PAP_YEAST
ID PAP_YEAST Reviewed; 568 AA.
AC P29468; D6VXT8;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Poly(A) polymerase;
DE Short=PAP;
DE EC=2.7.7.19;
DE AltName: Full=Polynucleotide adenylyltransferase;
GN Name=PAP1; OrderedLocusNames=YKR002W;
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], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 204510 / AB320;
RX PubMed=1840648; DOI=10.1038/354496a0;
RA Lingner J., Kellermann J., Keller W.;
RT "Cloning and expression of the essential gene for poly(A) polymerase from
RT S. cerevisiae.";
RL Nature 354:496-498(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1441752; DOI=10.1002/yea.320080908;
RA Duesterhoeft A., Philippsen P.;
RT "DNA sequencing and analysis of a 24.7 kb segment encompassing centromere
RT CEN11 of Saccharomyces cerevisiae reveals nine previously unknown open
RT reading frames.";
RL Yeast 8:749-759(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [4]
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 [5]
RP INTERACTION WITH FIR1.
RX PubMed=9236779; DOI=10.1007/s004380050491;
RA del Olmo M., Mizrahi N., Gross S., Moore C.L.;
RT "The Uba2 and Ufd1 proteins of Saccharomyces cerevisiae interact with
RT poly(A) polymerase and affect the polyadenylation activity of cell
RT extracts.";
RL Mol. Gen. Genet. 255:209-218(1997).
RN [6]
RP INTERACTION WITH RRP6.
RX PubMed=10611239; DOI=10.1128/mcb.20.2.604-616.2000;
RA Burkard K.T.D., Butler J.S.;
RT "A nuclear 3'-5' exonuclease involved in mRNA degradation interacts with
RT Poly(A) polymerase and the hnRNA protein Npl3p.";
RL Mol. Cell. Biol. 20:604-616(2000).
RN [7]
RP IDENTIFICATION IN THE CPF COMPLEX, SUBCELLULAR LOCATION, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=12819204; DOI=10.1074/jbc.m304454200;
RA Nedea E., He X., Kim M., Pootoolal J., Zhong G., Canadien V., Hughes T.,
RA Buratowski S., Moore C.L., Greenblatt J.;
RT "Organization and function of APT, a subcomplex of the yeast cleavage and
RT polyadenylation factor involved in the formation of mRNA and small
RT nucleolar RNA 3'-ends.";
RL J. Biol. Chem. 278:33000-33010(2003).
RN [8]
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550, AND IDENTIFICATION BY
RP 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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-537 IN COMPLEX WITH ATP ANALOG
RP AND MANGANESE IONS.
RX PubMed=10958780; DOI=10.1126/science.289.5483.1346;
RA Bard J., Zhelkovsky A.M., Helmling S., Earnest T.N., Moore C.L., Bohm A.;
RT "Structure of yeast poly(A) polymerase alone and in complex with 3'-dATP.";
RL Science 289:1346-1349(2000).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-530.
RX PubMed=17223131; DOI=10.1016/j.jmb.2006.12.030;
RA Balbo P.B., Toth J., Bohm A.;
RT "X-ray crystallographic and steady state fluorescence characterization of
RT the protein dynamics of yeast polyadenylate polymerase.";
RL J. Mol. Biol. 366:1401-1415(2007).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 5-529 OF MUTANT ALA-154 IN COMPLEX
RP WITH ATP; MAGNESIUM IONS AND OLIGONUCLEOTIDE, CATALYTIC ACTIVITY, FUNCTION,
RP COFACTOR, AND MUTAGENESIS OF ASP-154; ASN-189; LYS-215 AND ASN-226.
RX PubMed=17850751; DOI=10.1016/j.str.2007.07.010;
RA Balbo P.B., Bohm A.;
RT "Mechanism of poly(A) polymerase: structure of the enzyme-MgATP-RNA ternary
RT complex and kinetic analysis.";
RL Structure 15:1117-1131(2007).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-537 IN COMPLEX WITH FIP1,
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH FIP1, AND MUTAGENESIS OF
RP CYS-485 AND VAL-489.
RX PubMed=18537269; DOI=10.1021/bi800204k;
RA Meinke G., Ezeokonkwo C., Balbo P., Stafford W., Moore C., Bohm A.;
RT "Structure of yeast poly(A) polymerase in complex with a peptide from Fip1,
RT an intrinsically disordered protein.";
RL Biochemistry 47:6859-6869(2008).
CC -!- FUNCTION: Polymerase component of the cleavage and polyadenylation
CC factor (CPF) complex, which plays a key role in polyadenylation-
CC dependent pre-mRNA 3'-end formation and cooperates with cleavage
CC factors including the CFIA complex and NAB4/CFIB.
CC {ECO:0000269|PubMed:17850751, ECO:0000269|PubMed:18537269}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
CC Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173115; EC=2.7.7.19;
CC Evidence={ECO:0000269|PubMed:17850751, ECO:0000269|PubMed:18537269};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17850751};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17850751};
CC Note=Binds 2 magnesium ions. Also active with manganese.
