PAN2_NEUCR
ID PAN2_NEUCR Reviewed; 1310 AA.
AC P0C581; A7UWG8; Q7S6P3;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=PAN2-PAN3 deadenylation complex catalytic subunit pan2 {ECO:0000255|HAMAP-Rule:MF_03182};
DE EC=3.1.13.4 {ECO:0000255|HAMAP-Rule:MF_03182};
DE AltName: Full=PAB1P-dependent poly(A)-specific ribonuclease {ECO:0000255|HAMAP-Rule:MF_03182};
DE AltName: Full=Poly(A)-nuclease deadenylation complex subunit 2 {ECO:0000255|HAMAP-Rule:MF_03182};
DE Short=PAN deadenylation complex subunit 2 {ECO:0000255|HAMAP-Rule:MF_03182};
GN Name=par-1; Synonyms=pan2 {ECO:0000255|HAMAP-Rule:MF_03182};
GN ORFNames=NCU04792, NCU10733;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-351 AND 456-1100 IN COMPLEX
RP WITH ZINC, AND SUBUNIT.
RX PubMed=24880343; DOI=10.1038/nsmb.2837;
RA Jonas S., Christie M., Peter D., Bhandari D., Loh B., Huntzinger E.,
RA Weichenrieder O., Izaurralde E.;
RT "An asymmetric PAN3 dimer recruits a single PAN2 exonuclease to mediate
RT mRNA deadenylation and decay.";
RL Nat. Struct. Mol. Biol. 21:599-608(2014).
CC -!- FUNCTION: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation
CC complex, one of two cytoplasmic mRNA deadenylases involved in mRNA
CC turnover. PAN specifically shortens poly(A) tails of RNA and the
CC activity is stimulated by poly(A)-binding protein pabp-1. PAN
CC deadenylation is followed by rapid degradation of the shortened mRNA
CC tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by
CC two alternative mechanisms, namely exosome-mediated 3'-5'
CC exonucleolytic degradation, or deadenlyation-dependent mRNA decaping
CC and subsequent 5'-3' exonucleolytic degradation by rgb-30/xrn1. May
CC also be involved in post-transcriptional maturation of mRNA poly(A)
CC tails. {ECO:0000255|HAMAP-Rule:MF_03182}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03182};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03182};
CC Note=Binds 2 metal cations per subunit in the catalytic exonuclease
CC domain. {ECO:0000255|HAMAP-Rule:MF_03182};
CC -!- ACTIVITY REGULATION: Positively regulated by the regulatory subunit
CC par-2/pan3. {ECO:0000250, ECO:0000255|HAMAP-Rule:MF_03182}.
CC -!- SUBUNIT: Forms a heterotrimer with an asymmetric homodimer of the
CC regulatory subunit par-2/pan3 to form the poly(A)-nuclease (PAN)
CC deadenylation complex. {ECO:0000255|HAMAP-Rule:MF_03182,
CC ECO:0000269|PubMed:24880343}.
CC -!- INTERACTION:
CC P0C581; Q7SDP4: par-2; NbExp=6; IntAct=EBI-16108085, EBI-16108116;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03182}.
CC -!- DOMAIN: Contains a pseudo-UCH domain. This ubiquitin C-terminal
CC hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain
CC is predicted to be catalytically inactive because it lacks the active
CC site catalytic triad characteristic of thiol proteases, with residues
CC at the equivalent structural positions that are incompatible with
CC catalysis, and it cannot bind ubiquitin. It functions as a structural
CC scaffold for intra- and intermolecular interactions in the complex.
CC {ECO:0000255|HAMAP-Rule:MF_03182}.
CC -!- DOMAIN: The linker, or PAN3 interaction domain (PID), between the WD40
CC repeats and the pseudo-UCH domain mediates interaction with par-2/pan3.
CC {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:24880343}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. PAN2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03182}.
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DR EMBL; CM002241; EDO65208.2; -; Genomic_DNA.
DR RefSeq; XP_001728299.2; XM_001728247.2.
DR PDB; 4CZV; X-ray; 2.10 A; A/B=1-321.
DR PDB; 4CZW; X-ray; 2.60 A; A=456-1100.
DR PDB; 4CZX; X-ray; 1.85 A; A=1-321.
DR PDB; 4CZY; X-ray; 3.40 A; A/C=1-351.
DR PDBsum; 4CZV; -.
DR PDBsum; 4CZW; -.
DR PDBsum; 4CZX; -.
DR PDBsum; 4CZY; -.
DR AlphaFoldDB; P0C581; -.
DR SMR; P0C581; -.
DR DIP; DIP-61539N; -.
DR IntAct; P0C581; 1.
DR STRING; 5141.EFNCRP00000004582; -.
