Prideapplication/xmlftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067990/Peptides.xlsxftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067990/Sample_labeling.xlsxftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067990/protein_groups.xlsxftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067990/QE3_211109_OPL2014_AM_PecAmut_M_mar_F.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067990/QE3_211109_OPL2014_AM_PecAmut_M_mar_B.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067990/QE3_211109_OPL2014_AM_PecAmut_M_mar_D.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067990/QE3_211109_OPL2014_AM_PecAmut_M_mar_I.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067990/QE3_211109_OPL2014_AM_PecAmut_M_mar_G.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067990/QE3_211109_OPL2014_AM_PecAmut_M_mar_E.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067990/QE3_211109_OPL2014_AM_PecAmut_M_mar_A.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067990/QE3_211109_OPL2014_AM_PecAmut_M_mar_H.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067990/QE3_211109_OPL2014_AM_PecAmut_M_mar_C.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067990/uniprotkb_Mycobacterium_marinum_completeproteome_2013_03_ATCC_BAA_535M_5418entries.FASTAftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067990/semi-tryptic_search.zipprimary200OKc.jimenez@amsterdamumc.nlThang PhamData-dependent acquisitionMass SpectrometryTuberculosisAspartic acid proteaseMycobacterium marinumSubstrate specificityhttps://www.ebi.ac.uk/pride/archive/projects/PXD067990M. marinum wildtype, ∆pecA, and pecA/B/C triple frameshift mutant containing pTdTomato-L5 were cultivated in 7H9 medium containing 0.2% glycerol, ADC and 0.05% Tween-80 at 30 °C. One day prior to extraction of surface proteins, bacteria were washed two times in 7H9 containing 0.2% glycerol and 0.2% dextrose and grown in 100 ml starting from OD600 of 0.35. After growth overnight, the culture was washed with PBS and incubated with 0.5% Genapol X-080 supplemented with complete protease inhibitor cocktail (Roche) head-over-head for 30 min at room temperature. Extracted surface proteins were separated from cells by centrifugation and supernatants were filtered through 0.2 μm filters. Surface proteins were precipitated overnight on ice with tRNA and 100% TCA in acetone, washed two times in acetone and air-dried. Next, protein was solubilized in urea buffer (8M urea in 100 mM ammonium bicarbonate (ABC)). Samples were centrifuged and protein concentration of soluble protein (supernatant) was measured using Detergent Compatible Protein Assay (BioRad). Per sample, 50 μg of protein was reduced for 1h at room temperature by addition of TCEP (Tris(2-carboxyethyl) phosphine) in a final concentration of 5 