P1 proteinase
     (N-terminal protein)
Helper component proteinase
     (HC-pro)
     (EC 3.4.22.45)
Protein P3
6 kDa protein 1
     (6K1)
Cytoplasmic inclusion protein
     (CI)
     (EC 3.6.1.-)
6 kDa protein 2
     (6K2)
Viral genome-linked protein
     (VPg)
Nuclear inclusion protein A
     (NI-a)
     (NIa)
     (EC 3.4.22.44)
     (NIa-pro)
     (49 kDa proteinase)
     (49 kDa-Pro)
Nuclear inclusion protein B
     (NI-b)
     (NIb)
     (EC 2.7.7.48)
     (RNA-directed RNA polymerase)
Coat protein
     (CP)

Gene name

None

From

Turnip mosaic virus (strain Quebec) (TuMV)

[TaxID: 36396]

Taxonomy

Viruses; ssRNA positive-strand viruses, no DNA stage; Potyviridae; Potyvirus.

Virus hosts

Alliaria [TaxID: 126269]
Brassica [TaxID: 3705]
Calanthe [TaxID: 38206]
Capsella bursa-pastoris (Shepherd's purse) [TaxID: 3719]
Hesperis matronalis [TaxID: 264418]
Stellaria media (Common chickweed) [TaxID: 13274]
Trifolium hybridum (Alsike clover) [TaxID: 74517]

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC RNA] (ISOFORM GENOME POLYPROTEIN). PubMed=1431807 [NCBI, ExPASy, EBI, Israel, Japan] Nicolas O., Laliberte J.F.; "The complete nucleotide sequence of turnip mosaic potyvirus RNA."; J. Gen. Virol. 73:2785-2793(1992).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1534-3163 (ISOFORM GENOME POLYPROTEIN), AND PARTIAL PROTEIN SEQUENCE. PubMed=2254757 [NCBI, ExPASy, EBI, Israel, Japan] Tremblay M.F., Nicolas O., Sinha R., Lazure C., Laliberte J.F.; "Sequence of the 3'-terminal region of turnip mosaic virus RNA and the capsid protein gene."; J. Gen. Virol. 71:2769-2772(1990).
[3]	RIBOSOMAL FRAMESHIFT (ISOFORM PIPO). DOI=10.1073/pnas.0800468105; PubMed=18408156 [NCBI, ExPASy, EBI, Israel, Japan] Chung B.Y.-W., Miller W.A., Atkins J.F., Firth A.E.; "An overlapping essential gene in the Potyviridae."; Proc. Natl. Acad. Sci. U.S.A. 105:5897-5902(2008).
[4]	REVIEW. DOI=10.1016/S0168-1702(01)00220-9; PubMed=11226583 [NCBI, ExPASy, EBI, Israel, Japan] Urcuqui-Inchima S., Haenni A.L., Bernardi F.; "Potyvirus proteins: a wealth of functions."; Virus Res. 74:157-175(2001).

Comments

FUNCTION: Coat protein is involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification.
FUNCTION: Nuclear inclusion protein B is a RNA-dependent RNA polymerase that plays an essential role in the virus replication.
FUNCTION: Helper component proteinase is required for aphid transmission and also has proteolytic activity. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity (By similarity).
FUNCTION: Cytoplasmic inclusion protein has helicase activity. It may be involved in replication (By similarity).
FUNCTION: Both 6K peptides are indispensable for virus replication (By similarity).
FUNCTION: Nuclear inclusion protein A has RNA-binding and proteolytic activities.
CATALYTIC ACTIVITY: Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.
CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
CATALYTIC ACTIVITY: Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the potyviral polyprotein.
SUBCELLULAR LOCATION: Coat protein: Virion (Potential).

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by ribosomal frameshifting. Knockout of PIPO ORF is lethal for the virus. Because of a common N-terminus, some results depicted for the genome polyprotein might belong to the PIPO isoform.

Name	Genome polyprotein
Isoform ID	Q02597-1
Note: Produced by conventional translation.
This is the isoform sequence displayed in this entry.

Name	PIPO
Synonyms	Pretty interesting potyviridae ORF
Isoform ID	Q02597-2
Note: Produced by ribosomal frameshifting.
Features which should be applied to build the isoform sequence: VSP_034776, VSP_034777.

