RECA_ECOLI
ID RECA_ECOLI Reviewed; 353 AA.
AC P0A7G6; P03017; P26347; P78213;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Protein RecA {ECO:0000255|HAMAP-Rule:MF_00268};
DE AltName: Full=Recombinase A {ECO:0000255|HAMAP-Rule:MF_00268};
GN Name=recA {ECO:0000255|HAMAP-Rule:MF_00268};
GN Synonyms=lexB, recH, rnmB, tif, umuB, zab; OrderedLocusNames=b2699, JW2669;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-6.
RX PubMed=6244554; DOI=10.1073/pnas.77.1.313;
RA Horii T., Ogawa T., Ogawa H.;
RT "Organization of the recA gene of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:313-317(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-3.
RX PubMed=6930655; DOI=10.1073/pnas.77.5.2611;
RA Sancar A., Stachelek C., Konigsberg W., Rupp W.D.;
RT "Sequences of the recA gene and protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:2611-2615(1980).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2274037; DOI=10.1007/bf00633842;
RA Zhao X.J., McEntee K.;
RT "DNA sequence analysis of the recA genes from Proteus vulgaris, Erwinia
RT carotovora, Shigella flexneri and Escherichia coli B/r.";
RL Mol. Gen. Genet. 222:369-376(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 112.
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 [7]
RP PROTEIN SEQUENCE OF 90-107 AND 179-184, AND DNA-BINDING.
RX PubMed=7737176; DOI=10.1111/j.1432-1033.1995.0772m.x;
RA Morimatsu K., Horii T.;
RT "The DNA-binding site of the RecA protein. Photochemical cross-linking of
RT Tyr103 to single-stranded DNA.";
RL Eur. J. Biochem. 228:772-778(1995).
RN [8]
RP PROTEIN SEQUENCE OF 187-194, AND DNA-BINDING.
RX PubMed=7588783; DOI=10.1111/j.1432-1033.1995.419_2.x;
RA Gardner R.V., Voloshin O.N., Camerini-Otero R.D.;
RT "The identification of the single-stranded DNA-binding domain of the
RT Escherichia coli RecA protein.";
RL Eur. J. Biochem. 233:419-425(1995).
RN [9]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [10]
RP FUNCTION IN HOMOLOGOUS RECOMBINATION.
RX PubMed=7608206; DOI=10.1074/jbc.270.27.16360;
RA Dixon D.A., Kowalczykowski S.C.;
RT "Role of the Escherichia coli recombination hotspot, chi, in RecABCD-
RT dependent homologous pairing.";
RL J. Biol. Chem. 270:16360-16370(1995).
RN [11]
RP INDUCTION BY COLD-SHOCK.
RC STRAIN=CSH142;
RX PubMed=8898389; DOI=10.1111/j.1365-2958.1996.tb02582.x;
RA Jones P.G., Inouye M.;
RT "RbfA, a 30S ribosomal binding factor, is a cold-shock protein whose
RT absence triggers the cold-shock response.";
RL Mol. Microbiol. 21:1207-1218(1996).
RN [12]
RP FUNCTION WITH RECBCD.
RX PubMed=9230304; DOI=10.1016/s0092-8674(00)80315-3;
RA Anderson D.G., Kowalczykowski S.C.;
RT "The translocating RecBCD enzyme stimulates recombination by directing RecA
RT protein onto ssDNA in a chi-regulated manner.";
RL Cell 90:77-86(1997).
RN [13]
RP REGULATION BY LEXA, AND INDUCTION.
RC STRAIN=K12 / RW118;
RX PubMed=10760155; DOI=10.1046/j.1365-2958.2000.01826.x;
RA Fernandez De Henestrosa A.R., Ogi T., Aoyagi S., Chafin D., Hayes J.J.,
RA Ohmori H., Woodgate R.;
RT "Identification of additional genes belonging to the LexA regulon in
RT Escherichia coli.";
RL Mol. Microbiol. 35:1560-1572(2000).
RN [14]
RP INTERACTION WITH RECB, AND SUBUNIT.
RX PubMed=16483938; DOI=10.1016/j.molcel.2006.01.007;
RA Spies M., Kowalczykowski S.C.;
RT "The RecA binding locus of RecBCD is a general domain for recruitment of
RT DNA strand exchange proteins.";
RL Mol. Cell 21:573-580(2006).
