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Database: UniProt/SWISS-PROT
Entry: LIGD_MYCS2
LinkDB: LIGD_MYCS2
Original site: LIGD_MYCS2 
ID   LIGD_MYCS2              Reviewed;         762 AA.
AC   A0R3R7; I7FKR9;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 2.
DT   26-FEB-2020, entry version 93.
DE   RecName: Full=Multifunctional non-homologous end joining protein LigD;
DE   AltName: Full=NHEJ DNA polymerase;
DE   Includes:
DE     RecName: Full=DNA repair polymerase;
DE              Short=Pol;
DE     AltName: Full=Polymerase/primase;
DE   Includes:
DE     RecName: Full=3'-phosphoesterase;
DE              Short=3'-ribonuclease/3'-phosphatase;
DE              Short=PE;
DE   Includes:
DE     RecName: Full=DNA ligase;
DE              Short=Lig;
DE              EC=6.5.1.1;
DE     AltName: Full=Polydeoxyribonucleotide synthase [ATP];
GN   Name=ligD; OrderedLocusNames=MSMEG_5570, MSMEI_5419;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-136 AND ASP-138.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=15778718; DOI=10.1038/nsmb915;
RA   Gong C., Bongiorno P., Martins A., Stephanou N.C., Zhu H., Shuman S.,
RA   Glickman M.S.;
RT   "Mechanism of nonhomologous end-joining in mycobacteria: a low-fidelity
RT   repair system driven by Ku, ligase D and ligase C.";
RL   Nat. Struct. Mol. Biol. 12:304-312(2005).
RN   [5]
RP   FUNCTION, PROBABLE ACTIVE SITE, AND MUTAGENESIS OF LYS-484.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=16476729; DOI=10.1074/jbc.m513550200;
RA   Akey D., Martins A., Aniukwu J., Glickman M.S., Shuman S., Berger J.M.;
RT   "Crystal structure and nonhomologous end-joining function of the ligase
RT   component of Mycobacterium DNA ligase D.";
RL   J. Biol. Chem. 281:13412-13423(2006).
RN   [6]
RP   FUNCTION IN VIRAL REPLICATION, INTERACTION WITH VIRAL KU HOMOLOGS,
RP   DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 136-ASP--ASP-138 AND LYS-484.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=16949369; DOI=10.1016/j.molcel.2006.07.009;
RA   Pitcher R.S., Tonkin L.M., Daley J.M., Palmbos P.L., Green A.J.,
RA   Velting T.L., Brzostek A., Korycka-Machala M., Cresawn S., Dziadek J.,
RA   Hatfull G.F., Wilson T.E., Doherty A.J.;
RT   "Mycobacteriophage exploit NHEJ to facilitate genome circularization.";
RL   Mol. Cell 23:743-748(2006).
RN   [7]
RP   FUNCTION, AND MUTAGENESIS OF 136-ASP--ASP-138.
RX   PubMed=16446439; DOI=10.1073/pnas.0509083103;
RA   Zhu H., Nandakumar J., Aniukwu J., Wang L.K., Glickman M.S., Lima C.D.,
RA   Shuman S.;
RT   "Atomic structure and nonhomologous end-joining function of the polymerase
RT   component of bacterial DNA ligase D.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:1711-1716(2006).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17360246; DOI=10.1016/j.dnarep.2007.02.009;
RA   Pitcher R.S., Green A.J., Brzostek A., Korycka-Machala M., Dziadek J.,
RA   Doherty A.J.;
RT   "NHEJ protects mycobacteria in stationary phase against the harmful effects
RT   of desiccation.";
RL   DNA Repair 6:1271-1276(2007).
RN   [9]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17496093; DOI=10.1128/jb.00332-07;
RA   Stephanou N.C., Gao F., Bongiorno P., Ehrt S., Schnappinger D., Shuman S.,
RA   Glickman M.S.;
RT   "Mycobacterial nonhomologous end joining mediates mutagenic repair of
RT   chromosomal double-strand DNA breaks.";
RL   J. Bacteriol. 189:5237-5246(2007).
