ID   RAD32_SCHPO             Reviewed;         649 AA.
AC   Q09683;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-SEP-2026, entry version 184.
DE   RecName: Full=Double-strand break repair protein rad32;
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:P49959};
GN   Name=rad32 {ECO:0000303|PubMed:7885834,
GN   ECO:0000312|PomBase:SPAC13C5.07}; ORFNames=SPAC13C5.07;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=7885834; DOI=10.1093/nar/23.3.383;
RA   Tavassoli M., Shayeghi M., Nasim A., Watts F.Z.;
RT   "Cloning and characterisation of the Schizosaccharomyces pombe rad32 gene:
RT   a gene required for repair of double strand breaks and recombination.";
RL   Nucleic Acids Res. 23:383-388(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=12944482; DOI=10.1128/mcb.23.18.6564-6573.2003;
RA   Chahwan C., Nakamura T.M., Sivakumar S., Russell P., Rhind N.;
RT   "The fission yeast Rad32 (Mre11)-Rad50-Nbs1 complex is required for the S-
RT   phase DNA damage checkpoint.";
RL   Mol. Cell. Biol. 23:6564-6573(2003).
RN   [4]
RP   FUNCTION.
RX   PubMed=15654094; DOI=10.1534/genetics.104.037515;
RA   Farah J.A., Cromie G., Steiner W.W., Smith G.R.;
RT   "A novel recombination pathway initiated by the Mre11/Rad50/Nbs1 complex
RT   eliminates palindromes during meiosis in Schizosaccharomyces pombe.";
RL   Genetics 169:1261-1274(2005).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-248.
RX   PubMed=23080121; DOI=10.1093/nar/gks954;
RA   Limbo O., Moiani D., Kertokalio A., Wyman C., Tainer J.A., Russell P.;
RT   "Mre11 ATLD17/18 mutation retains Tel1/ATM activity but blocks DNA double-
RT   strand break repair.";
RL   Nucleic Acids Res. 40:11435-11449(2012).
RN   [6] {ECO:0007744|PDB:4FBK, ECO:0007744|PDB:4FBQ, ECO:0007744|PDB:4FBW, ECO:0007744|PDB:4FCX}
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 7-413 IN COMPLEX WITH MANGANESE
RP   AND NBS1, FUNCTION, COFACTOR, AND INTERACTION WITH NBS1.
RX   PubMed=22705791; DOI=10.1038/nsmb.2323;
RA   Schiller C.B., Lammens K., Guerini I., Coordes B., Feldmann H.,
RA   Schlauderer F., Moeckel C., Schele A., Straesser K., Jackson S.P.,
RA   Hopfner K.P.;
RT   "Structure of Mre11-Nbs1 complex yields insights into ataxia-
RT   telangiectasia-like disease mutations and DNA damage signaling.";
RL   Nat. Struct. Mol. Biol. 19:693-700(2012).
CC   -!- FUNCTION: Core component of the MRN complex, which plays a central role
CC       in double-strand break (DSB) repair, DNA recombination, maintenance of
CC       telomere integrity and meiosis (PubMed:15654094, PubMed:22705791,
CC       PubMed:23080121, PubMed:7885834). The MRN complex is involved in the
CC       repair of DNA double-strand breaks (DSBs) via homologous recombination
CC       (HR), an error-free mechanism which primarily occurs during S and G2
CC       phases (By similarity). The complex (1) mediates the end resection of
CC       damaged DNA, which generates proper single-stranded DNA, a key initial
CC       steps in HR, and is (2) required for the recruitment of other repair
CC       factors and efficient activation of ATM and ATR upon DNA damage (By
CC       similarity). Within the MRN complex, rad32 possesses both single-strand
CC       endonuclease activity and double-strand-specific 3'-5' exonuclease
CC       activity (Probable) (PubMed:22705791). Rad32 first endonucleolytically
CC       cleaves the 5' strand at DNA DSB ends to prevent non-homologous end
CC       joining (NHEJ) and licence HR (By similarity). It then generates a
CC       single-stranded DNA gap via 3' to 5' exonucleolytic degradation, which
CC       is required for single-strand invasion and recombination (By
CC       similarity). {ECO:0000250|UniProtKB:P49959,
CC       ECO:0000269|PubMed:15654094, ECO:0000269|PubMed:22705791,
CC       ECO:0000269|PubMed:23080121, ECO:0000269|PubMed:7885834,
CC       ECO:0000305|PubMed:22705791}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:22705791};
CC   -!- SUBUNIT: Forms a multisubunit endonuclease complex, MRN, together with
CC       nbn and rad50. {ECO:0000269|PubMed:12944482,
CC       ECO:0000269|PubMed:22705791}.
