GenomeNet

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   16-JAN-2019, entry version 88.
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   Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155).
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
RT   orthology 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
RP   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-
RT   fidelity 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.,
RA   Berger J.M.;
RT   "Crystal structure and nonhomologous end-joining function of the
RT   ligase 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
RT   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.,
RA   Lima C.D., Shuman S.;
RT   "Atomic structure and nonhomologous end-joining function of the
RT   polymerase 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
RT   effects 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.,
RA   Shuman S., 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
RT   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
RT   structure of 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
RT   break 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.,
RA   Sui L., 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
CC       breaks (DSB) with about 50% fidelity, and DSB with non-
CC       complementary 3' ends. Plays a partial role in NHEJ during 3'-
CC       overhang repair. NHEJ repairs DSB with blunt ends and 5' overhangs
CC       with a high level of nucleotide insertion/deletion, without a need
CC       for microhomology. Acts as a DNA ligase on singly nicked dsDNA, as
CC       a DNA-directed DNA polymerase on 5' overhangs, and adds non-
CC       templated nucleotides to 3' overhangs (terminal transferase).
CC       Fills in gaps in dsDNA, prefers a 5'-phosphate in the gap. Site-
CC       directed mutations leading to ligase loss alter the bias from
CC       insertion to deletion mutations, and indicate another ligase
CC       (LigC1 and/or LigC2) can compensate.
CC   -!- FUNCTION: The preference of the polymerase domain for rNTPs over
CC       dNTPs may be advantageous in dormant cells, where the dNTP pool
CC       may be 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
CC       viruses with short cos ends (4 bases) such as Mycobacterium phage
CC       Omega and Corndog, but not D29 which has a 9 base cos end.
CC       Stimulates dsDNA end joining by LigD; when expressed with
CC       endogenous or Mycobacterium phage Omega Ku, can reconstitute NHEJ
CC       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
CC       each 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
CC       Omega 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
CC       polymerase/primase domain (Pol) functions as an independent domain
CC       (PubMed:17174332). Deletion of the Pol domain (residues 1-288)
CC       yields a protein severely impaired in NHEJ on blunt or 5'-
CC       overhangs (PubMed:18281464). {ECO:0000269|PubMed:17174332,
CC       ECO:0000269|PubMed:18281464}.
CC   -!- DOMAIN: The central 3'-phosphoesterase domain (PE)
CC       (PubMed:17174332). Mutations in the PE domain argue against this
CC       domain being involved in residue deletion during NHEJ
CC       (PubMed:18281464). {ECO:0000269|PubMed:17174332,
CC       ECO:0000269|PubMed:18281464}.
CC   -!- DOMAIN: The C-terminal ATP-dependent ligase domain (Lig) functions
CC       as 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
CC       (PubMed:18281464). {ECO:0000269|PubMed:17174332,
CC       ECO:0000269|PubMed:18281464}.
CC   -!- DISRUPTION PHENOTYPE: Not essential for growth in the absence of
CC       DNA damage. 320-fold reduction in NHEJ on blunt-ended DSB, with a
CC       loss of nucleotide insertions. 100-fold less efficient repair of
CC       5'-overhang DSBs with little nucleotide insertion. Upon deletion,
CC       the fidelity of DNA repair depends on the form of the DSB; for
CC       blunt-ends fidelity is very low, for 5'-overhangs remains 50%
CC       faithful, for 3'-overhangs repair is fully faithful. NHEJ on
CC       blunt-ended plasmid is 24-fold further decreased in a triple
CC       ligC1-ligC2-ligD deletion. In quadruple ligB-ligC1-ligC2-ligD
CC       deletions NHEJ on blunt and 5'-overhangs is 0.22 and 0.12% of
CC       wild-type respectively; only 4-fold decrease in 3'-overhang NHEJ.
CC       100-fold decrease in viability when exposed to ionizing radiation
CC       in late and stationary phase; 1000-fold decrease in a double ligD-
CC       ku deletion. Decreased resistance to desiccation-induced DSBs.
CC       Mycobacterium phage Omega and Corndog are unable to infect a
CC       deletion strain. Loss of NHEJ on incompatible 3'-chromosomal
CC       overhangs, partial reduction in single-strand annealing DSB
CC       repair. {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
CC       bacteria lack the 3'-phosphoesterase domain entirely.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the LigD
CC       polymerase 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-
CC       dependent DNA ligase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK75957.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; 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.MSMEG_5570; -.
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   HOGENOM; HOG000222509; -.
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; Complete proteome; DNA damage; DNA recombination;
KW   DNA repair; DNA-binding; DNA-directed DNA polymerase; Exonuclease;
KW   Host-virus interaction; Hydrolase; Ligase; Manganese; Metal-binding;
KW   Multifunctional enzyme; Nuclease; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN         1    762       Multifunctional non-homologous end
FT                                joining protein LigD.
FT                                /FTId=PRO_0000425949.
