MUKB_ECOLI
ID MUKB_ECOLI Reviewed; 1486 AA.
AC P22523; P71227; P77164; Q47398;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Chromosome partition protein MukB;
DE AltName: Full=Structural maintenance of chromosome-related protein;
GN Name=mukB; OrderedLocusNames=b0924, JW0907;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=1989883; DOI=10.1002/j.1460-2075.1991.tb07935.x;
RA Niki H., Jaffe A., Imamura R., Ogura T., Hiraga S.;
RT "The new gene mukB codes for a 177 kd protein with coiled-coil domains
RT involved in chromosome partitioning of E. coli.";
RL EMBO J. 10:183-193(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANTS MUKB33 AND MUKB106.
RX PubMed=7988894; DOI=10.1111/j.1574-6968.1994.tb07196.x;
RA Yamanaka K., Mitani T., Feng J., Ogura T., Niki H., Hiraga S.;
RT "Two mutant alleles of mukB, a gene essential for chromosome partition in
RT Escherichia coli.";
RL FEMS Microbiol. Lett. 123:27-31(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7513784; DOI=10.1007/bf00280310;
RA Feng J., Yamanaka K., Niki H., Ogura T., Hiraga S.;
RT "New killing system controlled by two genes located immediately upstream of
RT the mukB gene in Escherichia coli.";
RL Mol. Gen. Genet. 243:136-147(1994).
RN [7]
RP PROTEIN SEQUENCE OF 9-21; 41-61; 353-363 AND 681-709, MODIFIES FUNCTION OF
RP TOPOISOMERASE IV, INTERACTION WITH MUKE; MUKF; ACP AND PARC, AND
RP MUTAGENESIS OF GLU-688 AND ASP-692.
RX PubMed=20921377; DOI=10.1073/pnas.1008678107;
RA Li Y., Stewart N.K., Berger A.J., Vos S., Schoeffler A.J., Berger J.M.,
RA Chait B.T., Oakley M.G.;
RT "Escherichia coli condensin MukB stimulates topoisomerase IV activity by a
RT direct physical interaction.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18832-18837(2010).
RN [8]
RP SUBUNIT.
RX PubMed=1464330; DOI=10.1002/j.1460-2075.1992.tb05617.x;
RA Niki H., Imamura R., Kitaoka M., Yamanaka K., Ogura T., Hiraga S.;
RT "E.coli MukB protein involved in chromosome partition forms a homodimer
RT with a rod-and-hinge structure having DNA binding and ATP/GTP binding
RT activities.";
RL EMBO J. 11:5101-5109(1992).
RN [9]
RP INTERACTION WITH FTSZ.
RX PubMed=9688555; DOI=10.1016/s0014-5793(98)00677-2;
RA Lockhart A., Kendrick-Jones J.;
RT "Interaction of the N-terminal domain of MukB with the bacterial tubulin
RT homologue FtsZ.";
RL FEBS Lett. 430:278-282(1998).
RN [10]
RP INTERACTION WITH MUKE AND MUKF, AND MUTAGENESIS OF SER-33; LYS-40;
RP ASP-1201; VAL-1381; LEU-1403; PHE-1404; ASP-1406; MET-1428 AND GLN-1429.
RX PubMed=10545099; DOI=10.1093/emboj/18.21.5873;
RA Yamazoe M., Onogi T., Sunako Y., Niki H., Yamanaka K., Ichimura T.,
RA Hiraga S.;
RT "Complex formation of MukB, MukE and MukF proteins involved in chromosome
RT partitioning in Escherichia coli.";
RL EMBO J. 18:5873-5884(1999).
RN [11]
RP FUNCTION.
RX PubMed=10660686; DOI=10.1073/pnas.030528397;
RA Sawitzke J.A., Austin S.;
RT "Suppression of chromosome segregation defects of Escherichia coli muk
RT mutants by mutations in topoisomerase I.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:1671-1676(2000).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=11886550; DOI=10.1046/j.1365-2958.2001.02691.x;
RA den Blaauwen T., Lindqvist A., Loewe J., Nanninga N.;
RT "Distribution of the Escherichia coli structural maintenance of chromosomes
RT (SMC)-like protein MukB in the cell.";
RL Mol. Microbiol. 42:1179-1188(2001).
RN [13]
RP IDENTIFICATION IN A COMPLEX WITH SPOT; ISCS AND ACP.
