ID LMBD2_REOVD Reviewed; 1289 AA. AC P11079; A4ZY21; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 2. DT 04-NOV-2026, entry version 115. DE RecName: Full=Outer capsid protein lambda-2; DE Short=Lambda2; DE AltName: Full=Lambda2(Cap); DE Includes: DE RecName: Full=mRNA guanylyltransferase; DE EC=2.7.7.50; DE Includes: DE RecName: Full=mRNA (guanine-N(7))-methyltransferase; DE EC=2.1.1.56; GN Name=L2; OS Reovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3). OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Spinareoviridae; Orthoreovirus; Orthoreovirus mammalis; OC Mammalian orthoreovirus. OX NCBI_TaxID=10886; OH NCBI_TaxID=40674; Mammalia. RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=2824487; DOI=10.1016/s0021-9258(18)49252-6; RA Seliger L.S., Zheng K., Shatkin A.J.; RT "Complete nucleotide sequence of reovirus L2 gene and deduced amino acid RT sequence of viral mRNA guanylyltransferase."; RL J. Biol. Chem. 262:16289-16293(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], SEQUENCE REVISION TO 609, RP CHARACTERIZATION OF GUANYLYLTRANSFERASE ACTIVITY, MUTAGENESIS OF LYS-44; RP LYS-89; LYS-94; LYS-171; LYS-190; LYS-197 AND LYS-226, AND FUNCTION RP (GUANYLYLTRANSFERASE). RX PubMed=10644745; DOI=10.1074/jbc.275.4.2804; RA Luongo C.L., Reinisch K.M., Harrison S.C., Nibert M.L.; RT "Identification of the guanylyltransferase region and active site in RT reovirus mRNA capping protein lambda2."; RL J. Biol. Chem. 275:2804-2810(2000). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Infectious clone; RX PubMed=18005692; DOI=10.1016/j.chom.2007.03.003; RA Kobayashi T., Antar A.A., Boehme K.W., Danthi P., Eby E.A., Guglielmi K.M., RA Holm G.H., Johnson E.M., Maginnis M.S., Naik S., Skelton W.B., Wetzel J.D., RA Wilson G.J., Chappell J.D., Dermody T.S.; RT "A plasmid-based reverse genetics system for animal double-stranded RNA RT viruses."; RL Cell Host Microbe 1:147-157(2007). RN [4] RP X-RAY CRYSTALLOGRAPHY, DOMAIN, SUBUNIT, AND SUBCELLULAR LOCATION. RC STRAIN=Reassortant F18; RX PubMed=10801118; DOI=10.1038/35010041; RA Reinisch K.M., Nibert M.L., Harrison S.C.; RT "Structure of the reovirus core at 3.6 A resolution."; RL Nature 404:960-967(2000). RN [5] RP STRUCTURE BY ELECTRON MICROSCOPY. RX PubMed=16216585; DOI=10.1016/j.str.2005.07.012; RA Zhang X., Ji Y., Zhang L., Harrison S.C., Marinescu D.C., Nibert M.L., RA Baker T.S.; RT "Features of reovirus outer capsid protein mu1 revealed by electron RT cryomicroscopy and image reconstruction of the virion at 7.0 Angstrom RT resolution."; RL Structure 13:1545-1557(2005). RN [6] {ECO:0007744|PDB:6ZTZ} RP STRUCTURE BY NMR OF 2-1289, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=32895380; DOI=10.1038/s41467-020-18243-9; RA Sutton G., Sun D., Fu X., Kotecha A., Hecksel C.W., Clare D.K., Zhang P., RA Stuart D.I., Boyce M.; RT "Assembly intermediates of orthoreovirus captured in the cell."; RL Nat. Commun. 11:4445-4445(2020). RN [7] {ECO:0007744|PDB:7ELL} RP STRUCTURE BY ELECTRON MICROSCOPY OF THE VIRAL PARTICLE, SUBUNIT, RP INTERACTION WITH CAPSID PROTEIN LAMBDA-1, INTERACTION WITH MU-1, AND RP INTERACTION WITH SIGMA-2. RX PubMed=34234134; DOI=10.1038/s41467-021-24455-4; RA Pan M., Alvarez-Cabrera A.L., Kang J.S., Wang L., Fan C., Zhou Z.H.; RT "Asymmetric reconstruction of mammalian reovirus reveals interactions among RT RNA, transcriptional factor 2 and capsid proteins."; RL Nat. Commun. 12:4176-4176(2021). RN [8] {ECO:0007744|PDB:9CYT, ECO:0007744|PDB:9CYX, ECO:0007744|PDB:9CYY} RP STRUCTURE BY ELECTRON MICROSCOPY, SUBCELLULAR LOCATION, FUNCTION, AND RP SUBUNIT. RX PubMed=39639006; DOI=10.1038/s41467-024-54968-7; RA Liu X., Xia X., Martynowycz M.W., Gonen T., Zhou Z.H.; RT "Molecular sociology of virus-induced cellular condensates supporting RT reovirus assembly and replication."; RL Nat. Commun. 