo {ECO:0000303|PubMed:24442234};
DE EC=3.1.25.- {ECO:0000269|PubMed:24442234};
GN OrderedLocusNames=MJ1321;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION AS AN ENDONUCLEASE, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, AND DNA-BINDING.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=24442234; DOI=10.4161/rna.27446;
RA Zander A., Holzmeister P., Klose D., Tinnefeld P., Grohmann D.;
RT "Single-molecule FRET supports the two-state model of Argonaute action.";
RL RNA Biol. 11:45-56(2014).
RN [3]
RP FUNCTION, SUBSTRATE AND TARGET BINDING, AND MUTAGENESIS OF TYR-442.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=27741323; DOI=10.1371/journal.pone.0164695;
RA Willkomm S., Zander A., Grohmann D., Restle T.;
RT "Mechanistic insights into archaeal and human Argonaute substrate binding
RT and cleavage properties.";
RL PLoS ONE 11:E0164695-E0164695(2016).
RN [4]
RP FUNCTION, ACTIVITY REGULATION, INDUCTION, AND MUTAGENESIS OF TYR-194;
RP HIS-213; TYR-217; GLU-246; ASP-438; LYS-483 AND GLU-541.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=28319081; DOI=10.1038/nmicrobiol.2017.34;
RA Zander A., Willkomm S., Ofer S., van Wolferen M., Egert L., Buchmeier S.,
RA Stoeckl S., Tinnefeld P., Schneider S., Klingl A., Albers S.V., Werner F.,
RA Grohmann D.;
RT "Guide-independent DNA cleavage by archaeal Argonaute from
RT Methanocaldococcus jannaschii.";
RL Nat. Microbiol. 2:17034-17034(2017).
RN [5] {ECO:0007744|PDB:5G5S, ECO:0007744|PDB:5G5T}
RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) IN COMPLEX WITH METAL WITH AND
RP WITHOUT GUIDE DNA, FUNCTION, COFACTOR, DOMAIN, MUTAGENESIS OF TYR-194;
RP HIS-213; TYR-217; GLU-246; LEU-270; TRP-274; LYS-435; ASP-438; GLN-457;
RP ASN-458; GLN-479; LYS-483; PHE-572; GLN-574 AND ASN-575, AND DNA-BINDING.
RX PubMed=28319084; DOI=10.1038/nmicrobiol.2017.35;
RA Willkomm S., Oellig C.A., Zander A., Restle T., Keegan R., Grohmann D.,
RA Schneider S.;
RT "Structural and mechanistic insights into an archaeal DNA-guided Argonaute
RT protein.";
RL Nat. Microbiol. 2:17035-17035(2017).
CC -!- FUNCTION: An endodeoxyribonuclease that may play a role in defense
CC against invading genetic elements. Uses short DNA sequences as guides
CC to bind complementary target strands, resulting in slicing of the
CC target DNA (PubMed:24442234, PubMed:27741323, PubMed:28319081,
CC PubMed:28319084). Also has guide-independent activity on target DNA
CC (PubMed:28319081). Probably a first round of guide-independent activity
CC on an invading plasmid or virus would generate guide DNAs for
CC subsequent, more efficient, guide-dependent degradation of invading
CC nucleic acids (PubMed:28319081). Endonucleolytically cleaves DNA in
CC short dsDNA (the guide DNA indicates where to cleave on the target DNA)
CC (PubMed:24442234, PubMed:27741323, PubMed:28319081, PubMed:28319084).
CC Efficient guide-dependent target DNA cleavage requires a minimal length
CC of 15 bp and is maximal at 19 bp (PubMed:28319081). Prefers guide DNA
CC with 5'-phosphorylated purines and 3'-pyrimidines; changing these bases
CC alters the cleavage activity and patterns (PubMed:28319084). Has no
CC activity on substrate with a mismatch at positions 10 and 11, ssDNA or
CC RNA, nor on DNA-RNA hybrids (PubMed:24442234). Digests longer (750 bp)
CC dsDNA as well as circular plasmid and naked genomic DNA, but not
CC chromatin, in a guide DNA-independent manner (PubMed:28319081).
CC Addition of endogenous histone A3 protects DNA from cleavage, while
CC cleavage is insensitive to methylation (PubMed:28319081). When plasmid
CC encoding active or mutated protein (Ala-541) is transformed into
CC Sulfolobus acidocaldarius about 25-fold fewer transformants are found
CC with active protein; reduced levels of plasmid are found in wild-type
CC transformed cells. While S.acidocaldarius grows at a similar
CC temperature to M.jannaschii (70 to 80 degrees Celsius) it has very
CC different histone-like proteins, which presumably do not protect
CC against MjAgo (PubMed:28319081). Binds ssDNA, dsDNA and DNA-RNA
CC hybrids; binding is most efficient with dsDNA (PubMed:24442234).
