ID   TPA1_YEAST              Reviewed;         644 AA.
AC   P40032; D3DLV1;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   02-SEP-2026, entry version 178.
DE   RecName: Full=Prolyl 3,4-dihydroxylase TPA1 {ECO:0000303|PubMed:16809762};
DE            EC=1.14.11.- {ECO:0000269|PubMed:24550462};
DE   AltName: Full=Termination and polyadenylation protein 1 {ECO:0000303|PubMed:16809762};
DE   AltName: Full=uS12 prolyl 3,4-dihydroxylase {ECO:0000303|PubMed:25728928};
GN   Name=TPA1 {ECO:0000303|PubMed:16809762};
GN   OrderedLocusNames=YER049W {ECO:0000312|SGD:S000000851};
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169868; DOI=10.1038/387s078;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA   Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA   Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA   Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(1997).
RN   [2]
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   [3]
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   [4]
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   [5]
RP   FUNCTION, AND INTERACTION WITH PAB1; SUP1 AND SUP35.
RX   PubMed=16809762; DOI=10.1128/mcb.02448-05;
RA   Keeling K.M., Salas-Marco J., Osherovich L.Z., Bedwell D.M.;
RT   "Tpa1p is part of an mRNP complex that influences translation termination,
RT   mRNA deadenylation, and mRNA turnover in Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 26:5237-5248(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-607, 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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH FRK1.
RX   PubMed=20489023; DOI=10.1126/science.1176495;
RA   Breitkreutz A., Choi H., Sharom J.R., Boucher L., Neduva V., Larsen B.,
RA   Lin Z.Y., Breitkreutz B.J., Stark C., Liu G., Ahn J., Dewar-Darch D.,
RA   Reguly T., Tang X., Almeida R., Qin Z.S., Pawson T., Gingras A.C.,
RA   Nesvizhskii A.I., Tyers M.;
RT   "A global protein kinase and phosphatase interaction network in yeast.";
RL   Science 328:1043-1046(2010).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 159-ASP--HIS-161.
RX   PubMed=24550462; DOI=10.1073/pnas.1311750111;
RA   Loenarz C., Sekirnik R., Thalhammer A., Ge W., Spivakovsky E.,
RA   Mackeen M.M., McDonough M.A., Cockman M.E., Kessler B.M., Ratcliffe P.J.,
RA   Wolf A., Schofield C.J.;
RT   "Hydroxylation of the eukaryotic ribosomal decoding center affects
RT   translational accuracy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:4019-4024(2014).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-644, FUNCTION, DISRUPTION
RP   PHENOTYPE, SUBUNIT, MUTAGENESIS OF 159-ASP--HIS-161, AND INTERACTION WITH
RP   ETT1.
RX   PubMed=20630870; DOI=10.1074/jbc.m110.106864;
RA   Henri J., Rispal D., Bayart E., van Tilbeurgh H., Seraphin B., Graille M.;
RT   "Structural and functional insights into Saccharomyces cerevisiae Tpa1, a
RT   putative prolylhydroxylase influencing translation termination and
RT   transcription.";
RL   J. Biol. Chem. 285:30767-30778(2010).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 21-644 IN COMPLEX WITH IRON AND
RP   2-OXOGLUTARATE, AND SUBUNIT.
RX   PubMed=20040577; DOI=10.1093/nar/gkp1151;
RA   Kim H.S., Kim H.L., Kim K.H., Kim D.J., Lee S.J., Yoon J.Y., Yoon H.J.,
RA   Lee H.Y., Park S.B., Kim S.J., Lee J.Y., Suh S.W.;
RT   "Crystal structure of Tpa1 from Saccharomyces cerevisiae, a component of
RT   the messenger ribonucleoprotein complex.";
RL   Nucleic Acids Res. 38:2099-2110(2010).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 21-644 IN COMPLEX WITH
RP   INHIBITORS, AND SUBUNIT.