CC   -!- INTERACTION:
CC       Q09683; O43070: nbs1; NbExp=6; IntAct=EBI-2124866, EBI-2125045;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12944482}.
CC       Chromosome, telomere {ECO:0000250|UniProtKB:P49959}. Chromosome
CC       {ECO:0000269|PubMed:23080121}. Note=Localizes to discrete nuclear foci
CC       after treatment with genotoxic agents. {ECO:0000269|PubMed:23080121}.
CC   -!- SIMILARITY: Belongs to the MRE11/RAD32 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X82322; CAA57765.1; ALT_TERM; Genomic_DNA.
DR   EMBL; CU329670; CAA90458.1; -; Genomic_DNA.
DR   PIR; S58097; S58097.
DR   RefSeq; NP_592935.1; NM_001018336.3.
DR   PDB; 4FBK; X-ray; 2.38 A; A/B=16-413.
DR   PDB; 4FBQ; X-ray; 2.50 A; A/B=16-413.
DR   PDB; 4FBW; X-ray; 2.20 A; A/B=7-413.
DR   PDB; 4FCX; X-ray; 3.00 A; A/B=15-413.
DR   AlphaFoldDB; Q09683; -.
DR   SMR; Q09683; -.
DR   BioGRID; 279207; 138.
DR   ComplexPortal; CPX-10302; MRN double-strand break repair complex.
DR   DIP; DIP-52388N; -.
DR   FunCoup; Q09683; 744.
DR   IntAct; Q09683; 2.
DR   STRING; 284812.Q09683; -.
DR   iPTMnet; Q09683; -.
DR   PaxDb; 284812-Q09683; -.
DR   GeneID; 2542757; -.
DR   KEGG; spo:2542757; -.
DR   PomBase; SPAC13C5.07; -.
DR   VEuPathDB; FungiDB:SPAC13C5.07; -.
DR   eggNOG; KOG2310; Eukaryota.
DR   HOGENOM; CLU_009535_3_0_1; -.
DR   InParanoid; Q09683; -.
DR   OMA; QNHTGHT; -.
DR   PhylomeDB; Q09683; -.
DR   Reactome; R-SPO-1834949; Cytosolic sensors of pathogen-associated DNA.
DR   Reactome; R-SPO-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR   Reactome; R-SPO-5685939; HDR through MMEJ (alt-NHEJ).
DR   Reactome; R-SPO-5693548; Sensing of DNA Double Strand Breaks.
DR   Reactome; R-SPO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   EvolutionaryTrace; Q09683; -.
DR   PRO; PR:Q09683; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005694; C:chromosome; EXP:UniProtKB.
DR   GO; GO:0140445; C:chromosome, telomeric repeat region; IDA:PomBase.
DR   GO; GO:0030870; C:Mre11 complex; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; EXP:UniProtKB.
DR   GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR   GO; GO:0045027; F:DNA end binding; ISO:PomBase.
DR   GO; GO:0008311; F:double-stranded DNA 3'-5' DNA exonuclease activity; ISO:PomBase.
DR   GO; GO:0030145; F:manganese ion binding; IDA:PomBase.
