MCM2_YEAST
ID MCM2_YEAST Reviewed; 868 AA.
AC P29469; D6VPX7;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=DNA replication licensing factor MCM2;
DE EC=3.6.4.12;
DE AltName: Full=Minichromosome maintenance protein 2;
GN Name=MCM2; OrderedLocusNames=YBL023C; ORFNames=YBL0438;
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 MUTAGENESIS OF CYS-364 AND CYS-367.
RX PubMed=2044961; DOI=10.1101/gad.5.6.944;
RA Yan H., Gibson S., Tye B.K.;
RT "Mcm2 and Mcm3, two proteins important for ARS activity, are related in
RT structure and function.";
RL Genes Dev. 5:944-957(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7725803; DOI=10.1002/yea.320101217;
RA van Dyck L., Jonniaux J.-L., Barreiros T.D.M., Kleine K., Goffeau A.;
RT "Analysis of a 17.4 kb DNA segment of yeast chromosome II encompassing the
RT ribosomal protein L19 as well as proteins with homologies to components of
RT the hnRNP and snRNP complexes and to the human proliferation-associated
RT p120 antigen.";
RL Yeast 10:1663-1673(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP RECONSTITUTION OF THE MCM2-7 COMPLEX, HELICASE ACTIVITY OF THE MCM2-7
RP COMPLEX, AND MUTAGENESIS OF LYS-549 AND ARG-676.
RX PubMed=18657510; DOI=10.1016/j.molcel.2008.05.020;
RA Bochman M.L., Schwacha A.;
RT "The Mcm2-7 complex has in vitro helicase activity.";
RL Mol. Cell 31:287-293(2008).
RN [5]
RP IDENTIFICATION IN THE MCM2-7 COMPLEX, FUNCTION OF THE MCM2-7 COMPLEX, AND
RP ELECTRON MICROSCOPY OF THE MCM2-7 COMPLEX.
RX PubMed=19896182; DOI=10.1016/j.cell.2009.10.015;
RA Remus D., Beuron F., Tolun G., Griffith J.D., Morris E.P., Diffley J.F.;
RT "Concerted loading of Mcm2-7 double hexamers around DNA during DNA
RT replication origin licensing.";
RL Cell 139:719-730(2009).
RN [6]
RP IDENTIFICATION IN THE MCM2-7 COMPLEX, FUNCTION OF THE MCM2-7 COMPLEX, AND
RP ELECTRON MICROSCOPY OF THE MCM2-7 COMPLEX.
RX PubMed=19910535; DOI=10.1073/pnas.0911500106;
RA Evrin C., Clarke P., Zech J., Lurz R., Sun J., Uhle S., Li H., Stillman B.,
RA Speck C.;
RT "A double-hexameric MCM2-7 complex is loaded onto origin DNA during
RT licensing of eukaryotic DNA replication.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:20240-20245(2009).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-85.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8276800; DOI=10.1016/s0021-9258(17)42340-4;
RA van Dyck L., Pearce D.A., Sherman F.;
RT "PIM1 encodes a mitochondrial ATP-dependent protease that is required for
RT mitochondrial function in the yeast Saccharomyces cerevisiae.";
RL J. Biol. Chem. 269:238-242(1994).
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]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-16; SER-23; SER-164
RP AND SER-170, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which
CC is the putative replicative helicase essential for 'once per cell
CC cycle' DNA replication initiation and elongation in eukaryotic cells.
CC The active ATPase sites in the MCM2-7 ring are formed through the
CC interaction surfaces of two neighboring subunits such that a critical
CC structure of a conserved arginine finger motif is provided in trans
CC relative to the ATP-binding site of the Walker A box of the adjacent
CC subunit. The six ATPase active sites, however, are likely to contribute
CC differentially to the complex helicase activity; specifically the MCM2-
CC MCM5 association is proposed to be reversible and to mediate a open
CC ring conformation which may facilitate DNA loading. Once loaded onto
CC DNA, double hexamers can slide on dsDNA in the absence of ATPase
CC activity. Necessary for cell growth. {ECO:0000269|PubMed:19896182,
CC ECO:0000269|PubMed:19910535}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Component of the MCM2-7 complex. The complex forms a toroidal
CC hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-
CC MCM3-MCM5; loaded onto DNA, forms a head-head double hexamer.
