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Protein

Xanthine dehydrogenase

Gene

ry

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

Functioni

Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid (By similarity).By similarity

Catalytic activityi

Xanthine + NAD+ + H2O = urate + NADH.
Hypoxanthine + NAD+ + H2O = xanthine + NADH.

Cofactori

Protein has several cofactor binding sites:
  • [2Fe-2S] clusterBy similarityNote: Binds 2 [2Fe-2S] clusters.By similarity
  • FADBy similarity
  • Mo-molybdopterinBy similarityNote: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi43 – 431Iron-sulfur 1By similarity
Metal bindingi48 – 481Iron-sulfur 1By similarity
Metal bindingi51 – 511Iron-sulfur 1By similarity
Metal bindingi73 – 731Iron-sulfur 1By similarity
Metal bindingi113 – 1131Iron-sulfur 2By similarity
Metal bindingi116 – 1161Iron-sulfur 2By similarity
Metal bindingi148 – 1481Iron-sulfur 2By similarity
Metal bindingi150 – 1501Iron-sulfur 2By similarity
Binding sitei335 – 3351FADBy similarity
Binding sitei358 – 3581FADBy similarity
Binding sitei406 – 4061FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei424 – 4241FADBy similarity
Metal bindingi772 – 7721MolybdenumBy similarity
Metal bindingi803 – 8031Molybdenum; via carbonyl oxygenBy similarity
Binding sitei807 – 8071SubstrateBy similarity
Binding sitei885 – 8851SubstrateBy similarity
Metal bindingi917 – 9171Molybdenum; via amide nitrogenBy similarity
Binding sitei919 – 9191SubstrateBy similarity
Metal bindingi1084 – 10841Molybdenum; via amide nitrogenBy similarity
Active sitei1267 – 12671Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi255 – 2628FADBy similarity
Nucleotide bindingi345 – 3495FADBy similarity

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB
  2. electron carrier activity Source: InterPro
  3. flavin adenine dinucleotide binding Source: UniProtKB
  4. iron ion binding Source: InterPro
  5. molybdopterin cofactor binding Source: UniProtKB
  6. oxidoreductase activity, acting on the aldehyde or oxo group of donors Source: GO_Central
  7. UDP-N-acetylmuramate dehydrogenase activity Source: InterPro
  8. xanthine dehydrogenase activity Source: UniProtKB
  9. xanthine oxidase activity Source: GO_Central

GO - Biological processi

  1. arginine metabolic process Source: FlyBase
  2. compound eye pigmentation Source: FlyBase
  3. determination of adult lifespan Source: FlyBase
  4. glycerophospholipid metabolic process Source: FlyBase
  5. purine nucleobase metabolic process Source: FlyBase
  6. pyrimidine nucleobase metabolic process Source: FlyBase
  7. tryptophan metabolic process Source: FlyBase
  8. xanthine catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD

Enzyme and pathway databases

ReactomeiREACT_180681. Vitamins B6 activation to pyridoxal phosphate.

Names & Taxonomyi

Protein namesi
Recommended name:
Xanthine dehydrogenase (EC:1.17.1.4)
Short name:
XD
Alternative name(s):
Protein rosy locus
Gene namesi
Name:ry
Synonyms:XDH
ORF Names:CG7642
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0003308. ry.

Subcellular locationi

Peroxisome By similarity

GO - Cellular componenti

  1. cytosol Source: GO_Central
  2. microtubule associated complex Source: FlyBase
  3. peroxisome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13351335Xanthine dehydrogenasePRO_0000166079Add
BLAST

Proteomic databases

PaxDbiP10351.

Expressioni

Gene expression databases

BgeeiP10351.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiP10351. 4 interactions.

Structurei

3D structure databases

ProteinModelPortaliP10351.
SMRiP10351. Positions 6-165, 193-529, 573-1317.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 91882Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini227 – 416190FAD-binding PCMH-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the xanthine dehydrogenase family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG4630.
GeneTreeiENSGT00390000003772.
InParanoidiP10351.
KOiK00106.
OMAiFHMENSY.
OrthoDBiEOG7QRQSZ.
PhylomeDBiP10351.

