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Protein

Myoblast determination protein 1

Gene

Myod1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation. Together with MYF5 and MYOG, co-occupies muscle-specific gene promoter core region during myogenesis. Induces fibroblasts to differentiate into myoblasts. Interacts with and is inhibited by the twist protein. This interaction probably involves the basic domains of both proteins.2 Publications

GO - Molecular functioni

  • chromatin binding Source: MGI
  • chromatin DNA binding Source: UniProtKB
  • core promoter binding Source: UniProtKB
  • DNA binding Source: MGI
  • enzyme binding Source: BHF-UCL
  • nuclear hormone receptor binding Source: MGI
  • protein heterodimerization activity Source: MGI
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
  • RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: MGI
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: MGI
  • RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
  • sequence-specific DNA binding Source: MGI
  • sequence-specific DNA binding transcription factor activity Source: MGI
  • transcription factor binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: MGI

GO - Biological processi

  • cardiac muscle cell differentiation Source: UniProtKB
  • cellular response to estradiol stimulus Source: UniProtKB
  • cellular response to glucocorticoid stimulus Source: MGI
  • cellular response to oxygen levels Source: MGI
  • cellular response to starvation Source: MGI
  • histone H3 acetylation Source: UniProtKB
  • histone H4 acetylation Source: UniProtKB
  • muscle organ development Source: MGI
  • myoblast differentiation Source: MGI
  • myoblast fate determination Source: MGI
  • myoblast fusion Source: MGI
  • myotube cell development Source: MGI
  • myotube differentiation Source: MGI
  • myotube differentiation involved in skeletal muscle regeneration Source: MGI
  • negative regulation of myoblast proliferation Source: MGI
  • positive regulation of muscle cell differentiation Source: MGI
  • positive regulation of myoblast differentiation Source: GO_Central
  • positive regulation of myoblast fusion Source: MGI
  • positive regulation of skeletal muscle fiber development Source: GO_Central
  • positive regulation of skeletal muscle tissue regeneration Source: MGI
  • positive regulation of transcription, DNA-templated Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • regulation of alternative mRNA splicing, via spliceosome Source: MGI
  • regulation of gene expression Source: CACAO
  • regulation of RNA splicing Source: MGI
  • regulation of transcription from RNA polymerase II promoter Source: MGI
  • skeletal muscle cell differentiation Source: UniProtKB
  • skeletal muscle fiber adaptation Source: MGI
  • skeletal muscle fiber development Source: MGI
  • skeletal muscle tissue development Source: MGI
  • striated muscle cell differentiation Source: MGI
  • transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Differentiation, Myogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_304595. CDO in myogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Myoblast determination protein 1
Gene namesi
Name:Myod1
Synonyms:Myod
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:97275. Myod1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • myofibril Source: MGI
  • nuclear chromatin Source: BHF-UCL
  • nucleoplasm Source: MGI
  • nucleus Source: UniProtKB
  • transcription factor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 318318Myoblast determination protein 1PRO_0000127361Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki1 – 1Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei104 – 1041N6-methyllysine; by EHMT2By similarity

Post-translational modificationi

Acetylated by a complex containing EP300 and PCAF. The acetylation is essential to activate target genes. Conversely, its deacetylation by SIRT1 inhibits its function.1 Publication
Ubiquitinated on the N-terminus; which is required for proteasomal degradation.By similarity
Phosphorylated by CDK9. This phosphorylation promotes its function in muscle differentiation (By similarity).By similarity
Methylation at Lys-104 by EHMT2/G9a inhibits myogenic activity.By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP10085.

PTM databases

PhosphoSiteiP10085.

Expressioni

Gene expression databases

BgeeiP10085.
CleanExiMM_MYOD1.
GenevisibleiP10085. MM.

Interactioni

Subunit structurei

Interacts with SUV39H1 and CDK9 (By similarity). Efficient DNA binding requires dimerization with another bHLH protein. Seems to form active heterodimers with ITF-2. Interacts with DDX5. Interacts with CHD2. Interacts with TSC22D3 isoform 1 and isoform 4. Interacts with SETD3 (PubMed:21832073).By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DDX5P178443EBI-4405734,EBI-351962From a different organism.
KAT5Q929935EBI-4405734,EBI-399080From a different organism.
Smarcd3Q6P9Z16EBI-4405734,EBI-7525857
Suv39h1O548643EBI-4405734,EBI-302230

Protein-protein interaction databases

BioGridi201673. 31 interactions.
DIPiDIP-37N.
IntActiP10085. 15 interactions.
MINTiMINT-263097.
STRINGi10090.ENSMUSP00000072330.

