ID PRP2_YEAST Reviewed; 876 AA.
AC P20095; D6W1I6;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 27-MAR-2024, entry version 212.
DE RecName: Full=Pre-mRNA-splicing factor ATP-dependent RNA helicase-like protein PRP2;
DE EC=3.6.4.13;
DE AltName: Full=Pre-mRNA-processing protein 2;
GN Name=PRP2; Synonyms=RNA2; OrderedLocusNames=YNR011C; ORFNames=N2048;
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].
RX PubMed=2147058; DOI=10.1093/nar/18.21.6447;
RA Chen J.H., Lin R.J.;
RT "The yeast PRP2 protein, a putative RNA-dependent ATPase, shares extensive
RT sequence homology with two other pre-mRNA splicing factors.";
RL Nucleic Acids Res. 18:6447-6447(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DBY939;
RA Beggs J.D.;
RL Submitted (FEB-1990) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=7900425; DOI=10.1002/yea.320101013;
RA Verhasselt P., Aert R., Voet M., Volckaert G.;
RT "Twelve open reading frames revealed in the 23.6 kb segment flanking the
RT centromere on the Saccharomyces cerevisiae chromosome XIV right arm.";
RL Yeast 10:1355-1361(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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 SUBCELLULAR LOCATION.
RX PubMed=3536958; DOI=10.1083/jcb.103.6.2103;
RA Last R.L., Woolford J.L. Jr.;
RT "Identification and nuclear localization of yeast pre-messenger RNA
RT processing components: RNA2 and RNA3 proteins.";
RL J. Cell Biol. 103:2103-2112(1986).
RN [7]
RP FUNCTION, AND INTERACTION WITH SPLICEOSOME.
RX PubMed=2251118; DOI=10.1093/nar/18.22.6559;
RA King D.S., Beggs J.D.;
RT "Interactions of PRP2 protein with pre-mRNA splicing complexes in
RT Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 18:6559-6564(1990).
RN [8]
RP FUNCTION AS A NTPASE, AND LACK OF HELICASE ACTIVITY.
RX PubMed=1534753; DOI=10.1002/j.1460-2075.1992.tb05291.x;
RA Kim S.-H., Smith J., Claude A., Lin R.-J.;
RT "The purified yeast pre-mRNA splicing factor PRP2 is an RNA-dependent
RT NTPase.";
RL EMBO J. 11:2319-2326(1992).
RN [9]
RP MUTAGENESIS OF SER-378.
RX PubMed=8112301; DOI=10.1002/j.1460-2075.1994.tb06331.x;
RA Plumpton M., McGarvey M., Beggs J.D.;
RT "A dominant negative mutation in the conserved RNA helicase motif 'SAT'
RT causes splicing factor PRP2 to stall in spliceosomes.";
RL EMBO J. 13:879-887(1994).
RN [10]
RP FUNCTION, AND INTERACTION WITH PRE-MRNA.
RX PubMed=8112302; DOI=10.1002/j.1460-2075.1994.tb06332.x;
RA Teigelkamp S., McGarvey M., Plumpton M., Beggs J.D.;
RT "The splicing factor PRP2, a putative RNA helicase, interacts directly with
RT pre-mRNA.";
RL EMBO J. 13:888-897(1994).
RN [11]
RP INTERACTION WITH SPP2.
RX PubMed=7493316;
RA Roy J., Kim K., Maddock J.R., Anthony J.G., Woolford J.L. Jr.;
RT "The final stages of spliceosome maturation require Spp2p that can interact
RT with the DEAH box protein Prp2p and promote step 1 of splicing.";
RL RNA 1:375-390(1995).
RN [12]
RP FUNCTION AS AN ATPASE, AND INTERACTION WITH SPLICEOSOME.
RX PubMed=8943336; DOI=10.1128/mcb.16.12.6810;
RA Kim S.-H., Lin R.-J.;
RT "Spliceosome activation by PRP2 ATPase prior to the first
RT transesterification reaction of pre-mRNA splicing.";
RL Mol. Cell. Biol. 16:6810-6819(1996).
