ID   RAD5_YEAST              Reviewed;        1169 AA.
AC   P32849; D6VY34;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   27-MAR-2024, entry version 206.
DE   RecName: Full=DNA repair protein RAD5;
DE            EC=3.6.4.-;
DE   AltName: Full=Radiation sensitivity protein 5;
DE   AltName: Full=Revertibility protein 2;
GN   Name=RAD5; Synonyms=REV2, SNM2; OrderedLocusNames=YLR032W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=1324406; DOI=10.1128/mcb.12.9.3807-3818.1992;
RA   Johnson R.E., Henderson S.T., Petes T.D., Prakash S., Bankmann M.,
RA   Prakash L.;
RT   "Saccharomyces cerevisiae RAD5-encoded DNA repair protein contains DNA
RT   helicase and zinc-binding sequence motifs and affects the stability of
RT   simple repetitive sequences in the genome.";
RL   Mol. Cell. Biol. 12:3807-3818(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 402-1063.
RX   PubMed=1394508; DOI=10.1007/bf00317921;
RA   Ahne F., Baur M., Eckardt-Schupp F.;
RT   "The REV2 gene of Saccharomyces cerevisiae: cloning and DNA sequence.";
RL   Curr. Genet. 22:277-282(1992).
RN   [5]
RP   CHARACTERIZATION.
RX   PubMed=7961763; DOI=10.1016/s0021-9258(18)46922-0;
RA   Johnson R.E., Prakash S., Prakash L.;
RT   "Yeast DNA repair protein RAD5 that promotes instability of simple
RT   repetitive sequences is a DNA-dependent ATPase.";
RL   J. Biol. Chem. 269:28259-28262(1994).
RN   [6]
RP   FUNCTION.
RX   PubMed=9016623; DOI=10.1093/nar/25.4.743;
RA   Ahne F., Ja B., Eckardt-Schupp F.;
RT   "The RAD5 gene product is involved in the avoidance of non-homologous end-
RT   joining of DNA double strand breaks in the yeast Saccharomyces
RT   cerevisiae.";
RL   Nucleic Acids Res. 25:743-749(1997).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-914, SUBUNIT, AND
RP   INTERACTION WITH RAD18 AND UBC13.
RX   PubMed=10880451; DOI=10.1093/emboj/19.13.3388;
RA   Ulrich H.D., Jentsch S.;
RT   "Two RING finger proteins mediate cooperation between ubiquitin-conjugating
RT   enzymes in DNA repair.";
RL   EMBO J. 19:3388-3397(2000).
RN   [8]
RP   FUNCTION.
RX   PubMed=10924462; DOI=10.1093/genetics/155.4.1633;
RA   Xiao W., Chow B.L., Broomfield S., Hanna M.;
RT   "The Saccharomyces cerevisiae RAD6 group is composed of an error-prone and
RT   two error-free postreplication repair pathways.";
RL   Genetics 155:1633-1641(2000).
RN   [9]
RP   FUNCTION.
RX   PubMed=11884624; DOI=10.1128/mcb.22.7.2419-2426.2002;
RA   Torres-Ramos C.A., Prakash S., Prakash L.;
RT   "Requirement of RAD5 and MMS2 for postreplication repair of UV-damaged DNA
RT   in Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 22:2419-2426(2002).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH POL30 AND UBC9.
RX   PubMed=12226657; DOI=10.1038/nature00991;
RA   Hoege C., Pfander B., Moldovan G.-L., Pyrowolakis G., Jentsch S.;
RT   "RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin
RT   and SUMO.";
RL   Nature 419:135-141(2002).
RN   [11]
RP   FUNCTION, SUBUNIT, INTERACTION WITH UBC13, AND MUTAGENESIS OF CYS-914;
RP   ILE-916; TYR-944 AND ASN-959.
RX   PubMed=12496280; DOI=10.1074/jbc.m212195200;
RA   Ulrich H.D.;
RT   "Protein-protein interactions within an E2-RING finger complex.
RT   Implications for ubiquitin-dependent DNA damage repair.";
RL   J. Biol. Chem. 278:7051-7058(2003).
RN   [12]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [13]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [14]
RP   FUNCTION, INTERACTION WITH POL30; RAD18 AND UBC13, AND MUTAGENESIS OF
RP   538-LYS-THR-539.
RX   PubMed=16224103; DOI=10.1093/nar/gki902;
RA   Chen S., Davies A.A., Sagan D., Ulrich H.D.;
RT   "The RING finger ATPase Rad5p of Saccharomyces cerevisiae contributes to
RT   DNA double-strand break repair in a ubiquitin-independent manner.";
RL   Nucleic Acids Res. 33:5878-5886(2005).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-129 AND
RP   SER-130, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [17]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Probable helicase, member of the UBC2/RAD6 epistasis group.