DOMAIN: The N-terminus of helper component proteinase is involved in interaction with stylets. The central part is involved in interaction with virions and the C-terminus is involved in cell-to cell movement of the virus.
PTM: VPg is covalently linked to the genomic RNA (By similarity).
PTM: The viral RNA of potyviruses is expressed as a single polyprotein which undergoes post-translational proteolytic processing by the main proteinase NIa-pro resulting in the production of at least ten individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically. 6K1 is essential for proper proteolytic separation of P3 from CI (By similarity).
SIMILARITY: Belongs to the potyviruses polyprotein family.
SIMILARITY: Contains 1 helicase ATP-binding domain.
SIMILARITY: Contains 1 helicase C-terminal domain.
SIMILARITY: Contains 1 peptidase C4 domain [view classification].
SIMILARITY: Contains 1 peptidase C6 domain [view classification].
SIMILARITY: Contains 1 peptidase S30 domain [view classification].
SIMILARITY: Contains 1 RdRp catalytic domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D10927; BAA01725.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D10601; BAA01452.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JQ1895; JQ1895.

3D structure databases

HSSP

P04517; 1LVM. [HSSP ENTRY / PDB]

ModBase

Q02597.

Protein family/group databases

MEROPS

C04.001; -.

Ontologies

GO:0019028;	Cellular component: viral capsid (inferred from electronic annotation from InterPro).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0008026;	Molecular function: ATP-dependent helicase activity (inferred from electronic annotation from InterPro).
GO:0004197;	Molecular function: cysteine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0003723;	Molecular function: RNA binding (inferred from electronic annotation from InterPro).
GO:0003968;	Molecular function: RNA-directed RNA polymerase activity (inferred from electronic annotation from InterPro).
GO:0005198;	Molecular function: structural molecule activity (inferred from electronic annotation from UniProtKB-KW).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
GO:0018144;	Biological process: RNA-protein covalent cross-linking (inferred from electronic annotation from UniProtKB-KW).
GO:0006410;	Biological process: transcription, RNA-dependent (inferred from electronic annotation from UniProtKB-KW).
GO:0019079;	Biological process: viral genome replication (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR014001; DEAD-like_N.
IPR001650; DNA/RNA_helicase_C.
IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
IPR014021; Helicase_SF1/SF2_ATP-bd.
IPR002540; Pept_S30_P1_potyvir.
IPR001730; Peptidase_C4.
IPR001456; Peptidase_C6.
IPR001592; Poty_coat.
IPR013648; PP_Potyviridae.
IPR001205; RNA_pol_P3D.
IPR007094; RNA_pol_PSvir.
Graphical view of domain structure.

Pfam

PF00270; DEAD; 1.
PF00271; Helicase_C; 1.
PF00863; Peptidase_C4; 1.
PF00851; Peptidase_C6; 1.
PF01577; Peptidase_S30; 1.
PF00767; Poty_coat; 1.
PF08440; Poty_PP; 1.
PF00680; RdRP_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00966; NIAPOTYPTASE.

SMART

SM00487; DEXDc; 1.
SM00490; HELICc; 1.
SMART graphical view of domain structure.

