ID RPA34_YEAST Reviewed; 233 AA. AC P47006; D6VW37; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 02-SEP-2026, entry version 189. DE RecName: Full=DNA-directed RNA polymerase I subunit RPA34; DE Short=A34; DE AltName: Full=DNA-directed DNA-dependent RNA polymerase 34.5 kDa polypeptide; DE Short=A34.5; GN Name=RPA34; OrderedLocusNames=YJL148W; ORFNames=J0637; 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]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX PubMed=8813765; RX DOI=10.1002/(sici)1097-0061(19960630)12:8%3c787::aid-yea954%3e3.0.co;2-4; RA Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D.; RT "Sequence analysis of a 40.7 kb segment from the left arm of yeast RT chromosome X reveals 14 known genes and 13 new open reading frames RT including homologues of genes clustered on the right arm of chromosome RT XI."; RL Yeast 12:787-797(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x; RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.; RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."; RL EMBO J. 15:2031-2049(1996). 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 FUNCTION, IDENTIFICATION IN THE RNA POL I COMPLEX, AND PHOSPHORYLATION. RX PubMed=9121426; DOI=10.1128/mcb.17.4.1787; RA Gadal O., Mariotte-Labarre S., Chedin S., Quemeneur E., Carles C., RA Sentenac A., Thuriaux P.; RT "A34.5, a nonessential component of yeast RNA polymerase I, cooperates with RT subunit A14 and DNA topoisomerase I to produce a functional rRNA synthesis RT machine."; RL Mol. Cell. Biol. 17:1787-1795(1997). RN [5] RP IDENTIFICATION IN THE RNA POL I COMPLEX. RX PubMed=11717393; DOI=10.1073/pnas.231181398; RA Fath S., Milkereit P., Peyroche G., Riva M., Carles C., Tschochner H.; RT "Differential roles of phosphorylation in the formation of transcriptional RT active RNA polymerase I."; RL Proc. Natl. Acad. Sci. U.S.A. 98:14334-14339(2001). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-12 AND SER-14, 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-60, 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-12 AND SER-14, 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 [9] RP FUNCTION, INTERACTION WITH RPA49, IDENTIFICATION BY MASS SPECTROMETRY, AND RP SUBUNIT. RX PubMed=20797630; DOI=10.1016/j.molcel.2010.07.028; RA Geiger S.R., Lorenzen K., Schreieck A., Hanecker P., Kostrewa D., RA Heck A.J., Cramer P.; RT "RNA polymerase I contains a TFIIF-related DNA-binding subcomplex."; RL Mol. Cell 39:583-594(2010). RN [10] RP ELECTRON MICROSCOPY OF THE RNA POLYMERASE I COMPLEX. RX PubMed=12145213; DOI=10.1093/emboj/cdf392; RA Bischler N., Brino L., Carles C., Riva M., Tschochner H., Mallouh V., RA Schultz P.; RT "Localization of the yeast RNA polymerase I-specific subunits."; RL EMBO J. 21:4136-4144(2002). RN [11] RP IDENTIFICATION IN THE RNA POL I COMPLEX. RX PubMed=11918799; DOI=10.1046/j.1365-2958.2002.02824.x; RA Van Mullem V., Landrieux E., Vandenhaute J., Thuriaux P.; RT "Rpa12p, a conserved RNA polymerase I subunit with two functional RT domains."; RL Mol. Microbiol. 