DR EnsemblFungi; EDO65208; EDO65208; NCU10733.
DR GeneID; 5847542; -.
DR KEGG; ncr:NCU10733; -.
DR VEuPathDB; FungiDB:NCU10733; -.
DR HOGENOM; CLU_002369_1_0_1; -.
DR InParanoid; P0C581; -.
DR Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0031251; C:PAN complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_03182; PAN2; 1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR030843; PAN2.
DR InterPro; IPR028881; PAN2_UCH_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF00929; RNase_T; 1.
DR Pfam; PF13423; UCH_1; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Exonuclease; Hydrolase; Metal-binding;
KW mRNA processing; Nuclease; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..1310
FT /note="PAN2-PAN3 deadenylation complex catalytic subunit
FT pan2"
FT /id="PRO_0000295351"
FT REPEAT 22..61
FT /note="WD 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 67..105
FT /note="WD 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 106..144
FT /note="WD 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 145..184
FT /note="WD 4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT DOMAIN 463..850
FT /note="USP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT DOMAIN 897..1070
FT /note="Exonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REGION 318..463
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182,
FT ECO:0000305|PubMed:24880343"
FT REGION 1121..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 525
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24880343,
FT ECO:0007744|PDB:4CZW"
FT BINDING 530
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24880343,
FT ECO:0007744|PDB:4CZW"
FT BINDING 535
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24880343,
FT ECO:0007744|PDB:4CZW"
FT BINDING 538
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24880343,
FT ECO:0007744|PDB:4CZW"
FT BINDING 645
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24880343,
FT ECO:0007744|PDB:4CZW"
FT BINDING 648
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24880343,
FT ECO:0007744|PDB:4CZW"
FT BINDING 700
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24880343,
FT ECO:0007744|PDB:4CZW"
FT BINDING 703
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24880343,
FT ECO:0007744|PDB:4CZW"
FT BINDING 900
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-
FT Rule:MF_03182"
FT BINDING 902
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-
FT Rule:MF_03182"
FT BINDING 1009
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-
FT Rule:MF_03182"
FT BINDING 1062
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-
FT Rule:MF_03182"
FT TURN 3..5
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:4CZX"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:4CZX"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:4CZX"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 122..137
FT /evidence="ECO:0007829|PDB:4CZX"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 153..166
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:4CZX"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 188..197
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 199..208
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:4CZV"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:4CZX"
FT TURN 228..231
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 263..271
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:4CZX"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:4CZX"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:4CZW"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:4CZW"
FT TURN 466..468
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 485..487
FT /evidence="ECO:0007829|PDB:4CZW"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 503..505
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 506..513
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 516..526
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 536..549
FT /evidence="ECO:0007829|PDB:4CZW"
FT STRAND 552..555
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 558..564
FT /evidence="ECO:0007829|PDB:4CZW"
FT TURN 571..574
FT /evidence="ECO:0007829|PDB:4CZW"
FT TURN 577..579
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 585..604