RX   PubMed=25728928; DOI=10.1016/j.str.2015.01.014;
RA   Horita S., Scotti J.S., Thinnes C., Mottaghi-Taromsari Y.S., Thalhammer A.,
RA   Ge W., Aik W., Loenarz C., Schofield C.J., McDonough M.A.;
RT   "Structure of the ribosomal oxygenase OGFOD1 provides insights into the
RT   regio- and stereoselectivity of prolyl hydroxylases.";
RL   Structure 23:639-652(2015).
CC   -!- FUNCTION: Prolyl 3,4-dihydroxylase that catalyzes 3,4-dihydroxylation
CC       of 'Pro-64' of small ribosomal subunit uS12 (RPS23A and RPS23B),
CC       thereby regulating protein translation termination efficiency. Part of
CC       a messenger ribonucleoprotein (mRNP) complex at the 3'-UTR of mRNAs. It
CC       associates specifically with components of the translation termination
CC       complex and is involved in both translation termination and in
CC       regulation of normal mRNA decay through translation termination-coupled
CC       poly(A) shortening. {ECO:0000269|PubMed:16809762,
CC       ECO:0000269|PubMed:20630870, ECO:0000269|PubMed:24550462}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[ribosomal protein uS12]-L-proline + 2-oxoglutarate + O2 =
CC         [ribosomal protein uS12]-(3S)-3-hydroxy-L-proline + succinate + CO2;
CC         Xref=Rhea:RHEA:54156, Rhea:RHEA-COMP:13816, Rhea:RHEA-COMP:13818,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:50342, ChEBI:CHEBI:85428;
CC         Evidence={ECO:0000269|PubMed:24550462, ECO:0000305|PubMed:25728928};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[ribosomal protein uS12]-(3S)-3-hydroxy-L-proline + 2-
CC         oxoglutarate + O2 = [ribosomal protein uS12]-(3S)-3,4-dihydroxy-L-
CC         proline + succinate + CO2; Xref=Rhea:RHEA:54160, Rhea:RHEA-
CC         COMP:13817, Rhea:RHEA-COMP:13818, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:85428, ChEBI:CHEBI:138052;
CC         Evidence={ECO:0000269|PubMed:24550462, ECO:0000305|PubMed:25728928};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000269|PubMed:20040577};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:20040577};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000305};
CC   -!- SUBUNIT: Monomer and homodimer (PubMed:20040577, PubMed:20630870).
CC       Interacts with FRK1, eRF1 (SUP1), eRF3 (SUP35) and polyadenylate-
CC       binding protein PAB1. Interacts with ETT1 (PubMed:16809762,
CC       PubMed:20489023). {ECO:0000269|PubMed:16809762,
CC       ECO:0000269|PubMed:20040577, ECO:0000269|PubMed:20489023,
CC       ECO:0000269|PubMed:20630870}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- DISRUPTION PHENOTYPE: Decrease of translation termination efficacy and
CC       an increase in mRNAs half-lives and longer mRNA poly(A) tails.
CC       {ECO:0000269|PubMed:20630870}.
CC   -!- MISCELLANEOUS: Present with 8910 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the TPA1 family. {ECO:0000305}.
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DR   EMBL; U18796; AAB64584.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07705.1; -; Genomic_DNA.
DR   PIR; S50552; S50552.
DR   RefSeq; NP_010969.1; NM_001178940.1.
DR   PDB; 3KT1; X-ray; 2.50 A; A=21-644.
DR   PDB; 3KT4; X-ray; 2.73 A; A=21-644.
DR   PDB; 3KT7; X-ray; 1.77 A; A=21-644.
DR   PDB; 3MGU; X-ray; 2.80 A; A=1-644.
DR   PDB; 4NHK; X-ray; 1.90 A; A=21-644.
DR   PDB; 4NHL; X-ray; 2.84 A; A=21-644.
DR   PDB; 4NHM; X-ray; 1.90 A; A=21-644.
DR   AlphaFoldDB; P40032; -.
DR   SMR; P40032; -.
DR   BioGRID; 36788; 117.
DR   DIP; DIP-2878N; -.
DR   FunCoup; P40032; 491.
DR   IntAct; P40032; 7.
DR   MINT; P40032; -.