mM and alkylated with iodoacetamide in the dark at a final concentration of 5.5 mM. Subsequently, samples were cleared of Genapol X-080 in samples using Filter Aided Sample Preparation (FASP). Briefly, samples were added Microfuge Amicon 10 kDa cut-off spin filters (Milipore) and centrifuged at 14000 xg for 15 min (15°C). Next, 6 washing steps were performed by adding 400 μl urea buffer to the filter and centrifuging at 14000xg for 15 min, prior to 3 washes with 50 mM ABC. Finally, 400 μl of 50 mM ABC was added to the filter in addition to 1 μg of modified sequencing-grade trypsin (Promega, V5111, 1:50 trypsin to protein ratio) and incubated for 18h in a humidified chamber at 37°C. Peptides were captured following centrifugation at 14000xg for 15 min including the flowthrough after addition of 250 µl of 100mM NaCl to the filter and centrifugation at 14000xg for 15 min. Peptides were concentrated in a vacuum-concentrator and desalted with OASIS HLB Cartridges. Growing cultures and extracting protein was carried out in three biological replicates. LC-MS/MS Peptides were separated by an Ultimate 3000 nanoLC‐MS/MS system (Dionex LC‐Packings) equipped with a 45 cm × 75 μm ID fused silica column custom packed with 1.9 μm 120 Å ReproSil Pur C18 aqua (Dr Maisch GMBH). After injection, peptides were trapped at 6 μl/min on a 10 mm ×100 μm ID trap column packed with 5 μm 120 Å ReproSil Pur C18 aqua in 0.05% formic acid. Peptides were separated at 300 nl/min in a 10–40% gradient (buffer A: 0.5% acetic acid (Fisher Scientific), buffer B: 80% ACN, 0.5% acetic acid) in 60 min (100‐min inject‐to‐inject). Eluting peptides were ionized at a potential of +2 kVa into a Q Exactive mass spectrometer (Thermo Fisher). Intact masses were measured at resolution 70,000 (at m/z 200) in the orbitrap using an AGC target value of 3E6 charges. The top 10 peptide signals (charge‐states 2+ and higher) were submitted to MS/MS in the HCD (higher‐energy collision) cell (1.6 amu isolation width, 25% normalized collision energy). MS/MS spectra were acquired at resolution 17,500 (at m/z 200) in the orbitrap using an AGC target value of 1E6 charges, a maxIT of 60 ms, and an underfill ratio of 0.1%. Dynamic exclusion was applied with a repeat count of 1 and an exclusion time of 30 s.PrideNot availableMS/MS spectra were searched against a Mycobacterium marinum reference proteome FASTA file (5418 entries) using MaxQuant 1.6.10.43 (Cox J & Mann M, 2008). Enzyme specificity was set to semi-specific (free N-terminus). Cysteine carboxyamidomethylation (Cys, +57.021464 Da) was treated as fixed modification and methionine oxidation (Met, +15.994915 Da) and N‐terminal acetylation (N‐terminal, +42.010565 Da) as variable modifications. Peptide precursor ions were searched with a maximum mass deviation of 