RAD50_PYRFU
ID RAD50_PYRFU Reviewed; 882 AA.
AC P58301;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=DNA double-strand break repair Rad50 ATPase {ECO:0000255|HAMAP-Rule:MF_00449, ECO:0000305};
DE AltName: Full=pfRad50 {ECO:0000303|PubMed:11029422};
GN Name=rad50 {ECO:0000255|HAMAP-Rule:MF_00449, ECO:0000303|PubMed:11029422};
GN OrderedLocusNames=PF1167;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=11029422; DOI=10.1128/jb.182.21.6036-6041.2000;
RA Hopfner K.-P., Karcher A., Shin D., Fairley C., Tainer J.A., Carney J.P.;
RT "Mre11 and Rad50 from Pyrococcus furiosus: cloning and biochemical
RT characterization reveal an evolutionarily conserved multiprotein machine.";
RL J. Bacteriol. 182:6036-6041(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [3]
RP FUNCTION AS AN ADENYLATE KINASE, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP SER-793.
RX PubMed=17349953; DOI=10.1016/j.molcel.2007.01.028;
RA Bhaskara V., Dupre A., Lengsfeld B., Hopkins B.B., Chan A., Lee J.H.,
RA Zhang X., Gautier J., Zakian V., Paull T.T.;
RT "Rad50 adenylate kinase activity regulates DNA tethering by Mre11/Rad50
RT complexes.";
RL Mol. Cell 25:647-661(2007).
RN [4]
RP FUNCTION.
RX PubMed=18957200; DOI=10.1016/j.cell.2008.09.054;
RA Hopkins B.B., Paull T.T.;
RT "The P. furiosus mre11/rad50 complex promotes 5' strand resection at a DNA
RT double-strand break.";
RL Cell 135:250-260(2008).
RN [5]
RP SUBUNIT, AND DOMAIN.
RX PubMed=22102415; DOI=10.1074/jbc.m111.307041;
RA Majka J., Alford B., Ausio J., Finn R.M., McMurray C.T.;
RT "ATP hydrolysis by RAD50 protein switches MRE11 enzyme from endonuclease to
RT exonuclease.";
RL J. Biol. Chem. 287:2328-2341(2012).
RN [6] {ECO:0007744|PDB:1F2T, ECO:0007744|PDB:1F2U}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-149 AND 735-882 IN COMPLEX WITH
RP ATP, ATPASE ACTIVITY, DNA-BINDING, SUBUNIT, AND MUTAGENESIS OF SER-793.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10892749; DOI=10.1016/s0092-8674(00)80890-9;
RA Hopfner K.-P., Karcher A., Shin D.S., Craig L., Arthur L.M., Carney J.P.,
RA Tainer J.A.;
RT "Structural biology of Rad50 ATPase: ATP-driven conformational control in
RT DNA double-strand break repair and the ABC-ATPase superfamily.";
RL Cell 101:789-800(2000).
RN [7] {ECO:0007744|PDB:1II8}
RP X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS) OF 1-195 AND 709-882, AND SUBUNIT.
RX PubMed=11371344; DOI=10.1016/s0092-8674(01)00335-x;
RA Hopfner K.-P., Karcher A., Craig L., Woo T.T., Carney J.P., Tainer J.A.;
RT "Structural biochemistry and interaction architecture of the DNA double-
RT strand break repair Mre11 nuclease and Rad50-ATPase.";
RL Cell 105:473-485(2001).
RN [8] {ECO:0007744|PDB:1L8D}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 396-506, COFACTOR, DOMAIN, AND
RP ZINC-BINDING.
RX PubMed=12152085; DOI=10.1038/nature00922;
RA Hopfner K.-P., Craig L., Moncalian G., Zinkel R.A., Usui T., Owen B.A.L.,
RA Karcher A., Henderson B., Bodmer J.-L., McMurray C.T., Carney J.P.,
RA Petrini J.H.J., Tainer J.A.;
RT "The Rad50 zinc-hook is a structure joining Mre11 complexes in DNA
RT recombination and repair.";
RL Nature 418:562-566(2002).