CC       Functions with the DNA repair protein RAD18 in error-free
CC       postreplication DNA repair. Involved in the maintenance of wild-type
CC       rates of instability of simple repetitive sequences such as poly(GT)
CC       repeats. Seems to be involved in maintaining a balance which acts in
CC       favor of error-prone non-homologous joining during DNA double-strand
CC       breaks repairs. Recruits the UBC13-MMS2 dimer to chromatin for DNA
CC       repair. {ECO:0000269|PubMed:10880451, ECO:0000269|PubMed:10924462,
CC       ECO:0000269|PubMed:11884624, ECO:0000269|PubMed:12226657,
CC       ECO:0000269|PubMed:12496280, ECO:0000269|PubMed:1324406,
CC       ECO:0000269|PubMed:16224103, ECO:0000269|PubMed:9016623}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=525 uM for ATP;
CC       pH dependence:
CC         Optimum pH is 7.0. for ATPase activity.;
CC   -!- SUBUNIT: Homodimer. Interacts with POL30, RAD18, UBC9 and UBC13.
CC       {ECO:0000269|PubMed:10880451, ECO:0000269|PubMed:12226657,
CC       ECO:0000269|PubMed:12496280, ECO:0000269|PubMed:16224103}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- MISCELLANEOUS: Present with 1520 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR   EMBL; M96644; AAA34951.1; -; Genomic_DNA.
DR   EMBL; Z73204; CAA97556.1; -; Genomic_DNA.
DR   EMBL; S46103; AAB23590.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09350.1; -; Genomic_DNA.
DR   PIR; S64859; S64859.
DR   RefSeq; NP_013132.1; NM_001181919.1.
DR   PDB; 5YRQ; X-ray; 2.00 A; A/B/D/E=5-20.
DR   PDBsum; 5YRQ; -.
DR   AlphaFoldDB; P32849; -.
DR   SASBDB; P32849; -.
DR   SMR; P32849; -.
DR   BioGRID; 31306; 370.
DR   DIP; DIP-5830N; -.
DR   IntAct; P32849; 5.
DR   MINT; P32849; -.
DR   STRING; 4932.YLR032W; -.
DR   iPTMnet; P32849; -.
DR   MaxQB; P32849; -.
DR   PaxDb; 4932-YLR032W; -.
DR   PeptideAtlas; P32849; -.
DR   EnsemblFungi; YLR032W_mRNA; YLR032W; YLR032W.
DR   GeneID; 850719; -.
DR   KEGG; sce:YLR032W; -.
DR   AGR; SGD:S000004022; -.
DR   SGD; S000004022; RAD5.
DR   VEuPathDB; FungiDB:YLR032W; -.
DR   eggNOG; KOG1001; Eukaryota.
DR   GeneTree; ENSGT00940000165376; -.
DR   HOGENOM; CLU_000315_2_5_1; -.
DR   InParanoid; P32849; -.
DR   OMA; KVEPWSN; -.
DR   OrthoDB; 200191at2759; -.
DR   BioCyc; YEAST:G3O-32191-MONOMER; -.
DR   BioGRID-ORCS; 850719; 8 hits in 10 CRISPR screens.
DR   PRO; PR:P32849; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P32849; Protein.
DR   GO; GO:0000785; C:chromatin; IDA:SGD.
DR   GO; GO:0000781; C:chromosome, telomeric region; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:SGD.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0000400; F:four-way junction DNA binding; IDA:SGD.
DR   GO; GO:0009378; F:four-way junction helicase activity; IDA:SGD.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0000403; F:Y-form DNA binding; IDA:SGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR   GO; GO:0042275; P:error-free postreplication DNA repair; IMP:SGD.
DR   GO; GO:0070987; P:error-free translesion synthesis; IDA:SGD.
DR   GO; GO:0042276; P:error-prone translesion synthesis; IDA:SGD.
DR   GO; GO:0010994; P:free ubiquitin chain polymerization; IDA:SGD.
DR   GO; GO:0006301; P:postreplication repair; IDA:SGD.
DR   GO; GO:0000209; P:protein polyubiquitination; IDA:SGD.
DR   CDD; cd18008; DEXDc_SHPRH-like; 1.
DR   CDD; cd23131; RING-HC_RAD5; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014905; HIRAN.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR45626:SF22; DNA REPAIR PROTEIN RAD5; 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF08797; HIRAN; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00910; HIRAN; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Cytoplasm; DNA damage; DNA repair;
KW   DNA-binding; Helicase; Hydrolase; Metal-binding; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..1169
FT                   /note="DNA repair protein RAD5"
FT                   /id="PRO_0000056130"
FT   DOMAIN          519..730
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          995..1165
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   ZN_FING         914..961
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          302..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           681..684
FT                   /note="DEGH box"
FT   BINDING         532..539
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         20
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         130
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MUTAGEN         538..539
FT                   /note="KT->AA: Increased sensitivity toward ionizing
FT                   radiation."