DR   STRING; 4932.YER049W; -.
DR   iPTMnet; P40032; -.
DR   PaxDb; 4932-YER049W; -.
DR   PeptideAtlas; P40032; -.
DR   EnsemblFungi; YER049W_mRNA; YER049W; YER049W.
DR   GeneID; 856775; -.
DR   KEGG; sce:YER049W; -.
DR   AGR; SGD:S000000851; -.
DR   SGD; S000000851; TPA1.
DR   VEuPathDB; FungiDB:YER049W; -.
DR   eggNOG; KOG3844; Eukaryota.
DR   HOGENOM; CLU_017005_0_0_1; -.
DR   InParanoid; P40032; -.
DR   OMA; GWYHIPQ; -.
DR   OrthoDB; 430522at2759; -.
DR   BioCyc; YEAST:G3O-30228-MONOMER; -.
DR   Reactome; R-SCE-9629569; Protein hydroxylation.
DR   BioGRID-ORCS; 856775; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P40032; -.
DR   PRO; PR:P40032; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P40032; protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0008198; F:ferrous iron binding; IMP:SGD.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR   GO; GO:0031543; F:peptidyl-proline dioxygenase activity; IDA:UniProtKB.
DR   GO; GO:0008143; F:poly(A) binding; IDA:SGD.
DR   GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IMP:SGD.
DR   GO; GO:0018188; P:peptidyl-proline di-hydroxylation; IDA:UniProtKB.
DR   GO; GO:0006450; P:regulation of translational fidelity; IMP:SGD.
DR   GO; GO:0006449; P:regulation of translational termination; IMP:UniProtKB.
DR   GO; GO:0006415; P:translational termination; IMP:SGD.
DR   FunFam; 2.60.120.620:FF:000014; Prolyl 3,4-dihydroxylase TPA1; 1.
DR   FunFam; 3.60.130.20:FF:000002; Prolyl 3,4-dihydroxylase TPA1; 1.
DR   Gene3D; 3.60.130.20; Oxoglutarate/iron-dependent oxygenase, C-terminal degradation domain; 1.
DR   Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase_dom.
DR   InterPro; IPR019601; Oxoglutarate/Fe-dep_Oase_C.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR043044; TPA1/Ofd1_C.
DR   InterPro; IPR039558; TPA1/OFD1_N.
DR   InterPro; IPR051842; uS12_prolyl_hydroxylase.
DR   PANTHER; PTHR12117; HISTONE ACETYLTRANSFERASE COMPLEX; 1.
DR   PANTHER; PTHR12117:SF0; PROLYL 3-HYDROXYLASE OGFOD1; 1.
DR   Pfam; PF13661; 2OG-FeII_Oxy_4; 1.
DR   Pfam; PF10637; Ofd1_CTDD; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
DR   PDBsum; 3KT1; -.
DR   PDBsum; 3KT4; -.
DR   PDBsum; 3KT7; -.
DR   PDBsum; 3MGU; -.
DR   PDBsum; 4NHK; -.
DR   PDBsum; 4NHL; -.
DR   PDBsum; 4NHM; -.
PE   1: Evidence at protein level;
KW   3D-structure; Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Vitamin C.
FT   CHAIN           1..644
FT                   /note="Prolyl 3,4-dihydroxylase TPA1"
FT                   /id="PRO_0000206670"
FT   DOMAIN          141..247
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         159
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805,
FT                   ECO:0000269|PubMed:20040577, ECO:0000269|PubMed:25728928"
FT   BINDING         161
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805,
FT                   ECO:0000269|PubMed:20040577, ECO:0000269|PubMed:25728928"
FT   BINDING         173
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000269|PubMed:20040577"
FT   BINDING         227
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805,
FT                   ECO:0000269|PubMed:20040577, ECO:0000269|PubMed:25728928"
FT   BINDING         238
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805,
FT                   ECO:0000269|PubMed:20040577"
FT   MOD_RES         607
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MUTAGEN         159..161
FT                   /note="HDD->ADN,ADA: Loss of function."