CC {ECO:0000269|PubMed:24442234, ECO:0000269|PubMed:27741323,
CC ECO:0000269|PubMed:28319081, ECO:0000269|PubMed:28319084,
CC ECO:0000305|PubMed:28319081}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:24442234, ECO:0000269|PubMed:28319084};
CC Note=Also liganded by DNA (PubMed:28319084).
CC {ECO:0000269|PubMed:28319084};
CC -!- ACTIVITY REGULATION: DNA cleavage is inhibited by EDTA.
CC {ECO:0000269|PubMed:24442234, ECO:0000269|PubMed:28319081}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is over 75 degrees Celsius for DNA cleavage, DNA-
CC binding occurs below that. {ECO:0000269|PubMed:24442234};
CC -!- INDUCTION: Constitutively expressed (at protein level)
CC (PubMed:28319081). {ECO:0000305|PubMed:28319081}.
CC -!- DOMAIN: Has 4 structurally distinct domains; N-terminal, PAZ (binds the
CC 3'-end of guide DNA), Mid (binds the phosphorylated 5'-end of guide
CC DNA) and PIWI (binds near the 5'-end of guide DNA) arranged in a
CC bilobal manner (PubMed:28319084). Upon binding of guide DNA the PAZ and
CC Mid domains separate, opening a channel probably for target DNA-
CC binding; a smaller channel also opens between the N-terminal and PIWI
CC domains (PubMed:28319084). The N-terminal and PAZ domains undergo
CC further major rearrangement when the binary Ago-guide DNA complex binds
CC target DNA; the PAZ domain binds the 3'-end of guide DNA in the absence
CC of target, upon ternary complex formation it is probably the N-terminal
CC domain that binds that end of the dsDNA (PubMed:24442234).
CC {ECO:0000269|PubMed:28319084, ECO:0000305|PubMed:24442234}.
CC -!- SIMILARITY: Belongs to the argonaute family. Long pAgo subfamily.
CC {ECO:0000305}.
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DR EMBL; L77117; AAB99334.1; -; Genomic_DNA.
DR PIR; H64464; H64464.
DR RefSeq; WP_010870838.1; NC_000909.1.
DR PDB; 5G5S; X-ray; 2.29 A; A=1-713.
DR PDB; 5G5T; X-ray; 2.85 A; A=1-713.
DR PDBsum; 5G5S; -.
DR PDBsum; 5G5T; -.
DR AlphaFoldDB; Q58717; -.
DR SMR; Q58717; -.
DR STRING; 243232.MJ_1321; -.
DR PRIDE; Q58717; -.
DR EnsemblBacteria; AAB99334; AAB99334; MJ_1321.
DR GeneID; 1452223; -.
DR KEGG; mja:MJ_1321; -.
DR eggNOG; arCOG03890; Archaea.
DR HOGENOM; CLU_362759_0_0_2; -.
DR OMA; NILWENW; -.
DR OrthoDB; 11100at2157; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR036085; PAZ_dom_sf.
DR InterPro; IPR003165; Piwi.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF02171; Piwi; 1.
DR SMART; SM00950; Piwi; 1.