RN [15]
RP INDUCTION BY HYDROXYUREA.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA Walker G.C.;
RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT coli.";
RL Mol. Cell 36:845-860(2009).
RN [16]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=22412352; DOI=10.1371/journal.pbio.1001281;
RA Erental A., Sharon I., Engelberg-Kulka H.;
RT "Two programmed cell death systems in Escherichia coli: an apoptotic-like
RT death is inhibited by the mazEF-mediated death pathway.";
RL PLoS Biol. 10:E1001281-E1001281(2012).
RN [17]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=26845522; DOI=10.7554/elife.10807;
RA Cooper D.L., Lovett S.T.;
RT "Recombinational branch migration by the RadA/Sms paralog of RecA in
RT Escherichia coli.";
RL Elife 5:0-0(2016).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND SUBUNIT.
RX PubMed=1731246; DOI=10.1038/355318a0;
RA Story R.M., Weber I.T., Steitz T.A.;
RT "The structure of the E. coli recA protein monomer and polymer.";
RL Nature 355:318-325(1992).
RN [19]
RP ERRATUM OF PUBMED:1731246.
RA Story R.M., Weber I.T., Steitz T.A.;
RL Nature 355:567-567(1992).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2-353 IN COMPLEX WITH ATP.
RX PubMed=1731253; DOI=10.1038/355374a0;
RA Story R.M., Steitz T.A.;
RT "Structure of the recA protein-ADP complex.";
RL Nature 355:374-376(1992).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=9033586; DOI=10.1038/nsb0297-101;
RA Yu X., Egelman E.H.;
RT "The RecA hexamer is a structural homologue of ring helicases.";
RL Nat. Struct. Biol. 4:101-104(1997).
CC -!- FUNCTION: Required for homologous recombination and the bypass of
CC mutagenic DNA lesions by the SOS response. Catalyzes ATP-driven
CC homologous pairing and strand exchange of DNA molecules necessary for
CC DNA recombinational repair. Catalyzes the hydrolysis of ATP in the
CC presence of single-stranded DNA, the ATP-dependent uptake of single-
CC stranded DNA by duplex DNA, and the ATP-dependent hybridization of
CC homologous single-stranded DNAs. The SOS response controls an
CC apoptotic-like death (ALD) induced (in the absence of the mazE-mazF
CC toxin-antitoxin module) in response to DNA damaging agents that is
CC mediated by RecA and LexA (PubMed:22412352).
CC {ECO:0000269|PubMed:22412352, ECO:0000269|PubMed:26845522,
CC ECO:0000269|PubMed:7608206, ECO:0000269|PubMed:9230304}.
CC -!- ACTIVITY REGULATION: The rate of DNA-strand exchange is stimulated by
CC RadA. {ECO:0000269|PubMed:26845522}.
CC -!- SUBUNIT: Polymerizes non-specifically on ssDNA to form filaments;
CC filament formation requires ATP or ATP-gamma-S. Interacts with and
CC activates LexA leading to autocatalytic cleavage of LexA, which
CC derepresses the SOS regulon and activates DNA repair. Interacts with
CC the C-terminus of RecB, facilitating loading of RecA onto ssDNA at chi
CC sites. Interaction is decreased by ATP. {ECO:0000269|PubMed:16483938,
CC ECO:0000269|PubMed:1731246, ECO:0000269|PubMed:1731253}.
CC -!- INTERACTION:
CC P0A7G6; P23367: mutL; NbExp=3; IntAct=EBI-370331, EBI-554913;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: Induced by DNA damage, repressed by LexA (PubMed:10760155).
CC Induced in response to low temperature (PubMed:8898389). Sensitive to
CC temperature through changes in the linking number of the DNA. Induced
CC by cold shock (42 to 15 degrees Celsius) (at protein level)
CC (PubMed:8898389). 5.1-fold induced by hydroxyurea treatment (at protein
CC level) (PubMed:20005847). mRNA levels are repressed in a mazE-mazF-
CC mediated manner (PubMed:22412352). {ECO:0000269|PubMed:10760155,
CC ECO:0000269|PubMed:20005847, ECO:0000269|PubMed:22412352,
CC ECO:0000269|PubMed:8898389}.