RX PubMed=12885413; DOI=10.1016/s0014-5793(03)00746-4;
RA Gully D., Moinier D., Loiseau L., Bouveret E.;
RT "New partners of acyl carrier protein detected in Escherichia coli by
RT tandem affinity purification.";
RL FEBS Lett. 548:90-96(2003).
RN [14]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=22380631; DOI=10.1111/j.1365-2958.2012.08021.x;
RA Li G., Young K.D.;
RT "Isolation and identification of new inner membrane-associated proteins
RT that localize to cell poles in Escherichia coli.";
RL Mol. Microbiol. 84:276-295(2012).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-227.
RX PubMed=10545328; DOI=10.1016/s0969-2126(00)80052-0;
RA van den Ent F., Lockhart A., Kendrick-Jones J., Loewe J.;
RT "Crystal structure of the N-terminal domain of MukB: a protein involved in
RT chromosome partitioning.";
RL Structure 7:1181-1187(1999).
CC -!- FUNCTION: Plays a central role in chromosome condensation, segregation
CC and cell cycle progression. Functions as a homodimer, which is
CC essential for chromosome partition. Involved in negative DNA
CC supercoiling in vivo, and by this means organizes and compacts
CC chromosomes. May achieve or facilitate chromosome segregation by
CC condensation of DNA from both sides of a centrally located replisome
CC during cell division. Stimulates both DNA relaxation and to a lesser
CC extent decatenation activity of topoisomerase IV.
CC {ECO:0000269|PubMed:10660686}.
CC -!- SUBUNIT: Homodimerization via its hinge domain. Binds to DNA via its C-
CC terminal region. Interacts, and probably forms a ternary complex, with
CC MukE and MukF via its C-terminal region. The complex formation is
CC stimulated by calcium or magnesium. Interacts with tubulin-related
CC protein FtsZ. Identified in a complex with SpoT; IscS and ACP.
CC Interacts with the ParC subunit of topoisomerase IV.
CC {ECO:0000269|PubMed:10545099, ECO:0000269|PubMed:12885413,
CC ECO:0000269|PubMed:1464330, ECO:0000269|PubMed:20921377,
CC ECO:0000269|PubMed:9688555}.
CC -!- INTERACTION:
CC P22523; P0AFI2: parC; NbExp=11; IntAct=EBI-542943, EBI-878544;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000269|PubMed:11886550,
CC ECO:0000269|PubMed:22380631}. Note=Restricted to the nucleoid region,
CC far from the cell poles.
CC -!- DOMAIN: The hinge domain, which separates the large intramolecular
CC coiled coil regions, allows the homodimerization, forming a V-shaped
CC homodimer. The N- and C-terminus together form the head domain.
CC -!- SIMILARITY: Belongs to the SMC family. MukB subfamily. {ECO:0000305}.
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DR EMBL; X57550; CAA40776.1; -; Genomic_DNA.
DR EMBL; D31701; BAA06510.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74010.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35670.1; -; Genomic_DNA.
DR EMBL; D26440; BAA05459.1; -; Genomic_DNA.
DR PIR; C64832; C64832.
DR PIR; JH0228; JH0228.
DR RefSeq; NP_415444.1; NC_000913.3.
DR RefSeq; WP_000572698.1; NZ_LN832404.1.
DR PDB; 1QHL; X-ray; 2.20 A; A=1-227.
DR PDB; 2WMM; X-ray; 2.30 A; A/B=645-804.
DR PDB; 3IBP; X-ray; 3.10 A; A=566-863.
DR PDB; 4MN4; X-ray; 2.30 A; C/D=645-804.
DR PDB; 6H2X; X-ray; 2.60 A; A=333-526, A=893-1053.
DR PDBsum; 1QHL; -.
DR PDBsum; 2WMM; -.
DR PDBsum; 3IBP; -.
DR PDBsum; 4MN4; -.
DR PDBsum; 6H2X; -.
DR AlphaFoldDB; P22523; -.
DR SMR; P22523; -.
DR BioGRID; 4261687; 403.
DR ComplexPortal; CPX-1090; MukBEF condensin complex.
DR DIP; DIP-10273N; -.
DR IntAct; P22523; 58.
DR MINT; P22523; -.
DR STRING; 511145.b0924; -.
DR jPOST; P22523; -.
DR PaxDb; P22523; -.
DR PRIDE; P22523; -.
DR EnsemblBacteria; AAC74010; AAC74010; b0924.