Family and domain databases

Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.90.1170.50. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. Beta-grasp_dom.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
IPR022407. OxRdtase_Mopterin_BS.
IPR014307. Xanthine_DH_ssu.
[Graphical view]
PfamiPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
PF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000127. Xanthine_DH. 1 hit.
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsiTIGR02963. xanthine_xdhA. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10351-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSNSVLVFFV NGKKVTEVSP DPECTLLTFL REKLRLCGTK LGCAEGGCGA
60 70 80 90 100
CTVMVSRLDR RANKIRHLAV NACLTPVCSM HGCAVTTVEG IGSTKTRLHP
110 120 130 140 150
VQERLAKAHG SQCGFCTPGI VMSMYALLRN AEQPSMRDLE VAFQGNLCRC
160 170 180 190 200
TGYRPILEGY KTFTKEFACG MGEKCCKVSG KGCGTDAETD DKLFERSEFQ
210 220 230 240 250
PLDPSQEPIF PPELQLSDAF DSQSLIFSSD RVTWYRPTNL EELLQLKAKH
260 270 280 290 300
PAAKLVVGNT EVGVEVKFKH FLYPHLINPT QVKELLEIKE NQDGIYFGAA
310 320 330 340 350
VSLMEIDALL RQRIEQLPES ETRLFQCTVD MLHYFAGKQI RNVACLGGNI
360 370 380 390 400
MTGSPISDMN PVLSAAGAQL EVASFVDGKL QKRSVHMGTG FFTGYRRNVI
410 420 430 440 450
EAHEVLLGIH FRKTTPDQYI VAFKQARRRD DDIAIVNAAI NVRFEEKSNI
460 470 480 490 500
VAEISMAFGG MAPTTVLAPR TSQLMVGQEW SHQLVERVAE SLCTELPLAA
510 520 530 540 550
SAPGGMIAYR RALVVSLFFK AYLAISLKLS KSGITSSDAL PSEERSGAET
560 570 580 590 600
FHTPVLKSAQ LFERVCSDQP ICDPIGRPKV HAAALKQATG EAIYTDDIPR
610 620 630 640 650
MDGEVYLAFV LSTKPRAKIT KLDASEALAL DGVHQFFCYK DLTEHENEVG
660 670 680 690 700
PVFHDEHVFA AGEVHCYGQI VGAIAADNKA LAQRAARLVK VEYEELSPVI
710 720 730 740 750
VTIEQAIEHK SYFPDYPRFV TKGNVEEALA QADHTFEGTC RMGGQEHFYL
760 770 780 790 800
ETHAALAVPR DSDELELFCS TQHPSEVQKL VAHVTALPAH RVVCRAKRLG
810 820 830 840 850
GGFGGKESRG ISVALPVALA AYRMGRPVRC MLDRDEDMLI TGTRHPFLFK
860 870 880 890 900
YKVGFTKEGL ITACDIECYN NAGWSMDLSF SVLERAMFHF ENCYRIPNVR
910 920 930 940 950
VGGWVCKTNL PSNTAFRGFG GPQGMYAGEH IIRDVARIVG RDVVDVMRLN
960 970 980 990 1000
FYKTGDYTHY HQQLEHFPIE RCLEDCLKQS RYDEKRQEIA RFNRENRWRK
1010 1020 1030 1040 1050
RGMAVVPTKY GIAFGVMHLN QAGSLINIYG DGSVLLSHGG VEIGQGLNTK
1060 1070 1080 1090 1100
MIQCAARALG IPSELIHISE TATDKVPNTS PTAASVGSDL NGMAVLDACE
1110 1120 1130 1140 1150
KLNKRLAPIK EALPGGTWKE WINKAYFDRV SLSATGFYAM PGIGYHPETN
1160 1170 1180 1190 1200
PNARTYSYYT NGVGVTVVEI DCLTGDHQVL STDIVMDIGS SLNPAIDIGQ
1210 1220 1230 1240 1250
IEGAFMQGYG LFTLEELMYS PQGMLYSRGP GMYKLPGFAD IPGEFNVSLL
1260 1270 1280 1290 1300
TGAPNPRAVY SSKAVGEPPL FIGSSAFFAI KEAIAAARED QGLSGDFPLE
1310 1320 1330
APSTSARIRI ACQDKFTELL EIPEPGSFTP WNIVP
Length:1,335
Mass (Da):146,927
Last modified:June 20, 2003 - v2
Checksum:i230368EA59B30AD8
GO

