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Record: 1 of 1 MiniMap

LANL Gene ID: PG1768GenBank Locus Tag: PG2024DNA Molecule Name: 1 GenBank ID: 34541613Gene Name: hagE agp rgp-1 rgpA prpR1 prtR rap-1 Definition: arginine-specific cysteine proteinase; gingipain R1Cellular Location: Extracellular, Periplasm [Evidence]Gene Start: 2124296Gene Stop: 2119179Gene Length: 5118Molecular Weight*: 185683pI*: 4.80Net Charge*: -49.31EC: 3.4.22.37 Functional Class: Protein fate; Degradation of proteins, peptides and glycopeptides Gene Ontology: Biological process GO:0009405 pathogenesis GO:0006508 proteolysis GO:0006310 DNA recombination GO:0006281 DNA repair GO:0006260 DNA replication Molecular function GO:0005524 ATP binding GO:0004197 cysteine-type endopeptidase activity GO:0008233 peptidase activity GO:0008234 cysteine-type peptidase activity GO:0003910 DNA ligase (ATP) activityPathway: pathway tablePrimary Evidence: See href="http://linker.lanl.gov/readonly/oragen/bacteria/pgin/hemagglutinin/summ_hemag.htm">Proteases/Hemagglutinin Analysis Veith,P., Talbo,G., Slakeski,N., Dashper,S., Moore,C.,Paolini,R., Reynolds,E., Major outer membrane proteins and proteolytic processing of RgpA, and Kgp of Porphyromonas gingivalis W50, Biochem J (2002) 363, 105-115, PMID: 11903053. Pavloff,N., Potempa,J., Pike,R.N., Prochazka,V., Kiefer,M.C., Travis,J. and Barr,P.J. Molecular cloning and structural characterization of the Arg-gingipain proteinase of Porphyromonas gingivalis. Biosynthesis as a proteinase-adhesin polyprotein. J. Biol. Chem. 270, 1007-1010 (1995) PMID: 7836351. Slakeski,N., Bhogal,P.S., O'Brien-Simpson,N.M. and Reynolds,E.C. Characterization of a second cell-associated Arg-specific cysteine proteinase of Porphyromonas gingivalis and identification of an adhesin-binding motif involved in association of the prtR and prtK proteinases and adhesins into large complexes. Microbiology 144 (Pt 6), 1583-1592 (1998). PMID: 9639929. Gharbia,S.E. and Shah,H.N. Molecular analysis of surface-associated enzymes of Porphyromonas gingivalis Clin Infect Dis 1995 Jun;20 Suppl 2:S160-6, PMID: 7548541. Aduse-Opoku,J., Muir,J., Slaney,J.M., Rangarajan,M. and Curtis,M.A. Characterization, genetic analysis, and expression of a protease antigen (PrpRI) of Porphyromonas gingivalis W50 Infect. Immun. 63 (12), 4744-4754 (1995), PMID: 7591131. Rangarajan,M., Aduse-Opoku,J., Slaney,J.M., Young,K.A. and Curtis,M.A. The prpR1 and the prR2 arginine-specific protease genes of Porphyromonas gingivalis W50 produce five biochemically distinct enzymes Mol Microbiol. 