CC {ECO:0000269|PubMed:19896182, ECO:0000269|PubMed:19910535}.
CC -!- INTERACTION:
CC P29469; P09119: CDC6; NbExp=4; IntAct=EBI-10533, EBI-4447;
CC P29469; Q08496: DIA2; NbExp=4; IntAct=EBI-10533, EBI-31943;
CC P29469; P30665: MCM4; NbExp=15; IntAct=EBI-10533, EBI-4326;
CC P29469; Q12306: SMT3; NbExp=2; IntAct=EBI-10533, EBI-17490;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 1690 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Early fractionation of eukaryotic MCM proteins yielded a
CC variety of dimeric, trimeric and tetrameric complexes with unclear
CC biological significance. Specifically a MCM467 subcomplex is shown to
CC have in vitro helicase activity which is inhibited by the MCM2 subunit.
CC The MCM2-7 hexamer is the proposed physiological active complex.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; X77291; CAA54503.1; -; Genomic_DNA.
DR EMBL; X53539; CAA37615.1; -; Genomic_DNA.
DR EMBL; Z35784; CAA84842.1; -; Genomic_DNA.
DR EMBL; X74544; CAA52635.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07097.1; -; Genomic_DNA.
DR PIR; S45757; S45757.
DR RefSeq; NP_009530.1; NM_001178263.1.
DR PDB; 3JA8; EM; 3.80 A; 2=1-868.
DR PDB; 3JC5; EM; 4.70 A; 2=1-868.
DR PDB; 3JC6; EM; 3.70 A; 2=1-868.
DR PDB; 3JC7; EM; 4.80 A; 2=1-868.
DR PDB; 5BK4; EM; 3.90 A; 2/A=1-868.
DR PDB; 5U8S; EM; 6.10 A; 2=1-868.
DR PDB; 5U8T; EM; 4.90 A; 2=1-868.
DR PDB; 5V8F; EM; 3.90 A; 2=1-868.
DR PDB; 5XF8; EM; 7.10 A; 2=1-868.
DR PDB; 6EYC; EM; 3.80 A; 2=1-868.
DR PDB; 6F0L; EM; 4.77 A; 2/A=1-868.
DR PDB; 6HV9; EM; 4.98 A; 2=1-868.
DR PDB; 6PTJ; EM; 3.80 A; 2=1-868.
DR PDB; 6PTN; EM; 5.80 A; 2/i=1-868.
DR PDB; 6PTO; EM; 7.00 A; 2/F/h=1-868.
DR PDB; 6RQC; EM; 4.40 A; 2=1-868.
DR PDB; 6SKL; EM; 3.70 A; 2=1-868.
DR PDB; 6SKO; EM; 3.40 A; 2=1-868.
DR PDB; 6U0M; EM; 3.90 A; 2=201-864.
DR PDB; 6WGF; EM; 7.70 A; 2=1-868.
DR PDB; 6WGG; EM; 8.10 A; 2=1-868.
DR PDB; 6WGI; EM; 10.00 A; 2=1-868.
DR PDB; 7P30; EM; 3.00 A; 2/A=1-868.
DR PDB; 7P5Z; EM; 3.30 A; 2/A=1-868.
DR PDB; 7PMN; EM; 3.20 A; 2=1-868.
DR PDB; 7V3U; EM; 3.20 A; 2/B=1-868.
DR PDB; 7V3V; EM; 2.90 A; 2/B=1-868.
DR PDB; 7W8G; EM; 2.52 A; 2/B=1-868.
DR PDBsum; 3JA8; -.
DR PDBsum; 3JC5; -.
DR PDBsum; 3JC6; -.
DR PDBsum; 3JC7; -.
DR PDBsum; 5BK4; -.
DR PDBsum; 5U8S; -.
DR PDBsum; 5U8T; -.
DR PDBsum; 5V8F; -.
DR PDBsum; 5XF8; -.
DR PDBsum; 6EYC; -.
DR PDBsum; 6F0L; -.
DR PDBsum; 6HV9; -.
DR PDBsum; 6PTJ; -.
DR PDBsum; 6PTN; -.
DR PDBsum; 6PTO; -.
DR PDBsum; 6RQC; -.
