ID RT107_YEAST Reviewed; 1070 AA.
AC P38850; D3DLA3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 27-MAR-2024, entry version 181.
DE RecName: Full=Regulator of Ty1 transposition protein 107;
DE AltName: Full=Establishes silent chromatin protein 4;
GN Name=RTT107; Synonyms=ESC4; OrderedLocusNames=YHR154W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION, AND PHOSPHORYLATION BY MEC1.
RX PubMed=14988729; DOI=10.1038/sj.emboj.7600129;
RA Rouse J.;
RT "Esc4p, a new target of Mec1p (ATR), promotes resumption of DNA synthesis
RT after DNA damage.";
RL EMBO J. 23:1188-1197(2004).
RN [6]
RP INTERACTION WITH RAD55 AND MMS22, AND SUBCELLULAR LOCATION.
RX PubMed=16569515; DOI=10.1016/j.dnarep.2006.02.005;
RA Chin J.K., Bashkirov V.I., Heyer W.-D., Romesberg F.E.;
RT "Esc4/Rtt107 and the control of recombination during replication.";
RL DNA Repair 5:618-628(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-532, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP FUNCTION, AND INTERACTION WITH RTT101.
RX PubMed=17978089; DOI=10.1091/mbc.e07-09-0961;
RA Roberts T.M., Zaidi I.W., Vaisica J.A., Peter M., Brown G.W.;
RT "Regulation of rtt107 recruitment to stalled DNA replication forks by the
RT cullin rtt101 and the rtt109 acetyltransferase.";
RL Mol. Biol. Cell 19:171-180(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; THR-532; SER-591;
RP SER-593; SER-800 AND SER-806, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-532; SER-720 AND SER-806, AND
RP 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 [11]
RP INTERACTION WITH MMS22, AND IDENTIFICATION IN A COMPLEX WITH RTT101 AND
RP MMS1.
RX PubMed=20139071; DOI=10.1074/jbc.m109.082107;
RA Mimura S., Yamaguchi T., Ishii S., Noro E., Katsura T., Obuse C.,
RA Kamura T.;
RT "Cul8/Rtt101 forms a variety of protein complexes that regulate DNA damage
RT response and transcriptional silencing.";
RL J. Biol. Chem. 285:9858-9867(2010).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 820-1070 IN COMPLEX WITH HTA1.
RX PubMed=22262834; DOI=10.1074/jbc.m111.311860;
RA Li X., Liu K., Li F., Wang J., Huang H., Wu J., Shi Y.;
RT "Structure of C-terminal tandem BRCT repeats of Rtt107 protein reveals
RT critical role in interaction with phosphorylated histone H2A during DNA
RT damage repair.";
RL J. Biol. Chem. 287:9137-9146(2012).
CC -!- FUNCTION: Required for resumption of chromosome replication after DNA
CC damage, specifically in S phase. Is recruited to chromatin in the
CC presence of RTT109 and RTT101 in response to stalled replication forks
CC and acts as a scaffold during DNA repair. {ECO:0000269|PubMed:14988729,
CC ECO:0000269|PubMed:17978089}.
CC -!- SUBUNIT: Forms a complex with the cullin-RING ligase (CRL) RTT101(MMS1-
CC MMS22). Interacts with MMS22 and RTT101. Interacts with histone H2A;
CC requires H2A to be phosphorylated (gamma-H2A). Interacts with RAD55.
CC {ECO:0000269|PubMed:16569515, ECO:0000269|PubMed:17978089,
CC ECO:0000269|PubMed:20139071, ECO:0000269|PubMed:22262834}.
CC -!- INTERACTION:
CC P38850; Q06164: MMS22; NbExp=9; IntAct=EBI-24788, EBI-31156;
CC P38850; P47050: RTT101; NbExp=5; IntAct=EBI-24788, EBI-25861;
CC P38850; Q12098: SLX4; NbExp=6; IntAct=EBI-24788, EBI-37788;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16569515}. Note=Recruited to chromatin in response
CC to replication fork stalling.
CC -!- PTM: Phosphorylated by MEC1. {ECO:0000269|PubMed:14988729}.
CC -!- MISCELLANEOUS: Present with 1380 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U10397; AAB68978.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06847.1; -; Genomic_DNA.
DR PIR; S46755; S46755.
DR RefSeq; NP_012024.1; NM_001179285.1.
DR PDB; 3T7I; X-ray; 2.30 A; A/B=820-1070.
DR PDB; 3T7J; X-ray; 2.04 A; A/B=820-1070.
DR PDB; 3T7K; X-ray; 2.03 A; A/B=820-1070.
DR PDB; 6J0V; X-ray; 2.31 A; A/B=1-513.
DR PDB; 6J0W; X-ray; 2.40 A; A/B=1-513.
