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Protein

Replication factor C subunit 4

Gene

RFC4

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

Functioni

The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1. This subunit may be involved in the elongation of the multiprimed DNA template.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi78 – 858ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-110312. Translesion synthesis by REV1.
R-HSA-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-HSA-110320. Translesion Synthesis by POLH.
R-HSA-174411. Polymerase switching on the C-strand of the telomere.
R-HSA-176187. Activation of ATR in response to replication stress.
R-HSA-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-HSA-5655862. Translesion synthesis by POLK.
R-HSA-5656121. Translesion synthesis by POLI.
R-HSA-5656169. Termination of translesion DNA synthesis.
R-HSA-5685938. HDR through Single Strand Annealing (SSA).
R-HSA-5685942. HDR through Homologous Recombination (HRR).
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-HSA-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-HSA-5696400. Dual Incision in GG-NER.
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-69091. Polymerase switching.
R-HSA-69473. G2/M DNA damage checkpoint.
SignaLinkiP35249.

Names & Taxonomyi

Protein namesi
Recommended name:
Replication factor C subunit 4
Alternative name(s):
Activator 1 37 kDa subunit
Short name:
A1 37 kDa subunit
Activator 1 subunit 4
Replication factor C 37 kDa subunit
Short name:
RF-C 37 kDa subunit
Short name:
RFC37
Gene namesi
Name:RFC4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:9972. RFC4.

Subcellular locationi

GO - Cellular componenti

  • Ctf18 RFC-like complex Source: UniProtKB
  • DNA replication factor C complex Source: UniProtKB
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34341.

Polymorphism and mutation databases

BioMutaiRFC4.
DMDMi1703052.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 363363Replication factor C subunit 4PRO_0000121757Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei6 – 61N6-acetyllysineCombined sources
Modified residuei13 – 131N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP35249.
MaxQBiP35249.
PaxDbiP35249.
PeptideAtlasiP35249.
PRIDEiP35249.

PTM databases

iPTMnetiP35249.
PhosphoSiteiP35249.

Expressioni

Gene expression databases

BgeeiP35249.
CleanExiHS_RFC4.
ExpressionAtlasiP35249. baseline and differential.
GenevisibleiP35249. HS.

Organism-specific databases

HPAiCAB004557.
HPA049123.
HPA058507.

Interactioni

Subunit structurei

Heterotetramer of subunits RFC2, RFC3, RFC4 and RFC5 that can form a complex either with RFC1 or with RAD17. The former interacts with PCNA in the presence of ATP, while the latter has ATPase activity but is not stimulated by PCNA.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RFC2P352508EBI-476655,EBI-476409
RFC3P409385EBI-476655,EBI-1055010
RFC5P4093711EBI-476655,EBI-712376
RNF41Q9H4P44EBI-476655,EBI-2130266

Protein-protein interaction databases

BioGridi111916. 87 interactions.
DIPiDIP-24267N.
IntActiP35249. 29 interactions.
MINTiMINT-1485723.
STRINGi9606.ENSP00000296273.

Structurei

3D structure databases

ProteinModelPortaliP35249.
SMRiP35249. Positions 39-357.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the activator 1 small subunits family.Curated