CC {ECO:0000269|PubMed:17850751};
CC -!- SUBUNIT: Component of the cleavage and polyadenylation factor (CPF)
CC complex, which is composed of PTI1, SYC1, SSU72, GLC7, MPE1, REF2,
CC PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1.
CC Interacts with FIR1 and RRP6. {ECO:0000269|PubMed:10611239,
CC ECO:0000269|PubMed:10958780, ECO:0000269|PubMed:12819204,
CC ECO:0000269|PubMed:17850751, ECO:0000269|PubMed:18537269,
CC ECO:0000269|PubMed:9236779}.
CC -!- INTERACTION:
CC P29468; Q06632: CFT1; NbExp=5; IntAct=EBI-12917, EBI-32872;
CC P29468; P45976: FIP1; NbExp=9; IntAct=EBI-12917, EBI-6940;
CC P29468; Q03735: NAB6; NbExp=2; IntAct=EBI-12917, EBI-27955;
CC P29468; Q01329: PTA1; NbExp=8; IntAct=EBI-12917, EBI-14145;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12819204,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 17100 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the poly(A) polymerase family. {ECO:0000305}.
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DR EMBL; X60307; CAA42852.1; -; Genomic_DNA.
DR EMBL; X65124; CAA46250.1; -; Genomic_DNA.
DR EMBL; Z28227; CAA82072.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09158.1; -; Genomic_DNA.
DR PIR; S19031; S19031.
DR RefSeq; NP_012927.3; NM_001179792.3.
DR PDB; 1FA0; X-ray; 2.60 A; A/B=1-537.
DR PDB; 2HHP; X-ray; 1.80 A; A=1-530.
DR PDB; 2O1P; X-ray; 2.70 A; A/B=1-538.
DR PDB; 2Q66; X-ray; 1.80 A; A=5-529.
DR PDB; 3C66; X-ray; 2.60 A; A/B=1-526.
DR PDBsum; 1FA0; -.
DR PDBsum; 2HHP; -.
DR PDBsum; 2O1P; -.
DR PDBsum; 2Q66; -.
DR PDBsum; 3C66; -.
DR AlphaFoldDB; P29468; -.
DR SMR; P29468; -.
DR BioGRID; 34134; 81.
DR ComplexPortal; CPX-1053; Cleavage and polyadenylation specificity factor complex.
DR DIP; DIP-2297N; -.
DR IntAct; P29468; 30.
DR MINT; P29468; -.
DR STRING; 4932.YKR002W; -.
DR iPTMnet; P29468; -.
DR MaxQB; P29468; -.
DR PaxDb; P29468; -.
DR PRIDE; P29468; -.
DR EnsemblFungi; YKR002W_mRNA; YKR002W; YKR002W.
DR GeneID; 853871; -.
DR KEGG; sce:YKR002W; -.
DR SGD; S000001710; PAP1.
DR VEuPathDB; FungiDB:YKR002W; -.
DR eggNOG; KOG2245; Eukaryota.
DR GeneTree; ENSGT00940000168779; -.
DR HOGENOM; CLU_011511_4_1_1; -.
DR InParanoid; P29468; -.
DR OMA; QWPTPVV; -.
DR BioCyc; YEAST:G3O-31980-MON; -.
DR BRENDA; 2.7.7.19; 984.
DR EvolutionaryTrace; P29468; -.
DR PRO; PR:P29468; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P29468; protein.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006378; P:mRNA polyadenylation; IDA:SGD.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IDA:ComplexPortal.
DR GO; GO:0043631; P:RNA polyadenylation; IDA:UniProtKB.
DR GO; GO:0071050; P:sno(s)RNA polyadenylation; IGI:SGD.
DR GO; GO:0030846; P:termination of RNA polymerase II transcription, poly(A)-coupled; IC:ComplexPortal.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR011068; NuclTrfase_I-like_C.
DR InterPro; IPR007012; PolA_pol_cen_dom.
DR InterPro; IPR007010; PolA_pol_RNA-bd_dom.
DR InterPro; IPR014492; PolyA_polymerase.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF04928; PAP_central; 1.
DR Pfam; PF04926; PAP_RNA-bind; 1.
DR PIRSF; PIRSF018425; PolyA_polymerase; 1.
DR SUPFAM; SSF55003; SSF55003; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; Magnesium; Manganese;
KW Metal-binding; mRNA processing; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..568
FT /note="Poly(A) polymerase"
FT /id="PRO_0000051621"
FT REGION 525..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87..89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17850751"
FT BINDING 99..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17850751"
FT BINDING 100..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17850751"
FT BINDING 100
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 100
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT BINDING 154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17850751"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17850751"
FT BINDING 224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17850751"
FT BINDING 233..234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17850751"
FT SITE 140
FT /note="Interaction with RNA"
FT SITE 145
FT /note="Interaction with RNA"
FT SITE 294
FT /note="Interaction with RNA"
FT SITE 314
FT /note="Interaction with RNA"
FT SITE 315
FT /note="Interaction with RNA"
FT SITE 387
FT /note="Interaction with RNA"
FT SITE 392
FT /note="Interaction with RNA"
FT SITE 487
FT /note="Interaction with RNA"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 154
FT /note="D->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:17850751"
FT MUTAGEN 189
FT /note="N->A: Slightly reduced rate of adenylyltransfer."