FT                   /evidence="ECO:0000269|PubMed:16224103"
FT   MUTAGEN         914
FT                   /note="C->S: Abolishes interaction with UBC13."
FT                   /evidence="ECO:0000269|PubMed:10880451,
FT                   ECO:0000269|PubMed:12496280"
FT   MUTAGEN         916
FT                   /note="I->A: Abolishes interaction with UBC13."
FT                   /evidence="ECO:0000269|PubMed:12496280"
FT   MUTAGEN         944
FT                   /note="Y->A: Abolishes interaction with UBC13."
FT                   /evidence="ECO:0000269|PubMed:12496280"
FT   MUTAGEN         959
FT                   /note="N->A: Abolishes interaction with UBC13."
FT                   /evidence="ECO:0000269|PubMed:12496280"
FT   CONFLICT        478
FT                   /note="Q -> R (in Ref. 4; AAB23590)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        635
FT                   /note="T -> N (in Ref. 4; AAB23590)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        846
FT                   /note="G -> S (in Ref. 4; AAB23590)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        898
FT                   /note="R -> S (in Ref. 4; AAB23590)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        973
FT                   /note="V -> A (in Ref. 4; AAB23590)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1063
FT                   /note="A -> R (in Ref. 4; AAB23590)"
FT                   /evidence="ECO:0000305"
FT   STRAND          5..8
FT                   /evidence="ECO:0007829|PDB:5YRQ"
SQ   SEQUENCE   1169 AA;  134002 MW;  226B720097433EE2 CRC64;
     MSHIEQEERK RFFNDDLDTS ETSLNFKSEN KESFLFANSH NDDDDDVVVS VSDTTEGEGD
     RSIVPVRREI EEEGQNQFIT ELLRIIPEMP KDLVMELNEK FGSQEEGLSL ALSHYFDHNS
     GTSISKIPSS PNQLNTLSDT SNSTLSPSSF HPKRRRIYGF RNQTRLEDKV TWKRFIGALQ
     VTGMATRPTV RPLKYGSQMK LKRSSEEISA TKVYDSRGRK KASMASLVRI FDIQYDREIG
     RVSEDIAQIL YPLLSSHEIS FEVTLIFCDN KRLSIGDSFI LQLDCFLTSL IFEERNDGES
     LMKRRRTEGG NKREKDNGNF GRTLTETDEE LESRSKRLAL LKLFDKLRLK PILDEQKALE
     KHKIELNSDP EIIDLDNDEI CSNQVTEVHN NLRDTQHEEE TMNLNQLKTF YKAAQSSESL
     KSLPETEPSR DVFKLELRNY QKQGLTWMLR REQEFAKAAS DGEASETGAN MINPLWKQFK
     WPNDMSWAAQ NLQQDHVNVE DGIFFYANLH SGEFSLAKPI LKTMIKGGIL SDEMGLGKTV
     AAYSLVLSCP HDSDVVDKKL FDIENTAVSD NLPSTWQDNK KPYASKTTLI VVPMSLLTQW
     SNEFTKANNS PDMYHEVYYG GNVSSLKTLL TKTKTPPTVV LTTYGIVQNE WTKHSKGRMT
     DEDVNISSGL FSVNFYRIII DEGHNIRNRT TVTSKAVMAL QGKCKWVLTG TPIINRLDDL
     YSLVKFLELD PWRQINYWKT FVSTPFESKN YKQAFDVVNA ILEPVLLRRT KQMKDKDGKP
     LVELPPKEVV IKRLPFSKSQ DLLYKFLLDK AEVSVKSGIA RGDLLKKYST ILVHILRLRQ
     VCCHPGLIGS QDENDEDLSK NNKLVTEQTV ELDSLMRVVS ERFDNSFSKE ELDAMIQRLK
     VKYPDNKSFQ SLECSICTTE PMDLDKALFT ECGHSFCEKC LFEYIEFQNS KNLGLKCPNC
     RNQIDACRLL ALVQTNSNSK NLEFKPYSPA SKSSKITALL KELQLLQDSS AGEQVVIFSQ
     FSTYLDILEK ELTHTFSKDV AKIYKFDGRL SLKERTSVLA DFAVKDYSRQ KILLLSLKAG
     GVGLNLTCAS HAYMMDPWWS PSMEDQAIDR LHRIGQTNSV KVMRFIIQDS IEEKMLRIQE
     KKRTIGEAMD TDEDERRKRR IEEIQMLFE
//