DR   GO; GO:0004518; F:nuclease activity; IDA:PomBase.
DR   GO; GO:0000014; F:single-stranded DNA endonuclease activity; ISO:PomBase.
DR   GO; GO:0000403; F:Y-form DNA binding; ISO:PomBase.
DR   GO; GO:0000729; P:DNA double-strand break processing; IMP:PomBase.
DR   GO; GO:0006302; P:double-strand break repair; IMP:PomBase.
DR   GO; GO:1990918; P:double-strand break repair involved in meiotic recombination; IMP:PomBase.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:PomBase.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:CACAO.
DR   GO; GO:0042138; P:meiotic DNA double-strand break formation; IMP:PomBase.
DR   GO; GO:0097552; P:mitochondrial double-strand break repair via homologous recombination; IBA:GO_Central.
DR   GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IBA:GO_Central.
DR   GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IMP:PomBase.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IMP:PomBase.
DR   GO; GO:0000723; P:telomere maintenance; IGI:PomBase.
DR   CDD; cd00840; MPP_Mre11_N; 1.
DR   DisProt; DP02842; -.
DR   FunFam; 3.30.110.110:FF:000004; Double-strand break repair protein; 1.
DR   FunFam; 3.60.21.10:FF:000011; Double-strand break repair protein; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 3.30.110.110; Mre11, capping domain; 1.
DR   IDEAL; IID50245; -.
DR   InterPro; IPR004843; Calcineurin-like_PHP.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR003701; Mre11.
DR   InterPro; IPR038487; Mre11_capping_dom.
DR   InterPro; IPR007281; Mre11_DNA-bd.
DR   InterPro; IPR041796; Mre11_N.
DR   NCBIfam; TIGR00583; mre11; 1.
DR   PANTHER; PTHR10139; DOUBLE-STRAND BREAK REPAIR PROTEIN MRE11; 1.
DR   PANTHER; PTHR10139:SF1; DOUBLE-STRAND BREAK REPAIR PROTEIN MRE11; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF04152; Mre11_DNA_bind; 1.
DR   PIRSF; PIRSF000882; DSB_repair_MRE11; 1.
DR   SMART; SM01347; Mre11_DNA_bind; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PDBsum; 4FBK; -.
DR   PDBsum; 4FBQ; -.
DR   PDBsum; 4FBW; -.
DR   PDBsum; 4FCX; -.
PE   1: Evidence at protein level;
KW   3D-structure; Chromosome; DNA damage; DNA repair; Endonuclease;
KW   Exonuclease; Hydrolase; Manganese; Meiosis; Metal-binding; Nuclease;
KW   Nucleus; Reference proteome; Telomere.
FT   CHAIN           1..649
FT                   /note="Double-strand break repair protein rad32"
FT                   /id="PRO_0000138683"
FT   REGION          553..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..596
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..636
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..649
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        134
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PIRSR:PIRSR000882-1"
FT   BINDING         25
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:22705791,
FT                   ECO:0007744|PDB:4FBQ, ECO:0007744|PDB:4FBW,
FT                   ECO:0007744|PDB:4FCX"
FT   BINDING         27
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:22705791,
FT                   ECO:0007744|PDB:4FBQ, ECO:0007744|PDB:4FBW,
FT                   ECO:0007744|PDB:4FCX"
FT   BINDING         65
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:22705791,
FT                   ECO:0007744|PDB:4FBQ, ECO:0007744|PDB:4FBW,
FT                   ECO:0007744|PDB:4FCX"
FT   BINDING         65
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:22705791,
FT                   ECO:0007744|PDB:4FBQ, ECO:0007744|PDB:4FBW,
FT                   ECO:0007744|PDB:4FCX"
FT   BINDING         133
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:22705791,
FT                   ECO:0007744|PDB:4FBQ, ECO:0007744|PDB:4FBW,
FT                   ECO:0007744|PDB:4FCX"
FT   BINDING         222
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:22705791,
FT                   ECO:0007744|PDB:4FBQ, ECO:0007744|PDB:4FBW,
FT                   ECO:0007744|PDB:4FCX"
FT   BINDING         250
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:22705791,
FT                   ECO:0007744|PDB:4FBQ, ECO:0007744|PDB:4FBW,
FT                   ECO:0007744|PDB:4FCX"
FT   BINDING         252
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:22705791,
FT                   ECO:0007744|PDB:4FBQ, ECO:0007744|PDB:4FBW,
FT                   ECO:0007744|PDB:4FCX"
FT   MUTAGEN         248
FT                   /note="W->R: Decreased repair of double strand breaks
FT                   (DSBs)."