RN   [10]
RP   FUNCTION IN GAP FILLING, COFACTOR, DOMAIN, AND DNA-BINDING.
RX   PubMed=17174332; DOI=10.1016/j.jmb.2006.10.046;
RA   Pitcher R.S., Brissett N.C., Picher A.J., Andrade P., Juarez R.,
RA   Thompson D., Fox G.C., Blanco L., Doherty A.J.;
RT   "Structure and function of a mycobacterial NHEJ DNA repair polymerase.";
RL   J. Mol. Biol. 366:391-405(2007).
RN   [11]
RP   FUNCTION, DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   136-ASP--ASP-138; GLU-310; HIS-336; LYS-484 AND GLU-533.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18281464; DOI=10.1101/gad.1631908;
RA   Aniukwu J., Glickman M.S., Shuman S.;
RT   "The pathways and outcomes of mycobacterial NHEJ depend on the structure of
RT   the broken DNA ends.";
RL   Genes Dev. 22:512-527(2008).
RN   [12]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=21219454; DOI=10.1111/j.1365-2958.2010.07463.x;
RA   Gupta R., Barkan D., Redelman-Sidi G., Shuman S., Glickman M.S.;
RT   "Mycobacteria exploit three genetically distinct DNA double-strand break
RT   repair pathways.";
RL   Mol. Microbiol. 79:316-330(2011).
RN   [13]
RP   INTERACTION WITH SIR2, AND SUBUNIT.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=21637345; DOI=10.1371/journal.pone.0020045;
RA   Li Z., Wen J., Lin Y., Wang S., Xue P., Zhang Z., Zhou Y., Wang X., Sui L.,
RA   Bi L.J., Zhang X.E.;
RT   "A Sir2-like protein participates in mycobacterial NHEJ.";
RL   PLoS ONE 6:E20045-E20045(2011).
CC   -!- FUNCTION: With Ku forms a non-homologous end joining (NHEJ) repair
CC       enzyme which repairs blunt-end and 5'-overhang DNA double strand breaks
CC       (DSB) with about 50% fidelity, and DSB with non-complementary 3' ends.
CC       Plays a partial role in NHEJ during 3'-overhang repair. NHEJ repairs
CC       DSB with blunt ends and 5' overhangs with a high level of nucleotide
CC       insertion/deletion, without a need for microhomology. Acts as a DNA
CC       ligase on singly nicked dsDNA, as a DNA-directed DNA polymerase on 5'
CC       overhangs, and adds non-templated nucleotides to 3' overhangs (terminal
CC       transferase). Fills in gaps in dsDNA, prefers a 5'-phosphate in the
CC       gap. Site-directed mutations leading to ligase loss alter the bias from
CC       insertion to deletion mutations, and indicate another ligase (LigC1
CC       and/or LigC2) can compensate.
CC   -!- FUNCTION: The preference of the polymerase domain for rNTPs over dNTPs
CC       may be advantageous in dormant cells, where the dNTP pool may be
CC       limiting. {ECO:0000250, ECO:0000269|PubMed:15778718,
CC       ECO:0000269|PubMed:16446439, ECO:0000269|PubMed:16476729,
CC       ECO:0000269|PubMed:16949369, ECO:0000269|PubMed:17174332,
CC       ECO:0000269|PubMed:17360246, ECO:0000269|PubMed:18281464}.
CC   -!- FUNCTION: The ligase activity is required for replication of viruses
CC       with short cos ends (4 bases) such as Mycobacterium phage Omega and
CC       Corndog, but not D29 which has a 9 base cos end. Stimulates dsDNA end
CC       joining by LigD; when expressed with endogenous or Mycobacterium phage
CC       Omega Ku, can reconstitute NHEJ in S.cerevisiae.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP +
CC         diphosphate.; EC=6.5.1.1;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 4 Mn(2+); 2 Mn(2+) for polymerase/primase activity, 1 each
CC       for 3-phosphoesterase and ligase. {ECO:0000250};
CC   -!- SUBUNIT: Interacts with Sir2 and probably also with Ku; may form a
CC       trimeric complex during NHEJ. Interacts with Mycobacterium phage Omega
CC       and Corndog Ku homologs (AC Q853W0, AC Q856K7).
