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Protein

Maternal protein tudor

Gene

tud

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

Functioni

Required during oogenesis for the formation of primordial germ cells and for normal abdominal segmentation.

GO - Biological processi

  • germ cell development Source: FlyBase
  • intracellular mRNA localization Source: FlyBase
  • mitochondrial rRNA export from mitochondrion Source: FlyBase
  • P granule organization Source: FlyBase
  • pole cell development Source: FlyBase
  • pole cell fate determination Source: FlyBase
  • pole plasm assembly Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Oogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Maternal protein tudor
Gene namesi
Name:tud
ORF Names:CG9450
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0003891. tud.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • mitochondrion Source: FlyBase
  • nucleus Source: FlyBase
  • P granule Source: FlyBase
  • pole plasm Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 25152515Maternal protein tudorPRO_0000183160Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei226 – 2261Phosphoserine1 Publication
Modified residuei235 – 2351Phosphoserine1 Publication
Modified residuei239 – 2391Phosphoserine1 Publication
Modified residuei800 – 8001Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP25823.
PRIDEiP25823.

PTM databases

iPTMnetiP25823.

Expressioni

Developmental stagei

Expressed throughout the life cycle.

Gene expression databases

BgeeiP25823.
GenevisibleiP25823. DM.

Interactioni

Subunit structurei

Interacts with vls.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AGO3Q7PLK05EBI-498741,EBI-3431981
aubO769227EBI-498741,EBI-98862

Protein-protein interaction databases

BioGridi63051. 5 interactions.
IntActiP25823. 4 interactions.
MINTiMINT-1334222.
STRINGi7227.FBpp0071508.

Structurei

Secondary structure

1
2515
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1982 – 19909Combined sources
Beta strandi1993 – 19986Combined sources
Helixi1999 – 20013Combined sources
Helixi2002 – 201413Combined sources
Beta strandi2029 – 20335Combined sources
Turni2035 – 20373Combined sources
Beta strandi2040 – 20489Combined sources
Beta strandi2054 – 20585Combined sources
Turni2059 – 20613Combined sources
Beta strandi2064 – 20685Combined sources
Helixi2075 – 20773Combined sources
Beta strandi2085 – 20895Combined sources
Helixi2093 – 20975Combined sources
Helixi2099 – 211113Combined sources
Turni2112 – 21154Combined sources
Beta strandi2116 – 21238Combined sources
Beta strandi2126 – 21283Combined sources
Beta strandi2130 – 21378Combined sources
Helixi2143 – 215917Combined sources
Beta strandi2164 – 217411Combined sources
Beta strandi2177 – 21826Combined sources
Helixi2183 – 21853Combined sources
Helixi2186 – 21949Combined sources
Beta strandi2217 – 22204Combined sources
Turni2221 – 22244Combined sources
Beta strandi2225 – 22284Combined sources
Beta strandi2231 – 22344Combined sources
Beta strandi2241 – 22444Combined sources
Turni2246 – 22483Combined sources
Beta strandi2251 – 22555Combined sources
Turni2262 – 22665Combined sources
Beta strandi2272 – 22776Combined sources
Helixi2285 – 229713Combined sources
Beta strandi2304 – 23096Combined sources
Beta strandi2318 – 23247Combined sources
Helixi2329 – 23379Combined sources
Helixi2344 – 23474Combined sources
Beta strandi2349 – 235810Combined sources
Beta strandi2361 – 23666Combined sources
Helixi2367 – 23693Combined sources
Helixi2370 – 238314Combined sources
Helixi2384 – 23863Combined sources
Beta strandi2398 – 24025Combined sources
Turni2404 – 24063Combined sources
Beta strandi2409 – 24179Combined sources
Beta strandi2419 – 24213Combined sources
Beta strandi2423 – 24264Combined sources
Turni2428 – 24303Combined sources
Beta strandi2433 – 24375Combined sources
Helixi2444 – 24474Combined sources
Beta strandi2452 – 24587Combined sources
Helixi2460 – 24623Combined sources
Helixi2465 – 247612Combined sources
Turni2477 – 24804Combined sources
Beta strandi2481 – 249010Combined sources
Beta strandi2492 – 24943Combined sources
Beta strandi2496 – 25027Combined sources
Helixi2507 – 25104Combined sources
Turni2512 – 25143Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NTHX-ray2.80A2344-2515[»]
3NTIX-ray2.80A2344-2515[»]
3NTKX-ray1.80A/B2346-2514[»]
4Q5WX-ray1.80A/B1978-2160[»]
4Q5YX-ray3.00A2164-2515[»]
ProteinModelPortaliP25823.
SMRiP25823. Positions 1978-2160, 2164-2515.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25823.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini455 – 51359Tudor 1PROSITE-ProRule annotationAdd
BLAST
Domaini641 – 69656Tudor 2PROSITE-ProRule annotationAdd
BLAST
Domaini1062 – 112261Tudor 3PROSITE-ProRule annotationAdd
BLAST
Domaini1355 – 141460Tudor 4PROSITE-ProRule annotationAdd
BLAST
Domaini1662 – 171857Tudor 5PROSITE-ProRule annotationAdd
BLAST
Domaini1839 – 189860Tudor 6PROSITE-ProRule annotationAdd
BLAST
Domaini2023 – 208260Tudor 7PROSITE-ProRule annotationAdd
BLAST
Domaini2211 – 226959Tudor 8PROSITE-ProRule annotationAdd
BLAST
Domaini2392 – 245160Tudor 9PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 9 Tudor domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IPR2. Eukaryota.
ENOG410ZHUW. LUCA.
GeneTreeiENSGT00730000110295.
InParanoidiP25823.
KOiK18405.
OMAiPRSFYVQ.
OrthoDBiEOG7VQJC5.
PhylomeDBiP25823.