Phylogenomic databases

eggNOGiKOG0989. Eukaryota.
COG0470. LUCA.
GeneTreeiENSGT00550000074917.
HOGENOMiHOG000224154.
HOVERGENiHBG002053.
InParanoidiP35249.
KOiK10755.
OMAiKNFARQT.
OrthoDBiEOG7SR4MP.
PhylomeDBiP35249.
TreeFamiTF314424.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR008921. DNA_pol3_clamp-load_cplx_C.
IPR027417. P-loop_NTPase.
IPR013748. Rep_factorC_C.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF08542. Rep_fac_C. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF48019. SSF48019. 1 hit.
SSF52540. SSF52540. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P35249-1) [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
MQAFLKGTSI STKPPLTKDR GVAASAGSSG ENKKAKPVPW VEKYRPKCVD
60 70 80 90 100
EVAFQEEVVA VLKKSLEGAD LPNLLFYGPP GTGKTSTILA AARELFGPEL
110 120 130 140 150
FRLRVLELNA SDERGIQVVR EKVKNFAQLT VSGSRSDGKP CPPFKIVILD
160 170 180 190 200
EADSMTSAAQ AALRRTMEKE SKTTRFCLIC NYVSRIIEPL TSRCSKFRFK
210 220 230 240 250
PLSDKIQQQR LLDIAKKENV KISDEGIAYL VKVSEGDLRK AITFLQSATR
260 270 280 290 300
LTGGKEITEK VITDIAGVIP AEKIDGVFAA CQSGSFDKLE AVVKDLIDEG
310 320 330 340 350
HAATQLVNQL HDVVVENNLS DKQKSIITEK LAEVDKCLAD GADEHLQLIS
360
LCATVMQQLS QNC
Length:363
Mass (Da):39,682
Last modified:October 1, 1996 - v2
Checksum:i6FEAB3794379F3E0
GO
Isoform 2 (identifier: P35249-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     269-303: IPAEKIDGVFAACQSGSFDKLEAVVKDLIDEGHAA → RVLDILNFFLVGFFVAFRKFSSNKYWVFSKCQVLH
     304-363: Missing.

Note: No experimental confirmation available.
Show »
Length:303
Mass (Da):33,675
Checksum:i145BFD9762926E18
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti292 – 2921V → A.1 Publication
Corresponds to variant rs2066497 [ dbSNP | Ensembl ].
VAR_014307
Natural varianti354 – 3541T → S in a breast cancer sample; somatic mutation. 1 Publication
VAR_036121

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei269 – 30335IPAEK…EGHAA → RVLDILNFFLVGFFVAFRKF SSNKYWVFSKCQVLH in isoform 2. 1 PublicationVSP_055862Add
BLAST
Alternative sequencei304 – 36360Missing in isoform 2. 1 PublicationVSP_055863Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87339 mRNA. Translation: AAB09785.1.
AF538718 Genomic DNA. Translation: AAM97933.1.
BT006987 mRNA. Translation: AAP35633.1.
AK297282 mRNA. Translation: BAG59753.1.
CR536561 mRNA. Translation: CAG38798.1.
CH471052 Genomic DNA. Translation: EAW78169.1.
CH471052 Genomic DNA. Translation: EAW78170.1.
CH471052 Genomic DNA. Translation: EAW78171.1.
BC017452 mRNA. Translation: AAH17452.1.
BC024022 mRNA. Translation: AAH24022.1.
CCDSiCCDS3283.1. [P35249-1]
PIRiA45253.
RefSeqiNP_002907.1. NM_002916.3. [P35249-1]
NP_853551.1. NM_181573.2. [P35249-1]
UniGeneiHs.732098.

Genome annotation databases

EnsembliENST00000296273; ENSP00000296273; ENSG00000163918. [P35249-1]
ENST00000392481; ENSP00000376272; ENSG00000163918. [P35249-1]
GeneIDi5984.
KEGGihsa:5984.
UCSCiuc003fqz.4. human. [P35249-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87339 mRNA. Translation: AAB09785.1.
AF538718 Genomic DNA. Translation: AAM97933.1.
BT006987 mRNA. Translation: AAP35633.1.
AK297282 mRNA. Translation: BAG59753.1.
CR536561 mRNA. Translation: CAG38798.1.
CH471052 Genomic DNA. Translation: EAW78169.1.
CH471052 Genomic DNA. Translation: EAW78170.1.
CH471052 Genomic DNA. Translation: EAW78171.1.
BC017452 mRNA. Translation: AAH17452.1.
BC024022 mRNA. Translation: AAH24022.1.
CCDSiCCDS3283.1. [P35249-1]
PIRiA45253.
RefSeqiNP_002907.1. NM_002916.3. [P35249-1]
NP_853551.1. NM_181573.2. [P35249-1]
UniGeneiHs.732098.