4.5 ppm and fragment ions with a maximum mass deviation of 20 ppm. Peptide and protein identifications were filtered at an FDR of 1% using the decoy database strategy. The minimal peptide length was seven amino acids. Peptides preceding or ending with R or K were classified as semi-tryptic peptides. Cleavage windows of semi-tryptic peptides were created using Excel and the amino acid probabilities at each position were analysed using the probability logo generator (pLogo) using the complete FASTA coding sequences (CDS) of M. marinum (NCBI) as background.ProteomicsConnie JimenezConnie Jimenez, OncoProteomics Laboratory, Dept of Medical Oncology, Amsterdam University Medical Centers, Amsterdam, The NetherlandsPARTIALMycobacterium Marinum Atcc Baa-53542595108 Meijers AS, Gallant JL, Speer A, Maaskant J, Hietamäki S, Ummels R, Paulußen FM, Grossmann TN, Pham TV, Piersma SR, Jiménez CR, Nejentsev S, Bitter W, Kuijl CP. Multiple aspartic proteases process PE and PPE proteins on the mycobacterial surface of pathogenic mycobacteria. J Biol Chem. 2026:113450 10.1016/j.jbc.2026.113450t.pham@amsterdamumc.nlAmsterdam UMCNetherlandsMycobacterium tuberculosis is the world's leading bacterial infectious agent. The absence of an effective vaccine and the rise of multidrug-resistant M. tuberculosis strains emphasize the need to identify novel targets for prevention and intervention strategies. Previously, the Mycobacterium marinum orthologue of the aspartic protease PecA (PE_PGRS35) was found on the bacterial cell surface, after secretion by the specialized Type VII secretion system. PecA was shown to be responsible for the processing of secreted PE_PGRS proteins, including itself. Both M. marinum and M. tuberculosis encode two additional predicted aspartic proteases with similar secretion domains (PE_PGRS16 and PE26). The roles of the M. marinum PecA, PecB, and PecC were studied using frameshift mutants generated by CRISPR-Cas9 technology. Numerous PecA substrates were identified using analysis of semi-tryptic peptides detected by proteomics of secreted, surface-associated protein fractions. The most abundant substrates are members of the PE and PPE protein families. In addition, analysis of semi-tryptic peptides revealed consensus cleavage sites. Interestingly, these cleavage sites were also situated within the Type VII secretion motif (YxxxD/E), thereby effectively removing the entire PE domain, further strengthening the notion that these domains function as secretion peptides. PecB and PecC were also predicted to process PE and PPE proteins, although to a lesser extent than PecA. Follow-up experiments revealed that PecC is involved in the processing of a small subset of the PPE protein family. Finally, our evidence indicates that PecA functions similarly in M. tuberculosis, as