Family and domain databases

InterProiIPR002999. Tudor.
[Graphical view]
PfamiPF00567. TUDOR. 9 hits.
[Graphical view]
SMARTiSM00333. TUDOR. 10 hits.
[Graphical view]
PROSITEiPS50304. TUDOR. 9 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25823-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGQARIALP SKVDLYITHV DHVGPYLKVY GHVNRDAASL ISERIRNLLP
60 70 80 90 100
TCFAIEPSWS VERQQALLIP GTFCIFKNIN GPAPGDVEYR RIRVVSADLE
110 120 130 140 150
GQSMRAEIDF VDFGYKRTVD SHDLMFPKQP KLLQNIPLHC FQYIVLGICS
160 170 180 190 200
EWDQTDLAEV RRLVVNQIVK ITVEPTQICD QKFASLRWKD FELNEFLVQQ
210 220 230 240 250
KQIGVSVDKQ LMMDHCKKLW KDNPQSPVTE YNNNSIHNSK TPMEIAREQL
260 270 280 290 300
AVRQSLAARL DAQRSVQVTP SRPLNADAPD YTPKHLPLVN VTNVQVQMPG
310 320 330 340 350
LNNTQKPVFV STNPYNRANY QPAVPAAQPY VPKANPRSQY TYYNVRMNKP
360 370 380 390 400
INAMPPPAGP HVPIQHFNQQ ANNVSLSYVP ARFTPPPTPS IAQHQIPIPA
410 420 430 440 450
FRTTSLTVGL TYDVVISYVE NGPYLFWVHL KSSDHDLSTM MGQIERTKLK
460 470 480 490 500
ALAQAPELGT ACVARFSEDG HLYRAMVCAV YAQRYRVVYV DYGNSELLSA
510 520 530 540 550
SDLFQIPPEL LEIKPFAFRF ALAGTKEIEP IDDSMKRIFK KSAIYRNFEL
560 570 580 590 600
TVQAPESVGS MQTCHLNQNG TNMLELLRQL KNSRQSYKKA EQLENDDAVE
610 620 630 640 650
IRFIDSPSNF YVQKVANIGK FEQLMDEMFS YYNANQRVPD QLILGAPCIV
660 670 680 690 700
KCDQEWYRAE ILRVDDSVIV RHVDFGYEQN VKRHLIGHIA EKHLEMPRQA
710 720 730 740 750
IKCCLKGFEN SELSEDKITD QFEMLAEESN IRRRTFSVRI FRIEPDGLNV
760 770 780 790 800
VNLLAKNLNV MKKLYKLSMP FEQYLSLEKG QFNANNTRAE SVISSELNKS
810 820 830 840 850
HILNSTSIGE TENRLQEQEK EQQQKKVDVR QQQLAVEIPQ AVKSVSGSKN
860 870 880 890 900
STDWDKRSST SAGSKDSKRQ QQQQIQRIDR HLDFSCETQS TGSYSSGMSS
910 920 930 940 950
PRKGNRQQNG RTPIQSPRHN EKQEAKKNAR FSNSESPRRS RDGQQGNQRS
960 970 980 990 1000
QNAPQGYAQK PQRQKSTLDG NISSKRSSGV GSDIASSSSE SVAAAKPEKY
1010 1020 1030 1040 1050
VSLDKPYALQ EMKTPSKEAA SLSWWLSPFQ FYIVPKSVSA KYDNIMRDMR
1060 1070 1080 1090 1100
EFYRQKQHQP LQLKVGSTVV VRQRKDNAIL RATVTACNHM MRKYRVFCVD
1110 1120 1130 1140 1150
TGSLITVTSE DIWQLEQRFA DPPCMAHRCS FHSVVTNYDP LYIVDRMETF
1160 1170 1180 1190 1200
VPVNAKVDCE FVSKEKSNQG SNTSSTCSYT VNIFVNGASL RDMLVKAEFL
1210 1220 1230 1240 1250
TEVAPEIRVN LLAGQQIRGK FTSIRDMTSF KVQFDYGNNV NFLCTYDDAK
1260 1270 1280 1290 1300
FVKSNPNLAR RFKEFYEGKS FALNVKNVCE NNIVHLRPVM PLFMEDRRSF
1310 1320 1330 1340 1350
ICPYPVVLSS FQALVVYTAK PYRVYVQPQA IVPSMQTLLD NMYEHYKAKG
1360 1370 1380 1390 1400