PROSITE

PS51192; HELICASE_ATP_BIND_1; 1.
PS51194; HELICASE_CTER; 1.
PS50507; RDRP_SSRNA_POS; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q02597.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Capsid protein; Complete proteome; Covalent protein-RNA linkage; Direct protein sequencing; Helicase; Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease; Ribosomal frameshifting; RNA replication; RNA-directed RNA polymerase; Suppressor of RNA silencing; Thiol protease; Transferase; Virion.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 362`	`362`	`P1 proteinase (Potential).`	`PRO_0000040473`
`CHAIN`	`363 820`	`458`	`Helper component proteinase (Potential).`	`PRO_0000040474`
`CHAIN`	`821 1175`	`355`	`Protein P3 (By similarity).`	`PRO_0000040475`
`CHAIN`	`1176 1227`	`52`	`6 kDa protein 1 (By similarity).`	`PRO_0000040476`
`CHAIN`	`1228 1870`	`643`	`Cytoplasmic inclusion protein (By similarity).`	`PRO_0000040477`
`CHAIN`	`1871 1923`	`53`	`6 kDa protein 2 (By similarity).`	`PRO_0000040478`
`CHAIN`	`1924 2115`	`192`	`Viral genome-linked protein (By similarity).`	`PRO_0000040479`
`CHAIN`	`2116 2358`	`243`	`Nuclear inclusion protein A (By similarity).`	`PRO_0000040480`
`CHAIN`	`2359 2875`	`517`	`Nuclear inclusion protein B (By similarity).`	`PRO_0000040481`
`CHAIN`	`2876 3163`	`288`	`Coat protein (By similarity).`	`PRO_0000040482`
`DOMAIN`	`1300 1452`	`153`	`Helicase ATP-binding.`
`DOMAIN`	`1471 1630`	`160`	`Helicase C-terminal.`
`DOMAIN`	`2600 2724`	`125`	`RdRp catalytic.`
`NP_BIND`	`1313 1320`	`8`	`ATP (Potential).`
`MOTIF`	`414 417`	`4`	`Involved in interaction with stylet and aphid transmission (By similarity).`
`MOTIF`	`672 674`	`3`	`Involved in virions binding and aphid transmission (By similarity).`
`MOTIF`	`1402 1405`	`4`	`DECH box.`
`MOTIF`	`1964 1971`	`8`	`Nuclear localization signal (Potential).`
`ACT_SITE`	`270 270`		`For P1 proteinase activity (By similarity).`
`ACT_SITE`	`279 279`		`For P1 proteinase activity (Potential).`
`ACT_SITE`	`313 313`		`For P1 proteinase activity (By similarity).`
`ACT_SITE`	`706 706`		`For helper component proteinase activity (By similarity).`
`ACT_SITE`	`779 779`		`For helper component proteinase activity (By similarity).`
`ACT_SITE`	`2161 2161`		`For nuclear inclusion protein A activity (By similarity).`
`ACT_SITE`	`2196 2196`		`For nuclear inclusion protein A activity (By similarity).`
`ACT_SITE`	`2266 2266`		`For nuclear inclusion protein A activity (By similarity).`
`SITE`	`362 363`	`2`	`Cleavage; by P1 proteinase (Potential).`
`SITE`	`820 821`	`2`	`Cleavage; by HC-pro (Potential).`
`SITE`	`1175 1176`	`2`	`Cleavage; by NIa-pro (By similarity).`
`SITE`	`1227 1228`	`2`	`Cleavage; by NIa-pro (By similarity).`
`SITE`	`1870 1871`	`2`	`Cleavage; by NIa-pro (By similarity).`
`SITE`	`2115 2116`	`2`	`Cleavage; by NIa-pro (By similarity).`
`SITE`	`2358 2359`	`2`	`Cleavage; by NIa-pro (By similarity).`
`SITE`	`2875 2876`	`2`	`Cleavage; by NIa-pro (By similarity).`
`MOD_RES`	`1986 1986`		`O-(5'-phospho-RNA)-tyrosine (By similarity).`
`VAR_SEQ`	`982 1051`		`LEKSYLQILDEAWNELSWSERCVIRYYPSKQAIFTQKDLP` `MQSEADLGGRYSESVISSYEWSKQQAKGVK -> GKKLSSADLGRGMERVKLVGALCYKILPVKASNLYTERFA` `NAKRSRFRRQIQRVGHILLRVEQTASKRSER (in isoform PIPO).`	`VSP_034776`
`VAR_SEQ`	`1052 3163`		`Missing (in isoform PIPO).`	`VSP_034777`
`CONFLICT`	`2862 2862`		`E -> G (in Ref. 2; BAA01452).`

Sequence information

Length: 3163 AA [This is the length of the unprocessed precursor]

Molecular weight: 357822 Da [This is the MW of the unprocessed precursor]

CRC64: 61B0F73B58DF6D59 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAVTFASAI TNAITNKTTS TGMVQFGSFP PMPLRSTTVT TVATPVGQPK LYTVRFGSLD 

        70         80         90        100        110        120 
PVIVKGGAGS LAKATRQQPS VEIDVSLSEA AALEVAKPKS SAVLRMHEEA NKERALFLDW 

       130        140        150        160        170        180 
EASLKRRSYG IAENEKVVMT TRGVSKIVPR SSRAMKQKRA RERRRAQQPI ILKWEPKLSG 

       190        200        210        220        230        240 
FSIGGGFSAS AIEAEEVRTK WPLHKTPSMK KRMVHKTCKM SDQGVDMLIR SLVKIFKAKS 

       250        260        270        280        290        300 
ANIEYIGKKP IKVDFIRKER TKFARIQVAH LLGKRAQRDL LAGMEENHFI DILSEYSGNG 

       310        320        330        340        350        360 
TTINPGVVCA GWSGIVVRNE TLTQKRSRSP SKAFVIRGEH EDKLYDARIK ITKTMSLKIV 

       370        380        390        400        410        420 
HFSARGANFW KGFDRCFLAY RSDNREHTCY SGLDVTECGE VAALMCLAMF PCGKITCPDC 