CC -!- DISRUPTION PHENOTYPE: Triple mazE-mazF-recA mutant cells no longer
CC undergo an apoptotic-like death upon DNA damage characterized by
CC membrane depolarization. {ECO:0000269|PubMed:22412352}.
CC -!- SIMILARITY: Belongs to the RecA family. {ECO:0000255|HAMAP-
CC Rule:MF_00268}.
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DR EMBL; V00328; CAA23618.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75741.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16561.2; -; Genomic_DNA.
DR PIR; G65049; RQECA.
DR RefSeq; NP_417179.1; NC_000913.3.
DR RefSeq; WP_000963143.1; NZ_STEB01000027.1.
DR PDB; 1AA3; NMR; -; A=269-331.
DR PDB; 1N03; EM; 20.00 A; A/B/C/D/E/F/G=2-353.
DR PDB; 1REA; X-ray; 2.70 A; A=2-353.
DR PDB; 1U94; X-ray; 1.90 A; A=2-353.
DR PDB; 1U98; X-ray; 2.00 A; A=2-353.
DR PDB; 1U99; X-ray; 2.60 A; A=2-353.
DR PDB; 1XMS; X-ray; 2.10 A; A=2-353.
DR PDB; 1XMV; X-ray; 1.90 A; A=2-353.
DR PDB; 2REB; X-ray; 2.30 A; A=2-353.
DR PDB; 2REC; EM; -; A/B/C/D/E/F=1-353.
DR PDB; 3CMT; X-ray; 3.15 A; A/D=2-335.
DR PDB; 3CMU; X-ray; 4.20 A; A=2-335.
DR PDB; 3CMV; X-ray; 4.30 A; A/B/C/D/E/F/G/H=2-335.
DR PDB; 3CMW; X-ray; 2.80 A; A/C=2-335.
DR PDB; 3CMX; X-ray; 3.40 A; A/D=2-335.
DR PDB; 4TWZ; X-ray; 2.80 A; A=2-353.
DR PDB; 7JY6; EM; 2.50 A; A/B/C/D/E/F/G/H/I=1-334.
DR PDB; 7JY7; EM; 2.90 A; A/B/C/D/E/F/G/H/I=1-334.
DR PDB; 7JY8; EM; 2.50 A; A/B/C/D/E/F/G/H/I=1-334.
DR PDB; 7JY9; EM; 2.80 A; A/B/C/D/E/F/G/H/I=1-334.
DR PDBsum; 1AA3; -.
DR PDBsum; 1N03; -.
DR PDBsum; 1REA; -.
DR PDBsum; 1U94; -.
DR PDBsum; 1U98; -.
DR PDBsum; 1U99; -.
DR PDBsum; 1XMS; -.
DR PDBsum; 1XMV; -.
DR PDBsum; 2REB; -.
DR PDBsum; 2REC; -.
DR PDBsum; 3CMT; -.
DR PDBsum; 3CMU; -.
DR PDBsum; 3CMV; -.
DR PDBsum; 3CMW; -.
DR PDBsum; 3CMX; -.
DR PDBsum; 4TWZ; -.
DR PDBsum; 7JY6; -.
DR PDBsum; 7JY7; -.
DR PDBsum; 7JY8; -.
DR PDBsum; 7JY9; -.
DR AlphaFoldDB; P0A7G6; -.
DR SMR; P0A7G6; -.
DR BioGRID; 4259218; 460.
DR BioGRID; 851502; 2.
DR ComplexPortal; CPX-5544; DNA polymerase V mutasome complex.
DR DIP; DIP-31832N; -.
DR IntAct; P0A7G6; 33.
DR STRING; 511145.b2699; -.
DR BindingDB; P0A7G6; -.
DR ChEMBL; CHEMBL3434; -.
DR SWISS-2DPAGE; P0A7G6; -.
DR jPOST; P0A7G6; -.
DR PaxDb; P0A7G6; -.
DR PRIDE; P0A7G6; -.
DR EnsemblBacteria; AAC75741; AAC75741; b2699.
DR EnsemblBacteria; BAA16561; BAA16561; BAA16561.
DR GeneID; 66673432; -.
DR GeneID; 947170; -.
DR KEGG; ecj:JW2669; -.
DR KEGG; eco:b2699; -.
DR PATRIC; fig|1411691.4.peg.4043; -.