RN [9] {ECO:0007744|PDB:1US8}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-147; 739-792 AND 794-882 OF
RP MUTANT ARG-793, AND SUBUNIT.
RX PubMed=14698290; DOI=10.1016/j.jmb.2003.11.026;
RA Moncalian G., Lengsfeld B., Bhaskara V., Hopfner K.-P., Karcher A.,
RA Alden E., Tainer J.A., Paull T.T.;
RT "The rad50 signature motif: essential to ATP binding and biological
RT function.";
RL J. Mol. Biol. 335:937-951(2004).
RN [10] {ECO:0007744|PDB:3QKR, ECO:0007744|PDB:3QKS, ECO:0007744|PDB:3QKT, ECO:0007744|PDB:3QKU}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-177 AND 726-882 IN COMPLEX WITH
RP ATP ANALOG, AND SUBUNIT.
RX PubMed=21441914; DOI=10.1038/nsmb.2038;
RA Williams G.J., Williams R.S., Williams J.S., Moncalian G., Arvai A.S.,
RA Limbo O., Guenther G., SilDas S., Hammel M., Russell P., Tainer J.A.;
RT "ABC ATPase signature helices in Rad50 link nucleotide state to Mre11
RT interface for DNA repair.";
RL Nat. Struct. Mol. Biol. 18:423-431(2011).
RN [11] {ECO:0007744|PDB:4NCH, ECO:0007744|PDB:4NCI, ECO:0007744|PDB:4NCJ, ECO:0007744|PDB:4NCK}
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 1-177 AND 726-882 OF MUTANTS IN
RP COMPLEX WITH ADP, FUNCTION, AND MUTAGENESIS OF ARG-797; LEU-802 AND
RP ARG-805.
RX PubMed=24493214; DOI=10.1002/embj.201386100;
RA Deshpande R.A., Williams G.J., Limbo O., Williams R.S., Kuhnlein J.,
RA Lee J.H., Classen S., Guenther G., Russell P., Tainer J.A., Paull T.T.;
RT "ATP-driven Rad50 conformations regulate DNA tethering, end resection, and
RT ATM checkpoint signaling.";
RL EMBO J. 33:482-500(2014).
CC -!- FUNCTION: Part of the Rad50/Mre11 complex, which is involved in the
CC early steps of DNA double-strand break (DSB) repair (PubMed:11029422,
CC PubMed:18957200). The complex may facilitate opening of the processed
CC DNA ends to aid in the recruitment of HerA and NurA (PubMed:18957200).
CC Rad50 controls the balance between DNA end bridging and DNA resection
CC via ATP-dependent structural rearrangements of the Rad50/Mre11 complex
CC (PubMed:24493214). The ATP-bound conformation promotes DNA end binding
CC and end tethering, and alters Mre11 nuclease activity
CC (PubMed:24493214). ATP hydrolysis promotes both Mre11 activity as well
CC as HerA/NurA activity (PubMed:24493214). Has also reversible adenylate
CC kinase activity (PubMed:17349953). {ECO:0000269|PubMed:11029422,
CC ECO:0000269|PubMed:17349953, ECO:0000269|PubMed:18957200,
CC ECO:0000269|PubMed:24493214}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00449,
CC ECO:0000269|PubMed:12152085};
CC Note=Binds 1 zinc ion per homodimer. {ECO:0000255|HAMAP-Rule:MF_00449,
CC ECO:0000269|PubMed:12152085};
CC -!- ACTIVITY REGULATION: The adenylate kinase inhibitor P(1),P(5)-
CC di(adenosine-5') pentaphosphate (Ap5A) inhibits adenylate kinase
CC activity, but does not affect ATPase activity.
CC {ECO:0000269|PubMed:17349953}.
CC -!- SUBUNIT: Homodimer (PubMed:10892749, PubMed:14698290). Forms a
CC heterotetramer composed of two Mre11 subunits and two Rad50 subunits
CC (PubMed:11371344, PubMed:21441914, PubMed:22102415). Homodimerization
CC is promoted by ATP binding (PubMed:10892749).
CC {ECO:0000269|PubMed:10892749, ECO:0000269|PubMed:11371344,
CC ECO:0000269|PubMed:14698290, ECO:0000269|PubMed:21441914,
CC ECO:0000269|PubMed:22102415}.