Structurei

Secondary structure

1
318
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi106 – 13328Combined sources
Helixi146 – 16217Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MDYX-ray2.80A102-166[»]
B/C/D105-166[»]
ProteinModelPortaliP10085.
SMRiP10085. Positions 102-166.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10085.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini109 – 16052bHLHPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG292792.
GeneTreeiENSGT00530000063004.
HOGENOMiHOG000234800.
HOVERGENiHBG006429.
InParanoidiP10085.
KOiK09064.
OMAiDPRLMHV.
OrthoDBiEOG76QFK1.
TreeFamiTF316344.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR002546. Basic.
IPR011598. bHLH_dom.
IPR022032. Myf5.
[Graphical view]
PfamiPF01586. Basic. 1 hit.
PF00010. HLH. 1 hit.
PF12232. Myf5. 1 hit.
[Graphical view]
SMARTiSM00520. BASIC. 1 hit.
SM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10085-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELLSPPLRD IDLTGPDGSL CSFETADDFY DDPCFDSPDL RFFEDLDPRL
60 70 80 90 100
VHMGALLKPE EHAHFPTAVH PGPGAREDEH VRAPSGHHQA GRCLLWACKA
110 120 130 140 150
CKRKTTNADR RKAATMRERR RLSKVNEAFE TLKRCTSSNP NQRLPKVEIL
160 170 180 190 200
RNAIRYIEGL QALLRDQDAA PPGAAAFYAP GPLPPGRGSE HYSGDSDASS
210 220 230 240 250
PRSNCSDGMM DYSGPPSGPR RQNGYDTAYY SEAARESRPG KSAAVSSLDC
260 270 280 290 300
LSSIVERIST DSPAAPALLL ADAPPESPPG PPEGASLSDT EQGTQTPSPD
310
AAPQCPAGSN PNAIYQVL
Length:318
Mass (Da):34,233
Last modified:July 27, 2011 - v2
Checksum:iAEC6572277A78D54
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531M → V in AAA39799 (PubMed:3690668).Curated
Sequence conflicti53 – 531M → V in CAA43836 (PubMed:1754380).Curated
Sequence conflicti53 – 531M → V in AAA39798 (PubMed:3286015).Curated
Sequence conflicti66 – 661P → S in AAA39799 (PubMed:3690668).Curated
Sequence conflicti66 – 661P → S in CAA43836 (PubMed:1754380).Curated
Sequence conflicti66 – 661P → S in AAA39798 (PubMed:3286015).Curated
Sequence conflicti234 – 2341A → V in AAA39799 (PubMed:3690668).Curated
Sequence conflicti234 – 2341A → V in CAA43836 (PubMed:1754380).Curated
Sequence conflicti234 – 2341A → V in AAA39798 (PubMed:3286015).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18779 mRNA. Translation: AAA39799.1.
X61655 Genomic DNA. Translation: CAA43836.1.
M84918 mRNA. Translation: AAA39798.1.
AK076157 mRNA. Translation: BAC36224.1.
AK142859 mRNA. Translation: BAE25213.1.
BC103613 mRNA. Translation: AAI03614.1.
BC103618 mRNA. Translation: AAI03619.1.
BC103619 mRNA. Translation: AAI03620.1.
CCDSiCCDS21277.1.
PIRiA29636.
RefSeqiNP_034996.2. NM_010866.2.
UniGeneiMm.1526.