DR EnsemblBacteria; BAA35670; BAA35670; BAA35670.
DR GeneID; 945549; -.
DR KEGG; ecj:JW0907; -.
DR KEGG; eco:b0924; -.
DR PATRIC; fig|1411691.4.peg.1352; -.
DR EchoBASE; EB0613; -.
DR eggNOG; COG3096; Bacteria.
DR HOGENOM; CLU_004430_0_0_6; -.
DR InParanoid; P22523; -.
DR OMA; FIAVYQH; -.
DR PhylomeDB; P22523; -.
DR BioCyc; EcoCyc:EG10618-MON; -.
DR EvolutionaryTrace; P22523; -.
DR PRO; PR:P22523; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0000796; C:condensin complex; IDA:EcoCyc.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0005525; F:GTP binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0051301; P:cell division; IMP:EcoCyc.
DR GO; GO:0030261; P:chromosome condensation; IDA:EcoCyc.
DR GO; GO:0007059; P:chromosome segregation; IMP:EcoliWiki.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0007062; P:sister chromatid cohesion; IMP:EcoliWiki.
DR Gene3D; 3.30.70.3500; -; 1.
DR HAMAP; MF_01800; MukB; 1.
DR InterPro; IPR012090; MukB.
DR InterPro; IPR032520; MukB_hinge.
DR InterPro; IPR042501; MukB_hinge_sf.
DR InterPro; IPR007406; MukB_N_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF04310; MukB; 1.
DR Pfam; PF16330; MukB_hinge; 1.
DR PIRSF; PIRSF005246; MukB; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Chromosome partition;
KW Coiled coil; Cytoplasm; Direct protein sequencing; DNA condensation;
KW DNA-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1486
FT /note="Chromosome partition protein MukB"
FT /id="PRO_0000068214"
FT REGION 645..804
FT /note="Sufficient for ParC binding"
FT REGION 666..783
FT /note="Flexible hinge"
FT COILED 326..418
FT /evidence="ECO:0000255"
FT COILED 444..480
FT /evidence="ECO:0000255"
FT COILED 509..603
FT /evidence="ECO:0000255"
FT COILED 835..923
FT /evidence="ECO:0000255"
FT COILED 977..1115
FT /evidence="ECO:0000255"
FT COILED 1209..1266
FT /evidence="ECO:0000255"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 33
FT /note="S->F: In mukB106; no effect."
FT /evidence="ECO:0000269|PubMed:10545099"
FT MUTAGEN 40
FT /note="K->L: No effect."
FT /evidence="ECO:0000269|PubMed:10545099"
FT MUTAGEN 688
FT /note="E->A: Does not rescue a ts-mutant of MukB."
FT /evidence="ECO:0000269|PubMed:20921377"
FT MUTAGEN 692
FT /note="D->A: Does not rescue a ts-mutant of MukB; less
FT binding of ParC."
FT /evidence="ECO:0000269|PubMed:20921377"
FT MUTAGEN 1201
FT /note="D->N: In mukB33; no effect."
FT /evidence="ECO:0000269|PubMed:10545099"
FT MUTAGEN 1381
FT /note="V->L: Abolishes DNA-binding, but remains associated
FT with MukE and MukF."
FT /evidence="ECO:0000269|PubMed:10545099"
FT MUTAGEN 1403
FT /note="L->P: Abolishes association with MukE and MukF, but
FT still binds DNA."
FT /evidence="ECO:0000269|PubMed:10545099"
FT MUTAGEN 1404
FT /note="F->L: No effect."
FT /evidence="ECO:0000269|PubMed:10545099"
FT MUTAGEN 1406
FT /note="D->N: No effect."
FT /evidence="ECO:0000269|PubMed:10545099"
FT MUTAGEN 1428
FT /note="M->L: No effect."
FT /evidence="ECO:0000269|PubMed:10545099"
FT MUTAGEN 1429
FT /note="Q->R: Abolishes association with MukE and MukF, but
FT still binds DNA."