CC -!- INTERACTION:
CC P58301; Q8U1N9: mre11; NbExp=11; IntAct=EBI-2505704, EBI-2014945;
CC P58301; P58301: rad50; NbExp=4; IntAct=EBI-2505704, EBI-2505704;
CC -!- DOMAIN: Binding of ATP induces a closed, compact conformation of the
CC Rad50/Mre11 complex. ATP hydrolysis opens the complex.
CC {ECO:0000269|PubMed:22102415}.
CC -!- DOMAIN: The two conserved Cys that bind zinc constitute the zinc-hook,
CC which separates the large intramolecular coiled coil regions. The 2 Cys
CC residues coordinate one molecule of zinc with the help of the 2 Cys
CC residues of the zinc-hook of another Rad50 molecule, thereby forming a
CC V-shaped homodimer. {ECO:0000255|HAMAP-Rule:MF_00449,
CC ECO:0000269|PubMed:12152085}.
CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00449, ECO:0000305}.
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DR EMBL; AE009950; AAL81291.1; -; Genomic_DNA.
DR RefSeq; WP_011012307.1; NZ_CP023154.1.
DR PDB; 1F2T; X-ray; 1.60 A; A=1-149, B=735-882.
DR PDB; 1F2U; X-ray; 1.60 A; A/C=1-149, B/D=735-882.
DR PDB; 1II8; X-ray; 3.02 A; A=1-195, B=709-882.
DR PDB; 1L8D; X-ray; 2.20 A; A/B=396-506.
DR PDB; 1US8; X-ray; 2.10 A; A=1-147, B=739-882.
DR PDB; 3QKR; X-ray; 3.40 A; A=1-195, B=704-882.
DR PDB; 3QKS; X-ray; 2.10 A; A=1-195, B=704-882.
DR PDB; 3QKT; X-ray; 1.90 A; A/B/C/D=1-177, A/B/C/D=726-882.
DR PDB; 3QKU; X-ray; 3.30 A; A/B=1-187, A/B=716-882.
DR PDB; 4NCH; X-ray; 2.30 A; A/B=1-177, A/B=726-882.
DR PDB; 4NCI; X-ray; 2.30 A; A=1-177, A=726-882.
DR PDB; 4NCJ; X-ray; 2.00 A; A/B/C/D=1-177, A/B/C/D=726-882.
DR PDB; 4NCK; X-ray; 1.99 A; A/B=1-177, A/B=726-882.
DR PDB; 6ZFF; X-ray; 3.00 A; A/B=378-516.
DR PDBsum; 1F2T; -.
DR PDBsum; 1F2U; -.
DR PDBsum; 1II8; -.
DR PDBsum; 1L8D; -.
DR PDBsum; 1US8; -.
DR PDBsum; 3QKR; -.
DR PDBsum; 3QKS; -.
DR PDBsum; 3QKT; -.
DR PDBsum; 3QKU; -.
DR PDBsum; 4NCH; -.
DR PDBsum; 4NCI; -.
DR PDBsum; 4NCJ; -.
DR PDBsum; 4NCK; -.
DR PDBsum; 6ZFF; -.
DR AlphaFoldDB; P58301; -.
DR SMR; P58301; -.
DR DIP; DIP-54373N; -.
DR IntAct; P58301; 2.
DR MINT; P58301; -.
DR STRING; 186497.PF1167; -.
DR PRIDE; P58301; -.
DR EnsemblBacteria; AAL81291; AAL81291; PF1167.
DR GeneID; 41712975; -.
DR KEGG; pfu:PF1167; -.
DR PATRIC; fig|186497.12.peg.1227; -.
DR eggNOG; arCOG00368; Archaea.
DR HOGENOM; CLU_004785_0_2_2; -.
DR OMA; VNFIYGP; -.
DR OrthoDB; 1771at2157; -.
DR PhylomeDB; P58301; -.
DR EvolutionaryTrace; P58301; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006302; P:double-strand break repair; IEA:UniProtKB-UniRule.
DR CDD; cd03240; ABC_Rad50; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00449; RAD50; 1.
