ID HIR2_YEAST Reviewed; 875 AA. AC P32480; D6W2A5; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 02-SEP-2026, entry version 208. DE RecName: Full=Protein HIR2; DE AltName: Full=Histone transcription regulator 2; GN Name=HIR2; OrderedLocusNames=YOR038C; ORFNames=OR26.31; 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], FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=8417331; DOI=10.1128/mcb.13.1.28-38.1993; RA Sherwood P.W., Tsang S.V., Osley M.A.; RT "Characterization of HIR1 and HIR2, two genes required for regulation of RT histone gene transcription in Saccharomyces cerevisiae."; RL Mol. Cell. Biol. 13:28-38(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169874; DOI=10.1038/387s098; 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 [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 1-113. RX PubMed=8027080; DOI=10.1016/s0021-9258(17)32434-1; RA Reed J.C., Bidwai A.P., Glover C.V.C.; RT "Cloning and disruption of CKB2, the gene encoding the 32-kDa regulatory RT beta'-subunit of Saccharomyces cerevisiae casein kinase II."; RL J. Biol. Chem. 269:18192-18200(1994). RN [5] RP FUNCTION, AND INTERACTION WITH HIR1. RX PubMed=9001207; DOI=10.1128/mcb.17.2.545; RA Spector M.S., Raff A., DeSilva H., Lee K., Osley M.A.; RT "Hir1p and Hir2p function as transcriptional corepressors to regulate RT histone gene transcription in the Saccharomyces cerevisiae cell cycle."; RL Mol. Cell. Biol. 17:545-552(1997). RN [6] RP FUNCTION. RX PubMed=9671488; DOI=10.1128/mcb.18.8.4783; RA Qian Z., Huang H., Hong J.Y., Burck C.L., Johnston S.D., Berman J., RA Carol A., Liebman S.W.; RT "Yeast Ty1 retrotransposition is stimulated by a synergistic interaction RT between mutations in chromatin assembly factor I and histone regulatory RT proteins."; RL Mol. Cell. Biol. 18:4783-4792(1998). RN [7] RP FUNCTION. RX PubMed=9671489; DOI=10.1128/mcb.18.8.4793; RA Kaufman P.D., Cohen J.L., Osley M.A.; RT "Hir proteins are required for position-dependent gene silencing in RT Saccharomyces cerevisiae in the absence of chromatin assembly factor I."; RL Mol. Cell. Biol. 18:4793-4806(1998). RN [8] RP FUNCTION, AND INTERACTION WITH SNF2; SNF5 AND SWI3. RX PubMed=10445029; DOI=10.1016/s1097-2765(00)80189-6; RA Dimova D., Nackerdien Z., Furgeson S., Eguchi S., Osley M.A.; RT "A role for transcriptional repressors in targeting the yeast Swi/Snf RT complex."; RL Mol. Cell 4:75-83(1999). RN [9] RP INTERACTION WITH ASF1. RX PubMed=11412995; DOI=10.1016/s0960-9822(01)00140-3; RA Sharp J.A., Fouts E.T., Krawitz D.C., Kaufman P.D.; RT "Yeast histone deposition protein Asf1p requires Hir proteins and PCNA for RT heterochromatic silencing."; RL Curr. Biol. 11:463-473(2001). RN [10] RP FUNCTION. RX PubMed=11937489; DOI=10.1101/gad.978902; RA Ng H.H., Robert F., Young R.A., Struhl K.; RT "Genome-wide location and regulated recruitment of the RSC nucleosome- RT remodeling complex."; RL Genes Dev. 16:806-819(2002). RN [11] RP FUNCTION. RX PubMed=12524332; DOI=10.1093/genetics/162.4.1557; RA Formosa T., Ruone S., Adams M.D., Olsen A.E., Eriksson P., Yu Y., RA Rhoades A.R., Kaufman P.D., Stillman D.J.; RT "Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause RT dependence on the Hir/Hpc pathway: polymerase passage may degrade chromatin RT structure."; RL Genetics 162:1557-1571(2002). RN [12] 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 [13] RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX RP WITH HIR1; HIR3 AND HPC2, AND INTERACTION WITH ASF1. RX PubMed=16303565; DOI=10.1016/j.cub.2005.10.053; RA Green E.M., Antczak A.J., Bailey A.O., Franco A.A., Wu K.J., RA Yates J.R. III, Kaufman P.D.; RT "Replication-independent histone deposition by the HIR complex and Asf1."; RL Curr. Biol. 15:2044-2049(2005). RN [14] RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A RP COMPLEX WITH HIR1; HIR3 AND HPC2. RX PubMed=16264190; DOI=10.1101/gad.1341105; RA Prochasson P., Florens L., Swanson S.K., Washburn M.P., Workman J.L.; RT "The HIR corepressor complex binds to nucleosomes generating a distinct RT protein/DNA complex resistant to remodeling by SWI/SNF."; RL Genes Dev. 19:2534-2539(2005). RN [15] RP FUNCTION. RX PubMed=16449659; DOI=10.1128/mcb.26.4.1496-1509.2006; RA Nourani A., Robert F., Winston F.; RT "Evidence that Spt2/Sin1, an HMG-like factor, plays roles in transcription RT elongation, chromatin structure, and genome stability in Saccharomyces RT cerevisiae."; RL Mol. Cell. Biol. 26:1496-1509(2006). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713, AND IDENTIFICATION BY RP 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 [17] RP INTERACTION WITH RTT106, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE. RX PubMed=19683497; DOI=10.1016/j.molcel.2009.06.023; RA Fillingham J., Kainth P., Lambert J.P., van Bakel H., Tsui K., RA Pena-Castillo L., Nislow C., Figeys D., Hughes T.R., Greenblatt J., RA Andrews B.J.; RT "Two-color cell array screen reveals interdependent roles for histone RT chaperones and a chromatin boundary regulator in histone gene repression."; RL Mol. Cell 35:340-351(2009). CC -!- FUNCTION: Component of the HIR complex, which cooperates with ASF1 to CC promote replication-independent chromatin assembly. The HIR complex is CC also required for the periodic repression of three of the four histone CC gene loci during the cell cycle as well as for autogenous regulation of CC the HTA1-HTB1 locus by H2A and H2B. DNA-binding by the HIR complex may CC repress transcription by inhibiting nucleosome remodeling by the CC SWI/SNF complex. The HIR complex may also be required for CC transcriptional silencing of centromeric, telomeric and mating-type CC loci in the absence of CAF-1. {ECO:0000269|PubMed:10445029, CC ECO:0000269|PubMed:11937489, ECO:0000269|PubMed:12524332, CC ECO:0000269|PubMed:16264190, ECO:0000269|PubMed:16303565, CC ECO:0000269|PubMed:16449659, ECO:0000269|PubMed:8417331, CC ECO:0000269|PubMed:9001207, ECO:0000269|PubMed:9671488, CC ECO:0000269|PubMed:9671489}. CC -!- SUBUNIT: Component of the HIR complex, composed of HIR1, HIR2, HIR3 and CC HPC2 (PubMed:16264190, PubMed:16303565, PubMed:9001207). This complex CC may consist of one copy of HIR1 and HIR3 and two copies of HIR2 and CC HPC2 (PubMed:16264190). The HIR complex interacts with ASF1 CC (PubMed:11412995, PubMed:16303565). Interacts with SNF2 CC (PubMed:10445029). Interacts with SNF5 (PubMed:10445029). Interacts CC with SWI3 (PubMed:10445029). Interacts with RTT106 (PubMed:19683497). CC {ECO:0000269|PubMed:10445029, ECO:0000269|PubMed:11412995, CC ECO:0000269|PubMed:16264190, ECO:0000269|PubMed:16303565, CC ECO:0000269|PubMed:19683497, ECO:0000269|PubMed:9001207}. CC -!- INTERACTION: CC P32480; P32479: HIR1; NbExp=9; IntAct=EBI-8323, EBI-8316; CC P32480; P47171: HIR3; NbExp=3; IntAct=EBI-8323, EBI-25715; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8417331}. Chromosome CC {ECO:0000269|PubMed:19683497}. Note=Localizes to the promoter region of CC histones HTA1-HTB1. {ECO:0000269|PubMed:19683497}. CC -!- DISRUPTION PHENOTYPE: Abolishes localization of RTT106 to the HTA1-HTB1 CC promoter. {ECO:0000269|PubMed:19683497}. CC -!- MISCELLANEOUS: Present with 922 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the WD repeat HIR1 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; L03839; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X87331; CAA60757.1; -; Genomic_DNA. DR EMBL; Z74946; CAA99228.1; -; Genomic_DNA. DR EMBL; U08849; AAA21657.1; -; Genomic_DNA. DR EMBL; BK006948; DAA10821.1; -; Genomic_DNA. DR PIR; S62177; S62177. DR RefSeq; NP_014681.1; NM_001183457.1. DR PDB; 8GHA; EM; 6.80 A; B=1-875. DR PDB; 8GHL; EM; 2.96 A; B/C/H/I=1-875. DR PDB; 8GHN; EM; 2.96 A; B/C/H/I=1-875. DR PDB; 9J5E; X-ray; 1.90 A; A=1-373. DR AlphaFoldDB; P32480; -. DR SMR; P32480; -. DR BioGRID; 34440; 460. DR ComplexPortal; CPX-124; HIR histone chaperone complex. DR DIP; DIP-2366N; -. DR FunCoup; P32480; 556. DR IntAct; P32480; 26. DR MINT; P32480; -. DR STRING; 4932.YOR038C; -. DR GlyGen; P32480; 1 site. DR iPTMnet; P32480; -. DR PaxDb; 4932-YOR038C; -. DR PeptideAtlas; P32480; -. DR EnsemblFungi; YOR038C_mRNA; YOR038C; YOR038C. DR GeneID; 854203; -. DR