PecA is also responsible for cleavage of PE_PGRS proteins in this species.Multiple aspartic proteases process PE and PPE proteins on the mycobacterial surface of pathogenic mycobacteria.Meijers Aniek S AS, Gallant James L JL, Speer Alexander A, Maaskant Janneke J, Hietamäki Saara S, Ummels Roy R, Paulußen Felix M FM, Grossmann Tom N TN, Pham Thang V TV, Piersma Sander R SR, Jiménez Connie R CR, Nejentsev Sergey S, Bitter Wilbert W, Kuijl Coen P CPfalseMultiple aspartic proteases process PE and PPE proteins on the mycobacterial surface of pathogenic mycobacteriaMycobacterium tuberculosis is the world’s leading bacterial infectious agent. The absence of an effective vaccine and the rise of multi-drug resistant M. tuberculosis strains emphasize the need to identify novel targets for prevention and intervention strategies. Previously, the M. marinum orthologue of the aspartic protease PecA (PE_PGRS35) was found on the bacterial cell surface of the pathogenic strain M. marinum, after secretion by the specialized type VII secretion system. PecA was shown to be responsible for the processing of secreted PE_PGRS proteins, including itself. Both M. marinum and M. tuberculosis encode two additional predicted aspartic proteases with similar secretion domains (PE_PGRS16 and PE26). In this study, the roles of the M. marinum PecA, PecB and PecC were studied using frameshift mutants generated by CRISPR-Cas9 technology. Numerous PecA substrates were identified using analysis of semi-tryptic peptides detected by proteomics of secreted, surface-associated protein fractions. The most abundant substrates are members of the PE and PPE protein families. In addition, analysis of semi-tryptic peptides revealed consensus cleavage sites. Interestingly, these cleavage sites were often located within the Type VII secretion motif (YxxxD/E) and thereby effectively removing the entire PE domain. PecB and PecC were also predicted to process PE and PPE proteins, although to a lesser extent than PecA. Follow-up experiments revealed that also PecC is involved in processing of a small subset of the PPE protein family. Finally, our evidence indicates that PecA plays a similar role in M. tuberculosis, as PecA is also responsible for cleavage of PE_PGRS proteins in this species.2026-08-192025-09-02PXD067990NEWT:3555NEWT:71647NEWT:330879NEWT:35554NEWT:32046NEWT:544496NEWT:2042546NEWT:32049NEWT:1392696NEWT:259447NEWT:295546NEWT:45351NEWT:445974NEWT:43179NEWT:180454NEWT:5722NCBITaxon:1280NEWT:1129NEWT:309807NEWT:55153NEWT:10244NEWT:309800NEWT:281395NEWT:1211601NEWT:876138NEWT:44271NEWT:43186NEWT:10036NEWT:1590NEWT:498019NEWT:1351NEWT:1438992NEWT:1352NEWT:2649997NEWT:1147161NEWT:638632NEWT:263737NEWT:224326NEWT:1333499NCBITaxon:79857NEWT:1096976NEWT:5702NEWT:95648NEWT:1589NEWT:135622NEWT:1