DR PDBsum; 6SKL; -.
DR PDBsum; 6SKO; -.
DR PDBsum; 6U0M; -.
DR PDBsum; 6WGF; -.
DR PDBsum; 6WGG; -.
DR PDBsum; 6WGI; -.
DR PDBsum; 7P30; -.
DR PDBsum; 7P5Z; -.
DR PDBsum; 7PMN; -.
DR PDBsum; 7V3U; -.
DR PDBsum; 7V3V; -.
DR PDBsum; 7W8G; -.
DR AlphaFoldDB; P29469; -.
DR SMR; P29469; -.
DR BioGRID; 32675; 202.
DR ComplexPortal; CPX-2944; MCM complex.
DR DIP; DIP-2291N; -.
DR IntAct; P29469; 53.
DR MINT; P29469; -.
DR STRING; 4932.YBL023C; -.
DR iPTMnet; P29469; -.
DR MaxQB; P29469; -.
DR PaxDb; P29469; -.
DR PRIDE; P29469; -.
DR EnsemblFungi; YBL023C_mRNA; YBL023C; YBL023C.
DR GeneID; 852258; -.
DR KEGG; sce:YBL023C; -.
DR SGD; S000000119; MCM2.
DR VEuPathDB; FungiDB:YBL023C; -.
DR eggNOG; KOG0477; Eukaryota.
DR GeneTree; ENSGT01050000244824; -.
DR HOGENOM; CLU_000995_0_0_1; -.
DR InParanoid; P29469; -.
DR OMA; DCVKCGY; -.
DR BioCyc; YEAST:G3O-28926-MON; -.
DR Reactome; R-SCE-68867; Assembly of the pre-replicative complex.
DR Reactome; R-SCE-68949; Orc1 removal from chromatin.
DR Reactome; R-SCE-68962; Activation of the pre-replicative complex.
DR Reactome; R-SCE-69052; Switching of origins to a post-replicative state.
DR PRO; PR:P29469; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P29469; protein.
DR GO; GO:0071162; C:CMG complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IDA:SGD.
DR GO; GO:0042555; C:MCM complex; IDA:SGD.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IDA:SGD.
DR GO; GO:0043596; C:nuclear replication fork; IDA:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0031298; C:replication fork protection complex; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:SGD.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IMP:SGD.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:ComplexPortal.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IMP:SGD.
DR GO; GO:1905775; P:negative regulation of DNA helicase activity; IDA:SGD.
DR GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IDA:SGD.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IDA:ComplexPortal.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008045; MCM2.
DR InterPro; IPR018525; MCM_CS.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
DR InterPro; IPR027925; MCM_N.
DR InterPro; IPR033762; MCM_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11630; PTHR11630; 1.
DR PANTHER; PTHR11630:SF44; PTHR11630:SF44; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF12619; MCM2_N; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF14551; MCM_N; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR PRINTS; PR01658; MCMPROTEIN2.
DR SMART; SM00350; MCM; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00847; MCM_1; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; DNA replication; DNA-binding;
KW Helicase; Hydrolase; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..868
FT /note="DNA replication licensing factor MCM2"
FT /id="PRO_0000194091"
FT DOMAIN 493..700
FT /note="MCM"
FT ZN_FING 341..367
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 675..678
FT /note="Arginine finger"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..65
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 543..550
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT VARIANT 392
FT /note="E -> K (in allele MCM2-1)"
FT MUTAGEN 364
FT /note="C->Y,F,S,H: Loss of activity."
FT /evidence="ECO:0000269|PubMed:2044961"
FT MUTAGEN 367
FT /note="C->Y,F,S,H: Loss of activity."
FT /evidence="ECO:0000269|PubMed:2044961"
FT MUTAGEN 549
FT /note="K->A: Reduces MCM2-7 complex helicase activity.
FT Abolishes MCM2-7 complex helicase activity; when associated
FT with MCM5 A-422. Reduces MCM2-7 complex helicase activity;
FT when associated with MCM3 A-415."
FT /evidence="ECO:0000269|PubMed:18657510"
FT MUTAGEN 676
FT /note="R->A: Loss of MCM2-7 complex helicase activity."