KEGG; sce:YOR038C; -. DR AGR; SGD:S000005564; -. DR SGD; S000005564; HIR2. DR VEuPathDB; FungiDB:YOR038C; -. DR eggNOG; KOG0973; Eukaryota. DR HOGENOM; CLU_004372_1_0_1; -. DR InParanoid; P32480; -. DR OMA; GHENCVA; -. DR OrthoDB; 1741719at2759; -. DR BioCyc; YEAST:G3O-33584-MONOMER; -. DR BioGRID-ORCS; 854203; 1 hit in 10 CRISPR screens. DR PRO; PR:P32480; -. DR Proteomes; UP000002311; Chromosome XV. DR RNAct; P32480; protein. DR GO; GO:0005694; C:chromosome; EXP:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:SGD. DR GO; GO:0000417; C:HIR complex; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0003714; F:transcription corepressor activity; IDA:SGD. DR GO; GO:0006325; P:chromatin organization; IDA:SGD. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:SGD. DR GO; GO:0016480; P:negative regulation of transcription by RNA polymerase III; IMP:SGD. DR GO; GO:0006334; P:nucleosome assembly; IDA:ComplexPortal. DR GO; GO:1902275; P:regulation of chromatin organization; IDA:ComplexPortal. DR GO; GO:0140673; P:transcription elongation-coupled chromatin remodeling; IGI:SGD. DR FunFam; 2.130.10.10:FF:001936; Protein HIR2; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR031120; HIR1-like. DR InterPro; IPR011494; HIRA-like_C. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR PANTHER; PTHR13831; MEMBER OF THE HIR1 FAMILY OF WD-REPEAT PROTEINS; 1. DR PANTHER; PTHR13831:SF1; PROTEIN HIR2; 1. DR Pfam; PF07569; Hira; 1. DR SUPFAM; SSF101908; Putative isomerase YbhE; 1. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. DR PDBsum; 8GHA; -. DR PDBsum; 8GHL; -. DR PDBsum; 8GHN; -. DR PDBsum; 9J5E; -. PE 1: Evidence at protein level; KW 3D-structure; Chromatin regulator; Chromosome; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; WD repeat. FT CHAIN 1..875 FT /note="Protein HIR2" FT /id="PRO_0000051017" FT REPEAT 10..47 FT /note="WD 1" FT REPEAT 118..158 FT /note="WD 2" FT REPEAT 163..201 FT /note="WD 3" FT REPEAT 237..277 FT /note="WD 4" FT REPEAT 278..316 FT /note="WD 5" FT REPEAT 320..359 FT /note="WD 6" FT REPEAT 546..587 FT /note="WD 7" FT REPEAT 589..626 FT /note="WD 8" FT REGION 398..473 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 424..446 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 713 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT CONFLICT 284..285 FT /note="KG -> NF (in Ref. 1)" FT /evidence="ECO:0000305" FT CONFLICT 373..374 FT /note="KK -> FL (in Ref. 1)" FT /evidence="ECO:0000305" FT STRAND 2..7 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 15..21 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 24..29 FT /evidence="ECO:0007829|PDB:9J5E" FT HELIX 30..32 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 33..38 FT /evidence="ECO:0007829|PDB:9J5E" FT HELIX 39..46 FT /evidence="ECO:0007829|PDB:9J5E" FT HELIX 52..54 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 58..62 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 71..76 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 78..94 FT /evidence="ECO:0007829|PDB:9J5E" FT TURN 98..101 FT /evidence="ECO:0007829|PDB:9J5E" FT HELIX 106..108 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 110..116 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 123..129 FT /evidence="ECO:0007829|PDB:9J5E" FT TURN 130..133 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 134..139 FT /evidence="ECO:0007829|PDB:9J5E" FT TURN 141..143 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 144..149 FT /evidence="ECO:0007829|PDB:9J5E" FT TURN 150..152 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 155..160 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 167..172 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 176..183 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 188..193 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 199..205 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 226..233 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 243..248 FT /evidence="ECO:0007829|PDB:9J5E" FT TURN 249..253 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 254..262 