DR InterPro; IPR045171; ABC_Rad50.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR InterPro; IPR022982; Rad50_ATPase_archaeal.
DR InterPro; IPR013134; Zn_hook_RAD50.
DR Pfam; PF13304; AAA_21; 1.
DR Pfam; PF13476; AAA_23; 1.
DR Pfam; PF04423; Rad50_zn_hook; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coiled coil; DNA damage; DNA repair; Hydrolase;
KW Metal-binding; Nucleotide-binding; Reference proteome; Zinc.
FT CHAIN 1..882
FT /note="DNA double-strand break repair Rad50 ATPase"
FT /id="PRO_0000138661"
FT DOMAIN 399..496
FT /note="Zinc-hook"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 257..588
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT COILED 629..735
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449"
FT BINDING 12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:10892749,
FT ECO:0000269|PubMed:21441914, ECO:0000269|PubMed:24493214,
FT ECO:0007744|PDB:1F2U, ECO:0007744|PDB:3QKT,
FT ECO:0007744|PDB:3QKU, ECO:0007744|PDB:4NCJ"
FT BINDING 32..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:10892749,
FT ECO:0000269|PubMed:21441914, ECO:0000269|PubMed:24493214,
FT ECO:0007744|PDB:1F2U, ECO:0007744|PDB:3QKT,
FT ECO:0007744|PDB:3QKU, ECO:0007744|PDB:4NCJ"
FT BINDING 60..64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:10892749,
FT ECO:0000269|PubMed:21441914, ECO:0000269|PubMed:24493214,
FT ECO:0007744|PDB:1F2U, ECO:0007744|PDB:3QKT,
FT ECO:0007744|PDB:3QKU, ECO:0007744|PDB:4NCJ"
FT BINDING 140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:10892749,
FT ECO:0000269|PubMed:21441914, ECO:0007744|PDB:1F2U,
FT ECO:0007744|PDB:3QKT, ECO:0007744|PDB:3QKU"
FT BINDING 444
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449,
FT ECO:0000269|PubMed:12152085"
FT BINDING 447
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00449,
FT ECO:0000269|PubMed:12152085"
FT BINDING 763..764
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:10892749,
FT ECO:0000269|PubMed:21441914, ECO:0007744|PDB:1F2U,
FT ECO:0007744|PDB:3QKT"
FT BINDING 791..796
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:10892749,
FT ECO:0000269|PubMed:21441914, ECO:0007744|PDB:1F2U,
FT ECO:0007744|PDB:3QKT"
FT MUTAGEN 793
FT /note="S->R: Prevents ATP binding and disrupts the
FT communication among the other ATP-binding loops. Prevents
FT also Rad50 dimerization. Decreases both ATPase and
FT adenylate kinase activities."
FT /evidence="ECO:0000269|PubMed:10892749,
FT ECO:0000269|PubMed:14698290, ECO:0000269|PubMed:17349953"
FT MUTAGEN 797
FT /note="R->G: Decreases ATP-induced dimerization. Increases
FT DNA end tethering."
FT /evidence="ECO:0000269|PubMed:24493214"
FT MUTAGEN 802
FT /note="L->W: Destabilizes the ATP-dimerized state. Promotes
FT HerA/NurA activity."
FT /evidence="ECO:0000269|PubMed:24493214"
FT MUTAGEN 805
FT /note="R->E: Increases ATP-induced dimerization. Increases
FT DNA end tethering. Fails to promote HerA/NurA activity."