FT /evidence="ECO:0000269|PubMed:10545099"
FT CONFLICT 266
FT /note="A -> R (in Ref. 1; CAA40776 and 2; BAA06510)"
FT /evidence="ECO:0000305"
FT CONFLICT 318..319
FT /note="EH -> DD (in Ref. 1; CAA40776)"
FT /evidence="ECO:0000305"
FT CONFLICT 1134
FT /note="H -> D (in Ref. 1; CAA40776)"
FT /evidence="ECO:0000305"
FT CONFLICT 1174..1175
FT /note="SE -> VQ (in Ref. 1; CAA40776)"
FT /evidence="ECO:0000305"
FT CONFLICT 1276..1277
FT /note="Missing (in Ref. 1; CAA40776 and 2; BAA06510)"
FT /evidence="ECO:0000305"
FT CONFLICT 1357..1380
FT /note="WLRAESGALSTGEAIGTGMSILVM -> CCAQSLVHCRPVRRWYRYVDSGV
FT (in Ref. 1; CAA40776)"
FT /evidence="ECO:0000305"
FT CONFLICT 1390..1486
FT /note="RRLRGKDISPCRLLFLDEAARLDARSIATLFELCERLQMQLIIAAPENISPE
FT KGTTYKLVRKVFQNTEHVHVVGLRGFAPQLPETLPGTDEAPSQAS -> AACAVKISLL
FT AACCSSMKQRDWMLVLSPRCLNCVSVCKCNSSSQRRKISARRKAPPINWCVKSSRIPNT
FT FMSSACEDLRRNSLKRFQELTKRLLRRVKIKQQCRLFFFRKLRFCTKKVAHYGALFFKL
FT LYIRLCKNVRRLYTEDKPDE (in Ref. 1; CAA40776)"
FT /evidence="ECO:0000305"
FT STRAND 6..15
FT /evidence="ECO:0007829|PDB:1QHL"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:1QHL"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:1QHL"
FT HELIX 38..51
FT /evidence="ECO:0007829|PDB:1QHL"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:1QHL"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1QHL"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:1QHL"
FT STRAND 99..108
FT /evidence="ECO:0007829|PDB:1QHL"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:1QHL"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:1QHL"
FT HELIX 132..136
FT /evidence="ECO:0007829|PDB:1QHL"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:1QHL"
FT HELIX 150..158
FT /evidence="ECO:0007829|PDB:1QHL"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:1QHL"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:1QHL"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:1QHL"
FT HELIX 191..205
FT /evidence="ECO:0007829|PDB:1QHL"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:1QHL"
FT HELIX 210..220
FT /evidence="ECO:0007829|PDB:1QHL"
FT HELIX 339..429
FT /evidence="ECO:0007829|PDB:6H2X"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:6H2X"
FT HELIX 440..460
FT /evidence="ECO:0007829|PDB:6H2X"
FT HELIX 463..485
FT /evidence="ECO:0007829|PDB:6H2X"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:6H2X"
FT HELIX 494..512
FT /evidence="ECO:0007829|PDB:6H2X"
FT HELIX 515..523
FT /evidence="ECO:0007829|PDB:6H2X"
FT HELIX 573..617
FT /evidence="ECO:0007829|PDB:3IBP"
FT HELIX 645..663
FT /evidence="ECO:0007829|PDB:2WMM"
FT HELIX 674..681
FT /evidence="ECO:0007829|PDB:2WMM"
FT HELIX 686..689
FT /evidence="ECO:0007829|PDB:2WMM"
FT HELIX 690..692
FT /evidence="ECO:0007829|PDB:2WMM"
FT TURN 695..697
FT /evidence="ECO:0007829|PDB:2WMM"