15:10638-10638(2024). CC -!- FUNCTION: Outer capsid protein involved in mRNA capping. Catalyzes the CC last 3 enzymatic activities for formation of the 5' cap structure on CC the viral plus-strand transcripts, namely the RNA guanylyltransferase, CC RNA-7N- and RNA-2'O-methyltransferase activities (Probable). Forms CC turrets at the fivefold axes, which enzymatically cap the mRNA CC transcripts produced by the polymerase on egress from the particle CC (PubMed:32895380). During virus assembly, the inner layer proteins CC lambda-2 and lambda-1 form the star core, followed by the stepwise CC attachment of sigma-2 that completes the core and mu1/sigma3 that CC complete the outer layer (PubMed:39639006). CC {ECO:0000269|PubMed:39639006, ECO:0000303|PubMed:32895380, CC ECO:0000305|PubMed:10644745}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'- CC end (5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate; CC Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S- CC adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'- CC triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA- CC COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, CC ChEBI:CHEBI:167617; EC=2.1.1.56; CC -!- SUBUNIT: Homopentamer (PubMed:10801118, PubMed:34234134, CC PubMed:39639006). Interacts with protein mu-NS; in viral inclusions (By CC similarity). Interacts with capsid protein lambda-1 (PubMed:34234134). CC Interacts with mu-1 (PubMed:34234134). Interacts with sigma-2 CC (PubMed:34234134). {ECO:0000250|UniProtKB:Q91RA6, CC ECO:0000269|PubMed:10801118, ECO:0000269|PubMed:34234134, CC ECO:0000269|PubMed:39639006}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:10801118, CC ECO:0000269|PubMed:32895380, ECO:0000269|PubMed:39639006}. CC Note=Localizes at the fivefold axes where it forms turrets (60 copies). CC {ECO:0000269|PubMed:39639006}. CC -!- DOMAIN: Contains 2 methylase domains. The first one is probably the N7- CC modifying enzyme and the second one, the O-methyltransferase. CC {ECO:0000269|PubMed:10801118}. CC -!- SIMILARITY: Belongs to the orthoreovirus lambda-2 protein family. CC {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; J03488; AAA47253.1; -; Genomic_RNA. DR EMBL; EF494436; ABP48914.1; -; Genomic_RNA. DR PIR; A28471; RMXRR3. DR PDB; 1EJ6; X-ray; 3.60 A; A=1-1289. DR PDB; 2CSE; EM; 7.00 A; U=1-1289. DR PDB; 6ZTZ; EM; -; O=2-1289. DR PDB; 7ELL; EM; 3.80 A; K=1-1289. DR PDB; 9CYT; EM; 3.70 A; J=1-1289. DR PDB; 9CYX; EM; 3.30 A; A=2-1289. DR PDB; 9CYY; EM; 3.00 A; J=1-1289. DR EMDB; EMD-13149; -. DR EMDB; EMD-13150; -. DR EMDB; EMD-46049; -. DR EMDB; EMD-46053; -. DR EMDB; EMD-46054; -. DR MDposit; P11079; -. DR SMR; P11079; -. DR EvolutionaryTrace; P11079; -. DR GO; GO:0019030; C:icosahedral viral capsid; IDA:CACAO. DR GO; GO:0039624; C:viral outer capsid; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:UniProtKB-EC. DR FunFam; 3.40.50.10760:FF:000001; Outer capsid protein lambda-2; 1. DR FunFam; 3.90.1810.10:FF:000001; Outer capsid protein lambda-2; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR Gene3D; 3.55.60.10; Reovirus components; 1. DR Gene3D; 3.90.1810.10; Reovirus components; 1. DR Gene3D; 3.40.50.10760; Reovirus core; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR010311; Reovirus_L2. DR InterPro; IPR048604; Reovirus_L2_4th. DR InterPro; IPR048603; Reovirus_L2_6th. DR InterPro; IPR048602; Reovirus_L2_7th. DR InterPro; IPR048294; Reovirus_L2_8th. DR InterPro; IPR048601; Reovirus_L2_GTase. DR InterPro; IPR048598; Reovirus_L2_MT1. DR InterPro; IPR048597; Reovirus_L2_MT2. DR InterPro; IPR048596; Reovirus_L2_N. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR Pfam; PF21062; Reovirus_L2_4th; 1. DR Pfam; PF21060; Reovirus_L2_6th; 1. DR Pfam; PF21061; Reovirus_L2_7th; 1. DR Pfam; PF06016; Reovirus_L2_8th; 1. DR Pfam; PF21063; Reovirus_L2_GTase; 1. DR Pfam; PF21065; Reovirus_L2_MT1; 1. DR Pfam; PF21066; Reovirus_L2_MT2; 1. DR Pfam; PF21064; Reovirus_L2_N; 1. DR PIRSF; PIRSF000845; Reovirus_L2; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Capsid protein; GTP-binding; Methyltransferase; KW mRNA capping; mRNA processing; Multifunctional enzyme; Nucleotide-binding; KW Nucleotidyltransferase; Outer capsid protein; S-adenosyl-L-methionine; KW Transferase; Virion. FT CHAIN 1..1289 FT /note="Outer capsid protein lambda-2" FT /id="PRO_0000222741" FT REGION 434..691 FT /note="Probable N7-modifying activity" FT /evidence="ECO:0000305|PubMed:10801118" FT REGION 804..1022 FT /note="Probable O-methyltransferase activity" FT /evidence="ECO:0000305|PubMed:10801118" FT BINDING 893..900 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT SITE 171 FT /note="Contributes to the autoguanylylation" FT /evidence="ECO:0000269|PubMed:10644745" FT SITE 190 FT /note="Involved in formation of the phosphoamide bond FT (autoguanylation)" FT /evidence="ECO:0000269|PubMed:10644745" FT MUTAGEN 44 FT /note="K->A: Almost no effect on autoguanylylation FT activity." FT /evidence="ECO:0000269|PubMed:10644745" FT MUTAGEN 89 FT /note="K->A: Almost no effect on autoguanylylation FT activity." FT /evidence="ECO:0000269|PubMed:10644745" FT MUTAGEN 94 FT /note="K->A: Almost no effect on autoguanylylation FT activity." FT /evidence="ECO:0000269|PubMed:10644745" FT MUTAGEN 171 FT /note="K->A: Almost complete loss of autoguanylylation FT activity." FT /evidence="ECO:0000269|PubMed:10644745" FT MUTAGEN 190 FT /note="K->A: Complete loss of autoguanylylation activity." FT /evidence="ECO:0000269|PubMed:10644745" FT MUTAGEN 197 FT /note="K->A: 90% loss of autoguanylylation activity." FT /evidence="ECO:0000269|PubMed:10644745" FT MUTAGEN 226 FT /note="K->A: No effect on autoguanylylation activity." FT /evidence="ECO:0000269|PubMed:10644745" FT CONFLICT 504 FT /note="E -> G (in Ref. 2; ABP48914)" FT /evidence="ECO:0000305" FT CONFLICT 509 FT /note="R -> G (in Ref. 2; ABP48914)" FT /evidence="ECO:0000305" FT CONFLICT 609 FT /note="G -> F (in Ref. 1; AAA47253)" FT /evidence="ECO:0000305" FT STRAND 7..9 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 11..13 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 27..34 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 42..47 FT /evidence="ECO:0007829|PDB:9CYY" FT TURN 49..51 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 54..59 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 61..63 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 70..73 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 79..100 FT /evidence="ECO:0007829|PDB:9CYY" FT TURN 103..105 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 113..124 FT /evidence="ECO:0007829|PDB:9CYY" FT TURN 130..132 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 133..135 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 142..148 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 154..159 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 164..167 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 171..174 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 182..184 FT /evidence="ECO:0007829|PDB:9CYX" FT TURN 188..191 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 195..200 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 204..210 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 211..213 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 220..222 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 228..236 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 244..246 FT /evidence="ECO:0007829|PDB:9CYX" FT HELIX 251..269 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 284..287 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 289..291 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 297..310 