FT /evidence="ECO:0000269|PubMed:18657510"
FT CONFLICT 164
FT /note="S -> T (in Ref. 1; CAA37615)"
FT /evidence="ECO:0000305"
FT CONFLICT 172..173
FT /note="MD -> IH (in Ref. 1; CAA37615)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="G -> P (in Ref. 1; CAA37615)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="A -> R (in Ref. 1; CAA37615)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="D -> H (in Ref. 1; CAA37615)"
FT /evidence="ECO:0000305"
FT CONFLICT 712
FT /note="E -> Q (in Ref. 1; CAA37615)"
FT /evidence="ECO:0000305"
FT CONFLICT 733..747
FT /note="Missing (in Ref. 1; CAA37615)"
FT /evidence="ECO:0000305"
FT CONFLICT 859..868
FT /note="RSFAIYTLGH -> SLSQFIPWVTKTLLFLRISGYEDKKFSVSIHVLAILFS
FT IYKFPLFFV (in Ref. 1; CAA37615)"
FT /evidence="ECO:0000305"
FT HELIX 478..487
FT /evidence="ECO:0007829|PDB:6SKO"
FT TURN 490..492
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 493..500
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 509..520
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 539..548
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 549..557
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 560..566
FT /evidence="ECO:0007829|PDB:6SKO"
FT TURN 568..570
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 573..577
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 578..582
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 589..593
FT /evidence="ECO:0007829|PDB:6SKO"
FT TURN 595..597
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 600..607
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 615..623
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 625..631
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 633..635
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 638..641
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 645..650
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 659..661
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 663..666
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 671..676
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 677..683
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 689..705
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 747..751
FT /evidence="ECO:0007829|PDB:6SKO"
FT TURN 752..754
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 755..758
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 760..773
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 780..799
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 807..823
FT /evidence="ECO:0007829|PDB:6SKO"
FT STRAND 827..829
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 831..846
FT /evidence="ECO:0007829|PDB:6SKO"
FT TURN 847..849
FT /evidence="ECO:0007829|PDB:6SKO"
FT HELIX 850..865
FT /evidence="ECO:0007829|PDB:6SKO"
SQ SEQUENCE 868 AA; 98780 MW; F38FF682581B0EC0 CRC64;
MSDNRRRRRE EDDSDSENEL PPSSPQQHFR GGMNPVSSPI GSPDMINPEG DDNEVDDVPD
IDEVEEQMNE VDLMDDNMYE DYAADHNRDR YDPDQVDDRE QQELSLSERR RIDAQLNERD
RLLRNVAYID DEDEEQEGAA QLDEMGLPVQ RRRRRRQYED LENSDDDLLS DMDIDPLREE
LTLESLSNVK ANSYSEWITQ PNVSRTIARE LKSFLLEYTD ETGRSVYGAR IRTLGEMNSE
SLEVNYRHLA ESKAILALFL AKCPEEMLKI FDLVAMEATE LHYPDYARIH SEIHVRISDF
PTIYSLRELR ESNLSSLVRV TGVVTRRTGV FPQLKYVKFN CLKCGSILGP FFQDSNEEIR
ISFCTNCKSK GPFRVNGEKT VYRNYQRVTL QEAPGTVPPG RLPRHREVIL LADLVDVSKP
GEEVEVTGIY KNNYDGNLNA KNGFPVFATI IEANSIKRRE GNTANEGEEG LDVFSWTEEE
EREFRKISRD RGIIDKIISS MAPSIYGHRD IKTAVACSLF GGVPKNVNGK HSIRGDINVL
LLGDPGTAKS QILKYVEKTA HRAVFATGQG ASAVGLTASV RKDPITKEWT LEGGALVLAD
KGVCLIDEFD KMNDQDRTSI HEAMEQQSIS ISKAGIVTTL QARCSIIAAA NPNGGRYNST
LPLAQNVSLT EPILSRFDIL CVVRDLVDEE ADERLATFVV DSHVRSHPEN DEDREGEELK
NNGESAIEQG EDEINEQLNA RQRRLQRQRK KEEEISPIPQ ELLMKYIHYA RTKIYPKLHQ
MDMDKVSRVY ADLRRESIST GSFPITVRHL ESILRIAESF AKMRLSEFVS SYDLDRAIKV
VVDSFVDAQK VSVRRQLRRS FAIYTLGH