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 INTERACTION WITH SPP2, AND MUTAGENESIS OF ASP-845; 845-ASP-CYS-846 AND
RP 854-TRP-LEU-855.
RX PubMed=15542821; DOI=10.1128/mcb.24.23.10101-10110.2004;
RA Silverman E.J., Maeda A., Wei J., Smith P., Beggs J.D., Lin R.-J.;
RT "Interaction between a G-patch protein and a spliceosomal DEXD/H-box ATPase
RT that is critical for splicing.";
RL Mol. Cell. Biol. 24:10101-10110(2004).
RN [16]
RP FUNCTION AS AN ATPASE, INTERACTION WITH SPLICEOSOME, DELETION MUTANTS, AND
RP MUTAGENESIS OF HIS-349; GLN-548; GLY-551 AND 845-ASP-CYS-846.
RX PubMed=14730020; DOI=10.1261/rna.5151404;
RA Edwalds-Gilbert G., Kim D.-H., Silverman E., Lin R.-J.;
RT "Definition of a spliceosome interaction domain in yeast Prp2 ATPase.";
RL RNA 10:210-220(2004).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
CC -!- FUNCTION: Involved in pre-mRNA splicing. Is required together with ATP
CC and at least one other factor, for the first cleavage-ligation
CC reaction. Functions as a molecular motor in the activation of the
CC precatalytic spliceosome for the first transesterification reaction of
CC pre-mRNA splicing by hydrolyzing ATP to cause the activation of the
CC spliceosome without the occurrence of splicing. Capable of hydrolyzing
CC nucleoside triphosphates in the presence of single-stranded RNAs such
CC as poly(U). {ECO:0000269|PubMed:14730020, ECO:0000269|PubMed:1534753,
CC ECO:0000269|PubMed:2251118, ECO:0000269|PubMed:8112302,
CC ECO:0000269|PubMed:8943336}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- SUBUNIT: Interacts directly with pre-mRNA. According to PubMed:2251118,
CC associated with spliceosomes prior to and throughout step 1 of the
CC splicing reaction. According to PubMed:8943336, it leaves the
CC spliceosome before reaction 1. Interacts with SPP2.
CC {ECO:0000269|PubMed:14730020, ECO:0000269|PubMed:15542821,
CC ECO:0000269|PubMed:2251118, ECO:0000269|PubMed:7493316,
CC ECO:0000269|PubMed:8112302, ECO:0000269|PubMed:8943336}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:3536958}.
CC -!- MISCELLANEOUS: Present with 172 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
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DR EMBL; X55936; CAA39401.1; -; Genomic_DNA.
DR EMBL; X55999; CAA39471.1; -; Genomic_DNA.
DR EMBL; X77395; CAA54579.1; -; Genomic_DNA.
DR EMBL; Z71626; CAA96288.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10552.1; -; Genomic_DNA.
DR PIR; S12334; S12334.
DR RefSeq; NP_014408.1; NM_001183188.1.
DR PDB; 5GM6; EM; 3.50 A; Y=1-876.
DR PDB; 5LQW; EM; 5.80 A; O=1-876.
DR PDB; 7DCO; EM; 2.50 A; x=1-876.
DR PDB; 7DCP; EM; 3.15 A; x=12-867.
DR PDB; 7DCQ; EM; 2.90 A; x=1-876.
DR PDB; 7DCR; EM; 3.15 A; x=1-876.
DR PDB; 7DD3; EM; 3.20 A; x=1-876.
DR PDBsum; 5GM6; -.
DR PDBsum; 5LQW; -.
DR PDBsum; 7DCO; -.
DR PDBsum; 7DCP; -.
DR PDBsum; 7DCQ; -.
DR PDBsum; 7DCR; -.
DR PDBsum; 7DD3; -.
DR AlphaFoldDB; P20095; -.
DR EMDB; EMD-30637; -.
DR EMDB; EMD-9524; -.
DR SMR; P20095; -.
DR BioGRID; 35836; 313.
DR DIP; DIP-3961N; -.
DR IntAct; P20095; 9.
DR MINT; P20095; -.