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 613..618
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 627..635
FT /evidence="ECO:0007829|PDB:4CZW"
FT STRAND 638..645
FT /evidence="ECO:0007829|PDB:4CZW"
FT TURN 646..648
FT /evidence="ECO:0007829|PDB:4CZW"
FT STRAND 651..656
FT /evidence="ECO:0007829|PDB:4CZW"
FT STRAND 659..662
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 682..690
FT /evidence="ECO:0007829|PDB:4CZW"
FT STRAND 693..700
FT /evidence="ECO:0007829|PDB:4CZW"
FT TURN 701..704
FT /evidence="ECO:0007829|PDB:4CZW"
FT STRAND 705..717
FT /evidence="ECO:0007829|PDB:4CZW"
FT STRAND 720..725
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 731..737
FT /evidence="ECO:0007829|PDB:4CZW"
FT STRAND 745..752
FT /evidence="ECO:0007829|PDB:4CZW"
FT STRAND 754..760
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 761..769
FT /evidence="ECO:0007829|PDB:4CZW"
FT STRAND 776..789
FT /evidence="ECO:0007829|PDB:4CZW"
FT TURN 790..793
FT /evidence="ECO:0007829|PDB:4CZW"
FT STRAND 794..802
FT /evidence="ECO:0007829|PDB:4CZW"
FT TURN 803..806
FT /evidence="ECO:0007829|PDB:4CZW"
FT STRAND 816..820
FT /evidence="ECO:0007829|PDB:4CZW"
FT STRAND 823..826
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 829..832
FT /evidence="ECO:0007829|PDB:4CZW"
FT TURN 837..839
FT /evidence="ECO:0007829|PDB:4CZW"
FT STRAND 840..849
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 850..852
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 859..862
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 867..870
FT /evidence="ECO:0007829|PDB:4CZW"
FT TURN 886..888
FT /evidence="ECO:0007829|PDB:4CZW"
FT STRAND 896..906
FT /evidence="ECO:0007829|PDB:4CZW"
FT STRAND 926..936
FT /evidence="ECO:0007829|PDB:4CZW"
FT TURN 940..943
FT /evidence="ECO:0007829|PDB:4CZW"
FT STRAND 945..951
FT /evidence="ECO:0007829|PDB:4CZW"
FT STRAND 957..959
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 962..965
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 969..972
FT /evidence="ECO:0007829|PDB:4CZW"
FT TURN 974..976
FT /evidence="ECO:0007829|PDB:4CZW"
FT STRAND 979..982
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 984..996
FT /evidence="ECO:0007829|PDB:4CZW"
FT STRAND 1000..1005
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 1006..1013
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 1019..1021
FT /evidence="ECO:0007829|PDB:4CZW"
FT STRAND 1022..1024
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 1025..1028
FT /evidence="ECO:0007829|PDB:4CZW"
FT TURN 1032..1034
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 1040..1047
FT /evidence="ECO:0007829|PDB:4CZW"
FT STRAND 1054..1056
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 1059..1078
FT /evidence="ECO:0007829|PDB:4CZW"
FT HELIX 1082..1089
FT /evidence="ECO:0007829|PDB:4CZW"
SQ SEQUENCE 1310 AA; 143936 MW; BD386DA31066DC79 CRC64;
MDSRDWTQLG CVAYPSPIHP DYHAGPASTI AFDNQDELLW IGTQKGFAGS FIGRELKRFT
AFRIHPETDG PLRQFLFVDK GVIFLGSRSV YMAARSGVPI WSIRHESMQD LRAMSFTSKG
TSEILVAGWQ NKMLVIDVNK GEVVKELPTQ DQYSFLKMSR YICAATNKGT VNILDPITFT
IKKQWQAHGA FINDLDTSND FIVTCGGSHR QTHNTPAILD PYVKVFDLKN MSAMNPVPFA
PLAAHVRMHP RMLTTAIVVN QAGQIHVTDL LNPSNSQVCY TQPQGVVLHF DVSRTGEGKA
LADNKHNTYV WGSPNKIQFT EIGIPPRLPD PPQPSLLPPD PDMLEELPLS RIGLPYYREQ
LFSALPPDII SDVGAPPQQI DPNILSTLTK TDWGYIGPNK TGLQRNQYMD TRSTMKTSNT
IRAPKFLSEK ARESQTGSED NTLATNETAM MTPNNDHWSL RPEAPPEYRI CEIKYSKFGV
DDFDFGFFNN TPYPGLENNI TNSYANSLLQ VMHYTPLLRN MALQHAATAC LADPCLLCEL
GYVFDMLQKG EGPSCHATNM LRALNHTSNA SVSGVLEDIA KDKNPSTLVK NLTMFLFDKI
SQDYKGTPPI STELERTLFK LNQPPNPLDL VKRLLETDAR YQIKCMHCQH VSPRTATTFV
NKLCYPAAKP NIRGMKAQRI TFSQVLKAGL ENEAVNKGYC TKCQRYQNLD QRKIIFNIPA
VLALCTEITT AEHRKLWSTP GWLPEEIGII VDQGHVYCYE GDDLKLHLNR GIHNITVYSL
VGTVVNVETK SPQKSHLVAT VNVGRAEPES KDQDRWHLFN DFSVRGISKV EALTFNAAWK
MPVVVMFQVK AANHRFNMDW KTRLDTSVLF RDNNPHALKT YELLDRETEI PGPDTVIAID
TEFIRLKERE IHIDEDGKSK TIRPISHAIA RASVVRGQGS REGVAFIDDY IHIKETIVDY
LTEWSGITPT DLDPINSQRN LVSPKTAYKK LWVLVNLGCK FLGHGLSQDF RVINIQVPRN
QVIDTSIIFM KPPSQRKISL AFLAWYLLKE DIQQNTHDSI EDAQTALKLY RKYEEFMANG
SFHDVLEALY KKGKTLNFKP PRISTGAAKD AGFGAVHRVG TPPVPAPGTT EGSFEISNSS
TATTGGSALS ATGGMGSASA SSSMPSTPVR KPIGLGGPFT VAGVVKPSPA TSLDNFGAGA
VGTGITTAAA TMGGGYGGYG TDGAYWGGPN DMAPTSMIGG SAFIPAKFPP GPPETRGFIP
YRPQVLLAER EAAAAAAAAA AAAAANNDVG GRGGVACGNG GAGGEQGKQE