FT                   /evidence="ECO:0000269|PubMed:23080121"
FT   STRAND          18..23
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   TURN            29..33
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   TURN            35..39
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   HELIX           40..54
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   STRAND          58..62
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   STRAND          67..71
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   HELIX           74..88
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   STRAND          89..91
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   HELIX           92..94
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   STRAND          97..101
FT                   /evidence="ECO:0007829|PDB:4FBK"
FT   HELIX           115..117
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   STRAND          123..125
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   STRAND          127..129
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   HELIX           133..135
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   HELIX           145..151
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   STRAND          154..157
FT                   /evidence="ECO:0007829|PDB:4FCX"
FT   STRAND          167..169
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   STRAND          172..176
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   STRAND          179..186
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   HELIX           191..199
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   STRAND          203..209
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   TURN            210..214
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   STRAND          215..223
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   STRAND          228..233
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   HELIX           236..238
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   STRAND          244..250
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   STRAND          255..261
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   TURN            262..265
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   STRAND          266..270
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   HELIX           281..284
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   STRAND          288..295
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   STRAND          298..305
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   STRAND          307..309
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   STRAND          312..318
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   HELIX           319..321
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   STRAND          327..329
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   HELIX           332..358
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   HELIX           367..372
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   STRAND          373..379
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   TURN            381..383
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   HELIX           389..394
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   TURN            395..399
FT                   /evidence="ECO:0007829|PDB:4FBW"
FT   STRAND          406..410
FT                   /evidence="ECO:0007829|PDB:4FBW"
SQ   SEQUENCE   649 AA;  73689 MW;  400B349EF4FA3428 CRC64;
     MPNDPSDMNN ELHNENTIRI LISSDPHVGY GEKDPVRGND SFVSFNEILE IARERDVDMI
     LLGGDIFHDN KPSRKALYQA LRSLRLNCLG DKPCELELLS DTSLTTGDTA VCNINYLDPN
     INVAIPVFSI HGNHDDPSGD GRYSALDILQ VTGLVNYFGR VPENDNIVVS PILLQKGFTK
     LALYGISNVR DERLYHSFRE NKVKFLRPDL YRDEWFNLLT VHQNHSAHTP TSYLPESFIQ
     DFYDFVLWGH EHECLIDGSY NPTQKFTVVQ PGSTIATSLS PGETAPKHCG ILNITGKDFH
     LEKIRLRTVR PFIMKDIILS EVSSIPPMVE NKKEVLTYLI SKVEEAITEA NAQWYEAQGT
     VPVVENEKPP LPLIRLRVDY TGGYQTENPQ RFSNRFVGRV ANATDVVQFY LKKKYTRSKR
     NDGLYTSAVE DIKINSLRVE SLVNEYLKTN RLECLPEDSL GEAVVNFVEK DDRDAIKECV
     ETQLNKQINL LVKKRVTEEN LEQEISSIIN DLPKISTTKR KDYEELPEEV SETSINIAEH
     TPVLKHTSSL LDHHSPLATS SSEHEMEATP SPALLKKTNK RRELPSSLTK KNTRTPQRSK
     EVKKVPARKL SQSTKKSDKN TQSTLLFYDP SSTTEAQYLD NEDDEILDD
//