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 263..265 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 269..272 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 277..281 FT /evidence="ECO:0007829|PDB:9J5E" FT TURN 282..285 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 286..290 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 292..295 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 302..307 FT /evidence="ECO:0007829|PDB:9J5E" FT TURN 308..311 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 312..316 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 325..330 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 334..341 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 345..350 FT /evidence="ECO:0007829|PDB:9J5E" FT HELIX 353..356 FT /evidence="ECO:0007829|PDB:9J5E" FT STRAND 358..360 FT /evidence="ECO:0007829|PDB:8GHN" FT HELIX 362..369 FT /evidence="ECO:0007829|PDB:9J5E" FT HELIX 373..378 FT /evidence="ECO:0007829|PDB:8GHN" FT HELIX 443..445 FT /evidence="ECO:0007829|PDB:8GHL" FT HELIX 488..491 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 492..497 FT /evidence="ECO:0007829|PDB:8GHL" FT HELIX 501..503 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 504..508 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 514..521 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 525..529 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 531..539 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 542..553 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 555..560 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 565..577 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 594..600 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 603..608 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 612..617 FT /evidence="ECO:0007829|PDB:8GHL" FT TURN 618..621 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 622..625 FT /evidence="ECO:0007829|PDB:8GHL" FT HELIX 631..634 FT /evidence="ECO:0007829|PDB:8GHL" FT TURN 636..638 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 651..657 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 662..666 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 671..675 FT /evidence="ECO:0007829|PDB:8GHL" FT TURN 676..679 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 680..685 FT /evidence="ECO:0007829|PDB:8GHL" FT HELIX 689..692 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 704..706 FT /evidence="ECO:0007829|PDB:8GHL" FT HELIX 711..714 FT /evidence="ECO:0007829|PDB:8GHL" FT HELIX 719..729 FT /evidence="ECO:0007829|PDB:8GHL" FT HELIX 735..750 FT /evidence="ECO:0007829|PDB:8GHL" FT HELIX 753..764 FT /evidence="ECO:0007829|PDB:8GHL" FT HELIX 772..790 FT /evidence="ECO:0007829|PDB:8GHL" FT HELIX 794..811 FT /evidence="ECO:0007829|PDB:8GHL" FT HELIX 814..825 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 826..828 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 832..835 FT /evidence="ECO:0007829|PDB:8GHL" FT HELIX 841..854 FT /evidence="ECO:0007829|PDB:8GHL" FT HELIX 861..870 FT /evidence="ECO:0007829|PDB:8GHL" SQ SEQUENCE 875 AA; 98445 MW; C77D677BF424680D CRC64; MRLLKYPLDI HNEQVNALAA LGPYIILAGS GGHVMAWRQQ QLVDTAFDRV MIKDLKPEVS FQVDQDTTGD IFFITGDLET LYIGSEHRLW GYSGWLCRDT NNINSVEKMN SKLLFECKSP STITDVKYDI NLGILFVLLS NENKILLFRH KTFDKLSEIT IDKASKPITG IIDPTGQTFT VMTSDRSILV YQINKTGTHK LINKLTQHVQ MYPLHYRISM SPQADILPVI NSVKGVPNNA TSCTALLDRN NNYKVTKTLV TPSSNGCRVL VYSPAFYEKP NLKKGTSTRY NLIATSGSTD GTILVWNTKR MKPLFNALQV SSTAINDMSW SQDGFTLFAI SNDATLYTFA FQEKDLGVAL PQTEIKSLQE VNKKLPKLEE PLAEQIPKSF PENIKLEESA SAAPIPNDIG RSAVGKKPTK KKTANNQTNG IKTIQSTSME FNTPSYTVPR DLKRKPKEAT PSNIAPGSKK QKKELQPIDF LDTGLLLPNT SFSRIRLATP KIRSTFKYSP INNPNLILDV KNGSGNEQRP TIVKLTSKVL DQDQVLFQDF IPKLITICTA GDTFWSFCSE DGSIYIYSDS GRKLMAPLVL GVSISFLEAC GTYLLCLTSI GELYCWNIEQ KKLAFPTNTI YPLLNPSLRY SDDILTRAEN ITLCSITKKG VPLVTLSNGD GYLFDKNMET WLLVSDGWWA YGSQYWDTTN TTGLSSSKAN TDSFNGSESN INEIVSDIKN DNQSIINFLE CKTNDELNRK GRIKNLQRFA RTILMKEGFE NMEEIVTLSH LENKILISIR LEEPEEFSKL MMVYCIRLSE LGYMDRLNDV FQWLYDDLPI SGTGSAFADK DFKRNLLKKI LIACGDIRQV QRVTTRYAKE MNIIS //