DR STRING; 4932.YNR011C; -.
DR iPTMnet; P20095; -.
DR MaxQB; P20095; -.
DR PaxDb; 4932-YNR011C; -.
DR PeptideAtlas; P20095; -.
DR EnsemblFungi; YNR011C_mRNA; YNR011C; YNR011C.
DR GeneID; 855745; -.
DR KEGG; sce:YNR011C; -.
DR AGR; SGD:S000005294; -.
DR SGD; S000005294; PRP2.
DR VEuPathDB; FungiDB:YNR011C; -.
DR eggNOG; KOG0923; Eukaryota.
DR GeneTree; ENSGT00940000158480; -.
DR HOGENOM; CLU_001832_7_2_1; -.
DR InParanoid; P20095; -.
DR OMA; HITLMNV; -.
DR OrthoDB; 3682876at2759; -.
DR BioCyc; YEAST:G3O-33328-MONOMER; -.
DR BioGRID-ORCS; 855745; 1 hit in 10 CRISPR screens.
DR PRO; PR:P20095; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P20095; Protein.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IDA:SGD.
DR GO; GO:0004386; F:helicase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000349; P:generation of catalytic spliceosome for first transesterification step; IDA:SGD.
DR GO; GO:0034247; P:snoRNA splicing; IMP:SGD.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF83; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE DHX16; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Hydrolase; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..876
FT /note="Pre-mRNA-splicing factor ATP-dependent RNA helicase-
FT like protein PRP2"
FT /id="PRO_0000055130"
FT DOMAIN 233..399
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 424..598
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 346..349
FT /note="DEAH box"
FT COMPBIAS 31..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 246..253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MUTAGEN 6..206
FT /note="Missing: No effect on activity."
FT MUTAGEN 89..552
FT /note="Missing: Loss of ATPase and splicing activity."
FT MUTAGEN 89..206
FT /note="Missing: Wild-type RNA-dependent ATPase activity;
FT bound tightly to the spliceosome and after addition of ATP
FT released from the spliceosome."
FT MUTAGEN 349
FT /note="H->D: Fails to release from the spliceosome; when
FT associated with H-548."
FT /evidence="ECO:0000269|PubMed:14730020"
FT MUTAGEN 378
FT /note="S->L: In PRP2-dn1; 40% of wild-type RNA-stimulated
FT ATPase activity; splicing activity abolished; accumulates
FT stalled splicing complexes."
FT /evidence="ECO:0000269|PubMed:8112301"
FT MUTAGEN 548
FT /note="Q->H: Fails to release from the spliceosome; when
FT associated with D-349."
FT /evidence="ECO:0000269|PubMed:14730020"
FT MUTAGEN 551
FT /note="G->N: Fails to release from the spliceosome."
FT /evidence="ECO:0000269|PubMed:14730020"
FT MUTAGEN 554..876
FT /note="Missing: Has small amount of ATPase activity, but no
FT splicing activity."
FT MUTAGEN 615..876
FT /note="Missing: Loss of activity."
FT MUTAGEN 824..876
FT /note="Missing: Spliceosome binding mutant; not active in
FT splicing; when associated with N-551."
FT MUTAGEN 833..876
FT /note="Missing: Spliceosome binding mutant; not active in
FT splicing; when associated with N-551."
FT MUTAGEN 834..876
FT /note="Missing: Spliceosome binding mutant; not active in
FT splicing; when associated with N-551. Almost wild-type RNA-
FT dependent ATPase activity."
FT MUTAGEN 845..846
FT /note="DC->NY: Spliceosome binding mutant; not active in
FT splicing; when associated with N-551, or D-349 and H-548.
FT Loss of interaction with SPP2."
FT /evidence="ECO:0000269|PubMed:14730020,
FT ECO:0000269|PubMed:15542821"
FT MUTAGEN 845
FT /note="D->L: Temperature-sensitive; decreased interaction
FT with SPP2, decreased cell growth on benomyl and decreased
FT splicing at elevated temperatures; when associated with D-
FT 349 and H-548."