DR PDB; 6J0X; X-ray; 2.31 A; A/B/C/D=1-513.
DR PDB; 6J0Y; X-ray; 1.80 A; A/B=2-513.
DR PDBsum; 3T7I; -.
DR PDBsum; 3T7J; -.
DR PDBsum; 3T7K; -.
DR PDBsum; 6J0V; -.
DR PDBsum; 6J0W; -.
DR PDBsum; 6J0X; -.
DR PDBsum; 6J0Y; -.
DR AlphaFoldDB; P38850; -.
DR SMR; P38850; -.
DR BioGRID; 36588; 440.
DR ComplexPortal; CPX-1157; CUL8-MMS1-MMS22-ESC4 E3 ubiquitin ligase complex.
DR ComplexPortal; CPX-1355; RTT107-SLX4-SLX1 complex.
DR DIP; DIP-6297N; -.
DR IntAct; P38850; 28.
DR MINT; P38850; -.
DR STRING; 4932.YHR154W; -.
DR GlyGen; P38850; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; P38850; -.
DR MaxQB; P38850; -.
DR PaxDb; 4932-YHR154W; -.
DR PeptideAtlas; P38850; -.
DR EnsemblFungi; YHR154W_mRNA; YHR154W; YHR154W.
DR GeneID; 856559; -.
DR KEGG; sce:YHR154W; -.
DR AGR; SGD:S000001197; -.
DR SGD; S000001197; RTT107.
DR VEuPathDB; FungiDB:YHR154W; -.
DR eggNOG; KOG2043; Eukaryota.
DR HOGENOM; CLU_002149_0_0_1; -.
DR InParanoid; P38850; -.
DR OMA; QRFYIQR; -.
DR OrthoDB; 19990at2759; -.
DR BioCyc; YEAST:G3O-31189-MONOMER; -.
DR PRO; PR:P38850; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38850; Protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0035361; C:Cul8-RING ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:1990683; P:DNA double-strand break attachment to nuclear envelope; IMP:SGD.
DR GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR GO; GO:0006334; P:nucleosome assembly; NAS:ComplexPortal.
DR GO; GO:2000001; P:regulation of DNA damage checkpoint; IMP:SGD.
DR GO; GO:1903775; P:regulation of DNA double-strand break processing; IMP:SGD.
DR GO; GO:0010526; P:retrotransposon silencing; IMP:SGD.
DR Gene3D; 3.40.50.10190; BRCT domain; 4.
DR IDEAL; IID50173; -.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR031906; RTT107_BRCT_6.
DR PANTHER; PTHR47667; REGULATOR OF TY1 TRANSPOSITION PROTEIN 107; 1.
DR PANTHER; PTHR47667:SF1; REGULATOR OF TY1 TRANSPOSITION PROTEIN 107; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF12738; PTCB-BRCT; 1.
DR Pfam; PF16770; RTT107_BRCT_5; 1.
DR Pfam; PF16771; RTT107_BRCT_6; 1.
DR SMART; SM00292; BRCT; 4.
DR SUPFAM; SSF52113; BRCT domain; 2.
DR PROSITE; PS50172; BRCT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1070
FT /note="Regulator of Ty1 transposition protein 107"
FT /id="PRO_0000097502"
FT DOMAIN 2..103
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 117..213
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 260..352
FT /note="BRCT 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 369..453
FT /note="BRCT 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 829..910
FT /note="BRCT 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 934..1049
FT /note="BRCT 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 572..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 532
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 800
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 806
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT TURN 6..9
FT /evidence="ECO:0007829|PDB:6J0X"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:6J0Y"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:6J0Y"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 82..86
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:6J0Y"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:6J0Y"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:6J0Y"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 136..148
FT /evidence="ECO:0007829|PDB:6J0Y"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:6J0Y"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 173..178
FT /evidence="ECO:0007829|PDB:6J0Y"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:6J0Y"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:6J0X"
FT HELIX 207..215