CC       {ECO:0000269|PubMed:16949369, ECO:0000269|PubMed:21637345}.
CC   -!- DOMAIN: The N-terminal divalent cation-dependent polymerase/primase
CC       domain (Pol) functions as an independent domain (PubMed:17174332).
CC       Deletion of the Pol domain (residues 1-288) yields a protein severely
CC       impaired in NHEJ on blunt or 5'-overhangs (PubMed:18281464).
CC       {ECO:0000269|PubMed:17174332, ECO:0000269|PubMed:18281464}.
CC   -!- DOMAIN: The central 3'-phosphoesterase domain (PE) (PubMed:17174332).
CC       Mutations in the PE domain argue against this domain being involved in
CC       residue deletion during NHEJ (PubMed:18281464).
CC       {ECO:0000269|PubMed:17174332, ECO:0000269|PubMed:18281464}.
CC   -!- DOMAIN: The C-terminal ATP-dependent ligase domain (Lig) functions as
CC       an independent domain (PubMed:17174332). Loss of the Lig domain
CC       (residues 449 to 762) forces NHEJ to rely on another ligase, which
CC       decreases fidelity for blunt and 5'-overhang DSB (PubMed:18281464).
CC       {ECO:0000269|PubMed:17174332, ECO:0000269|PubMed:18281464}.
CC   -!- DISRUPTION PHENOTYPE: Not essential for growth in the absence of DNA
CC       damage. 320-fold reduction in NHEJ on blunt-ended DSB, with a loss of
CC       nucleotide insertions. 100-fold less efficient repair of 5'-overhang
CC       DSBs with little nucleotide insertion. Upon deletion, the fidelity of
CC       DNA repair depends on the form of the DSB; for blunt-ends fidelity is
CC       very low, for 5'-overhangs remains 50% faithful, for 3'-overhangs
CC       repair is fully faithful. NHEJ on blunt-ended plasmid is 24-fold
CC       further decreased in a triple ligC1-ligC2-ligD deletion. In quadruple
CC       ligB-ligC1-ligC2-ligD deletions NHEJ on blunt and 5'-overhangs is 0.22
CC       and 0.12% of wild-type respectively; only 4-fold decrease in 3'-
CC       overhang NHEJ. 100-fold decrease in viability when exposed to ionizing
CC       radiation in late and stationary phase; 1000-fold decrease in a double
CC       ligD-ku deletion. Decreased resistance to desiccation-induced DSBs.
CC       Mycobacterium phage Omega and Corndog are unable to infect a deletion
CC       strain. Loss of NHEJ on incompatible 3'-chromosomal overhangs, partial
CC       reduction in single-strand annealing DSB repair.
CC       {ECO:0000269|PubMed:15778718, ECO:0000269|PubMed:16949369,
CC       ECO:0000269|PubMed:17360246, ECO:0000269|PubMed:17496093,
CC       ECO:0000269|PubMed:18281464, ECO:0000269|PubMed:21219454}.
CC   -!- MISCELLANEOUS: LigD has variable architecture; domain order can be
CC       permutated, domains can be independently encoded, while some bacteria
CC       lack the 3'-phosphoesterase domain entirely.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the LigD polymerase
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: In the central section; belongs to the LigD 3'-
CC       phosphoesterase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the ATP-dependent DNA
CC       ligase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK75957.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
DR   EMBL; CP000480; ABK75957.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP001663; AFP41860.1; -; Genomic_DNA.
DR   RefSeq; YP_889805.1; NC_008596.1.
DR   SMR; A0R3R7; -.
DR   STRING; 246196.MSMEI_5419; -.
DR   EnsemblBacteria; ABK75957; ABK75957; MSMEG_5570.
DR   EnsemblBacteria; AFP41860; AFP41860; MSMEI_5419.