349NEWT:96731NEWT:383379NEWT:10029NEWT:913645NEWT:44491NEWT:641809NEWT:27933NEWT:556484NEWT:317447NEWT:4688NEWT:7955NEWT:7959NEWT:2261NEWT:31156NEWT:3112NEWT:79329NEWT:4442NEWT:31155NEWT:192875NEWT:1214915NEWT:12637NEWT:59729NEWT:2164133NEWT:108061NEWT:60711NEWT:1316931NEWT:224308NEWT:3347NEWT:511145NEWT:160621NEWT:212790NEWT:931281NEWT:4432NEWT:5762NEWT:658457NEWT:1310161NEWT:77133NEWT:295358NEWT:145481NCBITaxon:79824NEWT:2246NEWT:2652724NCBITaxon:4563NEWT:5755NEWT:44689NEWT:44447NEWT:752555NEWT:498211NEWT:5759NEWT:1736231NEWT:5518NEWT:398007NEWT:1392NEWT:498217NEWT:498216NEWT:2242NEWT:11320NEWT:286NEWT:391619NEWT:246196NEWT:287NEWT:246197NEWT:1367269NEWT:633149NEWT:10239NEWT:44685NEWT:161934NEWT:4897NEWT:1148NEWT:5508NEWT:3329NEWT:5507NEWT:410661NEWT:55571NEWT:35500NEWT:1235816NEWT:1140NCBITaxon:2157NEWT:1143NEWT:4896NEWT:1287689NEWT:1390NEWT:11557NEWT:1094343NEWT:1462472NEWT:1336795NEWT:644042NEWT:294NEWT:1773NEWT:1182590NEWT:3712NEWT:82380NEWT:3711NEWT:935293NEWT:375146NEWT:2065263NEWT:118698NEWT:1616117NEWT:263NEWT:118696NEWT:52283NEWT:284812NEWT:8175NEWT:43330NEWT:980415NEWT:1603293NEWT:408169NEWT:44664NEWT:47946NEWT:3702NEWT:243277NEWT:1246791NEWT:7067NEWT:118694NEWT:2850NEWT:118691NEWT:33548NEWT:274NEWT:7070NEWT:408172NEWT:408170NEWT:96794NEWT:3708NEWT:332648NEWT:44670NEWT:536231NEWT:376219NEWT:219813NEWT:1436733NEWT:460519NEWT:1247411NEWT:572307NEWT:1432138NEWT:1424507NEWT:1194599NEWT:272844NEWT:9483NEWT:333760NEWT:1513458NEWT:1233681NCBITaxon:40559NEWT:506599NEWT:2853422NEWT:84588NEWT:1679718NEWT:480NEWT:67767NEWT:46835NEWT:109757NEWT:582580NEWT:300852NEWT:1502NEWT:376686NEWT:95486NEWT:508771NEWT:1883446NEWT:253NCBITaxon:2759NEWT:1233435NEWT:93061NEWT:93062NCBITaxon:4932NEWT:109760NEWT:943274NEWT:644223NEWT:235443NEWT:108458NEWT:5936NEWT:272623NEWT:272624NEWT:320637NEWT:2719099NEWT:983964NEWT:118499NEWT:11706NEWT:32644NEWT:527796NEWT:55529NEWT:499175NEWT:109779NEWT:3745NEWT:1715989NCBITaxon:4751NEWT:476272NEWT:3747NEWT:195051NEWT:3988NEWT:1116234NEWT:1255228NEWT:649908NEWT:410289NEWT:373153NEWT:3983NEWT:352472NEWT:1071661NEWT:1202532NEWT:360094NEWT:470NEWT:41364NEWT:1313NEWT:39491NCBITaxon:5811NEWT:29491NEWT:2014887NEWT:33952NEWT:153009NEWT:261756NEWT:571256NEWT:40483NEWT:63366NEWT:63367NEWT:215402NCBITaxon:548681NEWT:272634NEWT:9031NEWT:1872122NEWT:7091NEWT:1034015NEWT:141262NEWT:108931NEWT:1055524NEWT:4087NEWT:9778NEWT:306NEWT:150475NEWT:303NEWT:267872NEWT:7111NEWT:347515NEWT:9534NEWT:5180NEWT:256737NEWT:4090NEWT:4092NEWT:9541NEWT:8694NEWT:4093NEWT:4096NEWT:8692NEWT:2903NEWT:185579NEWT:941442NEWT:13076NEWT:1226408NEWT:7108NEWT:40479NEWT:43989NEWT:4076NEWT:317NEWT:1006581NEWT:885318NEWT:39488NEWT:550NEWT:4081NEWT:273068NEWT:554NEWT:98334NEWT:451516NEWT:4084NEWT:63577NEWT:36185NEWT:1225786NEWT:7574NEWT:1715256NEWT:30640NEWT:575412NEWT:929793NEWT