FT HELIX 698..704
FT /evidence="ECO:0007829|PDB:2WMM"
FT HELIX 706..710
FT /evidence="ECO:0007829|PDB:2WMM"
FT STRAND 712..715
FT /evidence="ECO:0007829|PDB:2WMM"
FT HELIX 717..719
FT /evidence="ECO:0007829|PDB:2WMM"
FT HELIX 721..724
FT /evidence="ECO:0007829|PDB:2WMM"
FT STRAND 732..739
FT /evidence="ECO:0007829|PDB:2WMM"
FT STRAND 743..745
FT /evidence="ECO:0007829|PDB:4MN4"
FT STRAND 751..754
FT /evidence="ECO:0007829|PDB:2WMM"
FT STRAND 757..763
FT /evidence="ECO:0007829|PDB:2WMM"
FT STRAND 766..771
FT /evidence="ECO:0007829|PDB:2WMM"
FT HELIX 780..802
FT /evidence="ECO:0007829|PDB:2WMM"
FT TURN 825..828
FT /evidence="ECO:0007829|PDB:3IBP"
FT STRAND 829..831
FT /evidence="ECO:0007829|PDB:3IBP"
FT HELIX 834..853
FT /evidence="ECO:0007829|PDB:3IBP"
FT HELIX 894..920
FT /evidence="ECO:0007829|PDB:6H2X"
FT HELIX 927..930
FT /evidence="ECO:0007829|PDB:6H2X"
FT HELIX 934..965
FT /evidence="ECO:0007829|PDB:6H2X"
FT HELIX 968..972
FT /evidence="ECO:0007829|PDB:6H2X"
FT HELIX 973..977
FT /evidence="ECO:0007829|PDB:6H2X"
FT HELIX 979..1045
FT /evidence="ECO:0007829|PDB:6H2X"
SQ SEQUENCE 1486 AA; 170230 MW; 38C7874BEB78D6D6 CRC64;
MIERGKFRSL TLINWNGFFA RTFDLDELVT TLSGGNGAGK STTMAAFVTA LIPDLTLLHF
RNTTEAGATS GSRDKGLHGK LKAGVCYSML DTINSRHQRV VVGVRLQQVA GRDRKVDIKP
FAIQGLPMSV QPTQLVTETL NERQARVLPL NELKDKLEAM EGVQFKQFNS ITDYHSLMFD
LGIIARRLRS ASDRSKFYRL IEASLYGGIS SAITRSLRDY LLPENSGVRK AFQDMEAALR
ENRMTLEAIR VTQSDRDLFK HLISEATNYV AADYMRHANE RRVHLDKALE FRRELHTSRQ
QLAAEQYKHV DMARELAEHN GAEGDLEADY QAASDHLNLV QTALRQQEKI ERYEADLDEL
QIRLEEQNEV VAEAIERQQE NEARAEAAEL EVDELKSQLA DYQQALDVQQ TRAIQYNQAI
AALNRAKELC HLPDLTADCA AEWLETFQAK ELEATEKMLS LEQKMSMAQT AHSQFEQAYQ
LVVAINGPLA RNEAWDVARE LLREGVDQRH LAEQVQPLRM RLSELEQRLR EQQEAERLLA
DFCKRQGKNF DIDELEALHQ ELEARIASLS DSVSNAREER MALRQEQEQL QSRIQSLMQR
APVWLAAQNS LNQLSEQCGE EFTSSQDVTE YLQQLLERER EAIVERDEVG ARKNAVDEEI
ERLSQPGGSE DQRLNALAER FGGVLLSEIY DDVSLEDAPY FSALYGPSRH AIVVPDLSQV
TEHLEGLTDC PEDLYLIEGD PQSFDDSVFS VDELEKAVVV KIADRQWRYS RFPEVPLFGR
AARESRIESL HAEREVLSER FATLSFDVQK TQRLHQAFSR FIGSHLAVAF ESDPEAEIRQ
LNSRRVELER ALSNHENDNQ QQRIQFEQAK EGVTALNRIL PRLNLLADDS LADRVDEIRE
RLDEAQEAAR FVQQFGNQLA KLEPIVSVLQ SDPEQFEQLK EDYAYSQQMQ RDARQQAFAL
TEVVQRRAHF SYSDSAEMLS GNSDLNEKLR ERLEQAEAER TRAREALRGH AAQLSQYNQV
LASLKSSYDT KKELLNDLQR ELQDIGVRAD SGAEERARIR RDELHAQLSN NRSRRNQLEK
ALTFCEAEMD NLTRKLRKLE RDYFEMREQV VTAKAGWCAV MRMVKDNGVE RRLHRRELAY
LSADDLRSMS DKALGALRLA VADNEHLRDV LRMSEDPKRP ERKIQFFVAV YQHLRERIRQ
DIIRTDDPVE AIEQMEIELS RLTEELTSRE QKLAISSRSV ANIIRKTIQR EQNRIRMLNQ
GLQNVSFGQV NSVRLNVNVR ETHAMLLDVL SEQHEQHQDL FNSNRLTFSE ALAKLYQRLN
PQIDMGQRTP QTIGEELLDY RNYLEMEVEV NRGSDGWLRA ESGALSTGEA IGTGMSILVM
VVQSWEDESR RLRGKDISPC RLLFLDEAAR LDARSIATLF ELCERLQMQL IIAAPENISP
EKGTTYKLVR KVFQNTEHVH VVGLRGFAPQ LPETLPGTDE APSQAS