FT /evidence="ECO:0000269|PubMed:24493214"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:1F2T"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:1F2T"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:1F2T"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:1F2T"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:1F2U"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:4NCH"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:1F2T"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:1F2T"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1F2U"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:1F2T"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:1F2T"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:1F2T"
FT HELIX 129..135
FT /evidence="ECO:0007829|PDB:1F2T"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:1US8"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:1F2T"
FT HELIX 152..161
FT /evidence="ECO:0007829|PDB:3QKT"
FT HELIX 167..173
FT /evidence="ECO:0007829|PDB:3QKT"
FT HELIX 181..186
FT /evidence="ECO:0007829|PDB:3QKU"
FT HELIX 189..205
FT /evidence="ECO:0007829|PDB:3QKT"
FT HELIX 208..221
FT /evidence="ECO:0007829|PDB:3QKT"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:3QKT"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:3QKT"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:3QKT"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:3QKT"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:3QKT"
FT HELIX 258..261
FT /evidence="ECO:0007829|PDB:3QKT"
FT HELIX 397..437
FT /evidence="ECO:0007829|PDB:1L8D"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:1L8D"
FT TURN 445..447
FT /evidence="ECO:0007829|PDB:1L8D"
FT HELIX 453..497
FT /evidence="ECO:0007829|PDB:1L8D"
FT HELIX 741..759
FT /evidence="ECO:0007829|PDB:1F2T"
FT TURN 760..762
FT /evidence="ECO:0007829|PDB:1F2T"
FT STRAND 766..771
FT /evidence="ECO:0007829|PDB:1F2T"
FT STRAND 774..782
FT /evidence="ECO:0007829|PDB:1F2T"
FT STRAND 785..787
FT /evidence="ECO:0007829|PDB:1F2T"
FT HELIX 789..791
FT /evidence="ECO:0007829|PDB:1F2T"
FT HELIX 794..813
FT /evidence="ECO:0007829|PDB:1F2T"
FT STRAND 817..823
FT /evidence="ECO:0007829|PDB:1F2T"
FT STRAND 825..828
FT /evidence="ECO:0007829|PDB:1II8"
FT HELIX 830..842
FT /evidence="ECO:0007829|PDB:1F2T"
FT HELIX 844..846
FT /evidence="ECO:0007829|PDB:1F2T"
FT STRAND 847..855
FT /evidence="ECO:0007829|PDB:1F2T"
FT HELIX 857..862
FT /evidence="ECO:0007829|PDB:1F2T"
FT STRAND 864..872
FT /evidence="ECO:0007829|PDB:1F2T"
FT STRAND 875..882
FT /evidence="ECO:0007829|PDB:1F2T"
SQ SEQUENCE 882 AA; 103840 MW; 3ADCBD250382A99E CRC64;
MKLERVTVKN FRSHSDTVVE FKEGINLIIG QNGSGKSSLL DAILVGLYWP LRIKDIKKDE
FTKVGARDTY IDLIFEKDGT KYRITRRFLK GYSSGEIHAM KRLVGNEWKH VTEPSSKAIS
AFMEKLIPYN IFLNAIYIRQ GQIDAILESD EAREKVVREV LNLDKFETAY KKLSELKKTI
NNRIKEYRDI LARTENIEEL IKENEQELIQ VLQEISKIEE VLPSKRSKVD MLRKEVLRLE
ETKVEIENSE RLLEKRRGDK RTLEERIKNT EEYLEKLKEK EKELEEQVKE ITSIKKDVDA
YLALKEFKNE YLDKKYKIEK ELTRVEELIN EIQKRIEELN EKESEKEKLE NEKKEILNKL
AILEKDHQLY EEIKAKKENL RQLKEKLGDK SPEDIKKLLE ELETKKTTIE EERNEITQRI
GELKNKIGDL KTAIEELKKA KGKCPVCGRE LTDEHREELL SKYHLDLNNS KNTLAKLIDR
KSELERELRR IDMEIKRLTP LLTVAEQIRS IEEELNVVNL EKIEKNATEY EKLLEELRTL
EGRIRGLAED LKKLAPLEKK LAALIHKKQE LEKELKELNT KLESFGFKSV EDLDSKLREL
EEIYKRYLTL LNSKKELEIT QREIAKAKET LEMSFEELAE VEADIERIEK KLSQLKQKYN
EEEYKKKREE KEELEKELAR LEAQKKELEK RRDTIKSTLE KLKAEKENRE RVKKEIKDLE
KAKDFTEELI EKVKKYKALA REAALSKIGE LASEIFAEFT EGKYSEVVVR AEENKVRLFV
VWEGKERPLT FLSGGERIAL GLAFRLAMSL YLAGEISLLI LDEPTPYLDE ERRRKLITIM
ERYLKKIPQV ILVSHDEELK DAADHVIRIS LENGSSKVEV VS