FT /evidence="ECO:0000269|PubMed:17850751"
FT MUTAGEN 215
FT /note="K->A: Reduces rate of adenylyltransfer about four-
FT fold."
FT /evidence="ECO:0000269|PubMed:17850751"
FT MUTAGEN 226
FT /note="N->A: Reduces rate of adenylyltransfer by half."
FT /evidence="ECO:0000269|PubMed:17850751"
FT MUTAGEN 485
FT /note="C->R: Abolishes interaction with FIP1; when
FT associated with Y-489."
FT /evidence="ECO:0000269|PubMed:18537269"
FT MUTAGEN 489
FT /note="V->Y: Abolishes interaction with FIP1; when
FT associated with R-485."
FT /evidence="ECO:0000269|PubMed:18537269"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:2HHP"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:2Q66"
FT HELIX 20..35
FT /evidence="ECO:0007829|PDB:2HHP"
FT HELIX 42..69
FT /evidence="ECO:0007829|PDB:2HHP"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:2HHP"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:2HHP"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:2HHP"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:2HHP"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:2HHP"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:2HHP"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:2HHP"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:2HHP"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:2HHP"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:2HHP"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:2HHP"
FT HELIX 182..200
FT /evidence="ECO:0007829|PDB:2HHP"
FT HELIX 204..220
FT /evidence="ECO:0007829|PDB:2HHP"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:2HHP"
FT HELIX 233..246
FT /evidence="ECO:0007829|PDB:2HHP"
FT HELIX 252..265
FT /evidence="ECO:0007829|PDB:2HHP"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:2HHP"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:1FA0"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:2HHP"
FT HELIX 293..296
FT /evidence="ECO:0007829|PDB:2HHP"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:2HHP"
FT TURN 312..315
FT /evidence="ECO:0007829|PDB:2HHP"
FT HELIX 318..339
FT /evidence="ECO:0007829|PDB:2HHP"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:2HHP"
FT HELIX 354..357
FT /evidence="ECO:0007829|PDB:2HHP"
FT STRAND 359..370
FT /evidence="ECO:0007829|PDB:2HHP"
FT HELIX 372..394
FT /evidence="ECO:0007829|PDB:2HHP"
FT STRAND 399..404
FT /evidence="ECO:0007829|PDB:2HHP"
FT STRAND 409..414
FT /evidence="ECO:0007829|PDB:2HHP"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:2HHP"
FT HELIX 420..427
FT /evidence="ECO:0007829|PDB:2HHP"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:1FA0"
FT HELIX 431..434
FT /evidence="ECO:0007829|PDB:2HHP"
FT HELIX 435..439
FT /evidence="ECO:0007829|PDB:1FA0"
FT TURN 444..446
FT /evidence="ECO:0007829|PDB:2Q66"
FT HELIX 451..455
FT /evidence="ECO:0007829|PDB:2Q66"
FT STRAND 458..470
FT /evidence="ECO:0007829|PDB:2HHP"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:2O1P"
FT HELIX 482..494
FT /evidence="ECO:0007829|PDB:2HHP"
FT TURN 497..500
FT /evidence="ECO:0007829|PDB:2HHP"
FT STRAND 502..513
FT /evidence="ECO:0007829|PDB:2HHP"
FT HELIX 514..516
FT /evidence="ECO:0007829|PDB:2HHP"
FT HELIX 519..521
FT /evidence="ECO:0007829|PDB:2HHP"
SQ SEQUENCE 568 AA; 64552 MW; 759DE5210DC8D881 CRC64;
MSSQKVFGIT GPVSTVGATA AENKLNDSLI QELKKEGSFE TEQETANRVQ VLKILQELAQ
RFVYEVSKKK NMSDGMARDA GGKIFTYGSY RLGVHGPGSD IDTLVVVPKH VTREDFFTVF
DSLLRERKEL DEIAPVPDAF VPIIKIKFSG ISIDLICARL DQPQVPLSLT LSDKNLLRNL
DEKDLRALNG TRVTDEILEL VPKPNVFRIA LRAIKLWAQR RAVYANIFGF PGGVAWAMLV
ARICQLYPNA CSAVILNRFF IILSEWNWPQ PVILKPIEDG PLQVRVWNPK IYAQDRSHRM
PVITPAYPSM CATHNITEST KKVILQEFVR GVQITNDIFS NKKSWANLFE KNDFFFRYKF
YLEITAYTRG SDEQHLKWSG LVESKVRLLV MKLEVLAGIK IAHPFTKPFE SSYCCPTEDD
YEMIQDKYGS HKTETALNAL KLVTDENKEE ESIKDAPKAY LSTMYIGLDF NIENKKEKVD
IHIPCTEFVN LCRSFNEDYG DHKVFNLALR FVKGYDLPDE VFDENEKRPS KKSKRKNLDA
RHETVKRSKS DAASGDNING TTAAVDVN