1997 Mar;23(5):955-65. PubMed: Kirszbaum,L., Sotiropoulos,C., Jackson,C., Cleal,S., Slakeski,N. and Reynolds,E.C. Complete nucleotide sequence of a gene prtR of Porphyromonas gingivalis W50 encoding a 132 kDa protein that contains an arginine-specific thiol endopeptidase domain and a haemagglutinin domain. Biochem. Biophys. Res. Commun. 207 (1), 424-431 (1995) PMID: 7857299. Pike,R., McGraw,W., Potempa,J. and Travis,J. Lysine- and arginine-specific proteinases from Porphyromonas gingivalis. Isolation, characterization, and evidence for the existence of complexes with hemagglutinins J. Biol. Chem. 269 (1), 406-411 (1994) PMID: 8276827. Okamoto,K., Misumi,Y., Kadowaki,T., Yoneda,M., Yamamoto,K. and Ikehara,Y. Structural characterization of argingipain, a novel arginine-specific cysteine proteinase as a major periodontal pathogenic factor from Porphyromonas gingivalis. Arch. Biochem. Biophys. 316 (2), 917-925 (1995) PMID: 7864651. Fletcher,H.M., Schenkein,H.A. and Macrina,F.L. Cloning and characterization of a new protease gene (prtH) from Porphyromonas gingivalis. Infect. Immun. 62, 4279-4286 (1994) PMID: 7927685.Secondary Evidence: Lamont,R.J. and Jenkinson, H.F. Life below the gum line: pathogenic mechanisms of Porphyromonas gingivalis. Microbiol. Mol. Biol. Reviews 62: 1244-1263 (1998) Progulske-Fox,A. and Lantz,M.S. Analysis of the prtP gene encoding porphypain, a cysteine proteinase of Porphyromonas gingivalis J. Bacteriol. 178 (10), 2734-2741 (1996)Comment: Gingipain R1 is an Arg-X thiol protease thought to be responsible for protein degradation associated with peridontal disease. This polyprotein also shows hemagglutinin/adhesin activity. For the R2 sequence, see PG0461. At 1706 amino acids, PG1768 is closer to Rgp-1 from strain HG66 than to PrtP from strain W12. Amino acid residues 228-719 constitute the alpha region or RIA (surface molecule) from the PrpR1 study; a slight variant is RIB, a lipid-modified form. Residues 719-1262 constitute the RI chain upon post-translational processing at arginines. Surface RI consists of the alpha chain (53 kDa) and a beta chain taken from the C-terminal half of the polyprotein. RIA and RIB appear as monomers. The study of PrtR suggests that RIA is a 45 kDa proteinase, and that the beta and gamma (C-terminal) regions comprise 44 kDa, 15 kDa, 17 kDa and 27 kDa adhesins (Lamont and Jenkinson, MMBR 62:no.4). Gene nomenclature and strains (from Lamont and Jenkinson): rgp-1 (HG66), rgpA(ATCC 33277), prpRI (W50), prtR (W50), prtH (W83), agp (381), cpgR (ATCC 33277). Veith et al. 2002 identified this protein by two-dimensional gel electrophoresis and peptide mass fingerprinting of outer membranes prepared from strain W50. They present the following results: The C-terminal