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 221..226
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 236..247
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:6J0Y"
FT TURN 263..268
FT /evidence="ECO:0007829|PDB:6J0Y"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 281..293
FT /evidence="ECO:0007829|PDB:6J0Y"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 307..313
FT /evidence="ECO:0007829|PDB:6J0Y"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 328..336
FT /evidence="ECO:0007829|PDB:6J0Y"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 345..354
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:6J0Y"
FT TURN 377..379
FT /evidence="ECO:0007829|PDB:6J0Y"
FT STRAND 381..386
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 390..402
FT /evidence="ECO:0007829|PDB:6J0Y"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:6J0Y"
FT STRAND 415..422
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 425..434
FT /evidence="ECO:0007829|PDB:6J0Y"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:6J0Y"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 446..455
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 464..466
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 475..477
FT /evidence="ECO:0007829|PDB:6J0Y"
FT HELIX 822..827
FT /evidence="ECO:0007829|PDB:3T7K"
FT STRAND 837..844
FT /evidence="ECO:0007829|PDB:3T7K"
FT HELIX 851..859
FT /evidence="ECO:0007829|PDB:3T7K"
FT STRAND 862..864
FT /evidence="ECO:0007829|PDB:3T7K"
FT HELIX 870..872
FT /evidence="ECO:0007829|PDB:3T7K"
FT STRAND 876..878
FT /evidence="ECO:0007829|PDB:3T7K"
FT HELIX 886..891
FT /evidence="ECO:0007829|PDB:3T7K"
FT STRAND 899..901
FT /evidence="ECO:0007829|PDB:3T7K"
FT HELIX 904..913
FT /evidence="ECO:0007829|PDB:3T7K"
FT HELIX 927..930
FT /evidence="ECO:0007829|PDB:3T7I"
FT HELIX 937..942
FT /evidence="ECO:0007829|PDB:3T7K"
FT STRAND 945..947
FT /evidence="ECO:0007829|PDB:3T7K"
FT HELIX 949..952
FT /evidence="ECO:0007829|PDB:3T7K"
FT STRAND 957..961
FT /evidence="ECO:0007829|PDB:3T7K"
FT HELIX 968..977
FT /evidence="ECO:0007829|PDB:3T7K"
FT STRAND 982..986
FT /evidence="ECO:0007829|PDB:3T7K"
FT TURN 988..990
FT /evidence="ECO:0007829|PDB:3T7K"
FT HELIX 993..995
FT /evidence="ECO:0007829|PDB:3T7K"
FT STRAND 1011..1015
FT /evidence="ECO:0007829|PDB:3T7K"
FT HELIX 1019..1032
FT /evidence="ECO:0007829|PDB:3T7K"
FT STRAND 1038..1041
FT /evidence="ECO:0007829|PDB:3T7K"
FT HELIX 1043..1051
FT /evidence="ECO:0007829|PDB:3T7K"
FT STRAND 1063..1067
FT /evidence="ECO:0007829|PDB:3T7K"
SQ SEQUENCE 1070 AA; 123017 MW; 767931285BB52580 CRC64;
MSTSLLFEQL NFLILVAAEA ELPIAHSTRK LLMDNSCNNC QIYELYNENL KDVKTDKDWF
MNKFGPQTVH FVISNTINFP FYKIVYFDLL IPVVSHTWVQ DSVKTKRHLR TNMYSPNPFH
LLRDCQVYIS KSSFNKCEYI LYSDLLHLLG GTLVNYISNR TTHVIVQSPQ DPIIATVSKL
TFGSFSSSST NKHTEKPLRE WKFVYPIWIL YHFKMAKPLK GELATLCELD MQDTSEEQLF
AKWEEVIGDK QTSSSQLTLH PNKTLFKNHH FAISPDLNFF TPLYWFLKGF IEDLDGKVTP
LSFSDDLKSV YQAFPDIDCY IGHSANSPIL EKTKSIKPEI HVGNVSWLFY MFALQKFTPV
SQCKLIHQPF HAKLFTSKEL TVAYTNYFGS QRFYIQRLVE ILGGLSTPEL TRKNTHLITK
STIGKKFKVA KKWSLDPQNA IIVTNHMWLE QCYMNNSKLN PKDSRFQNFK LDDNMGWNIG
QIGMDHSSLP TPKNLSMVTY DTQSISEKPP PTNDQMDQIN DNTNVLSKKD GTPISSFENS
IDEKIDKLQK ISGEVAVTHS GDLERSFVSR PSRASFPVVD SKKSNLQKKD SNSDISMETE
VFCEGHEKRE EKEFTKPITE YDAPKKQEIR EQSRKKNDID YKKEEEETEL QVQLGQRTKR
EIKTSKKNEK EKETNECHIE VDQMTNEKQG EESTGKLIST EDVTSKKDTD KFSHLFEGLS
DNDDHINDEK PAVNSKYTTP KTSQNITSGV DTPTTAQTQV FMPSSGNSRL AKTQAAKRLH
TDIESLNEFQ KNFKRKRIDS EEISLSQDVE RSNNNKELAT KAEKILARFN ELPNYDLKAV
CTGCFHDGFN EVDIEILNQL GIKIFDNIKE TDKLNCIFAP KILRTEKFLK SLSFEPLKFA
LKPEFIIDLL KQIHSKKDKL SQININLFDY EINGINESII SKTKLPTKVF ERANIRCINL
VNDIPGGVDT IGSVLKAHGI EKINVLRSKK CTFEDIIPND VSKQENGGIF KYVLIVTKAS
QVKKFTKLIN DRDKNETILI VEWNWCVESI FHLNVDFTSK KNVLYQKKNN
//