DR   GeneID; 4535131; -.
DR   KEGG; msg:MSMEI_5419; -.
DR   KEGG; msm:MSMEG_5570; -.
DR   PATRIC; fig|246196.19.peg.5431; -.
DR   eggNOG; ENOG4105DQE; Bacteria.
DR   eggNOG; COG1793; LUCA.
DR   eggNOG; COG3285; LUCA.
DR   KO; K10747; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:UniProtKB.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   CDD; cd04863; MtLigD_Pol_like; 1.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR014146; LigD_ligase_dom.
DR   InterPro; IPR014144; LigD_PE_domain.
DR   InterPro; IPR014145; LigD_pol_dom.
DR   InterPro; IPR033649; MtLigD_Pol-like.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF13298; LigD_N; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR02777; LigD_PE_dom; 1.
DR   TIGRFAMs; TIGR02778; ligD_pol; 1.
DR   TIGRFAMs; TIGR02779; NHEJ_ligase_lig; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW   DNA-directed DNA polymerase; Exonuclease; Host-virus interaction;
KW   Hydrolase; Ligase; Manganese; Metal-binding; Multifunctional enzyme;
KW   Nuclease; Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..762
FT                   /note="Multifunctional non-homologous end joining protein
FT                   LigD"
FT                   /id="PRO_0000425949"
FT   DNA_BIND        18..21
FT                   /evidence="ECO:0000250"
FT   DNA_BIND        31
FT                   /evidence="ECO:0000250"
FT   DNA_BIND        58..60
FT                   /evidence="ECO:0000250"
FT   DNA_BIND        68..72
FT                   /evidence="ECO:0000250"
FT   DNA_BIND        76
FT                   /evidence="ECO:0000250"
FT   DNA_BIND        88..93
FT                   /evidence="ECO:0000250"
FT   DNA_BIND        109
FT                   /evidence="ECO:0000250"
FT   NP_BIND         136..138
FT                   /note="Substrate; for polymerase activity"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         171..177
FT                   /note="Substrate; for polymerase activity"
FT                   /evidence="ECO:0000250"
FT   DNA_BIND        233..234
FT                   /evidence="ECO:0000250"
FT   REGION          14..260
FT                   /note="DNA repair polymerase domain (Pol)"
FT   REGION          296..453
FT                   /note="3'-phosphoesterase domain (PE)"
FT   REGION          463..760
FT                   /note="Ligase domain (Lig)"
FT   ACT_SITE        484
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000305"
FT   METAL           136
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000250"
FT   METAL           136
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000250"
FT   METAL           138
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000250"
FT   METAL           138
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000250"
FT   METAL           226
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000250"
FT   METAL           330
FT                   /note="Manganese 3; via pros nitrogen; catalytic; for 3'-
FT                   phosphoesterase activity"
FT                   /evidence="ECO:0000250"
FT   METAL           336
FT                   /note="Manganese 3; via tele nitrogen; catalytic; for 3'-
FT                   phosphoesterase activity"
FT                   /evidence="ECO:0000250"
FT   METAL           338
FT                   /note="Manganese 3; catalytic; for 3'-phosphoesterase
FT                   activity"
FT                   /evidence="ECO:0000250"
FT   METAL           486
FT                   /note="Manganese 4"
FT                   /evidence="ECO:0000250"
FT   METAL           616
FT                   /note="Manganese 4"
FT                   /evidence="ECO:0000250"
FT   BINDING         57
FT                   /note="Substrate; for polymerase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /note="Substrate; for polymerase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         229
FT                   /note="Substrate; for polymerase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         235
FT                   /note="Substrate; for polymerase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         243
FT                   /note="Substrate; for polymerase activity"
FT                   /evidence="ECO:0000250"
FT   SITE            372
FT                   /note="Transition state stabilizer; for 3'-phosphoesterase
FT                   activity"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         136..138
FT                   /note="DLD->ALA: In vivo 30% reduction in NHEJ on blunt-end
FT                   DSB, fidelity doubles, loss of non-templated nucleotide
FT                   insertion during NHEJ. No effect on efficiency of DSB on
FT                   5'- or 3'-overhangs, increased fidelity on 5'-overhangs. No
FT                   effect on viral infection."
