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Protein
Submitted name:

Uncharacterized protein

Gene

Dere\GG24263

Organism
Drosophila erecta (Fruit fly)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Protein inferred from homologyi

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseSAAS annotationImported, Hydrolase

Names & Taxonomyi

Protein namesi
Submitted name:
Uncharacterized proteinImported (EC:3.2.1.23Imported)
Gene namesi
Name:Dere\GG24263Imported
ORF Names:Dere_GG24263Imported, GG24263Imported
OrganismiDrosophila erecta (Fruit fly)Imported
Taxonomic identifieri7220 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000008711 Componenti: Unassembled WGS sequence

Organism-specific databases

FlyBaseiFBgn0116395. Dere\GG24263.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei12 – 3524HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Structurei

3D structure databases

ProteinModelPortaliB3N5A6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 376323Glyco_hydro_35InterPro annotationAdd
BLAST
Domaini599 – 63739BetaGal_dom4_5InterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 35 family.UniRule annotationSAAS annotation

Keywords - Domaini

Transmembrane, Transmembrane helixSequence analysis

Phylogenomic databases

KOiK12309.
OMAiIELWRRE.
OrthoDBiEOG7GXPCD.
PhylomeDBiB3N5A6.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR026283. B-gal_1-like.
IPR025300. BetaGal_jelly_roll_dom.
IPR008979. Galactose-bd-like.
IPR031330. Gly_Hdrlase_35_cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR001944. Glycoside_Hdrlase_35.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR23421. PTHR23421. 1 hit.
PfamiPF13364. BetaGal_dom4_5. 1 hit.
PF01301. Glyco_hydro_35. 1 hit.
[Graphical view]
PIRSFiPIRSF006336. B-gal. 1 hit.
PRINTSiPR00742. GLHYDRLASE35.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

B3N5A6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGCRYNGKL TIAISGCLII AVMALTVGLC VGLGGGTEAL EDQPRFTIDH
60 70 80 90 100
AANTFMLDGQ PFRYVSGSFH YFRAVPESWR SRLRTMRASG LNALDTYVEW
110 120 130 140 150
SLHNPHDGEY NWEGIADVVK FLEIAQQEDF YIILRPGPYI CAERDNGGLP
160 170 180 190 200
HWLFAKYPSI KMRTNDPNYI AEVGKWYAEL MPRLQHLFVG NGGKIIMVQV
210 220 230 240 250
ENEYGDYACD HDYLNWLRDE TEKYVTGKAL LFTVDIPNEK MSCGKIENVF
260 270 280 290 300
ATTDFGIDRI NEIDQIWAML RTLQPTGPLV NSEFYPGWLT HWQEQNQRRD
310 320 330 340 350
GQEVANALRT ILSYNASVNL YMFFGGTNFG FTAGANYNLD GGIGYAADIT
360 370 380 390 400
SYDYDAVMDE AGGVTTKYNL VKAVIGEFLP LPDITLNPAK RLAYGRVELT
410 420 430 440 450
PKLALLSTEG RAALSKGNPV ESIKPKTFEE LDLYSGLVLY ETELPSMDLD
460 470 480 490 500
PALLKIDQIN DRAHVFVDQE LVGTLSREAQ IYSLPLSKGW GSTLQLLVEN
510 520 530 540 550
QGRVNFYISN DTKGIFGEVS MQLHNGGYLP LENWRSTAFP LEQSAIELWR
560 570 580 590 600
REHSNQKVMD PLLARQRILR NGPILYTGSL TVTEVGDTYL NMAGWGKGVA
610 620 630 640 650
YVNGFNLGRY WPVAGPQVTL YVPNEILQVG ENSLVILEYQ RTNKTATGED
660 670
LPAVQFDAVA QLDGESGDVP LK
Length:672
Mass (Da):75,207
Last modified:September 2, 2008 - v1
Checksum:i634A8213A3F3223A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH954177 Genomic DNA. Translation: EDV57936.1.
RefSeqiXP_001968877.1. XM_001968841.2.

Genome annotation databases

EnsemblMetazoaiFBtr0144317; FBpp0142809; FBgn0116395.
GeneIDi6540666.
KEGGider:Dere_GG24263.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH954177 Genomic DNA. Translation: EDV57936.1.
RefSeqiXP_001968877.1. XM_001968841.2.

3D structure databases

ProteinModelPortaliB3N5A6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0144317; FBpp0142809; FBgn0116395.
GeneIDi6540666.
KEGGider:Dere_GG24263.

Organism-specific databases

FlyBaseiFBgn0116395. Dere\GG24263.

Phylogenomic databases

KOiK12309.
OMAiIELWRRE.
OrthoDBiEOG7GXPCD.
PhylomeDBiB3N5A6.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR026283. B-gal_1-like.
IPR025300. BetaGal_jelly_roll_dom.
IPR008979. Galactose-bd-like.
IPR031330. Gly_Hdrlase_35_cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR001944. Glycoside_Hdrlase_35.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR23421. PTHR23421. 1 hit.
PfamiPF13364. BetaGal_dom4_5. 1 hit.
PF01301. Glyco_hydro_35. 1 hit.
[Graphical view]
PIRSFiPIRSF006336. B-gal. 1 hit.
PRINTSiPR00742. GLHYDRLASE35.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Evolution of genes and genomes on the Drosophila phylogeny."
    Drosophila 12 Genomes Consortium
    Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.
    , Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.
    Nature 450:203-218(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Tucson 14021-0224.01Imported.

Entry informationi

Entry nameiB3N5A6_DROER
AccessioniPrimary (citable) accession number: B3N5A6
Entry historyi
Integrated into UniProtKB/TrEMBL: September 2, 2008
Last sequence update: September 2, 2008
Last modified: June 8, 2016
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

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.