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Protein

Propionyl-CoA carboxylase beta chain, mitochondrial

Gene

PCCB

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

Functioni

Catalytic activityi

ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA.

Pathwayi: propanoyl-CoA degradation

This protein is involved in step 1 of the subpathway that synthesizes succinyl-CoA from propanoyl-CoA.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Propionyl-CoA carboxylase alpha chain, mitochondrial (PCCA), Propionyl-CoA carboxylase beta chain, mitochondrial (PCCB)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
This subpathway is part of the pathway propanoyl-CoA degradation, which is itself part of Metabolic intermediate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes succinyl-CoA from propanoyl-CoA, the pathway propanoyl-CoA degradation and in Metabolic intermediate metabolism.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • propionyl-CoA carboxylase activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000114054-MONOMER.
ZFISH:ENSG00000114054-MONOMER.
ReactomeiR-HSA-196780. Biotin transport and metabolism.
R-HSA-3371599. Defective HLCS causes multiple carboxylase deficiency.
R-HSA-71032. Propionyl-CoA catabolism.
SABIO-RKP05166.
UniPathwayiUPA00945; UER00908.

Names & Taxonomyi

Protein namesi
Recommended name:
Propionyl-CoA carboxylase beta chain, mitochondrial (EC:6.4.1.3)
Short name:
PCCase subunit beta
Alternative name(s):
Propanoyl-CoA:carbon dioxide ligase subunit beta
Gene namesi
Name:PCCB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:8654. PCCB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • mitochondrial matrix Source: Reactome
  • mitochondrion Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Propionic acidemia type II (PA-2)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionLife-threatening disease characterized by episodic vomiting, lethargy and ketosis, neutropenia, periodic thrombocytopenia, hypogammaglobulinemia, developmental retardation, and intolerance to protein.
See also OMIM:606054
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00908017L → M in PA-2. 1 PublicationCorresponds to variant rs200185747dbSNPEnsembl.1
Natural variantiVAR_00027144R → P in PA-2. 1
Natural variantiVAR_02384767R → S in PA-2. 1 PublicationCorresponds to variant rs747053913dbSNPEnsembl.1
Natural variantiVAR_000272106S → R in PA-2. 1
Natural variantiVAR_023848107V → M in PA-2. 1 Publication1
Natural variantiVAR_023849112G → D in PA-2. 1 PublicationCorresponds to variant rs202247818dbSNPEnsembl.1
Natural variantiVAR_000273131G → R in PA-2. 1
Natural variantiVAR_009081140K → KICK in PA-2. 1
Natural variantiVAR_023850153A → P in PA-2. 1 PublicationCorresponds to variant rs202247819dbSNPEnsembl.1
Natural variantiVAR_023851165R → Q in PA-2; does not affect either heteromeric or homomeric assembly. 2 Publications1
Natural variantiVAR_000274165R → W in PA-2. 1 Publication1
Natural variantiVAR_000275168E → K in PA-2; common mutation. 2 PublicationsCorresponds to variant rs121964960dbSNPEnsembl.1
Natural variantiVAR_023852188G → R in PA-2. 1 PublicationCorresponds to variant rs746102997dbSNPEnsembl.1
Natural variantiVAR_000276198G → D in PA-2. Corresponds to variant rs762354873dbSNPEnsembl.1
Natural variantiVAR_009082205V → D in PA-2. 1 Publication1
Natural variantiVAR_009083228P → L in PA-2. Corresponds to variant rs374722096dbSNPEnsembl.1
Natural variantiVAR_023853246G → V in PA-2. 1 Publication1
Natural variantiVAR_023854341Missing in PA-2. 1 Publication1
Natural variantiVAR_000277408Missing in PA-2. 2 Publications1
Natural variantiVAR_000278410R → W in PA-2. 3 PublicationsCorresponds to variant rs121964959dbSNPEnsembl.1
Natural variantiVAR_009084428T → I in PA-2. 2 PublicationsCorresponds to variant rs28934887dbSNPEnsembl.1
Natural variantiVAR_023855430I → L in PA-2. 1 Publication1
Natural variantiVAR_023856435Y → C in PA-2. 1 PublicationCorresponds to variant rs121964961dbSNPEnsembl.1
Natural variantiVAR_023857439Y → C in PA-2. 1 PublicationCorresponds to variant rs769521436dbSNPEnsembl.1
Natural variantiVAR_009085442M → T in PA-2. 1 Publication1
Natural variantiVAR_023858468A → T in PA-2. 1 PublicationCorresponds to variant rs775563122dbSNPEnsembl.1
Natural variantiVAR_000279497A → V in PA-2; common mutation; does not affect either heteromeric or homomeric assembly. 1 PublicationCorresponds to variant rs142403318dbSNPEnsembl.1
Natural variantiVAR_000280512R → C in PA-2; affects heteromeric and homomeric assembly. 2 PublicationsCorresponds to variant rs186710233dbSNPEnsembl.1
Natural variantiVAR_000281519L → P in PA-2; affects heteromeric and homomeric assembly. 1 PublicationCorresponds to variant rs202247822dbSNPEnsembl.1
Natural variantiVAR_009086536N → D in PA-2; affects heteromeric and homomeric assembly. 1 PublicationCorresponds to variant rs202247823dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi5096.
MalaCardsiPCCB.
MIMi606054. phenotype.
OpenTargetsiENSG00000114054.
Orphaneti35. Propionic acidemia.
PharmGKBiPA32993.