:29204NEWT:28112NEWT:114155NEWT:6494NEWT:6491NEWT:507601NEWT:186441NEWT:643680NEWT:214092NCBITaxon:6157NEWT:6239NEWT:162425NEWT:216257NEWT:102169NEWT:9986NEWT:4054NEWT:8654NEWT:8658NEWT:1268063NEWT:8655NEWT:98351NEWT:1263854NEWT:118503NEWT:2059687NEWT:160488NEWT:28104NEWT:207559NEWT:407821NCBITaxon:2NEWT:85057NEWT:985076NEWT:568708NEWT:1215323NEWT:986NEWT:52641NEWT:7159NEWT:267671NEWT:28532NEWT:198618NEWT:353152NEWT:8496NEWT:7165NEWT:27448NEWT:40674NEWT:1194669NEWT:51329NEWT:243230NEWT:1080772NEWT:519NEWT:8479NEWT:8485NEWT:6063NEWT:49240NEWT:1328388NEWT:104395NEWT:9557NEWT:6289NEWT:6287NEWT:300641NEWT:727NEWT:9796NEWT:725NEWT:469008NEWT:256318NEWT:9321NEWT:206411NCBITaxon:6191NEWT:596153NEWT:229533NEWT:1836NEWT:2925NEWT:214053NEWT:80863NEWT:90675NEWT:105231NEWT:74649NEWT:52638NEWT:57075NEWT:4097NEWT:8697NEWT:8695NEWT:884204NEWT:9785NEWT:6279NEWT:1123869NEWT:9544NEWT:9545NEWT:7370NEWT:83906NCBITaxon:780NCBITaxon:1502NEWT:6282NEWT:1134506NEWT:255470NEWT:38783NEWT:4006NEWT:6426NCBITaxon:5476NEWT:6669NEWT:9935NEWT:89453NEWT:287889NEWT:1114301NEWT:51515NEWT:588596NEWT:51511NEWT:8845NEWT:92867NEWT:92866NEWT:5334NEWT:51750NEWT:202950NEWT:382352NEWT:413071NCBITaxon:10239NCBITaxon:714NEWT:295027NEWT:632957NEWT:11051NEWT:9925NEWT:89462NCBITaxon:9606NEWT:8839NEWT:90690NEWT:1436183NEWT:4232NEWT:2758385NEWT:11298NEWT:171101NEWT:714NEWT:5322NEWT:421932NEWT:312017NEWT:196627NEWT:200308NEWT:553470NEWT:242507NEWT:200302NEWT:870435NEWT:284593NEWT:100392NEWT:5315NEWT:9913NEWT:265872NEWT:105841NEWT:337330NEWT:2666255NEWT:2285NEWT:999810NCBITaxon:5693NEWT:28995NEWT:1392998NEWT:380394NEWT:114796NEWT:981087NEWT:180066NEWT:226900NEWT:231490NEWT:244704NEWT:7725NEWT:430615NEWT:563041NEWT:326423NEWT:452467NEWT:198822NEWT:36111NEWT:326424NEWT:1416333NEWT:35024NEWT:135461NEWT:1678078NEWT:749906NEWT:418985NEWT:1817808NEWT:749907NEWT:145263NEWT:69014NEWT:142809NEWT:694569NEWT:27606NEWT:9739NEWT:59202NEWT:9975NEWT:8643NEWT:51953NEWT:3197NEWT:860688NEWT:13443NEWT:8644NEWT:36329NEWT:62615NCBITaxon:3044782NEWT:1333550NEWT:160235NEWT:72407NEWT:8639NEWT:8637NEWT:349741NEWT:409859NEWT:157295NEWT:2096NEWT:509169NEWT:6210NEWT:192222NEWT:9721NEWT:137221NEWT:9963NEWT:1617910NEWT:565050NEWT:409860NEWT:2785785NEWT:411901NEWT:8626NEWT:105884NCBITaxon:9615NEWT:8621NEWT:58334NEWT:452659NEWT:1193501NEWT:58331NEWT:6689NEWT:8624NEWT:5116NEWT:8623NEWT:298315NEWT:8618NEWT:70448NEWT:9704NEWT:698936NEWT:8855NEWT:9940NEWT:3168NEWT:1247190NEWT:521001NEWT:192011NEWT:1813887NEWT:118702NEWT:118700NEWT:224911NEWT:118705NCBITaxon:11552NEWT:334249NEWT:6945NEWT:184922NEWT:6703NEWT:2104NEWT:6943NEWT:2NEWT:157546NEWT:870726NEWT:474186NEWT:38942NEWT:1493NEWT:307972NEWT:1496NEWT:2102NEWT:3674NEWT:660469NEWT:45474NEWT:1299114NEWT:1590841NEWT:2282334NEWT:4513NEWT:1247NEWT:70667NEWT:869728NEWT:6938NEWT:376741NCBITaxon:10407