RFC1_YEAST
ID RFC1_YEAST Reviewed; 861 AA.
AC P38630; D6W2S3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Replication factor C subunit 1;
DE Short=Replication factor C1;
DE AltName: Full=Activator 1 95 kDa subunit;
DE AltName: Full=Cell division control protein 44;
GN Name=RFC1; Synonyms=CDC44; OrderedLocusNames=YOR217W; ORFNames=YOR50-7;
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, AND MUTAGENESIS OF ASP-427; GLY-436; GLY-512 AND
RP ASP-513.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8264593; DOI=10.1128/mcb.14.1.255-267.1994;
RA Howell E.A., McAlear M.A., Rose D., Holm C.;
RT "CDC44: a putative nucleotide-binding protein required for cell cycle
RT progression that has homology to subunits of replication factor C.";
RL Mol. Cell. Biol. 14:255-267(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTIFICATION IN THE RFC COMPLEX.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7651383; DOI=10.1128/mcb.15.9.4661;
RA Cullmann G., Fien K., Kobayashi R., Stillman B.;
RT "Characterization of the five replication factor C genes of Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 15:4661-4671(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8840505;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<877::aid-yea969>3.0.co;2-s;
RA Galisson F., Dujon B.;
RT "Sequence and analysis of a 33 kb fragment from the right arm of chromosome
RT XV of the yeast Saccharomyces cerevisiae.";
RL Yeast 12:877-885(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [5]
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 [6]
RP INTERACTION WITH POL30.
RX PubMed=14530260; DOI=10.1074/jbc.m309206200;
RA Yao N., Coryell L., Zhang D., Georgescu R.E., Finkelstein J., Coman M.M.,
RA Hingorani M.M., O'Donnell M.;
RT "Replication factor C clamp loader subunit arrangement within the circular
RT pentamer and its attachment points to proliferating cell nuclear antigen.";
RL J. Biol. Chem. 278:50744-50753(2003).
RN [7]
RP INTERACTION WITH ECO1.
RX PubMed=12665596; DOI=10.1128/mcb.23.8.2999-3007.2003;
RA Kenna M.A., Skibbens R.V.;
RT "Mechanical link between cohesion establishment and DNA replication:
RT Ctf7p/Eco1p, a cohesion establishment factor, associates with three
RT different replication factor C complexes.";
RL Mol. Cell. Biol. 23:2999-3007(2003).
RN [8]
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 [9]
RP IDENTIFICATION IN THE RFC COMPLEX.
RX PubMed=15964801; DOI=10.1128/mcb.25.13.5445-5455.2005;
RA Bylund G.O., Burgers P.M.;
RT "Replication protein A-directed unloading of PCNA by the Ctf18 cohesion
RT establishment complex.";
RL Mol. Cell. Biol. 25:5445-5455(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38 AND SER-40, AND
RP IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38 AND SER-40, AND
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38; SER-40 AND THR-63, 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [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).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 295-785 IN COMPLEX WITH AN ATP
RP ANALOG; RCF2; RCF3; RCF4; RCF5 AND PCNA.
RX PubMed=15201901; DOI=10.1038/nature02585;
RA Bowman G.D., O'Donnell M., Kuriyan J.;
RT "Structural analysis of a eukaryotic sliding DNA clamp-clamp loader
RT complex.";
RL Nature 429:724-730(2004).
CC -!- FUNCTION: Component of the ATP-dependent clamp loader RFC complex for
CC the POL30/PCNA homotrimer DNA clamp. During a clamp loading circle, the
CC RFC:clamp complex binds to DNA and the recognition of the double-
CC stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The
CC complex presumably provides bipartite ATP sites in which one subunit
CC supplies a catalytic site for hydrolysis of ATP bound to the
CC neighboring subunit. Dissociation of RFC from the clamp leaves the
CC clamp encircling DNA. Replication factor C (RFC or activator 1) complex
CC acts during elongation of primed DNA templates by DNA polymerase delta
CC and epsilon. RFC has an essential but redundant activity in sister
CC chromatid cohesion establishment.
CC -!- SUBUNIT: Replication factor C (RFC) is a heteropentamer of subunits
CC RFC1, RFC2, RFC3, RFC4 and RFC5 and forms a complex with POL30/PCNA in
CC the presence of ATP. Interacts with ECO1 and POL30/PCNA.