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 314..316 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 324..335 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 351..353 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 361..364 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 366..371 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 383..386 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 390..392 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 400..405 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 407..417 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 429..432 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 435..440 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 450..452 FT /evidence="ECO:0007829|PDB:9CYY" FT TURN 458..461 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 463..475 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 481..493 FT /evidence="ECO:0007829|PDB:9CYY" FT TURN 499..501 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 503..506 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 511..515 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 521..526 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 530..535 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 545..551 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 555..558 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 571..576 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 580..584 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 585..587 FT /evidence="ECO:0007829|PDB:9CYX" FT HELIX 588..605 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 606..618 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 621..626 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 627..631 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 632..634 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 636..647 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 651..657 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 668..688 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 698..700 FT /evidence="ECO:0007829|PDB:9CYX" FT STRAND 702..713 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 715..717 FT /evidence="ECO:0007829|PDB:9CYX" FT HELIX 721..733 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 740..746 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 749..758 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 760..767 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 769..775 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 778..781 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 793..795 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 803..818 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 825..829 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 835..838 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 846..852 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 861..863 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 865..870 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 874..876 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 878..880 FT /evidence="ECO:0007829|PDB:9CYX" FT STRAND 884..888 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 892..899 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 903..914 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 920..925 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 930..932 FT /evidence="ECO:0007829|PDB:9CYY" FT TURN 937..939 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 940..943 FT /evidence="ECO:0007829|PDB:9CYY" FT TURN 944..947 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 948..951 FT /evidence="ECO:0007829|PDB:9CYY" FT TURN 952..955 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 956..959 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 