DR SUPFAM; SSF101690; SSF101690; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50822; PIWI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; DNA-binding; Endonuclease; Hydrolase;
KW Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..713
FT /note="Protein argonaute"
FT /id="PRO_0000107275"
FT DOMAIN 426..699
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150,
FT ECO:0000269|PubMed:28319084, ECO:0000305|PubMed:24442234"
FT REGION 18..129
FT /note="N-terminal structural domain"
FT /evidence="ECO:0000269|PubMed:28319084,
FT ECO:0000305|PubMed:24442234"
FT REGION 163..258
FT /note="PAZ structural domain"
FT /evidence="ECO:0000269|PubMed:28319084,
FT ECO:0000305|PubMed:24442234"
FT REGION 213..218
FT /note="Binds 3'-end of guide DNA"
FT /evidence="ECO:0000269|PubMed:28319084,
FT ECO:0007744|PDB:5G5T"
FT REGION 346..488
FT /note="Mid structural domain"
FT /evidence="ECO:0000269|PubMed:28319084,
FT ECO:0000305|PubMed:24442234"
FT REGION 457..460
FT /note="Binds 5'-phosphorylated end of guide DNA"
FT /evidence="ECO:0000269|PubMed:28319084,
FT ECO:0007744|PDB:5G5T"
FT REGION 625..632
FT /note="Binds 5'-phosphorylated end of guide DNA"
FT /evidence="ECO:0000269|PubMed:28319084,
FT ECO:0007744|PDB:5G5T"
FT REGION 678..679
FT /note="Binds 5'-phosphorylated end of guide DNA"
FT /evidence="ECO:0000269|PubMed:28319084,
FT ECO:0007744|PDB:5G5T"
FT BINDING 457
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0007744|PDB:5G5T"
FT BINDING 479
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000305|PubMed:28319084"
FT BINDING 483
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000305|PubMed:28319084"
FT SITE 107
FT /note="Interacts with guide DNA"
FT /evidence="ECO:0000269|PubMed:28319084,
FT ECO:0007744|PDB:5G5T"
FT SITE 157
FT /note="Interacts with guide DNA"
FT /evidence="ECO:0000269|PubMed:28319084,
FT ECO:0007744|PDB:5G5T"
FT SITE 191
FT /note="Interacts with guide DNA"
FT /evidence="ECO:0000269|PubMed:28319084,
FT ECO:0007744|PDB:5G5T"
FT SITE 194
FT /note="Interacts with 3'-end of guide DNA"
FT /evidence="ECO:0000269|PubMed:28319084,
FT ECO:0007744|PDB:5G5T"
FT SITE 217
FT /note="Interacts with guide DNA"
FT /evidence="ECO:0000269|PubMed:28319084,
FT ECO:0007744|PDB:5G5T"
FT SITE 479
FT /note="Interacts with guide DNA"
FT /evidence="ECO:0000269|PubMed:28319084,
FT ECO:0007744|PDB:5G5T"
FT SITE 669
FT /note="Interacts with guide DNA"
FT /evidence="ECO:0000269|PubMed:28319084,
FT ECO:0007744|PDB:5G5T"
FT MUTAGEN 194
FT /note="Y->A: No guide-independent plasmid cleavage. Loss of
FT guide-dependent cleavage of target DNA."
FT /evidence="ECO:0000269|PubMed:28319081,
FT ECO:0000269|PubMed:28319084"
FT MUTAGEN 213
FT /note="H->A: Significantly reduced guide-independent
FT plasmid cleavage. Decreased guide-dependent cleavage of
FT target DNA."
FT /evidence="ECO:0000269|PubMed:28319081,
FT ECO:0000269|PubMed:28319084"
FT MUTAGEN 217
FT /note="Y->A: Significantly reduced guide-independent
FT plasmid cleavage. Decreased guide-dependent cleavage of
FT target DNA."
FT /evidence="ECO:0000269|PubMed:28319081,
FT ECO:0000269|PubMed:28319084"
FT MUTAGEN 246
FT /note="E->A: Nearly complete loss of guide-independent
FT plasmid cleavage. Loss of guide-dependent cleavage of
FT target DNA."
FT /evidence="ECO:0000269|PubMed:28319081,
FT ECO:0000269|PubMed:28319084"
FT MUTAGEN 270
FT /note="L->P: Loss of guide-dependent cleavage of target DNA
FT when guide DNA starts with 5'-dT but not 5'-dG."
FT /evidence="ECO:0000269|PubMed:28319084"
FT MUTAGEN 274
FT /note="W->V: No change in guide-dependent cleavage of
FT target DNA."
FT /evidence="ECO:0000269|PubMed:28319084"
FT MUTAGEN 435
FT /note="K->A: Wild-type guide-dependent cleavage of target
FT DNA."
FT /evidence="ECO:0000269|PubMed:28319084"
FT MUTAGEN 438
FT /note="D->P: No guide-independent plasmid cleavage.
FT Decreased guide-dependent cleavage of target DNA."
FT /evidence="ECO:0000269|PubMed:28319081,
FT ECO:0000269|PubMed:28319084"
FT MUTAGEN 442
FT /note="Y->A: Alters binding kinetics of guide DNA, probably
FT due to loss of Mid domain binding to 5'-end of guide."
FT /evidence="ECO:0000269|PubMed:28319081"
FT MUTAGEN 457
FT /note="Q->A: Loss of guide-dependent cleavage of target
FT DNA."
FT /evidence="ECO:0000269|PubMed:28319084"
FT MUTAGEN 458
FT /note="N->A: Loss of guide-dependent cleavage of target
FT DNA."
