PCHE_PSEAE
ID PCHE_PSEAE Reviewed; 1438 AA.
AC G3XCV2; O85739; Q7DC78;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Pyochelin synthase PchE {ECO:0000305};
DE EC=6.2.1.69 {ECO:0000305|PubMed:9846750};
DE AltName: Full=L-cysteine--[L-cysteinyl-carrier protein] ligase {ECO:0000305};
DE AltName: Full=Nonribosomal peptide synthase PchE {ECO:0000305};
GN Name=pchE {ECO:0000303|PubMed:9846750};
GN OrderedLocusNames=PA4226 {ECO:0000312|EMBL:AAG07614.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9846750; DOI=10.1099/00221287-144-11-3135;
RA Reimmann C., Serino L., Beyeler M., Haas D.;
RT "Dihydroaeruginoic acid synthetase and pyochelin synthetase, products of
RT the pchEF genes, are induced by extracellular pyochelin in Pseudomonas
RT aeruginosa.";
RL Microbiology 144:3135-3148(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=11208777; DOI=10.1128/jb.183.3.813-820.2001;
RA Reimmann C., Patel H.M., Serino L., Barone M., Walsh C.T., Haas D.;
RT "Essential PchG-dependent reduction in pyochelin biosynthesis of
RT Pseudomonas aeruginosa.";
RL J. Bacteriol. 183:813-820(2001).
CC -!- FUNCTION: Involved in the biosynthesis of the siderophore pyochelin
CC (PubMed:9846750, PubMed:11208777). Accepts salicylate activated by PchD
CC at the first peptidyl carrier domain (ArCP), and activates and fixes
CC one molecule of cysteine at the second peptidyl carrier domain (PCP1)
CC via a thioester linkage to the phosphopanthetheine moiety (By
CC similarity). Then catalyzes the condensation reaction between the
CC salicylate bound to the first site and the cysteine bound to the second
CC site, and the cyclization of the cysteine to form the salicyl-
CC thiazolinyl-S-PCP1 intermediate at the second site (By similarity).
CC When this intermediate is released by the action of a thioesterase, it
CC produces the antifungal antibiotic dihydroaeruginoic acid (Dha or
CC hydroxyphenyl-thiazolinyl-carboxylate) (PubMed:11208777).
CC {ECO:0000250|UniProtKB:A0A0H2ZGB9, ECO:0000269|PubMed:11208777,
CC ECO:0000269|PubMed:9846750}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + holo-[peptidyl-carrier protein] + L-cysteine = AMP +
CC diphosphate + L-cysteinyl-[peptidyl-carrier protein];
CC Xref=Rhea:RHEA:61680, Rhea:RHEA-COMP:11480, Rhea:RHEA-COMP:15906,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:144926, ChEBI:CHEBI:456215;
CC EC=6.2.1.69; Evidence={ECO:0000305|PubMed:9846750};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61681;
CC Evidence={ECO:0000305|PubMed:9846750};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000305};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:11208777,
CC ECO:0000269|PubMed:9846750}.
CC -!- PATHWAY: Antifungal biosynthesis. {ECO:0000269|PubMed:11208777,
CC ECO:0000269|PubMed:9846750}.
CC -!- INDUCTION: Expression of the pchEF operon is strictly dependent on the
CC PchR regulator and is induced by extracellular pyochelin, the end
CC product of the pathway. Repressed by Fur and iron.
CC {ECO:0000269|PubMed:9846750}.
CC -!- DOMAIN: Modular protein that contains an aryl carrier protein (ArCP)
CC domain which bears a phosphopantetheinyl arm to attach the activated
CC salicylic acid, a condensation/cyclization domain involved in the
CC cyclization of the cysteine, an adenylation domain which activates the
CC cysteine residue into an aminoacyl-AMP ester and a peptidyl carrier
CC protein (PCP1) domain which bears a phosphopantetheinyl arm to attach
CC the activated cysteine. {ECO:0000250|UniProtKB:A0A0H2ZGB9}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene completely abolishes the
CC formation of both Dha and pyochelin and results in salicylate
CC accumulation. {ECO:0000269|PubMed:9846750}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {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; AF074705; AAC83656.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07614.1; -; Genomic_DNA.
DR PIR; T17402; T17402.
DR RefSeq; NP_252916.1; NC_002516.2.
DR RefSeq; WP_003148110.1; NZ_QZGE01000028.1.