domain of RgpA together with PG1838, PG1570 and PG0461 migrate as vertical streaks on 2D-PAGE at a MW 13-42 kDa higher than that calculated from their gene sequences. The electrophoretic behaviour of these proteins together with their immunoreactivity with a monoclonal antibody that recognises LPS is consistent with a modification that could anchor the proteins to the outer membrane. The proposed LPS-attachment site is in the conserved C-terminal 50 amino acid residues of each of these proteins. Based on signal peptide sequence comparisons to PG0626, PG0627, PG1592, PG1840, PG0836, PG0023, PG1893, the mature N-terminus of this protein is predicted to be pyroglutamate.RgpA, Kgp and HagA were identified as fully processed domains. The N- and C-termini of many of these domains were identified by mass spectrometry and or N-terminal sequence analysis. It was found that gaps existed between many of the domains. The proposed domain structure of RgpA is as follows: RgpA signal peptide (1-23), RgpA pro-domain (24-227), RgpA45 (228-688), RgpA44 (720-1081), RgpA15 (1139-1257), RgpA17 (1274-1404), RgpA27 (1432-1706). TIGR ID: PG2024Proteomic Data: Proteomic Data Search

TIGR Annotation		arginine-specific protease ArgI polyprotein, GroupD (cellular processes) ,GroupM (protein fate)
ORF #		PG-PP/PG-PPC1				PG-PP/PG-PPC2
		Spectral Count		Peptide Intensity		Spectral Count		Peptide Intensity
		Pro	qVal	Pro	qVal	Pro	qVal	Pro	qVal
TIGR	PG2024	0.06	0.061	-0.29	0.034	-0.35	0	-0.29	0.034
LANL	PG1768	1.04		0.82		0.79		0.78
Consensus		SP1		IP1		SP2		IP2

Human Oral Microbiome Database:
View in HOMD Genome Viewer Blast Summary: PSI-Blast Search PG1768 corresponds to the previously sequenced U15282 from strain HG66, X82680 from strain W50 and L26341 from W50. See also A55426, D26470, X85186. No other significant hits in gapped BLAST except to paralogs. See also D26470 from strain 381: residues 1-941 are virtually identical to residues 1-941 of D26470. Residues 1082-1702 are 95% similar to residues 32-653 of L27483 from strain W83. Residues 219-645 are 95% similar to residues 1-422 of X85186 from strain ATCC 33277. See Z29570. The published hagE sequence (AF026946 corresponds to the N-terminal residues of PG1768: residues 1-1687 are 99% similar to residues 20-1706 of PG1768. Top Blast Hits: Updated monthly Click here to view the entire PsiBlast results. gi|34541613|ref|NP_906092.1| hemagglutinin protein HagE [Po... 3346 0.0 gi|1813996|emb|CAA57997.1| protease precursor [Porphyromona... 3338 0.0 gi|1066835|gb|AAC18876.1| arginine-specific thiol protease ... 3336 0.0 gi|557068|gb|AAA69539.1| Arg-gingipain-1 proteinase 3324 0.0 gi|4103639|gb|AAD01810.1| hemagglutinin/protease [Porphyrom... 