FT /evidence="ECO:0000269|PubMed:15542821"
FT MUTAGEN 854..855
FT /note="WL->AA: Loss of interaction with SPP2."
FT /evidence="ECO:0000269|PubMed:15542821"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:7DCP"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:7DCQ"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:7DCR"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 229..238
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 252..262
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 272..279
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 280..294
FT /evidence="ECO:0007829|PDB:7DCQ"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:7DCQ"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 324..328
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 353..368
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 373..379
FT /evidence="ECO:0007829|PDB:7DCQ"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 383..389
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:7DCP"
FT HELIX 417..431
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 445..462
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 468..473
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:7DD3"
FT HELIX 480..486
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 494..503
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 513..518
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 521..527
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 529..540
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 543..550
FT /evidence="ECO:0007829|PDB:7DCQ"
FT TURN 551..553
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 555..557
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 559..565
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 567..571
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 572..574
FT /evidence="ECO:0007829|PDB:7DCP"
FT HELIX 581..583
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 588..597
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 602..605
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 613..625
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 631..633
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 637..642
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 645..647
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 649..660
FT /evidence="ECO:0007829|PDB:7DCQ"
FT TURN 662..666
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 668..679
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 680..683
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 684..687
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 689..696
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 703..716
FT /evidence="ECO:0007829|PDB:7DCQ"
FT TURN 717..719
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 721..726
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 731..751
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 753..763
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 771..782
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 786..790
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 792..797
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 800..803
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 807..809
FT /evidence="ECO:0007829|PDB:7DCP"
FT HELIX 814..820
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 828..831
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 833..845
FT /evidence="ECO:0007829|PDB:7DCQ"
FT STRAND 847..849
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 853..858
FT /evidence="ECO:0007829|PDB:7DCQ"
FT HELIX 860..866
FT /evidence="ECO:0007829|PDB:7DCQ"
SQ SEQUENCE 876 AA; 99814 MW; 7EB3E1EE93215F57 CRC64;
MSSITSETGK RRVKRTYEVT RQNDNAVRIE PSSLGEEEDK EAKDKNSALQ LKRSRYDPNK
VFSNTNQGPE KNNLKGEQLG SQKKSSKYDE KITSNNELTT KKGLLGDSEN ETKYASSNSK
FNVEVTHKIK NAKEIDKINR QRMWEEQQLR NAMAGQSDHP DDITLEGSDK YDYVFDTDAM
IDYTNEEDDL LPEEKLQYEA RLAQALETEE KRILTIQEAR KLLPVHQYKD ELLQEIKKNQ
VLIIMGETGS GKTTQLPQYL VEDGFTDQGK LQIAITQPRR VAATSVAARV ADEMNVVLGK
EVGYQIRFED KTTPNKTVLK YMTDGMLLRE FLTDSKLSKY SCIMIDEAHE RTLATDILIG
LLKDILPQRP TLKLLISSAT MNAKKFSEFF DNCPIFNVPG RRYPVDIHYT LQPEANYIHA
AITTIFQIHT TQSLPGDILV FLTGQEEIER TKTKLEEIMS KLGSRTKQMI ITPIYANLPQ
EQQLKIFQPT PENCRKVVLA TNIAETSLTI DGIRYVIDPG FVKENSYVPS TGMTQLLTVP
CSRASVDQRA GRAGRVGPGK CFRIFTKWSY LHELELMPKP EITRTNLSNT VLLLLSLGVT
DLIKFPLMDK PSIPTLRKSL ENLYILGALN SKGTITRLGK MMCEFPCEPE FAKVLYTAAT
HEQCQGVLEE CLTIVSMLHE TPSLFIGQKR DAAASVLSEV ESDHILYLEI FNQWRNSKFS
RSWCQDHKIQ FKTMLRVRNI RNQLFRCSEK VGLVEKNDQA RMKIGNIAGY INARITRCFI
SGFPMNIVQL GPTGYQTMGR SSGGLNVSVH PTSILFVNHK EKAQRPSKYV LYQQLMLTSK
EFIRDCLVIP KEEWLIDMVP QIFKDLIDDK TNRGRR
//