963..973 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 978..981 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 989..991 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 992..995 FT /evidence="ECO:0007829|PDB:9CYY" FT TURN 996..998 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 1003..1013 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 1018..1024 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 1038..1046 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 1052..1064 FT /evidence="ECO:0007829|PDB:9CYY" FT TURN 1065..1067 FT /evidence="ECO:0007829|PDB:9CYX" FT HELIX 1068..1070 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 1072..1081 FT /evidence="ECO:0007829|PDB:9CYY" FT TURN 1082..1085 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 1086..1092 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 1097..1104 FT /evidence="ECO:0007829|PDB:9CYY" FT TURN 1106..1109 FT /evidence="ECO:0007829|PDB:9CYX" FT STRAND 1110..1120 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 1127..1129 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 1137..1139 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 1141..1146 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 1153..1159 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 1162..1165 FT /evidence="ECO:0007829|PDB:9CYY" FT TURN 1168..1170 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 1171..1175 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 1181..1185 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 1189..1192 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 1196..1200 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 1202..1209 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 1211..1214 FT /evidence="ECO:0007829|PDB:9CYY" FT HELIX 1215..1218 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 1224..1226 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 1228..1230 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 1233..1236 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 1238..1242 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 1245..1250 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 1269..1271 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 1277..1279 FT /evidence="ECO:0007829|PDB:9CYY" FT STRAND 1284..1288 FT /evidence="ECO:0007829|PDB:9CYY" SQ SEQUENCE 1289 AA; 143976 MW; D96FCEE31855F41C CRC64; MANVWGVRLA DSLSSPTIET RTRQYTLHDL CSDLDANPGR EPWKPLRNQR TNNIVAVQLF RPLQGLVLDT QLYGFPGAFD DWERFMREKL RVLKYEVLRI YPISNYSNEH VNVFVANALV GAFLSNQAFY DLLPLLIIND TMIGDLLGTG ASLSQFFQSH GDVLEVAAGR KYLQMENYSN DDDDPPLFAK DLSDYAKAFY SDTYEVLDRF FWTHDSSAGV LVHYDKPTNG HHYLLGTLTQ MVSAPPYIIN ATDAMLLESC LEQFSANVRA RPAQPVTRLD QCYHLRWGAQ YVGEDSLTYR LGVLSLLATN GYQLARPIPR QLTNRWLSSF VSQIMSDGVN ETPLWPQERY VQIAYDSPSV VDGATQYGYV RKNQLRLGMR ISALQSLSDT PSPVQWLPQY TIDQAAMDEG DLMVSRLTQL PLRPDYGNIW VGDALSYYVD YNRSHRVVLS SELPQLPDTY FDGDEQYGRS LFSLARKIGD RSLVKDTAVL KHAYQAIDPN TGKEYLRSRQ SVAYFGASAG HSGADQPLVI EPWIQGKISG VPPPSSVRQF GYDVARGAIV DLARPFPSGD YQFVYSDVDQ VVDGHDDLSI SSGLVESLLS SCMHATAPGG SFVVKINFPT RPVWHYIEQK ILPNITSYML IKPFVTNNVE LFFVAFGVHQ HSSLTWTSGV YFFLVDHFYR YETLSTISRQ LPSFGYVDDG SSVTGIETIS IENPGFSNMT QAARIGISGL CANVGNARKS IAIYESHGAR VLTITSRRSP ASARRKSRLR YLPLIDPRSL EVQARTILPA DPVLFENVSG ASPHVCLTMM YNFEVSSAVY DGDVVLDLGT GPEAKILELI PATSPVTCVD IRPTAQPSGC WNVRTTFLEL DYLSDGWITG VRGDIVTCML SLGAAAAGKS MTFDAAFQQL IKVLSKSTAN VVLVQVNCPT DVVRSIKGYL EIDSTNKRYR FPKFGRDEPY SDMDALEKIC RTAWPNCSIT WVPLSYDLRW TRLALLESTT LSSASIRIAE LMYKYMPIMR IDIHGLPMEK RGNFIVGQNC SLVIPGFNAQ DVFNCYFNSA LAFSTEDVNA AMIPQVSAQF DATKGEWTLD MVFSDAGIYT MQALVGSNAN PVSLGSFVVD SPDVDITDAW PAQLDFTIAG TDVDITVNPY YRLMTFVRID GQWQIANPDK FQFFSSASGT LVMNVKLDIA DKYLLYYIRD VQSRDVGFYI QHPLQLLNTI TLPTNEDLFL SAPDMREWAV KESGNTICIL NSQGFVLPQD WDVLTDTISW SPSIPTYIVP PGDYTLTPL //