       430        440        450        460        470        480 
VIDSELSQGQ ASGPSMKHRL TQLRDVIKSS YPRFKHAVQI LDRYEQSLSS ANENYQDFAE 

       490        500        510        520        530        540 
IQSISDGVEK AAFPHVNKLN AILIKGATAT GEEFSQATKH LLEIARYLKN RTENIEKGSL 

       550        560        570        580        590        600 
KSFRNKVSQK AHINPTLMCD NQLDKNGNFI WGERGYHAKR FFSNYFEIID PKKGYTQYET 

       610        620        630        640        650        660 
RVVPNGSRKL AIGKLIVPTN FEVLREQMRG EPVEPYPVTV ECVSKSQGDF VHACCCVTTE 

       670        680        690        700        710        720 
SGDPVLSEIK MPTKHHLVIG NSGDPKYIDL PEIEENKMYI AKEGYCYINI FLAMLVNVKE 

       730        740        750        760        770        780 
SQAKEFTKVV RDKLVSELGK WPTLLDVATA CYFLKVFYPD VANAELPRML VDHKTKIIHV 

       790        800        810        820        830        840 
VDSYGSLSTG YHVLKTNTVE QLIKFTRCNL ESSLKHYRVG GTEWENAHGA DNIDNPQWCI 

       850        860        870        880        890        900 
KRLVKGVYRP KQLKEDMLAN PFLPLYALLS PGVILAFYNS GSLEHLMNHY ISADSNVAVL 

       910        920        930        940        950        960 
LVVLKSLAKK VSTSQSVLAQ LQIIERSLPE LIEAKANING PDDAATRACN RFMGMLLHMA 

       970        980        990       1000       1010       1020 
EPNYELANGG YTFLRDHSIS ILEKSYLQIL DEAWNELSWS ERCVIRYYPS KQAIFTQKDL 

      1030       1040       1050       1060       1070       1080 
PMQSEADLGG RYSESVISSY EWSKQQAKGV KDSVVNKLRS SMSWTSSKVS NSVCRTINYL 

      1090       1100       1110       1120       1130       1140 
VPDVFKFMNV LVCISLLIKM TAEANHIITT QRRLKLDIEE TERKKIEWEL AFHHNILTHS 

      1150       1160       1170       1180       1190       1200 
ASQHPTLDEF TAYIAEKAPH LSEHIEPEEK EVVHQAKRQS EQELERVIAF VALVLMMFDA 

      1210       1220       1230       1240       1250       1260 
ERSDCVTKIL NKLKGLVATV EPTVYHQTLN EIEDDLNERN LFVDFELSSD SEMLQQLPAE 

      1270       1280       1290       1300       1310       1320 
KTFASWWSHQ LSRGFTIPHY RTEGKFMTFT RATATEVAGK IAHESDKDIL LMGAVGSGKS 

      1330       1340       1350       1360       1370       1380 
TGLPYHLSRK GNVLLLEPTR PLAENVHKQL SQAPFHQNTT LRMRGLTAFG SAPISVMTSG 

      1390       1400       1410       1420       1430       1440 
FALNYFANNR SRIEEFDFVI FDECHVHDAN AMAMRCLIHE CDYSGKIIKV SATPPGREVE 

      1450       1460       1470       1480       1490       1500 
FSTQYPVSIS TEDTLSFQDF VNAQGSGSNC DVISKGDNIL VYVASYNEVD TLSKLLIERD 

      1510       1520       1530       1540       1550       1560 
FKVTKVDGRT MKVGNIEITT SGTPSRKHFI VATNIIENGV TLDIDVVADF GTKVLPYLDT 

      1570       1580       1590       1600       1610       1620 
DNRMLSTTKT SINYGERIQR LGRVGRHKPG HALRIGHTER GLSEVPSCIA TEAALKCFTY 

      1630       1640       1650       1660       1670       1680 
GLPVITNNVS TSILGNVTVK QARTMSVFEI TPFYTSQVVR YDGSMHPQVH ALLKRFKLRD 

      1690       1700       1710       1720       1730       1740 
SEIVLTKLAI PNRGVNAGSQ PVSMHDSVQM LKIGVTLRIP FMCRDIPEKL HLDMWDVVVK 

      1750       1760       1770       1780       1790       1800 
FKGDAGFGRL SSSASKVAYT LQTDVNSIQR TVTIIDTLIA EERRKQEYFK TVTSNCVSSS 