DR EchoBASE; EB0816; -.
DR eggNOG; COG0468; Bacteria.
DR HOGENOM; CLU_040469_3_2_6; -.
DR InParanoid; P0A7G6; -.
DR OMA; DYGEQAL; -.
DR PhylomeDB; P0A7G6; -.
DR BioCyc; EcoCyc:EG10823-MON; -.
DR BioCyc; MetaCyc:EG10823-MON; -.
DR EvolutionaryTrace; P0A7G6; -.
DR PRO; PR:P0A7G6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009355; C:DNA polymerase V complex; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:EcoCyc.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:EcoliWiki.
DR GO; GO:0048870; P:cell motility; IMP:EcoliWiki.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0006310; P:DNA recombination; IMP:CACAO.
DR GO; GO:0035825; P:homologous recombination; TAS:EcoCyc.
DR GO; GO:0000725; P:recombinational repair; TAS:EcoCyc.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:EcoCyc.
DR GO; GO:0009432; P:SOS response; IDA:ComplexPortal.
DR GO; GO:0019985; P:translesion synthesis; IDA:ComplexPortal.
DR CDD; cd00983; recA; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00268; RecA; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013765; DNA_recomb/repair_RecA.
DR InterPro; IPR020584; DNA_recomb/repair_RecA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR023400; RecA_C.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR PANTHER; PTHR45900; PTHR45900; 1.
DR Pfam; PF00154; RecA; 1.
DR PRINTS; PR00142; RECA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54752; SSF54752; 1.
DR TIGRFAMs; TIGR02012; tigrfam_recA; 1.
DR PROSITE; PS00321; RECA_1; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing;
KW DNA damage; DNA recombination; DNA repair; DNA-binding; Nucleotide-binding;
KW Reference proteome; SOS response; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6244554,
FT ECO:0000269|PubMed:6930655"
FT CHAIN 2..353
FT /note="Protein RecA"
FT /id="PRO_0000122703"
FT REGION 330..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 67..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268,
FT ECO:0000269|PubMed:1731253"
FT CONFLICT 191
FT /note="Missing (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 8..22
FT /evidence="ECO:0007829|PDB:1U94"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:1XMV"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:3CMW"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:7JY6"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:7JY8"
FT HELIX 46..51
FT /evidence="ECO:0007829|PDB:1U94"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:1U94"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:1U94"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:1U94"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:1U94"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:1U94"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1U94"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1U94"
FT HELIX 123..136
FT /evidence="ECO:0007829|PDB:1U94"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:1U94"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:1U94"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:1U94"
FT HELIX 167..186
FT /evidence="ECO:0007829|PDB:1U94"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:1U94"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:3CMW"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:7JY9"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:7JY6"
FT HELIX 214..219
FT /evidence="ECO:0007829|PDB:1U94"
FT STRAND 221..253
FT /evidence="ECO:0007829|PDB:1U94"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:1U94"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:1U94"
FT HELIX 271..281
FT /evidence="ECO:0007829|PDB:1U94"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:1U94"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:1U94"
FT STRAND 297..302
FT /evidence="ECO:0007829|PDB:1U94"
FT HELIX 303..312
FT /evidence="ECO:0007829|PDB:1U94"
FT HELIX 314..328
FT /evidence="ECO:0007829|PDB:1U94"
SQ SEQUENCE 353 AA; 37973 MW; 866EF8F83BE32A36 CRC64;
MAIDENKQKA LAAALGQIEK QFGKGSIMRL GEDRSMDVET ISTGSLSLDI ALGAGGLPMG
RIVEIYGPES SGKTTLTLQV IAAAQREGKT CAFIDAEHAL DPIYARKLGV DIDNLLCSQP
DTGEQALEIC DALARSGAVD VIVVDSVAAL TPKAEIEGEI GDSHMGLAAR MMSQAMRKLA
GNLKQSNTLL IFINQIRMKI GVMFGNPETT TGGNALKFYA SVRLDIRRIG AVKEGENVVG
SETRVKVVKN KIAAPFKQAE FQILYGEGIN FYGELVDLGV KEKLIEKAGA WYSYKGEKIG
QGKANATAWL KDNPETAKEI EKKVRELLLS NPNSTPDFSV DDSEGVAETN EDF