3294 0.0 gi|1314751|gb|AAA99810.1| Lys-gingipain 1952 0.0 gi|2827775|sp|P28784|CPG1_PORGI Gingipain R1 precursor (Gin... 1804 0.0 gi|1536824|dbj|BAA11870.1| Lys-gingipain [Porphyromonas gin... 1586 0.0 gi|1890077|gb|AAB49691.1| hemagglutinin [Porphyromonas ging... 1501 0.0 gi|2182812|gb|AAB60809.1| lysine-specific cysteine proteina... 1485 0.0InterPro Summary: InterProScan InterPro IPR000977 Family ATP-dependent DNA ligase PS00697 DNA_LIGASE_A1 InterPro IPR001769 Family Peptidase C25, gingipain PF01364 Peptidase_C25 InterPro IPR005536 Domain Peptidase C25, C-terminal ig-like region PF03785 Peptidase_C25_C InterPro IPR011628 Domain Cleaved adhesin PF07675 Cleaved_Adhesin InterPro IPR012600 Domain Propetide, peptidase C25 PF08126 Propeptide_C25 InterPro IPR013783 Domain Immunoglobulin-like fold G3DSA:2.60.40.10 Ig-like_fold InterPro IPR014756 Domain Immunoglobulin E-set SSF81296 Ig_E-set noIPR unintegrated unintegrated G3DSA:3.40.50.10390 G3DSA:3.40.50.10390 G3DSA:3.40.50.1460 G3DSA:3.40.50.1460 SSF52129 SSF52129 COGS Summary: COGS Search No hit to the COGs database. Blocks Summary: Blocks Search ***** PF01364 (Peptidase family C25) with a combined E-value of 5.6e-282. PF01364A 46-95 PF01364B 243-250 PF01364C 258-311 PF01364D 371-408 PF01364E 489-539 PF01364F 1610-1663 PF01364G 1664-1702 PF01364B 1403-1410 PF01364C 699-752 ProDom Summary: Protein Domain Search Residues 1082-1114 are 87% similar to a (PROTEASE PRTH EC 3.4.22.-) protein domain (PD125301 which is seen in PRTH_PORGI. Residues 1369-1635 are identical to a (PROTEASE PRECURSOR SIGNAL THIOL HEMAGGLUTININ REPEAT) protein domain (PD002028 which is seen in Q51838_PORGI. Residues 1636-1706 are identical to a (PROTEASE PRECURSOR THIOL SIGNAL) protein domain (PD004371 which is seen in P72194_PORGI. Residues 1-218 are identical to a (PROTEASE CYSTEINE PRECURSOR THIOL) protein domain (PD005390 which is seen in CPG1_PORGI. Residues 1375-1408 are 85% similar to a (PROTEASE PRECURSOR SIGNAL HEMAGGLUTININ THIOL REPEAT) protein domain (PD001858 which is seen in P72194_PORGI. Residues 437-645 are identical to a (PROTEASE PROTEINASE CYSTEINE PRECURSOR) protein domain (PD007636 which is seen in CPG1_PORGI. Residues 1577-1626 are 76% similar to a (PROTEASE THIOL REPEAT PRECURSOR) protein domain (PD013956 which is seen in Q51839_PORGI. Residues 219-436 are identical to a (PROTEASE THIOL CYSTEINE PRECURSOR) protein domain (PD005006 which is seen in Q51838_PORGI. Paralogs: Local Blast Search PG1768 is paralogously related to PG0461, a predicted Arg-X protease. Residues 2-659 are 84% similar to residues 3-662 of PG0461. Further similarities (53-54%) are seen to PG1164, PG1602 and PG1605. For fragmentary similarities, see PG1606, PG1922, PG0022, PG0376. Pfam Summary: Pfam Search Residues 228 to 576 (E-value = 1.4e-280) place PG1768 in the Peptidase_C25 family which is described as Peptidase family C25 (PF01364) Residues 578 to 657 (E-value = 4.1e-54) place PG1768 in the Peptidase_C25_C family which is described as Peptidase family C25, C terminal ig-like domain (PF03785) Structural Feature(s): Feature Type Start Stop cleavable signal 1 23 non-globular 582 732 non-globular 823 1006 Top PDB Hits: No significant hits to the PDB database (E-value < E-10). Gene Protein Sequence: MKNLNKFVSIALCSSLLGGMAFAQQTELGRNPNVRLLESTQQSVTKVQFR MDNLKFTEVQTPKGMAQVPTYTEGVNLSEKGMPTLPILSRSLAVSDTREM KVEVVSSKFIEKKNVLIAPSKGMIMRNEDPKKIPYVYGKSYSQNKFFPGE IATLDDPFILRDVRGQVVNFAPLQYNPVTKTLRIYTEITVAVSETSEQGK NILNKKGTFAGFEDTYKRMFMNYEPGRYTPVEEKQNGRMIVIVAKKYEGD IKDFVDWKNQRGLRTEVKVAEDIASPVTANAIQQFVKQEYEKEGNDLTYV LLIGDHKDIPAKITPGIKSDQVYGQIVGNDHYNEVFIGRFSCESKEDLKT QIDRTIHYERNITTEDKWLGQALCIASAEGGPSADNGESDIQHENVIANL LTQYGYTKIIKCYDPGVTPKNIIDAFNGGISLANYTGHGSETAWGTSHFG TTHVKQLTNSNQLPFIFDVACVNGDFLFSMPCFAEALMRAQKDGKPTGTV AIIASTINQSWASPMRGQDEMNEILCEKHPNNIKRTFGGVTMNGMFAMVE KYKKDGEKMLDTWTVFGDPSLLVRTLVPTKMQVTAPAQINLTDASVNVSC DYNGAIATISANGKMFGSAVVENGTATINLTGLTNESTLTLTVVGYNKET VIKTINTNGEPNPYQPVSNLTATTQGQKVTLKWDAPSTKTNATTNTARSV DGIRELVLLSVSDAPELLRSGQAEIVLEAHDVWNDGSGYQILLDADHDQY GQVIPSDTHTLWPNCSVPANLFAPFEYTVPENADPSCSPTNMIMDGTASV NIPAGTYDFAIAAPQANAKIWIAGQGPTKEDDYVFEAGKKYHFLMKKMGS GDGTELTISEGGGSDYTYTVYRDGTKIKEGLTATTFEEDGVAAGNHEYCV EVKYTAGVSPKVCKDVTVEGSNEFAPVQNLTGSAVGQKVTLKWDAPNGTP NPNPNPNPNPNPGTTTLSESFENGIPASWKTIDADGDGHGWKPGNAPGIA GYNSNGCVYSESFGLGGIGVLTPDNYLITPALDLPNGGKLTFWVCAQDAN YASEHYAVYASSTGNDASNFTNALLEETITAKGVRSPEAIRGRIQGTWRQ KTVDLPAGTKYVAFRHFQSTDMFYIDLDEVEIKANGKRADFTETFESSTH GEAPAEWTTIDADGDGQGWLCLSSGQLDWLTAHGGTNVVSSFSWNGMALN PDNYLISKDVTGATKVKYYYAVNDGFPGDHYAVMISKTGTNAGDFTVVFE ETPNGINKGGARFGLSTEADGAKPQSVWIERTVDLPAGTKYVAFRHYNCS DLNYILLDDIQFTMGGSPTPTDYTYTVYRDGTKIKEGLTETTFEEDGVAT GNHEYCVEVKYTAGVSPKKCVNVTVNSTQFNPVKNLKAQPDGGDVVLKWE APSAKKTEGSREVKRIGDGLFVTIEPANDVRANEAKVVLAADNVWGDNTG YQFLLDADHNTFGSVIPATGPLFTGTASSDLYSANFEYLIPANADPVVTT QNIIVTGQGEVVIPGGVYDYCITNPEPASGKMWIAGDGGNQPARYDDFTF EAGKKYTFTMRRAGMGDGTDMEVEDDSPASYTYTVYRDGTKIKEGLTETT YRDAGMSAQSHEYCVEVKYTAGVSPKVCVDYIPDGVADVTAQKPYTLTVV GKTITVTCQGEAMIYDMNGRRLAAGRNTVVYTAQGGYYAVMVVVDGKSYV EKLAIK Gene Nucleotide Sequence: Sequence Viewer ATGAAAAACTTGAACAAGTTTGTTTCGATTGCTCTTTGCTCTTCCTTATT AGGAGGAATGGCATTTGCGCAGCAGACAGAGTTGGGACGCAATCCGAATG TGAGATTGCTCGAATCCACTCAGCAATCGGTGACAAAGGTTCAGTTCCGT ATGGACAACCTCAAGTTCACCGAAGTTCAAACCCCTAAGGGAATGGCACA AGTGCCGACCTATACAGAAGGGGTTAATCTTTCTGAAAAAGGGATGCCTA