3D structure databases

ProteinModelPortaliP35249.
SMRiP35249. Positions 39-357.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111916. 87 interactions.
DIPiDIP-24267N.
IntActiP35249. 29 interactions.
MINTiMINT-1485723.
STRINGi9606.ENSP00000296273.

PTM databases

iPTMnetiP35249.
PhosphoSiteiP35249.

Polymorphism and mutation databases

BioMutaiRFC4.
DMDMi1703052.

Proteomic databases

EPDiP35249.
MaxQBiP35249.
PaxDbiP35249.
PeptideAtlasiP35249.
PRIDEiP35249.

Protocols and materials databases

DNASUi5984.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296273; ENSP00000296273; ENSG00000163918. [P35249-1]
ENST00000392481; ENSP00000376272; ENSG00000163918. [P35249-1]
GeneIDi5984.
KEGGihsa:5984.
UCSCiuc003fqz.4. human. [P35249-1]

Organism-specific databases

CTDi5984.
GeneCardsiRFC4.
HGNCiHGNC:9972. RFC4.
HPAiCAB004557.
HPA049123.
HPA058507.
MIMi102577. gene.
neXtProtiNX_P35249.
PharmGKBiPA34341.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0989. Eukaryota.
COG0470. LUCA.
GeneTreeiENSGT00550000074917.
HOGENOMiHOG000224154.
HOVERGENiHBG002053.
InParanoidiP35249.
KOiK10755.
OMAiKNFARQT.
OrthoDBiEOG7SR4MP.
PhylomeDBiP35249.
TreeFamiTF314424.

Enzyme and pathway databases

ReactomeiR-HSA-110312. Translesion synthesis by REV1.
R-HSA-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-HSA-110320. Translesion Synthesis by POLH.
R-HSA-174411. Polymerase switching on the C-strand of the telomere.
R-HSA-176187. Activation of ATR in response to replication stress.
R-HSA-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-HSA-5655862. Translesion synthesis by POLK.
R-HSA-5656121. Translesion synthesis by POLI.
R-HSA-5656169. Termination of translesion DNA synthesis.
R-HSA-5685938. HDR through Single Strand Annealing (SSA).
R-HSA-5685942. HDR through Homologous Recombination (HRR).
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-HSA-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-HSA-5696400. Dual Incision in GG-NER.
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-69091. Polymerase switching.
R-HSA-69473. G2/M DNA damage checkpoint.
SignaLinkiP35249.

Miscellaneous databases

ChiTaRSiRFC4. human.
GeneWikiiRFC4.
GenomeRNAii5984.
PROiP35249.
SOURCEiSearch...

Gene expression databases

BgeeiP35249.
CleanExiHS_RFC4.
ExpressionAtlasiP35249. baseline and differential.
GenevisibleiP35249. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR008921. DNA_pol3_clamp-load_cplx_C.
IPR027417. P-loop_NTPase.
IPR013748. Rep_factorC_C.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF08542. Rep_fac_C. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF48019. SSF48019. 1 hit.
SSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Studies of the cloned 37-kDa subunit of activator 1 (replication factor C) of HeLa cells."
    Chen M., Pan Z.-Q., Hurwitz J.
    Proc. Natl. Acad. Sci. U.S.A. 89:5211-5215(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
  2. Hurwitz J.
    Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "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 2).
    Tissue: Brain.
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. NIEHS SNPs program
    Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-292.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung and Testis.
  9. "Purification and characterization of human DNA damage checkpoint Rad complexes."
    Lindsey-Boltz L.A., Bermudez V.P., Hurwitz J., Sancar A.
    Proc. Natl. Acad. Sci. U.S.A. 98:11236-11241(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAD17.
  10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6 AND LYS-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-354.

Entry informationi

Entry nameiRFC4_HUMAN
AccessioniPrimary (citable) accession number: P35249
Secondary accession number(s): B4DM41, D3DNV2, Q6FHX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 168 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

Miscellaneous

Despite of the presence of a putative ATP-binding motif, this protein does not bind ATP.

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. 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.