43:1105-1113(2002). RN [12] RP IDENTIFICATION IN THE RNA POL I COMPLEX. RX PubMed=12407181; DOI=10.1073/pnas.232580799; RA Peyroche G., Levillain E., Siaut M., Callebaut I., Schultz P., Sentenac A., RA Riva M., Carles C.; RT "The A14-A43 heterodimer subunit in yeast RNA pol I and their relationship RT to Rpb4-Rpb7 pol II subunits."; RL Proc. Natl. Acad. Sci. U.S.A. 99:14670-14675(2002). RN [13] 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 [14] 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 [15] RP STRUCTURE BY ELECTRON MICROSCOPY (12.00 ANGSTROMS) OF THE POL I COMPLEX, RP FUNCTION, AND SUBUNIT. RX PubMed=18160037; DOI=10.1016/j.cell.2007.10.051; RA Kuhn C.D., Geiger S.R., Baumli S., Gartmann M., Gerber J., Jennebach S., RA Mielke T., Tschochner H., Beckmann R., Cramer P.; RT "Functional architecture of RNA polymerase I."; RL Cell 131:1260-1272(2007). RN [16] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, AND RP SUBUNIT. RX PubMed=24153184; DOI=10.1038/nature12636; RA Fernandez-Tornero C., Moreno-Morcillo M., Rashid U.J., Taylor N.M., RA Ruiz F.M., Gruene T., Legrand P., Steuerwald U., Muller C.W.; RT "Crystal structure of the 14-subunit RNA polymerase I."; RL Nature 502:644-649(2013). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, AND RP SUBUNIT. RX PubMed=24153182; DOI=10.1038/nature12712; RA Engel C., Sainsbury S., Cheung A.C., Kostrewa D., Cramer P.; RT "RNA polymerase I structure and transcription regulation."; RL Nature 502:650-655(2013). CC -!- FUNCTION: DNA-dependent RNA polymerases catalyze the transcription of CC DNA into RNA using the four ribonucleoside triphosphates as substrates. CC Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA CC precursors. Besides, RNA polymerase I has intrinsic RNA cleavage CC activity. The heterodimer formed by RPA34 and RPA49 stimulates CC transcript elongation by Pol I. {ECO:0000269|PubMed:18160037, CC ECO:0000269|PubMed:20797630, ECO:0000269|PubMed:24153182, CC ECO:0000269|PubMed:24153184, ECO:0000269|PubMed:9121426}. CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting CC of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8, CC RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of CC a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5, CC RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and CC RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43 CC form the stalk that mediates interactions with transcription initiation CC factors and newly synthesized RNA. Forms a TFIIF-like heterodimer with CC RPA49; the heterodimer formed by RPA34 and RPA49 can be dissociated CC from the Pol I core giving rise to a 12 subunit form A* of Pol I CC (formerly called pol A) that shows impaired transcript elongation CC activity and increased sensitivity to alpha-amanitin. The heterodimer CC formed by RPA34 and RPA49 stabilizes subunit RPA12 and stimulates CC RPA12-dependent RNA cleavage. {ECO:0000269|PubMed:11717393, CC ECO:0000269|PubMed:11918799, ECO:0000269|PubMed:12407181, CC ECO:0000269|PubMed:18160037, ECO:0000269|PubMed:20797630, CC ECO:0000269|PubMed:24153182, ECO:0000269|PubMed:24153184, CC ECO:0000269|PubMed:9121426}. CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}. CC -!- MISCELLANEOUS: Present with 3360 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the eukaryotic RPA34 RNA polymerase subunit CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z49423; CAA89443.1; -; Genomic_DNA. DR EMBL; X87371; CAA60807.1; -; Genomic_DNA. DR EMBL; BK006943; DAA08653.1; -; Genomic_DNA. DR PIR; S55165; S55165. DR RefSeq; NP_012387.1; NM_001181581.1. DR PDB; 4C2M; X-ray; 2.80 A; 3/N=1-233. DR PDB; 4C3H; X-ray; 3.27 A; N=1-233. DR PDB; 4C3I; X-ray; 3.00 A; N=1-233. DR PDB; 4C3J; X-ray; 3.35 A; N=1-233. DR