Chemistry databases

DrugBankiDB00121. Biotin.
DB00161. L-Valine.

Polymorphism and mutation databases

BioMutaiPCCB.
DMDMi124106304.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 28Mitochondrion1 PublicationAdd BLAST28
ChainiPRO_000000029329 – 539Propionyl-CoA carboxylase beta chain, mitochondrialAdd BLAST511

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei71PhosphoserineCombined sources1
Modified residuei99N6-acetyllysine; alternateBy similarity1
Modified residuei99N6-succinyllysine; alternateBy similarity1
Modified residuei248N6-succinyllysineBy similarity1
Modified residuei474N6-acetyllysine; alternateBy similarity1
Modified residuei474N6-succinyllysine; alternateBy similarity1
Modified residuei489N6-acetyllysine; alternateBy similarity1
Modified residuei489N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP05166.
MaxQBiP05166.
PaxDbiP05166.
PeptideAtlasiP05166.
PRIDEiP05166.

PTM databases

iPTMnetiP05166.
PhosphoSitePlusiP05166.

Expressioni

Gene expression databases

BgeeiENSG00000114054.
CleanExiHS_PCCB.
ExpressionAtlasiP05166. baseline and differential.
GenevisibleiP05166. HS.

Organism-specific databases

HPAiHPA036939.
HPA036940.

Interactioni

Subunit structurei

Probably a dodecamer composed of six biotin-containing alpha subunits and six beta subunits.

Protein-protein interaction databases

BioGridi111129. 14 interactors.
DIPiDIP-38244N.
IntActiP05166. 10 interactors.
MINTiMINT-3004663.
STRINGi9606.ENSP00000419027.

Structurei

3D structure databases

ProteinModelPortaliP05166.
SMRiP05166.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini32 – 290CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST259
Domaini294 – 533CoA carboxyltransferase C-terminalPROSITE-ProRule annotationAdd BLAST240

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni32 – 533CarboxyltransferasePROSITE-ProRule annotationAdd BLAST502
Regioni325 – 358Acyl-CoA bindingSequence analysisAdd BLAST34

Sequence similaritiesi

Belongs to the AccD/PCCB family.Curated
Contains 1 CoA carboxyltransferase C-terminal domain.PROSITE-ProRule annotation
Contains 1 CoA carboxyltransferase N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0540. Eukaryota.
COG4799. LUCA.
GeneTreeiENSGT00530000063337.
HOGENOMiHOG000218693.
HOVERGENiHBG003970.
InParanoidiP05166.
KOiK01966.
PhylomeDBiP05166.
TreeFamiTF314350.

Family and domain databases

Gene3Di3.90.226.10. 2 hits.
InterProiIPR000022. Carboxyl_trans.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]
PfamiPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 2 hits.
PROSITEiPS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 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. AlignAdd to basket

Isoform 1 (identifier: P05166-1) [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
MAAALRVAAV GARLSVLASG LRAAVRSLCS QATSVNERIE NKRRTALLGG
60 70 80 90 100
GQRRIDAQHK RGKLTARERI SLLLDPGSFV ESDMFVEHRC ADFGMAADKN
110 120 130 140 150
KFPGDSVVTG RGRINGRLVY VFSQDFTVFG GSLSGAHAQK ICKIMDQAIT
160 170 180 190 200
VGAPVIGLND SGGARIQEGV ESLAGYADIF LRNVTASGVI PQISLIMGPC
210 220 230 240 250
AGGAVYSPAL TDFTFMVKDT SYLFITGPDV VKSVTNEDVT QEELGGAKTH
260 270 280 290 300
TTMSGVAHRA FENDVDALCN LRDFFNYLPL SSQDPAPVRE CHDPSDRLVP
310 320 330 340 350
ELDTIVPLES TKAYNMVDII HSVVDEREFF EIMPNYAKNI IVGFARMNGR
360 370 380 390 400
TVGIVGNQPK VASGCLDINS SVKGARFVRF CDAFNIPLIT FVDVPGFLPG
410 420 430 440 450
TAQEYGGIIR HGAKLLYAFA EATVPKVTVI TRKAYGGAYD VMSSKHLCGD
460 470 480 490 500
TNYAWPTAEI AVMGAKGAVE IIFKGHENVE AAQAEYIEKF ANPFPAAVRG
510 520 530
FVDDIIQPSS TRARICCDLD VLASKKVQRP WRKHANIPL
Length:539
Mass (Da):58,216
Last modified:January 23, 2007 - v3
Checksum:iA2DAAC00312D3C0F
GO
Isoform 2 (identifier: P05166-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     124-124: Q → QQIIGWAQWLPLVISALWEAE