CGCTTCCCATTCTATCACGCTCTTTGGCGGTTTCAGACACTCGTGAGATG AAGGTAGAGGTTGTTTCCTCAAAGTTCATCGAAAAGAAAAATGTCCTGAT TGCACCCTCCAAGGGCATGATTATGCGTAACGAAGATCCGAAAAAGATCC CTTACGTTTATGGAAAGAGCTACTCGCAAAACAAATTCTTCCCGGGAGAG ATCGCCACGCTTGATGATCCTTTTATCCTTCGTGATGTGCGTGGACAGGT TGTAAACTTTGCGCCTTTGCAGTATAACCCTGTGACAAAGACGTTGCGCA TCTATACGGAAATCACTGTGGCAGTGAGCGAAACTTCGGAGCAAGGCAAA AATATTCTGAACAAGAAAGGTACATTTGCCGGCTTTGAAGACACATACAA GCGCATGTTCATGAACTACGAGCCAGGGCGTTACACACCGGTAGAGGAAA AACAAAATGGTCGTATGATCGTCATCGTAGCCAAAAAGTATGAGGGAGAT ATTAAAGATTTCGTTGATTGGAAAAACCAACGCGGTCTCCGTACCGAGGT GAAAGTGGCAGAAGATATTGCTTCTCCCGTTACAGCTAATGCTATTCAGC AATTCGTTAAGCAAGAATACGAGAAAGAAGGTAATGATTTGACCTATGTT CTTTTGATTGGCGATCACAAAGATATTCCTGCCAAAATTACTCCGGGGAT CAAATCCGACCAGGTATATGGACAAATAGTAGGTAATGACCACTACAACG AAGTCTTCATCGGTCGTTTCTCATGTGAGAGCAAAGAGGATCTGAAGACA CAAATCGATCGGACTATTCACTATGAGCGCAATATAACCACGGAAGACAA ATGGCTCGGTCAGGCTCTTTGTATTGCTTCGGCTGAAGGAGGCCCATCCG CAGACAATGGTGAAAGTGATATCCAGCATGAGAATGTAATCGCCAATCTG CTTACCCAGTATGGTTATACCAAGATTATCAAATGTTATGATCCGGGAGT AACTCCTAAAAACATTATTGATGCTTTCAACGGAGGAATCTCGTTGGCCA ACTATACGGGCCACGGTAGCGAAACAGCTTGGGGTACGTCTCACTTCGGC ACCACTCATGTGAAGCAGCTTACCAACAGCAACCAGCTACCGTTTATTTT CGACGTAGCTTGTGTGAATGGCGATTTCCTATTCAGCATGCCTTGTTTCG CAGAAGCATTGATGCGTGCACAAAAAGATGGTAAGCCGACAGGTACTGTT GCTATCATAGCGTCTACGATCAACCAGTCTTGGGCTTCTCCTATGCGCGG GCAGGATGAGATGAACGAAATTCTGTGCGAAAAACACCCGAACAACATCA AGCGTACTTTCGGTGGTGTCACCATGAACGGTATGTTTGCTATGGTGGAA AAGTATAAAAAGGATGGTGAGAAGATGCTCGACACATGGACTGTATTCGG CGACCCCTCGCTGCTCGTTCGTACACTTGTCCCGACCAAAATGCAGGTTA CGGCTCCGGCTCAGATTAATTTGACGGATGCTTCAGTCAACGTATCTTGC GATTATAATGGTGCTATTGCTACCATTTCAGCCAATGGAAAGATGTTCGG TTCTGCAGTTGTCGAAAATGGAACAGCTACAATCAATCTGACAGGTCTGA CAAATGAAAGCACGCTTACCCTTACAGTAGTTGGTTACAACAAAGAGACG GTTATTAAGACCATCAACACTAATGGTGAGCCTAACCCCTACCAGCCTGT TTCCAACTTGACTGCTACAACGCAGGGTCAGAAAGTAACGCTCAAGTGGG ATGCACCGAGCACGAAAACCAATGCAACCACTAATACCGCTCGCAGCGTG GATGGCATACGAGAACTGGTTCTTCTGTCAGTCAGCGATGCCCCCGAACT TCTTCGCAGCGGTCAGGCCGAGATTGTTCTTGAAGCTCACGATGTTTGGA ATGATGGATCCGGTTATCAGATTCTTTTGGATGCAGACCATGATCAATAT GGACAGGTTATACCCAGTGATACCCATACTCTTTGGCCGAACTGTAGTGT CCCGGCCAATCTGTTCGCTCCGTTCGAATATACGGTTCCGGAAAATGCAG ATCCTTCTTGTTCCCCTACCAATATGATAATGGATGGTACTGCATCCGTT AATATACCGGCCGGAACTTATGACTTTGCAATTGCTGCTCCTCAAGCAAA TGCAAAGATTTGGATTGCCGGACAAGGACCGACGAAAGAAGATGATTATG TATTTGAAGCCGGTAAAAAATACCATTTCCTTATGAAGAAGATGGGTAGC GGTGATGGAACTGAATTGACTATAAGCGAAGGTGGTGGAAGCGATTACAC CTATACTGTCTATCGTGACGGCACGAAGATCAAGGAAGGTCTGACGGCTA CGACATTCGAAGAAGACGGTGTAGCTGCAGGCAATCATGAGTATTGCGTG GAAGTTAAGTACACAGCCGGCGTATCTCCGAAGGTATGTAAAGACGTTAC GGTAGAAGGATCCAATGAATTTGCTCCTGTACAGAACCTGACCGGTAGTG CAGTCGGCCAGAAAGTAACGCTTAAGTGGGATGCACCTAATGGTACCCCG