DR PDB; 7EMY; EM; 2.97 A; A/B=1-1438.
DR PDB; 7EN1; EM; 3.47 A; A/B=1-1438.
DR PDB; 7EN2; EM; 3.78 A; A/B=1-1438.
DR PDBsum; 7EMY; -.
DR PDBsum; 7EN1; -.
DR PDBsum; 7EN2; -.
DR AlphaFoldDB; G3XCV2; -.
DR SMR; G3XCV2; -.
DR STRING; 287.DR97_3685; -.
DR PaxDb; G3XCV2; -.
DR PRIDE; G3XCV2; -.
DR EnsemblBacteria; AAG07614; AAG07614; PA4226.
DR GeneID; 880048; -.
DR KEGG; pae:PA4226; -.
DR PATRIC; fig|208964.12.peg.4427; -.
DR PseudoCAP; PA4226; -.
DR HOGENOM; CLU_000022_40_2_6; -.
DR InParanoid; G3XCV2; -.
DR OMA; CAPESIR; -.
DR OrthoDB; 572620at2; -.
DR PhylomeDB; G3XCV2; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Ligase; Phosphopantetheine;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1438
FT /note="Pyochelin synthase PchE"
FT /id="PRO_0000454826"
FT DOMAIN 6..85
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1350..1425
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 136..442
FT /note="Condensation/cyclization"
FT /evidence="ECO:0000305"
FT REGION 563..950
FT /note="Adenylation"
FT /evidence="ECO:0000305"
FT MOD_RES 46
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1385
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT HELIX 8..23
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 27..32
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:7EN1"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 46..59
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 74..87
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 109..117
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 142..155
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 189..203
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 215..223
FT /evidence="ECO:0007829|PDB:7EMY"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 227..235
FT /evidence="ECO:0007829|PDB:7EMY"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 241..256
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 269..294
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 318..325
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 327..339
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 344..359
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 360..372
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 379..383
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 389..397
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 404..421
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 426..435
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 458..463
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 469..472
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 478..484
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 489..497
FT /evidence="ECO:0007829|PDB:7EMY"
FT TURN 498..500
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 505..522
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 527..530
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 535..545
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 558..566
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 570..574
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 579..581
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 582..598
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 606..609
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 615..626
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 630..633
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 640..650
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 653..659
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 664..666
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 668..670
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 671..675
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 690..697
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 701..703
FT /evidence="ECO:0007829|PDB:7EN1"
FT STRAND 705..710
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 711..725
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 732..734
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 743..749
FT /evidence="ECO:0007829|PDB:7EMY"
FT TURN 750..755
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 757..759
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 763..765
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 769..779
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 783..786
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 788..795
FT /evidence="ECO:0007829|PDB:7EMY"
FT TURN 799..801
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 809..815
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 821..825
FT /evidence="ECO:0007829|PDB:7EMY"
FT TURN 826..828
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 835..839
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 842..844
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 849..852
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 872..877
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 881..883