Note: No experimental confirmation available.
Show »
Length:559
Mass (Da):60,521
Checksum:i07788B2E955626AA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti58 – 59QH → HD in AAB28900 (PubMed:8225321).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00908017L → M in PA-2. 1 PublicationCorresponds to variant rs200185747dbSNPEnsembl.1
Natural variantiVAR_00027144R → P in PA-2. 1
Natural variantiVAR_02384767R → S in PA-2. 1 PublicationCorresponds to variant rs747053913dbSNPEnsembl.1
Natural variantiVAR_000272106S → R in PA-2. 1
Natural variantiVAR_023848107V → M in PA-2. 1 Publication1
Natural variantiVAR_023849112G → D in PA-2. 1 PublicationCorresponds to variant rs202247818dbSNPEnsembl.1
Natural variantiVAR_000273131G → R in PA-2. 1
Natural variantiVAR_009081140K → KICK in PA-2. 1
Natural variantiVAR_023850153A → P in PA-2. 1 PublicationCorresponds to variant rs202247819dbSNPEnsembl.1
Natural variantiVAR_023851165R → Q in PA-2; does not affect either heteromeric or homomeric assembly. 2 Publications1
Natural variantiVAR_000274165R → W in PA-2. 1 Publication1
Natural variantiVAR_000275168E → K in PA-2; common mutation. 2 PublicationsCorresponds to variant rs121964960dbSNPEnsembl.1
Natural variantiVAR_023852188G → R in PA-2. 1 PublicationCorresponds to variant rs746102997dbSNPEnsembl.1
Natural variantiVAR_000276198G → D in PA-2. Corresponds to variant rs762354873dbSNPEnsembl.1
Natural variantiVAR_009082205V → D in PA-2. 1 Publication1
Natural variantiVAR_009083228P → L in PA-2. Corresponds to variant rs374722096dbSNPEnsembl.1
Natural variantiVAR_023853246G → V in PA-2. 1 Publication1
Natural variantiVAR_048163287P → S.1 PublicationCorresponds to variant rs2228310dbSNPEnsembl.1
Natural variantiVAR_023854341Missing in PA-2. 1 Publication1
Natural variantiVAR_000277408Missing in PA-2. 2 Publications1
Natural variantiVAR_000278410R → W in PA-2. 3 PublicationsCorresponds to variant rs121964959dbSNPEnsembl.1
Natural variantiVAR_009084428T → I in PA-2. 2 PublicationsCorresponds to variant rs28934887dbSNPEnsembl.1
Natural variantiVAR_023855430I → L in PA-2. 1 Publication1
Natural variantiVAR_023856435Y → C in PA-2. 1 PublicationCorresponds to variant rs121964961dbSNPEnsembl.1
Natural variantiVAR_023857439Y → C in PA-2. 1 PublicationCorresponds to variant rs769521436dbSNPEnsembl.1
Natural variantiVAR_009085442M → T in PA-2. 1 Publication1
Natural variantiVAR_023858468A → T in PA-2. 1 PublicationCorresponds to variant rs775563122dbSNPEnsembl.1
Natural variantiVAR_000279497A → V in PA-2; common mutation; does not affect either heteromeric or homomeric assembly. 1 PublicationCorresponds to variant rs142403318dbSNPEnsembl.1
Natural variantiVAR_000280512R → C in PA-2; affects heteromeric and homomeric assembly. 2 PublicationsCorresponds to variant rs186710233dbSNPEnsembl.1
Natural variantiVAR_000281519L → P in PA-2; affects heteromeric and homomeric assembly. 1 PublicationCorresponds to variant rs202247822dbSNPEnsembl.1
Natural variantiVAR_009086536N → D in PA-2; affects heteromeric and homomeric assembly. 1 PublicationCorresponds to variant rs202247823dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_042568124Q → QQIIGWAQWLPLVISALWEA E in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73424 mRNA. Translation: CAA51825.1.
S67325 mRNA. Translation: AAB28900.1.
AJ006487
, AJ006488, AJ006489, AJ006490, AJ006491, AJ006492, AJ006493, AJ006494, AJ006495, AJ006496, AJ006497, AJ006498, AJ006499 Genomic DNA. Translation: CAA07066.1.
AK295312 mRNA. Translation: BAH12030.1.
AC069524 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79118.1.
BC013768 mRNA. Translation: AAH13768.1.
BC053661 mRNA. Translation: AAH53661.1.
M13573 mRNA. Translation: AAA60036.1.
M31167 Genomic DNA. Translation: AAA60037.1.
M31169 Genomic DNA. Translation: AAA60038.1.
CCDSiCCDS3089.1. [P05166-1]
CCDS54643.1. [P05166-2]
PIRiT45009.
RefSeqiNP_000523.2. NM_000532.4. [P05166-1]
NP_001171485.1. NM_001178014.1. [P05166-2]
UniGeneiHs.63788.