NEWT:1736309NEWT:4751NEWT:10360NEWT:47664NEWT:557436NEWT:317548NEWT:15819NEWT:3654NEWT:237561NEWT:5833NEWT:3659NEWT:6928NEWT:1239NEWT:36745NEWT:400727NEWT:272563NEWT:11009NEWT:79220NEWT:82688NEWT:5823NEWT:3885NEWT:3888NEWT:5821NEWT:44139NCBITaxon:4895NCBITaxon:4896NEWT:6915NEWT:3649NEWT:101510NEWT:28903NEWT:3880NEWT:272559NEWT:28909NEWT:515849NEWT:3641NEWT:466585NEWT:1000589NEWT:85963NEWT:85962NEWT:143361NEWT:12993NEWT:398580NEWT:4565NEWT:1264690NEWT:515619NEWT:1299NEWT:316407NEWT:34305NCBITaxon:183674NEWT:167387NEWT:84645NEWT:44586NEWT:1123294NEWT:626528NEWT:139927NEWT:4558NEWT:209285NEWT:5888NEWT:211586NEWT:747078NEWT:1282NEWT:1283NEWT:431241NEWT:4550NEWT:1000561NEWT:2133NEWT:4555NEWT:294381NEWT:197NEWT:1390363NEWT:35889NEWT:288705NEWT:29176NEWT:4787NEWT:3217NEWT:4547NEWT:3218NEWT:556182NEWT:1270NEWT:374990NEWT:1432059NEWT:156471NEWT:4784NEWT:360106NEWT:156476NEWT:4543NEWT:4785NEWT:360104NEWT:1857017NEWT:10117NEWT:10116NEWT:1280NEWT:10358NEWT:1735272NEWT:83334NEWT:83332NEWT:317513NEWT:580240NEWT:294128NEWT:11676NEWT:100226NEWT:4530NEWT:54126NEWT:75058NEWT:13616NEWT:172NEWT:296543NEWT:173NEWT:316435NEWT:42157NEWT:1895NEWT:1034304NEWT:105023NEWT:866628NEWT:215358NEWT:64152NEWT:4924NEWT:749200NEWT:8049NEWT:9378NEWT:990346NEWT:145953NEWT:257309NEWT:100816NEWT:203124NEWT:192952NEWT:230741NEWT:8296NEWT:117008NCBITaxon:1313NEWT:44544NEWT:529818NEWT:4911NEWT:645463NEWT:129249NEWT:1077286NEWT:943129NEWT:1221594NEWT:990119NEWT:77216NEWT:1111708NEWT:227321NEWT:493760NEWT:106590NEWT:260710NEWT:257313NEWT:3827NEWT:400772NEWT:128161NEWT:930945NEWT:1162296NEWT:106592NEWT:46704NEWT:1187947NEWT:269796NEWT:10312NCBITaxon:1773NEWT:54571NEWT:9598NEWT:8030NEWT:1423772NEWT:53232NEWT:1639NEWT:188229NEWT:3818NEWT:4909NEWT:759272NEWT:432359NEWT:1182263NEWT:943146NEWT:2711NEWT:537457NEWT:9103NEWT:715877NEWT:862238NEWT:29159NEWT:10306NEWT:9595NEWT:8022NEWT:145943NEWT:595536NEWT:240906NEWT:593117NEWT:89920NEWT:29158NEWT:3633NEWT:3635NEWT:5811NEWT:3879NEWT:180923NEWT:1328881NEWT:411483NEWT:76336NEWT:3870NEWT:884019NEWT:198215NEWT:411490NEWT:200298NEWT:169963NEWT:225117NEWT:746128NEWT:5801NEWT:43665NEWT:1266464NEWT:1205NEWT:367830NEWT:178616NEWT:375451NEWT:357NEWT:9172NEWT:2010198NEWT:1277351NEWT:106178NEWT:411469NEWT:84023NEWT:1679NEWT:559292NEWT:411464NEWT:411460NEWT:2762NEWT:1174673NEWT:1328426NEWT:562NEWT:28035NEWT:411470NEWT:2094720NCBITaxon:2697049NCBITaxon:138NEWT:28038NEWT:1663NEWT:62141NEWT:1423NEWT:4932NEWT:3603NEWT:2759NEWT:3848NEWT:3847NEWT:38293NEWT:1428NEWT:339NEWT:327159NEWT:178876NEWT:1660NEWT:327160NEWT:573NEWT:571NEWT:241368NEWT:518766NEWT:42528NEWT:2664373NEWT:190802NEWT:9417NEWT:1216979NEWT:7237NEWT:115104NEWT:1121114NEWT:663NEWT:8570NEWT:1081927NEWT:1238993NEWT:67825NEWT:187878NEWT:220668NEWT:1821314NEWT:1249668NEWT:426430NEWT:9407NEWT:9646NEWT:1808362NEWT:5286NEWT:7227NEWT:7469NEWT:9402NEWT:9644NEWT:415540NEWT:675060NEWT:334542NEWT:313625NEWT:27592NEWT:426428NEWT:227289NEWT:63459NEWT:1276815NEWT:40324NEWT:588858NEWT:9638NEWT:9639NCBITaxon:11071NEWT:242231NEWT:197221NEWT:7215NEWT:2172103NCBITaxon:59201NEWT:7460NEWT:504457NEWT:434271NEWT:747679NEWT:66712NEWT:42752NEWT:746360NEWT:89764NEWT:470150NEWT:9627NEWT:543734NEWT:1009714NEWT:73239NEWT:38018NEWT:226186NEWT:9870NEWT:8782NEWT:115357NEWT:435590NEWT:1902NEWT:1908NEWT:13164NEWT:216129NEWT:2664179NEWT:623NEWT:7038NEWT:6192NCBITaxon:38727NEWT:2829NEWT:366581NEWT:216599NEWT:405534NEWT:216595NEWT:40559NEWT:51208NEWT:9689NEWT:8355NEWT:633NEWT:9685NEWT:7029NEWT:1283300NEWT:9694NEWT:186990NEWT:632NEWT:1204551NEWT:6183NEWT:99586NEWT:630NEWT:334747NEWT:61235NEWT:392021NEWT:343691NEWT:1457551NEWT:15368NEWT:1491466NEWT:436486NEWT:51655NEWT:170187NEWT:260707NEWT:121845NEWT:8595NEWT:186763NEWT:185431NEWT:29760NEWT:260704NEWT:1719NEWT:703612NEWT:260705NEWT:692672NEWT:2697049NEWT:1505907NEWT:1216981NEWT:1109443NEWT:1249885NEWT:7004NEWT:9669NCBITaxon:6073NEWT:1089448NEWT:1415167NEWT:1329349NEWT:607699NEWT:426688NEWT:208963NEWT:208964NEWT:27337NEWT:575584NEWT:185687NEWT:3039NEWT:8727NEWT:8726NEWT:10090NEWT:8729NEWT:4120NEWT:8720NEWT:5693NEWT:2186NEWT:8724NEWT:8723NEWT:283166NEWT:37334NCBITaxon:10357NCBITaxon:10114NCBITaxon:10359NEWT:1203258NEWT:242619NEWT:49317NEWT:160791NEWT:34073NEWT:696811NEWT:373995NEWT:5689NEWT:8715NEWT:544404NEWT:92519NEWT:37349NEWT:4113NEWT:837NEWT:36015NEWT:81866NEWT:5691NEWT:563192NEWT:48479NEWT:61435NEWT:627025NEWT:1097677NEWT:375939NEWT:61674NEWT:1117957NEWT:6526NEWT:8709NEWT:4100NEWT:1159556NEWT:5671NEWT:1076NEWT:4102NEWT:4101NEWT:6763NEWT:8700NEWT:3498NEWT:803NEWT:29722NEWT:1692259NEWT:1486917NEWT:419947NEWT:468911NEWT:36470NEWT:817NEWT:7604NEWT:818NEWT:135588NEWT:1843183NEWT:5661NEWT:51866NEWT:29719NEWT:58002NEWT:5665NEWT:6754NEWT:6997NEWT:452589NEWT:509068NEWT:5666NEWT:4577NEWT:813NEWT:5664NEWT:2157NEWT:146479NEWT:1042986NEWT:1911079NEWT:69373NEWT:1843192NEWT:206189NCBITaxon:620NEWT:264203NEWT:1480154NEWT:1274414NEWT:9612NEWT:38626NEWT:38865NEWT:3077NEWT:9615NEWT:10299NEWT:6100NEWT:713604NEWT:112273NEWT:1147787NEWT:62977NEWT:1440772NEWT:1355477NEWT:8759NEWT:9605NEWT:9606NEWT:90371NEWT:641501NEWT:4153NEWT:9601NEWT:278839NEWT:35128NEWT:7668NEWT:8756NEWT:915099NEWT:74940NEWT:13551NEWT:10041NEWT:9600NEWT:1450511NEWT:1143193NEWT:1122233NEWT:890382NEWT:174934NEWT:179392NEWT:2823525NEWT:9838NEWT:9839NEWT:546414NEWT:227086NEWT:3055NEWT:11167NEWT:9835NEWT:4146NEWT:5478NEWT:6326NEWT:5476NEWT:1450520NEWT:1042311NEWT:1882945NEWT:299767NEWT:235909NEWT:28835NEWT:47311NEWT:1274432NEWT:2053667NEWT:1274426NEWT:9825NEWT:1274423NEWT:393765NEWT:39946NEWT:9823NEWT:95602NEWT:8732NEWT:314539NEWT:39947NEWT:718274NEWT:1274420NEWT:578458NEWT:60520425951080000-0003-0333-2492