CC {ECO:0000269|PubMed:12665596, ECO:0000269|PubMed:14530260,
CC ECO:0000269|PubMed:15201901, ECO:0000269|PubMed:15964801,
CC ECO:0000269|PubMed:7651383}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 2360 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the activator 1 large subunit family.
CC {ECO:0000305}.
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DR EMBL; U03102; AAC48916.1; -; Unassigned_DNA.
DR EMBL; U26027; AAC49060.1; -; Genomic_DNA.
DR EMBL; X92441; CAA63180.1; -; Genomic_DNA.
DR EMBL; Z75125; CAA99434.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10989.1; -; Genomic_DNA.
DR PIR; S44763; S44763.
DR RefSeq; NP_014860.1; NM_001183636.1.
DR PDB; 1SXJ; X-ray; 2.85 A; A=295-785.
DR PDB; 7THJ; EM; 3.80 A; A=1-861.
DR PDB; 7THV; EM; 4.00 A; A=1-861.
DR PDB; 7TI8; EM; 3.50 A; A=1-861.
DR PDB; 7TIB; EM; 3.40 A; A=1-861.
DR PDB; 7TIC; EM; 3.90 A; A=1-861.
DR PDB; 7TID; EM; 3.30 A; A=1-861.
DR PDB; 7TKU; EM; 4.00 A; A=1-861.
DR PDBsum; 1SXJ; -.
DR PDBsum; 7THJ; -.
DR PDBsum; 7THV; -.
DR PDBsum; 7TI8; -.
DR PDBsum; 7TIB; -.
DR PDBsum; 7TIC; -.
DR PDBsum; 7TID; -.
DR PDBsum; 7TKU; -.
DR AlphaFoldDB; P38630; -.
DR SMR; P38630; -.
DR BioGRID; 34612; 308.
DR ComplexPortal; CPX-545; DNA replication factor C complex.
DR DIP; DIP-2527N; -.
DR ELM; P38630; -.
DR IntAct; P38630; 16.
DR MINT; P38630; -.
DR STRING; 4932.YOR217W; -.
DR iPTMnet; P38630; -.
DR MaxQB; P38630; -.
DR PaxDb; P38630; -.
DR PRIDE; P38630; -.
DR EnsemblFungi; YOR217W_mRNA; YOR217W; YOR217W.
DR GeneID; 854392; -.
DR KEGG; sce:YOR217W; -.
DR SGD; S000005743; RFC1.
DR VEuPathDB; FungiDB:YOR217W; -.
DR eggNOG; KOG1968; Eukaryota.
DR HOGENOM; CLU_003574_1_0_1; -.
DR InParanoid; P38630; -.
DR OMA; PVGAENC; -.
DR BioCyc; YEAST:G3O-33719-MON; -.
DR Reactome; R-SCE-110312; Translesion synthesis by REV1.
DR Reactome; R-SCE-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-SCE-110320; Translesion Synthesis by POLH.
DR Reactome; R-SCE-5655862; Translesion synthesis by POLK.
DR Reactome; R-SCE-5656121; Translesion synthesis by POLI.
DR Reactome; R-SCE-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-SCE-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SCE-69091; Polymerase switching.
DR EvolutionaryTrace; P38630; -.
DR PRO; PR:P38630; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P38630; protein.
DR GO; GO:0005663; C:DNA replication factor C complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003689; F:DNA clamp loader activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IMP:SGD.
DR GO; GO:0006261; P:DNA-templated DNA replication; IDA:ComplexPortal.
DR GO; GO:0006272; P:leading strand elongation; IDA:SGD.
DR GO; GO:0006298; P:mismatch repair; IGI:SGD.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:SGD.
DR Gene3D; 3.40.50.10190; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR013725; DNA_replication_fac_RFC1_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012178; RFC1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF08519; RFC1; 1.
DR PIRSF; PIRSF036578; RFC1; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF48019; SSF48019; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; DNA replication;
KW DNA-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..861
FT /note="Replication factor C subunit 1"
FT /id="PRO_0000121776"
FT DOMAIN 153..243
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 830..834
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 855..860
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 10..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..822
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..861
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 299
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 353..361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 456
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 38
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 63
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 427
FT /note="D->H: In cs mutant CDC44-2; causes cell cycle
FT arrest."