PDB; 4YM7; X-ray; 5.50 A; AN/BN/CN/DN/EN/FN=1-233. DR PDB; 5G5L; EM; 4.80 A; N=1-233. DR PDB; 5LMX; EM; 4.90 A; N=1-233. DR PDB; 5M3F; EM; 3.80 A; N=1-233. DR PDB; 5M3M; EM; 4.00 A; N=1-233. DR PDB; 5M5W; EM; 3.80 A; N=1-233. DR PDB; 5M5X; EM; 4.00 A; N=1-233. DR PDB; 5M5Y; EM; 4.00 A; N=1-233. DR PDB; 5M64; EM; 4.60 A; N=1-233. DR PDB; 5N5Y; EM; 7.70 A; N=1-233. DR PDB; 5N5Z; EM; 7.70 A; N=1-233. DR PDB; 5N60; EM; 7.70 A; N=1-233. DR PDB; 5N61; EM; 3.40 A; N=1-233. DR PDB; 5OA1; EM; 4.40 A; N=1-233. DR PDB; 5W5Y; EM; 3.80 A; N=1-233. DR PDB; 5W64; EM; 4.20 A; N=1-233. DR PDB; 5W65; EM; 4.30 A; N=1-233. DR PDB; 5W66; EM; 3.90 A; N=1-233. DR PDB; 6H67; EM; 3.60 A; N=1-233. DR PDB; 6H68; EM; 4.60 A; N=1-233. DR PDB; 6HKO; EM; 3.42 A; N=1-233. DR PDB; 6RQH; EM; 3.70 A; N=1-233. DR PDB; 6RQL; EM; 2.90 A; N=1-233. DR PDB; 6RQT; EM; 4.00 A; N=1-233. DR PDB; 6RRD; EM; 3.10 A; N=1-233. DR PDB; 6RUI; EM; 2.70 A; N=1-233. DR PDB; 6RUO; EM; 3.50 A; N=1-233. DR PDB; 6RWE; EM; 3.00 A; N=1-233. DR PDB; 6TPS; EM; 3.54 A; N=1-233. DR PDB; 9G1V; EM; 2.70 A; N=1-233. DR PDB; 9G23; EM; 3.40 A; N=1-233. DR PDB; 9G24; EM; 3.50 A; N=1-233. DR PDB; 9G26; EM; 3.40 A; N=1-233. DR PDB; 9G29; EM; 3.30 A; N=1-233. DR PDB; 9G2C; EM; 3.50 A; N=1-233. DR AlphaFoldDB; P47006; -. DR EMDB; EMD-0146; -. DR EMDB; EMD-0147; -. DR EMDB; EMD-0238; -. DR EMDB; EMD-10006; -. DR EMDB; EMD-10007; -. DR EMDB; EMD-10038; -. DR EMDB; EMD-10544; -. DR EMDB; EMD-3446; -. DR EMDB; EMD-3447; -. DR EMDB; EMD-3448; -. DR EMDB; EMD-3449; -. DR EMDB; EMD-3590; -. DR EMDB; EMD-3591; -. DR EMDB; EMD-3592; -. DR EMDB; EMD-3593; -. DR EMDB; EMD-3727; -. DR EMDB; EMD-4088; -. DR EMDB; EMD-4147; -. DR EMDB; EMD-4148; -. DR EMDB; EMD-4982; -. DR EMDB; EMD-4984; -. DR EMDB; EMD-4985; -. DR EMDB; EMD-4987; -. DR EMDB; EMD-50955; -. DR EMDB; EMD-50962; -. DR EMDB; EMD-50963; -. DR EMDB; EMD-50965; -. DR EMDB; EMD-50970; -. DR EMDB; EMD-50972; -. DR EMDB; EMD-8771; -. DR EMDB; EMD-8773; -. DR EMDB; EMD-8774; -. DR EMDB; EMD-8775; -. DR EMDB; EMD-8776; -. DR EMDB; EMD-8777; -. DR SMR; P47006; -. DR BioGRID; 33610; 565. DR ComplexPortal; CPX-1664; DNA-directed RNA Polymerase I complex. DR DIP; DIP-7973N; -. DR FunCoup; P47006; 286. DR IntAct; P47006; 44. DR MINT; P47006; -. DR STRING; 4932.YJL148W; -. DR iPTMnet; P47006; -. DR PaxDb; 4932-YJL148W; -. DR PeptideAtlas; P47006; -. DR EnsemblFungi; YJL148W_mRNA; YJL148W; YJL148W. DR GeneID; 853293; -. DR KEGG; sce:YJL148W; -. DR AGR; SGD:S000003684; -. DR SGD; S000003684; RPA34. DR VEuPathDB; FungiDB:YJL148W; -. DR eggNOG; ENOG502S2EI; Eukaryota. DR HOGENOM; CLU_090034_0_0_1; -. DR InParanoid; P47006; -. DR OMA; HFPTGYG; -. DR OrthoDB; 4089784at2759; -. DR BioCyc; YEAST:G3O-31592-MONOMER; -. DR BioGRID-ORCS; 853293; 3 hits in 10 CRISPR screens. DR EvolutionaryTrace; P47006; -. DR PRO; PR:P47006; -. DR Proteomes; UP000002311; Chromosome X. DR RNAct; P47006; protein. DR GO; GO:0005730; C:nucleolus; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal. DR GO; GO:0005736; C:RNA polymerase I complex; IDA:UniProtKB. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IDA:UniProtKB. DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IDA:ComplexPortal. DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IDA:ComplexPortal. DR GO; GO:0006360; P:transcription by RNA polymerase I; IDA:UniProtKB. DR GO; GO:0006362; P:transcription elongation by RNA polymerase I; IDA:ComplexPortal. DR GO; GO:0006361; P:transcription initiation at RNA polymerase I promoter; IDA:ComplexPortal. DR Gene3D; 6.20.250.70; -; 1. DR InterPro; IPR013240; DNA-dir_RNA_pol1_su_RPA34. DR InterPro; IPR053263; Euk_RPA34_RNAP_subunit. DR PANTHER; PTHR28155; ACR243WP; 1. DR PANTHER; PTHR28155:SF1; DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA34.5-DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF08208; RNA_polI_A34; 1. DR PDBsum; 4C2M; -. DR PDBsum; 4C3H; -. DR PDBsum; 4C3I; -. DR PDBsum; 4C3J; -. DR PDBsum; 4YM7; -. DR PDBsum; 5G5L; -. DR PDBsum; 5LMX; -. DR PDBsum; 5M3F; -. DR PDBsum; 5M3M; -. DR PDBsum; 5M5W; -. DR PDBsum; 5M5X; -. DR PDBsum; 5M5Y; -. DR PDBsum; 5M64; -. DR PDBsum; 5N5Y; -. DR PDBsum; 5N5Z; -. DR PDBsum; 5N60; -. DR PDBsum; 5N61; -. DR PDBsum; 5OA1; -. DR PDBsum; 5W5Y; -. DR PDBsum; 5W64; -. DR PDBsum; 5W65; -. DR PDBsum; 5W66; -. DR PDBsum; 6H67; -. DR PDBsum; 6H68; -. DR PDBsum; 6HKO; -. DR PDBsum; 6RQH; -. DR PDBsum; 6RQL; -. DR PDBsum; 6RQT; -. DR PDBsum; 6RRD; -. DR PDBsum; 6RUI; -. DR PDBsum; 6RUO; -. DR PDBsum; 6RWE; -. DR PDBsum; 6TPS; -. DR PDBsum; 9G1V; -. DR PDBsum; 9G23; -. DR PDBsum; 9G24; -. DR PDBsum; 9G26; -. DR PDBsum; 9G29; -. DR PDBsum; 9G2C; -. PE 1: Evidence at protein level; KW 3D-structure; DNA-directed RNA polymerase; Nucleus; Phosphoprotein; KW Reference proteome; Ribosome biogenesis; Transcription. FT CHAIN 1..233 FT /note="DNA-directed RNA polymerase I subunit RPA34" FT /id="PRO_0000203031" FT REGION 179..233 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 179..191 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 208..233 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 10 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:19779198" FT MOD_RES 12 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:19779198" FT MOD_RES 14 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" FT MOD_RES 60 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT STRAND 29..31 FT /evidence="ECO:0007829|PDB:6RUI" FT HELIX 35..37 FT /evidence="ECO:0007829|PDB:4C2M" FT STRAND 52..59 FT /evidence="ECO:0007829|PDB:6RUI" FT STRAND 60..62 FT /evidence="ECO:0007829|PDB:6RRD" FT HELIX 64..66 FT /evidence="ECO:0007829|PDB:6RUI" FT STRAND 68..71 FT /evidence="ECO:0007829|PDB:4C3I" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:6RUI" FT STRAND 80..82 FT /evidence="ECO:0007829|PDB:6RUI" FT STRAND 85..89 FT /evidence="ECO:0007829|PDB:6RUI" FT HELIX 93..96 FT /evidence="ECO:0007829|PDB:4C2M" FT STRAND 99..101 FT /evidence="ECO:0007829|PDB:4C2M" FT STRAND 108..111 FT /evidence="ECO:0007829|PDB:6RUI" FT STRAND 113..117 FT /evidence="ECO:0007829|PDB:6RUI" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:4C3I" FT STRAND 125..127 FT /evidence="ECO:0007829|PDB:4C2M" FT HELIX 129..131 FT /evidence="ECO:0007829|PDB:5N61" FT STRAND 134..142 FT /evidence="ECO:0007829|PDB:6RUI" FT HELIX 145..148 FT /evidence="ECO:0007829|PDB:6RUI" FT HELIX 150..153 FT /evidence="ECO:0007829|PDB:6RUI" FT HELIX 155..160 FT /evidence="ECO:0007829|PDB:6RUI" FT HELIX 177..179 FT /evidence="ECO:0007829|PDB:4C2M" SQ SEQUENCE 233 AA; 26875 MW; DCD42DFEC574EDB6 CRC64; MSKLSKDYVS DSDSDDEVIS NEFSIPDGFK KCKHLKNFPL NGDNKKKAKQ QQVWLIKFPS NVDISKLKSL PVDFESSTTM TIDKHDYKIM DDTDIESSLT QDNLSNMTLL VPSESKESLK IASTAKDNAP LQFDKVFSVS ETAKIPAIDY SKVRVPRKDV PKVEGLKLEH FATGYDAEDF HVAEEVKENK KEPKKRSHHD DEEESSEKKK KKKEKREKRE KKDKKDKKKK HRD //