FT                   /evidence="ECO:0000269|PubMed:16446439,
FT                   ECO:0000269|PubMed:16949369, ECO:0000269|PubMed:18281464"
FT   MUTAGEN         136
FT                   /note="D->A: Loss of templated and non-templated DNA
FT                   synthesis, but not ligase activity."
FT                   /evidence="ECO:0000269|PubMed:15778718"
FT   MUTAGEN         138
FT                   /note="D->A: Loss of templated and non-templated DNA
FT                   synthesis, but not ligase activity."
FT                   /evidence="ECO:0000269|PubMed:15778718"
FT   MUTAGEN         310
FT                   /note="E->A: No effect on efficiency or fidelity on NHEJ of
FT                   blunt, 5'-overhangs or 3'-overhangs."
FT                   /evidence="ECO:0000269|PubMed:18281464"
FT   MUTAGEN         336
FT                   /note="H->A: No effect on efficiency or fidelity on NHEJ of
FT                   blunt, 5'-overhangs or 3'-overhangs."
FT                   /evidence="ECO:0000269|PubMed:18281464"
FT   MUTAGEN         484
FT                   /note="K->A: 2.7 and 3.7-fold decrease in efficiency of
FT                   NHEJ on blunt and 5'-overhangs respectively. Considerably
FT                   decreases NHEJ fidelity on both DSBs. No viral infection."
FT                   /evidence="ECO:0000269|PubMed:16476729,
FT                   ECO:0000269|PubMed:16949369, ECO:0000269|PubMed:18281464"
FT   MUTAGEN         533
FT                   /note="E->A: 3-fold and 9-fold decrease in efficiency of
FT                   NHEJ on blunt and 5'-overhangs respectively, with very
FT                   decreased fidelity on both DSBs. No viral infection."
FT                   /evidence="ECO:0000269|PubMed:18281464"
SQ   SEQUENCE   762 AA;  85516 MW;  ED1853A73A3E552E CRC64;
     MARHPWGMER YERVRLTNPD KVLYPATGTT KAEVFDYYLS IAQVMVPHIA GRPVTRKRWP
     NGVAEEAFFE KQLASSAPSW LERGSITHKS GTTTYPIINT REGLAWVAQQ ASLEVHVPQW
     RFEDGDQGPA TRIVFDLDPG EGVTMTQLCE IAHEVRALMT DLDLETYPLT SGSKGLHLYV
     PLAEPISSRG ASVLARRVAQ QLEQAMPKLV TATMTKSLRA GKVFLDWSQN NAAKTTIAPY
     SLRGRDHPTV AAPRTWDEIA DPELRHLRFD EVLDRLDEYG DLLAPLDADA PIADKLTTYR
     SMRDASKTPE PVPKEIPKTG NNDKFVIQEH HARRLHYDLR LERDGVLVSF AVPKNLPETT
     AENRLAVHTE DHPIEYLAFH GSIPKGEYGA GDMVIWDSGS YETEKFRVPE ELDNPDDSHG
     EIIVTLHGEK VDGRYALIQT KGKNWLAHRM KDQKNARPED FAPMLATEGS VAKYKAKQWA
     FEGKWDGYRV IIDADHGQLQ IRSRTGREVT GEYPQFKALA ADLAEHHVVL DGEAVALDES
     GVPSFGQMQN RARSTRVEFW AFDILWLDGR SLLRAKYSDR RKILEALADG GGLIVPDQLP
     GDGPEAMEHV RKKRFEGVVA KKWDSTYQPG RRSSSWIKDK IWNTQEVVIG GWRQGEGGRS
     SGIGALVLGI PGPEGLQFVG RVGTGFTEKE LSKLKDMLKP LHTDESPFNA PLPKVDARGV
     TFVRPELVGE VRYSERTSDG RLRQPSWRGL RPDKTPDEVV WE
//
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