FT                   /evidence="ECO:0000269|PubMed:20630870,
FT                   ECO:0000269|PubMed:24550462"
FT   MUTAGEN         159
FT                   /note="H->A: Loss of function."
FT   HELIX           27..29
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   HELIX           32..35
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   HELIX           37..48
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   STRAND          56..60
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   HELIX           64..77
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   STRAND          81..84
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   STRAND          86..92
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   HELIX           111..120
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   HELIX           123..133
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   STRAND          139..142
FT                   /evidence="ECO:0007829|PDB:3MGU"
FT   STRAND          145..150
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   STRAND          155..159
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   STRAND          166..173
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   HELIX           180..182
FT                   /evidence="ECO:0007829|PDB:4NHK"
FT   HELIX           183..185
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   STRAND          189..191
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   STRAND          194..196
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   STRAND          205..208
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   STRAND          214..219
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   TURN            222..224
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   STRAND          227..229
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   STRAND          238..246
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   HELIX           247..249
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   HELIX           252..254
FT                   /evidence="ECO:0007829|PDB:4NHK"
FT   HELIX           259..268
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   HELIX           269..277
FT                   /evidence="ECO:0007829|PDB:3KT4"
FT   HELIX           278..282
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   HELIX           294..304
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   HELIX           332..338
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   TURN            339..341
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   HELIX           344..346
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   HELIX           349..362
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   STRAND          363..369
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   HELIX           373..389
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   HELIX           391..393
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   HELIX           396..398
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   TURN            409..411
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   STRAND          415..417
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   STRAND          419..421
FT                   /evidence="ECO:0007829|PDB:3KT1"
FT   HELIX           428..436
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   HELIX           439..441
FT                   /evidence="ECO:0007829|PDB:3MGU"
FT   HELIX           443..457
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   TURN            461..463
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   HELIX           466..479
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   HELIX           481..491
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   STRAND          492..495
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   STRAND          497..505
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   TURN            507..509
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   HELIX           521..523
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   STRAND          527..540
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   TURN            546..550
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   STRAND          555..558
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   STRAND          588..592
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   STRAND          596..604
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   STRAND          609..612
FT                   /evidence="ECO:0007829|PDB:3KT7"
FT   HELIX           613..616
FT                   /evidence="ECO:0007829|PDB:4NHL"
FT   STRAND          623..634
FT                   /evidence="ECO:0007829|PDB:3KT7"
SQ   SEQUENCE   644 AA;  74041 MW;  1273410E75479A46 CRC64;
     MKRKTAEVKG EKERNSKQIS LEEDKIKGMF NPKIWDKTFQ DGLKKEIEDS QPYNWGTIHE
     LVNDDLLRAV RKEIETEIHF TKKETDIYRV NQSGDLANLS GLDWDDLSRL PNLFKLRQIL
     YSKQYRDFFG YVTKAGKLSG SKTDMSINTY TKGCHLLTHD DVIGSRRISF ILYLPDPDRK
     WKSHYGGGLR LFPSILPNVP HSDPSAKLVP QFNQIAFFKV LPGFSFHDVE EVKVDKHRLS
     IQGWYHIPQV GEEGYIPGEE EAWVRNNTST LAQIESNVLE DFEFPKDERN ILSFHEVKHF
     EKMLKGDAGA KTDNTPKESM TSVISDSVKL SEAEFTYLSQ YISPEHLSSK GIEKLQKQFV
     ENSSLQIESF LNDDKSELLK KVIKQKELEQ ECPYHSKDVK APWKTAIPPH KARYLYIDGK
     EYRNFQTEAD ILEALNNNDL PNFQFTKDAI KIISDASGNS RENNFDAELA LIDLAVFHKS
     TIFKKYLALL TSLCPVSEQI LIRRFRPGMD FTLATKCRFN ELLKSNPDII DAVLEGTLCL
     TPSAGWESGE LGGYELYMMD DDEDNKQYLK EDVEDASVYR ADDSGDSVLI NDPPAWNTFN
     LVLRDESVLE FVKYVSWSAK SSRWDVKMKW DVKSCDEDGQ EDEA
//