DSLKKFDVGQ ICAVRSSDGN WYRARISGKD SNAACFEVFY IDYGNTEEIK
1410 1420 1430 1440 1450
RDDIKALDAK FYEHASGFAV EINLPIGRPS NDTKLKARIS EILEEKVVTI
1460 1470 1480 1490 1500
KSIEVRRSHL IADVILENNQ SVIDLLKAEK LVPGKDLDYM RKQMEKGKSR
1510 1520 1530 1540 1550
TYEYIETVDL TLDEEEDKGR KETVSKSGSA NASPKKKQHN DKDREPKKSK
1560 1570 1580 1590 1600
PAEPARTVAP QPVALKTPSP VPAEPAPVPK PATPVPEVVE VPEINPTVRE
1610 1620 1630 1640 1650
AAAESKQAPA QEDPYKDLDC VVLSHCDNPA QFYVHPIDQL SKLNQLHENL
1660 1670 1680 1690 1700
QIVSPSLPQL MNVVNGADCV SMYSVDKCWY RAKIIDAELM VLLFIDYGNT
1710 1720 1730 1740 1750
DCVSDATDIK ESMWSHIEPF CLPCALPIRP KGTADWVDAA NGIFNESYSK
1760 1770 1780 1790 1800
VPRLEYLTQG DHYTTSYVNM YIDGEDVAKK LIADGFARPL EYLASGCSCY
1810 1820 1830 1840 1850
ISHVNGICDF FIQLERDSKA LELIELYLRK KDTLKPLEGF EKGLIVAALF
1860 1870 1880 1890 1900
EDDELWYRAQ LQKELPDSRY EVLFIDYGNT STTSKCLMLS EEIASLPSLS
1910 1920 1930 1940 1950
KKCSLQLPDA YISWSPEAEA KFAELTGEGE LVFTTQLLKP GQDHVTIDLL
1960 1970 1980 1990 2000
LDGENIIDRL LPLCQRKEPK EASKESLAVT TKAIITHVEN TSRIYLQFSE
2010 2020 2030 2040 2050
KDSLMDIICE KLNGSKLQPK TEKAAVDDMC VVQFADDLEF YRSRILEVLE
2060 2070 2080 2090 2100
DDQYKVILID YGNTTVVDKL YELPQEFTLI KPVAEICSME PSAIFEKNKA
2110 2120 2130 2140 2150
LTLTTFDALL DSCKGVVAVE FVNKSASPPV VRLTTKDKRS LKIYEHLQKL
2160 2170 2180 2190 2200
VQAELKLIQK RNENSECIIS YGNSPKSFYV QMKHNSADLD LIVKTLQSLK
2210 2220 2230 2240 2250
KEKLKKLIDP TTNSNGVCYS QEDACYYRCS IKSVLDPSQG FEVFLLDYGN
2260 2270 2280 2290 2300
TLVVPEVWQL PQEIEPIPSL ALHCQLSKIP MDVSDEKLEE AFAALLEQHF
2310 2320 2330 2340 2350
GELYEITTQP NEDETKPLIA ELRINYKDFV QELVSTVTGV QKPLEAELHN
2360 2370 2380 2390 2400
CVVVQFDGPM SFYVQMESDV PALEQMTDKL LDAEQDLPAF SDLKEGALCV
2410 2420 2430 2440 2450
AQFPEDEVFY RAQIRKVLDD GKCEVHFIDF GNNAVTQQFR QLPEELAKPA
2460 2470 2480 2490 2500
RYSRHCELDA STISKCDAAL LQSFIDTRFS ETFQVEILAT KGTGTHVVRL
2510
FYQSKNISEK LQECQ
Length:2,515
Mass (Da):285,267
Last modified:August 30, 2005 - v2
Checksum:i1218700174D66701
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti116 – 1161K → N in CAA44286 (PubMed:1936993).Curated
Sequence conflicti635 – 6384NQRV → TREF in CAA44286 (PubMed:1936993).Curated
Sequence conflicti1763 – 17631Y → I in CAA44286 (PubMed:1936993).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62420 mRNA. Translation: CAA44286.1.
AE013599 Genomic DNA. Translation: AAF46693.1.
PIRiA41519.
RefSeqiNP_476773.1. NM_057425.3.