Genome annotation databases

EnsembliENST00000251654; ENSP00000251654; ENSG00000114054. [P05166-1]
ENST00000469217; ENSP00000419027; ENSG00000114054. [P05166-2]
GeneIDi5096.
KEGGihsa:5096.
UCSCiuc003eqy.3. human. [P05166-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73424 mRNA. Translation: CAA51825.1.
S67325 mRNA. Translation: AAB28900.1.
AJ006487
, AJ006488, AJ006489, AJ006490, AJ006491, AJ006492, AJ006493, AJ006494, AJ006495, AJ006496, AJ006497, AJ006498, AJ006499 Genomic DNA. Translation: CAA07066.1.
AK295312 mRNA. Translation: BAH12030.1.
AC069524 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79118.1.
BC013768 mRNA. Translation: AAH13768.1.
BC053661 mRNA. Translation: AAH53661.1.
M13573 mRNA. Translation: AAA60036.1.
M31167 Genomic DNA. Translation: AAA60037.1.
M31169 Genomic DNA. Translation: AAA60038.1.
CCDSiCCDS3089.1. [P05166-1]
CCDS54643.1. [P05166-2]
PIRiT45009.
RefSeqiNP_000523.2. NM_000532.4. [P05166-1]
NP_001171485.1. NM_001178014.1. [P05166-2]
UniGeneiHs.63788.

3D structure databases

ProteinModelPortaliP05166.
SMRiP05166.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111129. 14 interactors.
DIPiDIP-38244N.
IntActiP05166. 10 interactors.
MINTiMINT-3004663.
STRINGi9606.ENSP00000419027.

Chemistry databases

DrugBankiDB00121. Biotin.
DB00161. L-Valine.

PTM databases

iPTMnetiP05166.
PhosphoSitePlusiP05166.

Polymorphism and mutation databases

BioMutaiPCCB.
DMDMi124106304.

Proteomic databases

EPDiP05166.
MaxQBiP05166.
PaxDbiP05166.
PeptideAtlasiP05166.
PRIDEiP05166.

Protocols and materials databases

DNASUi5096.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000251654; ENSP00000251654; ENSG00000114054. [P05166-1]
ENST00000469217; ENSP00000419027; ENSG00000114054. [P05166-2]
GeneIDi5096.
KEGGihsa:5096.
UCSCiuc003eqy.3. human. [P05166-1]

Organism-specific databases

CTDi5096.
DisGeNETi5096.
GeneCardsiPCCB.
GeneReviewsiPCCB.
HGNCiHGNC:8654. PCCB.
HPAiHPA036939.
HPA036940.
MalaCardsiPCCB.
MIMi232050. gene.
606054. phenotype.
neXtProtiNX_P05166.
OpenTargetsiENSG00000114054.
Orphaneti35. Propionic acidemia.
PharmGKBiPA32993.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0540. Eukaryota.
COG4799. LUCA.
GeneTreeiENSGT00530000063337.
HOGENOMiHOG000218693.
HOVERGENiHBG003970.
InParanoidiP05166.
KOiK01966.
PhylomeDBiP05166.
TreeFamiTF314350.

Enzyme and pathway databases

UniPathwayiUPA00945; UER00908.
BioCyciMetaCyc:ENSG00000114054-MONOMER.
ZFISH:ENSG00000114054-MONOMER.
ReactomeiR-HSA-196780. Biotin transport and metabolism.
R-HSA-3371599. Defective HLCS causes multiple carboxylase deficiency.
R-HSA-71032. Propionyl-CoA catabolism.
SABIO-RKP05166.

Miscellaneous databases

ChiTaRSiPCCB. human.
GenomeRNAii5096.
PROiP05166.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000114054.
CleanExiHS_PCCB.
ExpressionAtlasiP05166. baseline and differential.
GenevisibleiP05166. HS.

Family and domain databases

Gene3Di3.90.226.10. 2 hits.
InterProiIPR000022. Carboxyl_trans.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]
PfamiPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 2 hits.
PROSITEiPS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPCCB_HUMAN
AccessioniPrimary (citable) accession number: P05166
Secondary accession number(s): B7Z2Z4, Q16813, Q96CX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 170 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. 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.