FT /evidence="ECO:0007829|PDB:7EN1"
FT STRAND 890..896
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 901..903
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 907..913
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 914..917
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 920..922
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 927..931
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 937..949
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 952..955
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 956..964
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 969..976
FT /evidence="ECO:0007829|PDB:7EMY"
FT TURN 979..982
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 984..990
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 1009..1027
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 1030..1032
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 1035..1047
FT /evidence="ECO:0007829|PDB:7EMY"
FT TURN 1048..1050
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 1051..1053
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 1058..1063
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 1067..1082
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 1088..1092
FT /evidence="ECO:0007829|PDB:7EMY"
FT TURN 1094..1096
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 1098..1102
FT /evidence="ECO:0007829|PDB:7EMY"
FT TURN 1103..1106
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 1108..1116
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 1121..1124
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 1128..1133
FT /evidence="ECO:0007829|PDB:7EMY"
FT TURN 1136..1138
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 1139..1148
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 1153..1157
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 1162..1171
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 1176..1178
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 1182..1184
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 1188..1190
FT /evidence="ECO:0007829|PDB:7EMY"
FT TURN 1191..1193
FT /evidence="ECO:0007829|PDB:7EN1"
FT STRAND 1194..1201
FT /evidence="ECO:0007829|PDB:7EMY"
FT TURN 1203..1205
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 1209..1219
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 1220..1233
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 1236..1245
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 1249..1251
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 1255..1264
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 1268..1271
FT /evidence="ECO:0007829|PDB:7EMY"
FT TURN 1275..1277
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 1278..1284
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 1292..1302
FT /evidence="ECO:0007829|PDB:7EMY"
FT TURN 1305..1307
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 1310..1314
FT /evidence="ECO:0007829|PDB:7EMY"
FT STRAND 1324..1326
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 1328..1339
FT /evidence="ECO:0007829|PDB:7EMY"
FT HELIX 1354..1367
FT /evidence="ECO:0007829|PDB:7EN1"
FT HELIX 1378..1381
FT /evidence="ECO:0007829|PDB:7EN1"
FT HELIX 1385..1398
FT /evidence="ECO:0007829|PDB:7EN1"
FT HELIX 1405..1410
FT /evidence="ECO:0007829|PDB:7EN1"
FT HELIX 1414..1422
FT /evidence="ECO:0007829|PDB:7EN1"
SQ SEQUENCE 1438 AA; 156422 MW; 22194DF7BC07E234 CRC64;
MDLPPDSRTA LRDWLTEQLA DLLGEPLADV RALADDDDLL GCGLDSIRLM YLQERLRARG
STLDFAQLAQ RPCLGAWLDL LACADRLSAP ATVALPTAQD RDQPFELSSV QQAYWLGRGA
GEVLGNVSCH AFLEFRTRDV DPQRLAAAAE CVRQRHPMLR ARFLDGRQQI LPTPPLSCFD
LQDWRTLQVD EAERDWQALR DWRAHECLAV ERGQVFLLGL VRMPGGEDRL WLSLDLLAAD
VESLRLLLAE LGVAYLAPER LAEPPALHFA DYLAHRAAQR AEAAARARDY WLERLPRLPD
APALPLACAP ESIRQPRTRR LAFQLSAGES RRLERLAAQH GVTLSSVFGC AFALVLARWS
ESAEFLLNVP LFDRHADDPR IGEVIADFTT LLLLECRMQA GVSFAEAVKS FQRNLHGAID
HAAFPALEVL REARRQGQPR SAPVVFASNL GEEGFVPAAF RDAFGDLHDM LSQTPQVWLD
HQLYRVGDGI LLAWDSVVGL FPEGLPETMF EAYVGLLQRL CDSAWGQPAD LPLPWAQQAR
RALLNGQPAC ATARTLHRDF FLRAAEAPDA DALLYRDQRV TRGELAERAL RIAGGLREAG
VRPGDAVEVS LPRGPQQVAA VFGVLAAGAC YVPLDIDQPP ARRRLIEEAA GVCLAITEED
DPQALPPRLD VQRLLRGPAL AAPVPLAPQA SAYVIYTSGS TGVPKGVEVS HAAAINTIDA
LLDLLRVNAS DRLLAVSALD FDLSVFDLFG GLGAGASLVL PAQEQARDAA AWAEAIQRHA
VSLWNSAPAL LEMALSLPAS QADYRSLRAV LLSGDWVALD LPGRLRPRCA EGCRLHVLGG
ATEAGIWSNL QSVDTVPPHW RSIPYGRPLP GQAYRVVDTH GRDVPDLVVG ELWIGGASLA
RGYRNDPELS ARRFVHDAQG RWYRTGDRGR YWGDGTLEFL GRVDQQVKVR GQRIELGEVE
AALCAQAGVE SACAAVLGGG VASLGAVLVP RLAPRAEGSM DLPAAQPFAG LAEAEAVLTR
EILGALLEAP LELDDGLRRR WLDWLADSAA SALPSLDEAL RRLGWQAAGL TAMGNALRGL
LAGEQAPAAL LLDPWLAPQA VAARLPDGRE ALARLLEALP TPAAGERLRV AVLDTRAGLW
LDQGMASLLR PGLELTLFER SRVLLDAAAT RLPERIVVQA LDDGLLPAEH LGRYDRVISF
AALHAYEASR EGLALAAALL RPQGRLLLVD LLCESPLALL GAALLDDRPL RLAELPSLLA
DLAAAGLAPR CLWRSERIAL VEALAPGLGL DAAALQAGLE QRLPQAMRPE RLWCLPSLPL
NGNGKVDRRR LAESMTRALG ECRHEPSAEE PLEAHEQALA ECWEAVLKRP VRRREASFFS
LGGDSLLATR LLAGIRERFG VRLGMADFYR QPTLAGLARH LQVQTVEIEE TQLEEGVL