Genome annotation databases

EnsemblMetazoaiFBtr0071582; FBpp0071508; FBgn0003891.
GeneIDi37417.
KEGGidme:Dmel_CG9450.
UCSCiCG9450-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62420 mRNA. Translation: CAA44286.1.
AE013599 Genomic DNA. Translation: AAF46693.1.
PIRiA41519.
RefSeqiNP_476773.1. NM_057425.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NTHX-ray2.80A2344-2515[»]
3NTIX-ray2.80A2344-2515[»]
3NTKX-ray1.80A/B2346-2514[»]
4Q5WX-ray1.80A/B1978-2160[»]
4Q5YX-ray3.00A2164-2515[»]
ProteinModelPortaliP25823.
SMRiP25823. Positions 1978-2160, 2164-2515.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63051. 5 interactions.
IntActiP25823. 4 interactions.
MINTiMINT-1334222.
STRINGi7227.FBpp0071508.

PTM databases

iPTMnetiP25823.

Proteomic databases

PaxDbiP25823.
PRIDEiP25823.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0071582; FBpp0071508; FBgn0003891.
GeneIDi37417.
KEGGidme:Dmel_CG9450.
UCSCiCG9450-RA. d. melanogaster.

Organism-specific databases

CTDi37417.
FlyBaseiFBgn0003891. tud.

Phylogenomic databases

eggNOGiENOG410IPR2. Eukaryota.
ENOG410ZHUW. LUCA.
GeneTreeiENSGT00730000110295.
InParanoidiP25823.
KOiK18405.
OMAiPRSFYVQ.
OrthoDBiEOG7VQJC5.
PhylomeDBiP25823.

Miscellaneous databases

ChiTaRSitud. fly.
EvolutionaryTraceiP25823.
GenomeRNAii37417.
PROiP25823.

Gene expression databases

BgeeiP25823.
GenevisibleiP25823. DM.

Family and domain databases

InterProiIPR002999. Tudor.
[Graphical view]
PfamiPF00567. TUDOR. 9 hits.
[Graphical view]
SMARTiSM00333. TUDOR. 10 hits.
[Graphical view]
PROSITEiPS50304. TUDOR. 9 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Tudor, a posterior-group gene of Drosophila melanogaster, encodes a novel protein and an mRNA localized during mid-oogenesis."
    Golumbeski G.S., Bardsley A., Tax F., Boswell R.E.
    Genes Dev. 5:2060-2070(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "Valois, a component of the nuage and pole plasm, is involved in assembly of these structures, and binds to Tudor and the methyltransferase Capsuleen."
    Anne J., Mechler B.M.
    Development 132:2167-2177(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VLS.
  5. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-235; SER-239 AND SER-800, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiTUD_DROME
AccessioniPrimary (citable) accession number: P25823
Secondary accession number(s): Q9W2J8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: August 30, 2005
Last modified: June 8, 2016
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

The TUD mRNA accumulates within the posterior region of the developing oocyte during the early to middle stages of oogenesis.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.