FT   DNA_BIND     18     21       {ECO:0000250}.
FT   DNA_BIND     31     31       {ECO:0000250}.
FT   DNA_BIND     58     60       {ECO:0000250}.
FT   DNA_BIND     68     72       {ECO:0000250}.
FT   DNA_BIND     76     76       {ECO:0000250}.
FT   DNA_BIND     88     93       {ECO:0000250}.
FT   DNA_BIND    109    109       {ECO:0000250}.
FT   NP_BIND     136    138       Substrate; for polymerase activity.
FT                                {ECO:0000250}.
FT   NP_BIND     171    177       Substrate; for polymerase activity.
FT                                {ECO:0000250}.
FT   DNA_BIND    233    234       {ECO:0000250}.
FT   REGION       14    260       DNA repair polymerase domain (Pol).
FT   REGION      296    453       3'-phosphoesterase domain (PE).
FT   REGION      463    760       Ligase domain (Lig).
FT   ACT_SITE    484    484       N6-AMP-lysine intermediate.
FT                                {ECO:0000305}.
FT   METAL       136    136       Manganese 1. {ECO:0000250}.
FT   METAL       136    136       Manganese 2. {ECO:0000250}.
FT   METAL       138    138       Manganese 1. {ECO:0000250}.
FT   METAL       138    138       Manganese 2. {ECO:0000250}.
FT   METAL       226    226       Manganese 2. {ECO:0000250}.
FT   METAL       330    330       Manganese 3; via pros nitrogen;
FT                                catalytic; for 3'-phosphoesterase
FT                                activity. {ECO:0000250}.
FT   METAL       336    336       Manganese 3; via tele nitrogen;
FT                                catalytic; for 3'-phosphoesterase
FT                                activity. {ECO:0000250}.
FT   METAL       338    338       Manganese 3; catalytic; for 3'-
FT                                phosphoesterase activity. {ECO:0000250}.
FT   METAL       486    486       Manganese 4. {ECO:0000250}.
FT   METAL       616    616       Manganese 4. {ECO:0000250}.
FT   BINDING      57     57       Substrate; for polymerase activity.
FT                                {ECO:0000250}.
FT   BINDING     116    116       Substrate; for polymerase activity.
FT                                {ECO:0000250}.
FT   BINDING     229    229       Substrate; for polymerase activity.
FT                                {ECO:0000250}.
FT   BINDING     235    235       Substrate; for polymerase activity.
FT                                {ECO:0000250}.
FT   BINDING     243    243       Substrate; for polymerase activity.
FT                                {ECO:0000250}.
FT   SITE        372    372       Transition state stabilizer; for 3'-
FT                                phosphoesterase activity. {ECO:0000250}.
FT   MUTAGEN     136    138       DLD->ALA: In vivo 30% reduction in NHEJ
FT                                on blunt-end DSB, fidelity doubles, loss
FT                                of non-templated nucleotide insertion
FT                                during NHEJ. No effect on efficiency of
FT                                DSB on 5'- or 3'-overhangs, increased
FT                                fidelity on 5'-overhangs. No effect on
FT                                viral infection.
FT                                {ECO:0000269|PubMed:16446439,
FT                                ECO:0000269|PubMed:16949369,
FT                                ECO:0000269|PubMed:18281464}.
FT   MUTAGEN     136    136       D->A: Loss of templated and non-templated
FT                                DNA synthesis, but not ligase activity.
FT                                {ECO:0000269|PubMed:15778718}.
FT   MUTAGEN     138    138       D->A: Loss of templated and non-templated
FT                                DNA synthesis, but not ligase activity.
FT                                {ECO:0000269|PubMed:15778718}.
FT   MUTAGEN     310    310       E->A: No effect on efficiency or fidelity
FT                                on NHEJ of blunt, 5'-overhangs or 3'-
FT                                overhangs. {ECO:0000269|PubMed:18281464}.
FT   MUTAGEN     336    336       H->A: No effect on efficiency or fidelity
FT                                on NHEJ of blunt, 5'-overhangs or 3'-
FT                                overhangs. {ECO:0000269|PubMed:18281464}.
FT   MUTAGEN     484    484       K->A: 2.7 and 3.7-fold decrease in
FT                                efficiency of NHEJ on blunt and 5'-
FT                                overhangs respectively. Considerably
FT                                decreases NHEJ fidelity on both DSBs. No
FT                                viral infection.
FT                                {ECO:0000269|PubMed:16476729,
FT                                ECO:0000269|PubMed:16949369,
FT                                ECO:0000269|PubMed:18281464}.
FT   MUTAGEN     533    533       E->A: 3-fold and 9-fold decrease in
FT                                efficiency of NHEJ on blunt and 5'-
FT                                overhangs respectively, with very
FT                                decreased fidelity on both DSBs. No viral
FT                                infection. {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
//
DBGET integrated database retrieval system