FT /evidence="ECO:0000269|PubMed:28319084"
FT MUTAGEN 479
FT /note="Q->A: Decreased guide-dependent cleavage of target
FT DNA."
FT /evidence="ECO:0000269|PubMed:28319084"
FT MUTAGEN 483
FT /note="K->A: No guide-independent plasmid cleavage. Loss of
FT guide-dependent cleavage of target DNA."
FT /evidence="ECO:0000269|PubMed:28319081,
FT ECO:0000269|PubMed:28319084"
FT MUTAGEN 541
FT /note="E->A: No guide-dependent or -independent cleavage of
FT target DNA."
FT /evidence="ECO:0000269|PubMed:28319081"
FT MUTAGEN 572
FT /note="F->A: Loss of guide-dependent cleavage of target DNA
FT when guide DNA starts with 5'-dT but not 5'-dG."
FT /evidence="ECO:0000269|PubMed:28319084"
FT MUTAGEN 574
FT /note="Q->A: Loss of guide-dependent cleavage of target DNA
FT when guide DNA starts with 5'-dT but not 5'-dG."
FT /evidence="ECO:0000269|PubMed:28319084"
FT MUTAGEN 575
FT /note="N->A: Loss of guide-dependent cleavage of target DNA
FT when guide DNA starts with 5'-dT but not 5'-dG."
FT /evidence="ECO:0000269|PubMed:28319084"
FT TURN 2..4
FT /evidence="ECO:0007829|PDB:5G5T"
FT STRAND 5..15
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:5G5S"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:5G5T"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 112..120
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:5G5T"
FT STRAND 132..145
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 148..163
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:5G5S"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 173..177
FT /evidence="ECO:0007829|PDB:5G5S"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 189..198
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 223..229
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:5G5T"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:5G5T"
FT HELIX 264..269
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 278..291
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:5G5S"
FT TURN 349..353
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 355..363
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 364..369
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 370..388
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 410..418
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 426..432
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 436..439
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 440..450
FT /evidence="ECO:0007829|PDB:5G5S"
FT TURN 451..453
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 454..460
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 461..465
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 468..470
FT /evidence="ECO:0007829|PDB:5G5T"
FT HELIX 471..483
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 490..493
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 498..504
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 514..523
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 528..535
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 545..554
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 564..571
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 575..588
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 591..600
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 611..616
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 619..623
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 634..643
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 646..650
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 654..664
FT /evidence="ECO:0007829|PDB:5G5S"
FT STRAND 672..677
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 682..695
FT /evidence="ECO:0007829|PDB:5G5S"
FT HELIX 702..706
FT /evidence="ECO:0007829|PDB:5G5S"
SQ SEQUENCE 713 AA; 84583 MW; EB0B3265C600DF2D CRC64;
MVLNKVTYKI NAYKIKEEFI PKEVHFYRIK SFVNEAFNFY RFVNFYGGMI INKKDKSFVL
PYKVDNKVLK YKDGNNEIPI DIEYIKSLKL EYVKPEIAEK LVRGYLKSVH KIEPELSRII
KNIRKHKVVE NIKVESYCEY EVKKHDGDYY LILNFRHTAS ITKHLWDFVN RDKALLEEYV
GKKIIFKPNP KVRYTISLVD APNPQKIEEI MSHIIKYYKW SEDMVKSTFG EIDYNQPIMY
CEEILEPFAP QFCNLVFYMD ELDSYILKEL QSYWRLSNEN KGKIINEIAK KLRFIDNTPK
ELEFMKFNNT PLLVKDVNKN PTKIYSTNTL FTWIYNQNAK IYLPYDVPEI IRNKNLLTYI
LIDEEIKDEL KAIKDKVNKM FRNYNKIANK TELPKFNYAN RWKYFSTDDI RGIIKEIKSE
FNDEICFALI IGKEKYKDND YYEILKKQLF DLKIISQNIL WENWRKDDKG YMTNNLLIQI
MGKLGIKYFI LDSKTPYDYI MGLDTGLGIF GNHRVGGCTV VYDSEGKIRR IQPIETPAPG
ERLHLPYVIE YLENKANIDM ENKNILFLRD GFIQNSERND LKEISKELNS NIEVISIRKN
NKYKVFTSDY RIGSVFGNDG IFLPHKTPFG SNPVKLSTWL RFNCGNEEGL KINESIMQLL
YDLTKMNYSA LYGEGRYLRI PAPIHYADKF VKALGKNWKI DEELLKHGFL YFI