FT /evidence="ECO:0000269|PubMed:8264593"
FT MUTAGEN 436
FT /note="G->R: In cs mutant CDC44-3/4; causes cell cycle
FT arrest."
FT /evidence="ECO:0000269|PubMed:8264593"
FT MUTAGEN 512
FT /note="G->A: In cs mutant CDC44-9; no effect."
FT /evidence="ECO:0000269|PubMed:8264593"
FT MUTAGEN 513
FT /note="D->N: In cs mutants CDC44-1/5/8 and CDC44-9; causes
FT cell cycle arrest."
FT /evidence="ECO:0000269|PubMed:8264593"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 314..325
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 327..332
FT /evidence="ECO:0007829|PDB:1SXJ"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 359..369
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 385..390
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:1SXJ"
FT TURN 402..406
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 418..423
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 436..446
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 451..456
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 464..466
FT /evidence="ECO:0007829|PDB:1SXJ"
FT TURN 467..469
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 470..474
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 480..493
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 502..509
FT /evidence="ECO:0007829|PDB:1SXJ"
FT TURN 510..512
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 514..521
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 523..527
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 535..544
FT /evidence="ECO:0007829|PDB:1SXJ"
FT TURN 545..548
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 550..558
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 561..563
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 568..570
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 574..581
FT /evidence="ECO:0007829|PDB:1SXJ"
FT TURN 585..587
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 588..595
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 596..602
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 610..631
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 638..640
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 641..648
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 650..654
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 669..687
FT /evidence="ECO:0007829|PDB:1SXJ"
FT TURN 688..692
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 699..703
FT /evidence="ECO:0007829|PDB:1SXJ"
FT TURN 704..706
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 707..714
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 725..730
FT /evidence="ECO:0007829|PDB:1SXJ"
FT TURN 731..733
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 737..746
FT /evidence="ECO:0007829|PDB:1SXJ"
SQ SEQUENCE 861 AA; 94903 MW; A7D9208D66DD9A98 CRC64;
MVNISDFFGK NKKSVRSSTS RPTRQVGSSK PEVIDLDTES DQESTNKTPK KMPVSNVIDV
SETPEGEKKL PLPAKRKASS PTVKPASSKK TKPSSKSSDS ASNITAQDVL DKIPSLDLSN
VHVKENAKFD FKSANSNADP DEIVSEIGSF PEGKPNCLLG LTIVFTGVLP TLERGASEAL
AKRYGARVTK SISSKTSVVV LGDEAGPKKL EKIKQLKIKA IDEEGFKQLI AGMPAEGGDG
EAAEKARRKL EEQHNIATKE AELLVKKEEE RSKKLAATRV SGGHLERDNV VREEDKLWTV
KYAPTNLQQV CGNKGSVMKL KNWLANWENS KKNSFKHAGK DGSGVFRAAM LYGPPGIGKT
TAAHLVAQEL GYDILEQNAS DVRSKTLLNA GVKNALDNMS VVGYFKHNEE AQNLNGKHFV
IIMDEVDGMS GGDRGGVGQL AQFCRKTSTP LILICNERNL PKMRPFDRVC LDIQFRRPDA
NSIKSRLMTI AIREKFKLDP NVIDRLIQTT RGDIRQVINL LSTISTTTKT INHENINEIS
KAWEKNIALK PFDIAHKMLD GQIYSDIGSR NFTLNDKIAL YFDDFDFTPL MIQENYLSTR
PSVLKPGQSH LEAVAEAANC ISLGDIVEKK IRSSEQLWSL LPLHAVLSSV YPASKVAGHM
AGRINFTAWL GQNSKSAKYY RLLQEIHYHT RLGTSTDKIG LRLDYLPTFR KRLLDPFLKQ
GADAISSVIE VMDDYYLTKE DWDSIMEFFV GPDVTTAIIK KIPATVKSGF TRKYNSMTHP
VAIYRTGSTI GGGGVGTSTS TPDFEDVVDA DDNPVPADDE ETQDSSTDLK KDKLIKQKAK
PTKRKTATSK PGGSKKRKTK A