      1810       1820       1830       1840       1850       1860 
NFSLQSITNA IKSRMMKDHP CENISVLEGA KSQLLEFRNL NSDHSFVTKT DGISRSFMRD 

      1870       1880       1890       1900       1910       1920 
YGALEAVNHQ STNEMSKFLQ LKGKWNKTLI TRDVLVICGV LGGGVWMVVQ HFRSKVSEPV 

      1930       1940       1950       1960       1970       1980 
THEAKGKKQR QKLKFRNARD NKMGREVYGD DDTIEHFFGD AYTKKGKSKG RTRGIGHKNR 

      1990       2000       2010       2020       2030       2040 
KFINMYGFDP EDFSAVRFVD PLTGATLDDN PFTDITLVQK HFGDIRMDLL GEDELDSNEI 

      2050       2060       2070       2080       2090       2100 
RMNKTIQAYY MNNKTGKALK VDLTPHIPLK VCDLHATIAG FPERENELRQ TGKAQPINID 

      2110       2120       2130       2140       2150       2160 
EVPRANNELV PVDHESNSMF RGLRDYNPIS NNICHLTNVS DGASNSLYGV GFGPLILTNR 

      2170       2180       2190       2200       2210       2220 
HLFERNNGEL IIKSRHGEFV IKNTTQLHLL PIPDRDLLLI RLPKDVPPFP QKLGFRQPEK 

      2230       2240       2250       2260       2270       2280 
GERICMVGSN FQTKSITSIV SETSTIMPVE NSQFWKHWIS TKDGQCGSPM VSTKDGKILG 

      2290       2300       2310       2320       2330       2340 
LHSLANFQNS INYFAAFPDD FTEKYLHTIE AHEWVKHWKY NTSAISWGSL NIQASQPVSL 

      2350       2360       2370       2380       2390       2400 
FKVSKLISDL DSTAVYAQTQ QNRWMFEQLT GNLKAIAHCP SQLVTKHTVK GKCQMFDLYL 

      2410       2420       2430       2440       2450       2460 
KLHDEAREYF QPMLGQYQKS KLNREAYAKD LLKYATPIEA GNIDCDLFEK TVEIVISDLR 

      2470       2480       2490       2500       2510       2520 
GYGFETCNYV TDENDIFEAL NMKSAVGALY KGKKKDYFAE FTPEVKEEIL KQSCERLFLG 

      2530       2540       2550       2560       2570       2580 
KMGVWNGSLK AELRPLEKVE ANKTRTFTAA PLDTLLGGKV CVDDFNNQFY DHNLRAPWDV 

      2590       2600       2610       2620       2630       2640 
GMTKFYCGWD RLLESLPDGW VYCDADGSQF DSSLSPYLIN AVLNIRLGFM EEWDVGEVML 

      2650       2660       2670       2680       2690       2700 
RNLYTEIVYT PISTPDGTLV KKFKGNNSGQ PSTVVDNTLM VILAVNYSLK KGGIPSELRD 

      2710       2720       2730       2740       2750       2760 
SIIRFFVNGD DLLLSVHPEY EYILDTMADN FRELGLKYTF DSRTREKGDL WFMSHQGHRR 

      2770       2780       2790       2800       2810       2820 
EGIWIPKLEP ERIVSILEWD RSKEPCHRLE AICAAMIESW GYDKLTHEIR KFYAWMIEQA 

      2830       2840       2850       2860       2870       2880 
PFSSLAQEGK APYIAETALR KLYLDKEPAQ EDLTQYLQAI FEDYEDGVEA CVYHQAGETL 

      2890       2900       2910       2920       2930       2940 
DADLTEEQKQ AEKEKKEREK AEKERERQKQ LAFKKGKDVA QEEGKRDKEV NAGTSGTFSV 

      2950       2960       2970       2980       2990       3000 
PRLKSLTSKM RVPRYEKRVA LNLDHLILYT PEQTDLSNTR STRKQFDTWF EGVMADYELT 

      3010       3020       3030       3040       3050       3060 
EDKMQIILNG LRVWCIENGT SPNINGMWVM MDGDDQVEFP IKPLIDHAKP TFRQIMAHFS 

      3070       3080       3090       3100       3110       3120 
DVAEAYIEKR NQDRPYMPRY GLQRNLTDMS LARYAFDFYE MTSRTPIRAR EAHIQMKAAA 

      3130       3140       3150       3160 
LRGANNNLFG LDGNVGTTVE NTERHTTEDV NRNMHNLLGV QGL

Q02597 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools