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Protein

Serine protease nudel

Gene

ndl

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the extracellular signaling pathway that establishes the dorsal-ventral pathway of the embryo. Three proteases; ndl, gd and snk process easter to create active easter. Active easter defines cell identities along the dorsal-ventral continuum by activating the spz ligand for the Tl receptor in the ventral region of the embryo. Nudel, pipe and windbeutel together trigger the protease cascade within the extraembryonic perivitelline compartment which induces dorsoventral polarity of the Drosophila embryo.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1185Charge relay systemBy similarity1
Active sitei1233Charge relay systemBy similarity1
Active sitei1332Charge relay systemBy similarity1

GO - Molecular functioni

  • peptidase activity Source: FlyBase
  • serine-type endopeptidase activity Source: FlyBase
  • serine-type peptidase activity Source: FlyBase

GO - Biological processi

  • dorsal/ventral axis specification Source: FlyBase
  • egg activation Source: FlyBase
  • eggshell chorion assembly Source: FlyBase
  • maternal specification of dorsal/ventral axis, oocyte, soma encoded Source: FlyBase
  • oocyte dorsal/ventral axis specification Source: FlyBase
  • protein processing Source: FlyBase
  • proteolysis Source: FlyBase
  • Toll signaling pathway Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS01.013.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine protease nudel (EC:3.4.21.-)
Gene namesi
Name:ndl
ORF Names:CG10129
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0002926. ndl.

Subcellular locationi

  • Secretedextracellular spaceextracellular matrix 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 43Sequence analysisAdd BLAST43
ChainiPRO_000002813644 – 2616Serine protease nudelAdd BLAST2573

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei215Phosphoserine1 Publication1
Modified residuei220Phosphoserine1 Publication1
Glycosylationi291N-linked (GlcNAc...)Sequence analysis1
Glycosylationi347N-linked (GlcNAc...)Sequence analysis1
Glycosylationi379N-linked (GlcNAc...)Sequence analysis1
Glycosylationi417N-linked (GlcNAc...)Sequence analysis1
Glycosylationi492N-linked (GlcNAc...)Sequence analysis1
Glycosylationi515N-linked (GlcNAc...)Sequence analysis1
Modified residuei574Phosphoserine1 Publication1
Modified residuei581Phosphoserine1 Publication1
Glycosylationi598N-linked (GlcNAc...)Sequence analysis1
Glycosylationi794O-linked (Xyl...) (glycosaminoglycan)Sequence analysis1
Glycosylationi827N-linked (GlcNAc...)Sequence analysis1
Glycosylationi829O-linked (Xyl...) (glycosaminoglycan)Sequence analysis1
Glycosylationi861N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi891 ↔ 905By similarity
Disulfide bondi899 ↔ 918By similarity
Disulfide bondi912 ↔ 927By similarity
Disulfide bondi957 ↔ 982By similarity
Disulfide bondi964 ↔ 995By similarity
Glycosylationi975N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi989 ↔ 1004By similarity
Glycosylationi1064N-linked (GlcNAc...)Sequence analysis1
Modified residuei1134Phosphoserine1 Publication1
Modified residuei1136Phosphoserine1 Publication1
Disulfide bondi1170 ↔ 1186By similarity
Disulfide bondi1276 ↔ 1338Sequence analysis
Disulfide bondi1305 ↔ 1317By similarity
Disulfide bondi1328 ↔ 1359By similarity
Disulfide bondi1396 ↔ 1408By similarity
Disulfide bondi1401 ↔ 1421By similarity
Disulfide bondi1415 ↔ 1430By similarity
Glycosylationi1445N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1728 ↔ 1745By similarity
Disulfide bondi1734 ↔ 1764By similarity
Disulfide bondi1758 ↔ 1773By similarity
Disulfide bondi1776 ↔ 1789By similarity
Disulfide bondi1783 ↔ 1802By similarity
Disulfide bondi1796 ↔ 1811By similarity
Glycosylationi1878N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1956N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2023N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2055 ↔ 2071By similarity
Glycosylationi2144N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2173N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2177 ↔ 2230By similarity
Glycosylationi2197N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2237N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2269N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2310 ↔ 2320By similarity
Disulfide bondi2315 ↔ 2333By similarity
Disulfide bondi2327 ↔ 2344By similarity
Disulfide bondi2351 ↔ 2364By similarity
Disulfide bondi2358 ↔ 2377By similarity
Disulfide bondi2371 ↔ 2387By similarity
Glycosylationi2420N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2421 ↔ 2435By similarity
Disulfide bondi2428 ↔ 2448By similarity
Disulfide bondi2442 ↔ 2457By similarity
Glycosylationi2556N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2601N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Requires cleavage for activation (presumably).1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

PaxDbiP98159.
PRIDEiP98159.

PTM databases

iPTMnetiP98159.

Expressioni

Tissue specificityi

Follicle.1 Publication

Gene expression databases

BgeeiFBgn0002926.
GenevisibleiP98159. DM.

Interactioni

Protein-protein interaction databases

BioGridi64189. 1 interactor.
IntActiP98159. 3 interactors.
STRINGi7227.FBpp0076693.

Structurei

3D structure databases

ProteinModelPortaliP98159.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati261 – 269WIID 19
Repeati320 – 328WIID 29
Repeati399 – 407WIID 39
Repeati446 – 454WIID 49
Repeati477 – 485WIID 59
Repeati528 – 536WIID 69
Domaini889 – 929LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST41
Domaini929 – 956LDL-receptor class A 2; truncatedPROSITE-ProRule annotationAdd BLAST28
Domaini955 – 1006LDL-receptor class A 3PROSITE-ProRule annotationAdd BLAST52
Domaini1145 – 1383Peptidase S1 1PROSITE-ProRule annotationAdd BLAST239
Domaini1394 – 1432LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST39
Domaini1713 – 1743LDL-receptor class A 5; truncatedPROSITE-ProRule annotationAdd BLAST31
Domaini1745 – 1775LDL-receptor class A 6; truncatedPROSITE-ProRule annotationAdd BLAST31
Domaini1774 – 1813LDL-receptor class A 7PROSITE-ProRule annotationAdd BLAST40
Domaini2027 – 2301Peptidase S1 2PROSITE-ProRule annotationAdd BLAST275
Domaini2308 – 2346LDL-receptor class A 8PROSITE-ProRule annotationAdd BLAST39
Domaini2349 – 2389LDL-receptor class A 9PROSITE-ProRule annotationAdd BLAST41
Domaini2387 – 2419LDL-receptor class A 10; truncatedPROSITE-ProRule annotationAdd BLAST33
Domaini2419 – 2459LDL-receptor class A 11PROSITE-ProRule annotationAdd BLAST41

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1031 – 1033Cell attachment siteSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1489 – 1702Ser/Thr-richAdd BLAST214

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 11 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 2 peptidase S1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00860000133744.
InParanoidiP98159.
OMAiCEDMTDE.
OrthoDBiEOG091G0DF7.
PhylomeDBiP98159.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
Gene3Di4.10.400.10. 7 hits.
InterProiIPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR009003. Peptidase_S1_PA.
IPR015420. Peptidase_S1A_nudel.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF09342. DUF1986. 1 hit.
PF00057. Ldl_recept_a. 4 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00192. LDLa. 9 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF57424. SSF57424. 7 hits.
PROSITEiPS01209. LDLRA_1. 6 hits.
PS50068. LDLRA_2. 8 hits.
PS50240. TRYPSIN_DOM. 2 hits.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P98159-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNYNMDEMEA TRLLRHPRRW WSIGFGKRIV AISILVIIVL LFSLVYHGLV
60 70 80 90 100
VEKIDQVQQI AALNARHQVL FNQPFEEDQS ALIVSPQTLH FKLLDEDMNK
110 120 130 140 150
DMEDSKNRRR KHMRQMLVKF RLNKKHRMRR DLHGLDLLDP VRMEANMQHL
160 170 180 190 200
YTKLRSKRAR EALSQLEHEF VRCKKHTPQD CMSAFLRMYK MAKEVTEKME
210 220 230 240 250
KMKAIMREQQ PKLESSSMES HEQKGTFSPA DLIQVTTAEA TTVAVHATEK
260 270 280 290 300
PARTKIKPSR ISWIIDGHDH DESPVYTDGA PKKETTKAPW NTTQLVEITT
310 320 330 340 350
TKIDATATER TTVESTTEKI SWILDHFDKP QEILRTTEGP GQRIIRNVTT
360 370 380 390 400
TSASSEPIVD TENTNSDHVP TTENGLVFNI TTDGPVETTK STAQRKLSFD
410 420 430 440 450
WILDGEENVE PEVKSTNTTT TTAATTTTGA TSETIIVTTE LPKITFDWII
460 470 480 490 500
DGREVVEPQE TTTEVTGTTE RLRKMPFDWI IDGEEVVEPQ ENVTTTTIAT
510 520 530 540 550
TVAVSTTEIN ERIHNSTAYP TKPKPVKFDW IIDGGESSGE VSTSSTSQPK
560 570 580 590 600
LTTREAISNP ESPRSSHPLD NPTSIENMLE SFEQHEEQKP ILRVLNANES
610 620 630 640 650
SSETVTDGYE RQLWLKKFED QARPNQNELI DTFGTALDAK ALDKMGPKIN
660 670 680 690 700
PLNGHTWNAA DAQILSLCER VALRMRNKVA TMSDGETKEK GETFTASPSV
710 720 730 740 750
QFTSRAPGGF PVSGETMKAS AQFMFNPNFG MPSIPVCFYM TPANFRMPMW
760 770 780 790 800
SNTPTFMGMQ GAHFGGSSNP GAGIFFVPQQ FGPSGNFFGG SGGSGAGGQG
810 820 830 840 850
ANIFSKNASP QKPTNGQQQV YCSYMQNQSG QGAGQSQTSS QQQQGGQSAF
860 870 880 890 900
SNANFKMRHA NQTNTANQQG QIIYASYAGL PQQPIQERSR CPEPDQFSCF
910 920 930 940 950
GQQECIPAAR WCDNVVDCSD GSDESACTCA DRVDEERLCD GYEDCPMGED
960 970 980 990 1000
ELGCFGCESL AYSCYENPQD FAKRNRSTIS MCYSRLERCD GFMNCLNGRD
1010 1020 1030 1040 1050
EEQCSMLVTD VADHMSHGAS ASEGYLYHNY RGDWHPVCNN GEKWAALACQ
1060 1070 1080 1090 1100
MDENSRMDHS ASLNVSFQTL TLPGPFIEPS LHAGVHFAQA CHGRNSHDSL
1110 1120 1130 1140 1150
VDHVAYVKCP PMQCGLPSKS SMLEHSKRVR RAVSDSKEIV GDGRIVGGSY
1160 1170 1180 1190 1200
TSALQWPFVV AIYRNGKFHC GGTIYSDRWI ISAAHCVINY GKYFYEVRAG
1210 1220 1230 1240 1250
LLRRSSYSPA TQIQPVSHVV VHQAYERRSM RNDLSLLRLL NPLQFNRWVK
1260 1270 1280 1290 1300
PICLPDKGRT TVGDDWIWGP VEHTLCTVVG WGAIREKGPS SDPMRQVIVP
1310 1320 1330 1340 1350
IRKKCTDPED QASEDICAGD PDGGRDACQG DSGGPLFCRS VSNPDEFYLA
1360 1370 1380 1390 1400
GVVSHGNGCA RPQEFGVYTR VTLYLDWLEM ATTPRLLPKL QPLQLCPGFI
1410 1420 1430 1440 1450
CVWGGKRCIA KRQRCDRNVD CLGGEDEVGC TYNFLPDMVG GVRQNISTTT
1460 1470 1480 1490 1500
ESDYHPVKES EEKSKMREVI PIDDEDLKAE QDEEDLLKST TSLGQTETTQ
1510 1520 1530 1540 1550
GPMDLSFAEQ ITSTTSDDLS ITDETTSTDF TVSDSATSPS TLLPTTTNPS
1560 1570 1580 1590 1600
TWLPSTNIET STFSFTTTES EASTKQETLP TTVAQTTTIP TSTEDLKKLT
1610 1620 1630 1640 1650
DLVTEFIEST TFETTMEVET TTLSLTSTDA PKLVTTEGVK ETTTTEDTTT
1660 1670 1680 1690 1700
ISSIVTLTTT PLATISTTIL TTEKHVAVTT LAPTTTTESA KTTTTHSSST
1710 1720 1730 1740 1750
HSEKDQIQIP NKFVCKKMSQ IVDIMMRCDR KVDCEDGTDE LDCTCKDYLK
1760 1770 1780 1790 1800
GSLKGLICDG KADCEDLTDE QNCVECQSNE FRCPLSKTCL PLSSRCDNKV
1810 1820 1830 1840 1850
DCKFKEDEKD CFALTNGHDV HFDVHQQPKF SSTGIFSRNG HGVWRVVCAH
1860 1870 1880 1890 1900
ETGYHEHQAK TADAVCALLG FNGAHYFNSS EFVTQHEMQP ITPELKGGRN
1910 1920 1930 1940 1950
RMSAQIHSMV GDNVQFTENE VIIPELGHPS ASRPEKDRLL PRKCVGIYVE
1960 1970 1980 1990 2000
CNPYSNKTTP LKTFSAGQVV KEKPIEQVPV LSPTIETHNT PNVHFKPQIP
2010 2020 2030 2040 2050
AMVVNKKDEI LDRLDKLIKS KKNKTILVNE QLHEAIEELH WPWLADVYMN
2060 2070 2080 2090 2100
GDLWCIGVLI DKHWVMVHES CLSGIDLETH YVSVLLGGGK TKRSAHRSNH
2110 2120 2130 2140 2150
EQIRRVDCFE GVPKSNVLLL HLERPVRFTH HVLPTFLPDS SHQNQSHARQ
2160 2170 2180 2190 2200
CISVLHDDAT GRIKTVAITR IHNATNCDSC YKLQEKQPPA NLMRLLNVSA
2210 2220 2230 2240 2250
EDMASISEEV ELINGVAPTE LPAITKFTTC NQFGLKNVSD AHHNPSDQGV
2260 2270 2280 2290 2300
LVCRDSHTGW FPTALFNYNN SDCQSFKQPF GIRTLELVYK SLQDIIDKPS
2310 2320 2330 2340 2350
CKMLLPAPDC STHRCPLGTC LPQAAMCNGR SDCHDGSDEE ETKCRQQKQQ
2360 2370 2380 2390 2400
CAPGEMKCRT SFKCVPKSKF CDHVPDCEDM TDEPTICSCF TYLQATDPSK
2410 2420 2430 2440 2450
ICDGKRNCWD KSDESSVLCN CTADHFQCSS SPEDCIPRDF VCDKEKDCPN
2460 2470 2480 2490 2500
GEDERYCFGI EHPLHLQKKD FWTNSQHTQP EIAPQYGQVI EQTYGIWHTK
2510 2520 2530 2540 2550
CFPKSKPPQV DEVREICKKL GYNPYRQPSY RLIDDEENKP VHTYELADRQ
2560 2570 2580 2590 2600
GRSFSNESLM GKYRDSTKAL IISKFSPLQL NERLTLFLKS SRPIAELVRW
2610
NATDSSMCYR LEIRCA
Length:2,616
Mass (Da):292,492
Last modified:May 10, 2004 - v2
Checksum:i052F92CBAE9EB163
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti83I → T in AAA83086 (PubMed:7671306).Curated1
Sequence conflicti120F → L in AAA83086 (PubMed:7671306).Curated1
Sequence conflicti363N → T in AAA83086 (PubMed:7671306).Curated1
Sequence conflicti831Q → R in AAA83086 (PubMed:7671306).Curated1
Sequence conflicti864N → S in AAA83086 (PubMed:7671306).Curated1
Sequence conflicti1150Y → H in AAA83086 (PubMed:7671306).Curated1
Sequence conflicti1344P → A in AAA83086 (PubMed:7671306).Curated1
Sequence conflicti1410A → S in AAA83086 (PubMed:7671306).Curated1
Sequence conflicti1607I → M in AAA83086 (PubMed:7671306).Curated1
Sequence conflicti1632K → I in AAA83086 (PubMed:7671306).Curated1
Sequence conflicti1670L → P in AAA83086 (PubMed:7671306).Curated1
Sequence conflicti1794S → K in AAA83086 (PubMed:7671306).Curated1
Sequence conflicti1863D → N in AAA83086 (PubMed:7671306).Curated1
Sequence conflicti1886 – 1888HEM → QEK in AAA83086 (PubMed:7671306).Curated3
Sequence conflicti1903S → A in AAA83086 (PubMed:7671306).Curated1
Sequence conflicti2147H → N in AAA83086 (PubMed:7671306).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29153 mRNA. Translation: AAA83086.1.
AE014296 Genomic DNA. Translation: AAF50656.1.
PIRiA57096.
RefSeqiNP_523947.2. NM_079223.2.
UniGeneiDm.2737.

Genome annotation databases

EnsemblMetazoaiFBtr0076984; FBpp0076693; FBgn0002926.
GeneIDi38738.
KEGGidme:Dmel_CG10129.
UCSCiCG10129-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29153 mRNA. Translation: AAA83086.1.
AE014296 Genomic DNA. Translation: AAF50656.1.
PIRiA57096.
RefSeqiNP_523947.2. NM_079223.2.
UniGeneiDm.2737.

3D structure databases

ProteinModelPortaliP98159.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi64189. 1 interactor.
IntActiP98159. 3 interactors.
STRINGi7227.FBpp0076693.

Protein family/group databases

MEROPSiS01.013.

PTM databases

iPTMnetiP98159.

Proteomic databases

PaxDbiP98159.
PRIDEiP98159.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0076984; FBpp0076693; FBgn0002926.
GeneIDi38738.
KEGGidme:Dmel_CG10129.
UCSCiCG10129-RA. d. melanogaster.

Organism-specific databases

CTDi38738.
FlyBaseiFBgn0002926. ndl.

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00860000133744.
InParanoidiP98159.
OMAiCEDMTDE.
OrthoDBiEOG091G0DF7.
PhylomeDBiP98159.

Miscellaneous databases

GenomeRNAii38738.
PROiP98159.

Gene expression databases

BgeeiFBgn0002926.
GenevisibleiP98159. DM.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
Gene3Di4.10.400.10. 7 hits.
InterProiIPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR009003. Peptidase_S1_PA.
IPR015420. Peptidase_S1A_nudel.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF09342. DUF1986. 1 hit.
PF00057. Ldl_recept_a. 4 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00192. LDLa. 9 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF57424. SSF57424. 7 hits.
PROSITEiPS01209. LDLRA_1. 6 hits.
PS50068. LDLRA_2. 8 hits.
PS50240. TRYPSIN_DOM. 2 hits.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNUDEL_DROME
AccessioniPrimary (citable) accession number: P98159
Secondary accession number(s): Q9VRX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 10, 2004
Last modified: November 30, 2016
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.