Sequence cautioni

The sequence AAM11042.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061A → P in CAA68409. 1 PublicationCurated
Sequence conflicti106 – 1061A → P no nucleotide entry (PubMed:3036645)Curated
Sequence conflicti316 – 3161Q → L in CAA68409. 1 PublicationCurated
Sequence conflicti316 – 3161Q → L no nucleotide entry (PubMed:3036646)Curated
Sequence conflicti542 – 5421S → P in CAA68409. 1 PublicationCurated
Sequence conflicti542 – 5421S → P no nucleotide entry (PubMed:3036646)Curated
Sequence conflicti709 – 7091H → L in CAA68409. 1 PublicationCurated
Sequence conflicti709 – 7091H → L no nucleotide entry (PubMed:3036646)Curated
Sequence conflicti730 – 7301A → S in CAA68409. 1 PublicationCurated
Sequence conflicti730 – 7301A → S no nucleotide entry (PubMed:3036646)Curated
Sequence conflicti988 – 9881E → D in CAA68409. 1 PublicationCurated
Sequence conflicti988 – 9881E → D no nucleotide entry (PubMed:3036646)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00308 Genomic DNA. Translation: CAA68409.1.
AE014297 Genomic DNA. Translation: AAF54895.1.
BT015293 mRNA. Translation: AAT94522.1.
AY094689 mRNA. Translation: AAM11042.1. Different initiation.
PIRiS07245.
RefSeqiNP_524337.1. NM_079613.3.
UniGeneiDm.2436.

Genome annotation databases

EnsemblMetazoaiFBtr0082704; FBpp0082172; FBgn0003308.
GeneIDi41605.
KEGGidme:Dmel_CG7642.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00308 Genomic DNA. Translation: CAA68409.1.
AE014297 Genomic DNA. Translation: AAF54895.1.
BT015293 mRNA. Translation: AAT94522.1.
AY094689 mRNA. Translation: AAM11042.1. Different initiation.
PIRiS07245.
RefSeqiNP_524337.1. NM_079613.3.
UniGeneiDm.2436.

3D structure databases

ProteinModelPortaliP10351.
SMRiP10351. Positions 6-165, 193-529, 573-1317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP10351. 4 interactions.

Proteomic databases

PaxDbiP10351.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0082704; FBpp0082172; FBgn0003308.
GeneIDi41605.
KEGGidme:Dmel_CG7642.

Organism-specific databases

CTDi41605.
FlyBaseiFBgn0003308. ry.

Phylogenomic databases

eggNOGiCOG4630.
GeneTreeiENSGT00390000003772.
InParanoidiP10351.
KOiK00106.
OMAiFHMENSY.
OrthoDBiEOG7QRQSZ.
PhylomeDBiP10351.

Enzyme and pathway databases

ReactomeiREACT_180681. Vitamins B6 activation to pyridoxal phosphate.

Miscellaneous databases

GenomeRNAii41605.
NextBioi824612.
PROiP10351.

Gene expression databases

BgeeiP10351.

Family and domain databases

Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.90.1170.50. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. Beta-grasp_dom.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
IPR022407. OxRdtase_Mopterin_BS.
IPR014307. Xanthine_DH_ssu.
[Graphical view]
PfamiPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
PF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000127. Xanthine_DH. 1 hit.
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsiTIGR02963. xanthine_xdhA. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Riley M.A.
    Submitted (FEB-1987) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Canton-S.
  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. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
    Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  5. "Mutations affecting expression of the rosy locus in Drosophila melanogaster."
    Lee C.S., Curtis D., Gray M., Bender W.
    Genetics 116:55-66(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-231, FUNCTION.
    Strain: Canton-S.
  6. "Sequence of the structural gene for xanthine dehydrogenase (rosy locus) in Drosophila melanogaster."
    Keith T.P., Riley M.A., Kreitman M., Lewontin R.C., Curtis D., Chambers G.
    Genetics 116:67-73(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 199-1335.
    Strain: Canton-S.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 544-1335.
    Strain: Berkeley.
    Tissue: Head.

Entry informationi

Entry nameiXDH_DROME
AccessioniPrimary (citable) accession number: P10351
Secondary accession number(s): Q6AWF5, Q8SXC4, Q9VFZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: June 20, 2003
Last modified: February 4, 2015
This is version 147 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.