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Protein

Disintegrin and metalloproteinase domain-containing protein 30

Gene

ADAM30

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

May be involved in spermatogenesis and fertilization.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi172 – 1721Zinc; in inhibited formBy similarity
Metal bindingi338 – 3381Zinc; catalyticPROSITE-ProRule annotation
Active sitei339 – 3391PROSITE-ProRule annotation
Metal bindingi342 – 3421Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi348 – 3481Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  1. metalloendopeptidase activity Source: InterPro
  2. metallopeptidase activity Source: ProtInc
  3. zinc ion binding Source: ProtInc

GO - Biological processi

  1. binding of sperm to zona pellucida Source: Reactome
  2. multicellular organism reproduction Source: Reactome
  3. single fertilization Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_163933. Interaction With The Zona Pellucida.

Protein family/group databases

MEROPSiM12.232.

Names & Taxonomyi

Protein namesi
Recommended name:
Disintegrin and metalloproteinase domain-containing protein 30 (EC:3.4.24.-)
Short name:
ADAM 30
Gene namesi
Name:ADAM30
ORF Names:UNQ2509/PRO5997
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:208. ADAM30.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini199 – 687489ExtracellularSequence AnalysisAdd
BLAST
Transmembranei688 – 70821HelicalSequence AnalysisAdd
BLAST
Topological domaini709 – 79082CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: ProtInc
  2. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24525.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence AnalysisAdd
BLAST
Propeptidei28 – 198171By similarityPRO_0000029136Add
BLAST
Chaini199 – 790592Disintegrin and metalloproteinase domain-containing protein 30PRO_0000029137Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi222 – 2221N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi313 ↔ 388By similarity
Disulfide bondi353 ↔ 373By similarity
Disulfide bondi355 ↔ 361By similarity
Glycosylationi372 – 3721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi438 – 4381N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi457 ↔ 477By similarity
Glycosylationi473 – 4731N-linked (GlcNAc...)Sequence Analysis
Glycosylationi625 – 6251N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi633 ↔ 644By similarity
Disulfide bondi638 ↔ 650By similarity
Disulfide bondi652 ↔ 661By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ9UKF2.
PRIDEiQ9UKF2.

PTM databases

PhosphoSiteiQ9UKF2.

Expressioni

Tissue specificityi

Expressed specifically in testis.

Gene expression databases

BgeeiQ9UKF2.
CleanExiHS_ADAM30.
GenevestigatoriQ9UKF2.

Organism-specific databases

HPAiHPA026080.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000358407.

Structurei

3D structure databases

ProteinModelPortaliQ9UKF2.
SMRiQ9UKF2. Positions 199-625.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini203 – 393191Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini399 – 48587DisintegrinPROSITE-ProRule annotationAdd
BLAST
Domaini629 – 66335EGF-likePROSITE-ProRule annotationAdd
BLAST
Repeati732 – 74091
Repeati741 – 74992
Repeati750 – 75893
Repeati759 – 76794
Repeati768 – 77695

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni732 – 776455 X 9 AA approximate repeatsAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi170 – 1778Cysteine switchBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi486 – 632147Cys-richAdd
BLAST

Domaini

The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Sequence similaritiesi

Contains 1 disintegrin domain.PROSITE-ProRule annotation
Contains 1 EGF-like domain.PROSITE-ProRule annotation
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG276852.
GeneTreeiENSGT00760000118888.
HOGENOMiHOG000230883.
HOVERGENiHBG006978.
InParanoidiQ9UKF2.
KOiK08615.
OMAiICGRLQC.
OrthoDBiEOG7FFMR2.
PhylomeDBiQ9UKF2.
TreeFamiTF314733.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR001762. Blood-coag_inhib_Disintegrin.
IPR018358. Disintegrin_CS.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamiPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PRINTSiPR00289. DISINTEGRIN.
SMARTiSM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
[Graphical view]
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Alpha (identifier: Q9UKF2-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRSVQIFLSQ CRLLLLLVPT MLLKSLGEDV IFHPEGEFDS YEVTIPEKLS
60 70 80 90 100
FRGEVQGVVS PVSYLLQLKG KKHVLHLWPK RLLLPRHLRV FSFTEHGELL
110 120 130 140 150
EDHPYIPKDC NYMGSVKESL DSKATISTCM GGLRGVFNID AKHYQIEPLK
160 170 180 190 200
ASPSFEHVVY LLKKEQFGNQ VCGLSDDEIE WQMAPYENKA RLRDFPGSYK
210 220 230 240 250
HPKYLELILL FDQSRYRFVN NNLSQVIHDA ILLTGIMDTY FQDVRMRIHL
260 270 280 290 300
KALEVWTDFN KIRVGYPELA EVLGRFVIYK KSVLNARLSS DWAHLYLQRK
310 320 330 340 350
YNDALAWSFG KVCSLEYAGS VSTLLDTNIL APATWSAHEL GHAVGMSHDE
360 370 380 390 400
QYCQCRGRLN CIMGSGRTGF SNCSYISFFK HISSGATCLN NIPGLGYVLK
410 420 430 440 450
RCGNKIVEDN EECDCGSTEE CQKDRCCQSN CKLQPGANCS IGLCCHDCRF
460 470 480 490 500
RPSGYVCRQE GNECDLAEYC DGNSSSCPND VYKQDGTPCK YEGRCFRKGC
510 520 530 540 550
RSRYMQCQSI FGPDAMEAPS ECYDAVNLIG DQFGNCEITG IRNFKKCESA
560 570 580 590 600
NSICGRLQCI NVETIPDLPE HTTIISTHLQ AENLMCWGTG YHLSMKPMGI
610 620 630 640 650
PDLGMINDGT SCGEGRVCFK KNCVNSSVLQ FDCLPEKCNT RGVCNNRKNC
660 670 680 690 700
HCMYGWAPPF CEEVGYGGSI DSGPPGLLRG AIPSSIWVVS IIMFRLILLI
710 720 730 740 750
LSVVFVFFRQ VIGNHLKPKQ EKMPLSKAKT EQEESKTKTV QEESKTKTGQ
760 770 780 790
EESEAKTGQE ESKAKTGQEE SKANIESKRP KAKSVKKQKK
Length:790
Mass (Da):88,940
Last modified:May 10, 2004 - v2
Checksum:i42EC8A5F6B5ACDA3
GO
Isoform Beta (identifier: Q9UKF2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     763-771: Missing.