AATCCAAATCCAAATCCGAATCCAAATCCGAATCCCGGAACAACTACACT TTCCGAATCATTCGAAAATGGTATTCCTGCCTCATGGAAGACGATCGATG CAGACGGTGACGGGCATGGCTGGAAGCCTGGAAATGCTCCCGGAATCGCT GGCTACAATAGCAATGGTTGTGTATATTCAGAGTCATTCGGTCTTGGTGG TATAGGAGTTCTTACCCCTGACAACTATCTGATAACACCGGCATTGGATT TGCCTAACGGAGGTAAGTTGACTTTCTGGGTATGCGCACAGGATGCTAAT TATGCATCCGAGCACTATGCGGTGTATGCATCTTCGACCGGTAACGATGC ATCCAACTTCACGAATGCTTTGTTGGAAGAGACGATTACGGCAAAAGGTG TTCGCTCGCCGGAAGCTATTCGTGGTCGTATACAGGGTACTTGGCGCCAG AAGACGGTAGACCTTCCCGCAGGTACGAAATATGTTGCTTTCCGTCACTT CCAAAGCACGGATATGTTCTACATCGACCTTGATGAGGTTGAGATCAAGG CCAATGGCAAGCGCGCAGACTTCACGGAAACGTTCGAGTCTTCTACTCAT GGAGAGGCACCAGCGGAATGGACTACTATCGATGCCGATGGCGATGGTCA GGGTTGGCTCTGTCTGTCTTCCGGACAATTGGACTGGCTGACAGCTCATG GCGGCACCAACGTAGTAAGCTCTTTCTCATGGAATGGAATGGCTTTGAAT CCTGATAACTATCTCATCTCAAAGGATGTTACAGGCGCAACGAAGGTAAA GTACTACTATGCAGTCAACGACGGTTTTCCCGGGGATCACTATGCGGTGA TGATCTCCAAGACGGGCACGAACGCCGGAGACTTCACGGTTGTTTTCGAA GAAACGCCTAACGGAATAAATAAGGGCGGAGCAAGATTCGGTCTTTCCAC GGAAGCCGATGGCGCCAAACCTCAAAGTGTATGGATCGAGCGTACGGTAG ATTTGCCTGCGGGCACGAAGTATGTTGCTTTCCGTCACTACAATTGCTCG GATTTGAACTACATTCTTTTGGATGATATTCAGTTCACCATGGGTGGCAG CCCCACCCCGACCGATTATACCTACACGGTGTATCGTGATGGTACGAAGA TCAAGGAAGGTTTGACCGAAACGACCTTCGAAGAAGACGGCGTAGCTACG GGCAATCATGAGTATTGCGTGGAAGTGAAGTACACAGCCGGCGTATCTCC GAAGAAATGTGTAAACGTAACTGTTAATTCGACACAGTTCAATCCTGTAA AGAACCTGAAGGCACAACCGGATGGCGGCGACGTGGTTCTCAAGTGGGAA GCCCCGAGCGCAAAGAAGACAGAAGGTTCTCGTGAAGTAAAACGGATCGG AGACGGTCTTTTCGTTACGATCGAACCTGCAAACGATGTACGTGCCAACG AAGCCAAGGTTGTGCTCGCAGCAGACAACGTATGGGGAGACAATACGGGT TACCAGTTCTTGTTGGATGCCGATCACAATACATTCGGAAGTGTCATTCC GGCAACCGGTCCTCTCTTTACCGGAACAGCTTCTTCCGATCTTTACAGTG CGAACTTCGAGTATTTGATCCCGGCCAATGCCGATCCTGTTGTTACTACA CAGAATATTATCGTTACAGGACAGGGTGAAGTTGTAATCCCCGGTGGTGT TTACGACTATTGCATTACGAACCCGGAACCTGCATCCGGAAAGATGTGGA TCGCAGGAGATGGAGGCAACCAGCCTGCACGTTATGACGATTTCACATTC GAAGCAGGCAAGAAGTACACCTTCACGATGCGTCGCGCCGGAATGGGAGA TGGAACTGATATGGAAGTCGAAGACGATTCACCTGCAAGCTATACCTATA CAGTCTATCGTGACGGCACGAAGATCAAGGAAGGTCTGACCGAAACGACC TACCGCGATGCAGGAATGAGTGCACAATCTCATGAGTATTGCGTGGAAGT TAAGTACACAGCCGGCGTATCTCCGAAGGTTTGTGTGGATTATATTCCTG ACGGAGTGGCAGACGTAACGGCTCAGAAGCCTTACACGCTGACAGTTGTA GGAAAGACGATCACGGTAACTTGCCAAGGCGAAGCTATGATCTACGACAT GAACGGTCGTCGTCTGGCAGCCGGTCGCAACACGGTTGTTTACACGGCTC AGGGCGGCTACTATGCAGTTATGGTTGTCGTTGACGGCAAGTCTTACGTA GAGAAACTCGCTATCAAG Los Alamos National Laboratory • Est 1943 Operated by Los Alamos National Security, LLC for the U.S. Department of Energy's National Nuclear Security Administration Inside | © Copyright 2006 LANS LLC All rights reserved | Disclaimer/Privacy

`Feature Type`	`Start`	`Stop`
`cleavable signal`	`1`	`23`
`non-globular`	`582`	`732`
`non-globular`	`823`	`1006`