Show »
Length:781
Mass (Da):87,981
Checksum:iEC875E91BA95B28F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti336 – 3361S → P in AAF03781. (PubMed:10512762)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti359 – 3591L → P.2 Publications
Corresponds to variant rs2641348 [ dbSNP | Ensembl ].
VAR_024597
Natural varianti737 – 7371T → A.
Corresponds to variant rs35273427 [ dbSNP | Ensembl ].
VAR_061738

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei763 – 7719Missing in isoform Beta. 1 PublicationVSP_005494

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF171932 mRNA. Translation: AAF03780.1.
AF171933 mRNA. Translation: AAF03781.1.
AY358734 mRNA. Translation: AAQ89096.1.
AK292483 mRNA. Translation: BAF85172.1.
AL359752 Genomic DNA. Translation: CAI18978.1.
CCDSiCCDS907.1. [Q9UKF2-1]
RefSeqiNP_068566.2. NM_021794.3. [Q9UKF2-1]
UniGeneiHs.283011.

Genome annotation databases

EnsembliENST00000369400; ENSP00000358407; ENSG00000134249. [Q9UKF2-1]
GeneIDi11085.
KEGGihsa:11085.
UCSCiuc001eij.3. human. [Q9UKF2-1]

Polymorphism databases

DMDMi47117918.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF171932 mRNA. Translation: AAF03780.1.
AF171933 mRNA. Translation: AAF03781.1.
AY358734 mRNA. Translation: AAQ89096.1.
AK292483 mRNA. Translation: BAF85172.1.
AL359752 Genomic DNA. Translation: CAI18978.1.
CCDSiCCDS907.1. [Q9UKF2-1]
RefSeqiNP_068566.2. NM_021794.3. [Q9UKF2-1]
UniGeneiHs.283011.

3D structure databases

ProteinModelPortaliQ9UKF2.
SMRiQ9UKF2. Positions 199-625.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000358407.

Protein family/group databases

MEROPSiM12.232.

PTM databases

PhosphoSiteiQ9UKF2.

Polymorphism databases

DMDMi47117918.

Proteomic databases

PaxDbiQ9UKF2.
PRIDEiQ9UKF2.

Protocols and materials databases

DNASUi11085.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369400; ENSP00000358407; ENSG00000134249. [Q9UKF2-1]
GeneIDi11085.
KEGGihsa:11085.
UCSCiuc001eij.3. human. [Q9UKF2-1]

Organism-specific databases

CTDi11085.
GeneCardsiGC01M120436.
HGNCiHGNC:208. ADAM30.
HPAiHPA026080.
MIMi604779. gene.
neXtProtiNX_Q9UKF2.
PharmGKBiPA24525.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG276852.
GeneTreeiENSGT00760000118888.
HOGENOMiHOG000230883.
HOVERGENiHBG006978.
InParanoidiQ9UKF2.
KOiK08615.
OMAiICGRLQC.
OrthoDBiEOG7FFMR2.
PhylomeDBiQ9UKF2.
TreeFamiTF314733.

Enzyme and pathway databases

ReactomeiREACT_163933. Interaction With The Zona Pellucida.

Miscellaneous databases

GenomeRNAii11085.
NextBioi42148.
PROiQ9UKF2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UKF2.
CleanExiHS_ADAM30.
GenevestigatoriQ9UKF2.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR001762. Blood-coag_inhib_Disintegrin.
IPR018358. Disintegrin_CS.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamiPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PRINTSiPR00289. DISINTEGRIN.
SMARTiSM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
[Graphical view]
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of two novel metalloproteinase-disintegrin (ADAM) cDNAs that show testis-specific gene expression."
    Cerretti D.P., DuBose R.F., Black R.A., Nelson N.
    Biochem. Biophys. Res. Commun. 263:810-815(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), VARIANT PRO-359.
    Tissue: Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), VARIANT PRO-359.
    Tissue: Testis.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiADA30_HUMAN
AccessioniPrimary (citable) accession number: Q9UKF2
Secondary accession number(s): A8K8W8, Q5T3X6, Q9UKF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: May 10, 2004
Last modified: January 7, 2015
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. 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.