Genome annotation databases

EnsembliENSMUST00000072514; ENSMUSP00000072330; ENSMUSG00000009471.
GeneIDi17927.
KEGGimmu:17927.
UCSCiuc012fkv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18779 mRNA. Translation: AAA39799.1.
X61655 Genomic DNA. Translation: CAA43836.1.
M84918 mRNA. Translation: AAA39798.1.
AK076157 mRNA. Translation: BAC36224.1.
AK142859 mRNA. Translation: BAE25213.1.
BC103613 mRNA. Translation: AAI03614.1.
BC103618 mRNA. Translation: AAI03619.1.
BC103619 mRNA. Translation: AAI03620.1.
CCDSiCCDS21277.1.
PIRiA29636.
RefSeqiNP_034996.2. NM_010866.2.
UniGeneiMm.1526.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MDYX-ray2.80A102-166[»]
B/C/D105-166[»]
ProteinModelPortaliP10085.
SMRiP10085. Positions 102-166.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201673. 31 interactions.
DIPiDIP-37N.
IntActiP10085. 15 interactions.
MINTiMINT-263097.
STRINGi10090.ENSMUSP00000072330.

PTM databases

PhosphoSiteiP10085.

Proteomic databases

PRIDEiP10085.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000072514; ENSMUSP00000072330; ENSMUSG00000009471.
GeneIDi17927.
KEGGimmu:17927.
UCSCiuc012fkv.1. mouse.

Organism-specific databases

CTDi4654.
MGIiMGI:97275. Myod1.

Phylogenomic databases

eggNOGiNOG292792.
GeneTreeiENSGT00530000063004.
HOGENOMiHOG000234800.
HOVERGENiHBG006429.
InParanoidiP10085.
KOiK09064.
OMAiDPRLMHV.
OrthoDBiEOG76QFK1.
TreeFamiTF316344.

Enzyme and pathway databases

ReactomeiREACT_304595. CDO in myogenesis.

Miscellaneous databases

EvolutionaryTraceiP10085.
NextBioi292797.
PROiP10085.
SOURCEiSearch...

Gene expression databases

BgeeiP10085.
CleanExiMM_MYOD1.
GenevisibleiP10085. MM.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR002546. Basic.
IPR011598. bHLH_dom.
IPR022032. Myf5.
[Graphical view]
PfamiPF01586. Basic. 1 hit.
PF00010. HLH. 1 hit.
PF12232. Myf5. 1 hit.
[Graphical view]
SMARTiSM00520. BASIC. 1 hit.
SM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Expression of a single transfected cDNA converts fibroblasts to myoblasts."
    Davis R.L., Weintraub H., Lassar A.B.
    Cell 51:987-1000(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Characterisation of a genomic clone covering the structural mouse MyoD1 gene and its promoter region."
    Zingg J.-M., Alva G.P., Jost J.-P.
    Nucleic Acids Res. 19:6433-6439(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Myogenic lineage determination and differentiation: evidence for a regulatory gene pathway."
    Pinney D.F., Pearson-White S.H., Konieczny S.F., Latham K.E., Emerson C.P. Jr.
    Cell 53:781-793(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head.
  5. "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].
  6. "MyoD1: a nuclear phosphoprotein requiring a Myc homology region to convert fibroblasts to myoblasts."
    Tapscott S.J., Davis R.L., Thayer M.J., Cheng P.-F., Weintraub H., Lassar A.B.
    Science 242:405-411(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "p300 is required for MyoD-dependent cell cycle arrest and muscle-specific gene transcription."
    Puri P.L., Avantaggiati M.L., Balsano C., Sang N., Graessmann A., Giordano A., Levrero M.
    EMBO J. 16:369-383(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION.
  8. "The basic domain of myogenic basic helix-loop-helix (bHLH) proteins is the novel target for direct inhibition by another bHLH protein, Twist."
    Hamamori Y., Wu H.Y., Sartorelli V., Kedes L.
    Mol. Cell. Biol. 17:6563-6573(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INHIBITION BY TWIST.
  9. "Control of muscle development by dueling HATs and HDACs."
    McKinsey T.A., Zhang C.L., Olson E.N.
    Curr. Opin. Genet. Dev. 11:497-504(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ACETYLATION/DEACETYLATION.
  10. "Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state."
    Fulco M., Schiltz R.L., Iezzi S., King M.T., Zhao P., Kashiwaya Y., Hoffman E., Veech R.L., Sartorelli V.
    Mol. Cell 12:51-62(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEACETYLATION BY SIRT1.
  11. "The RNA helicases p68/p72 and the noncoding RNA SRA are coregulators of MyoD and skeletal muscle differentiation."
    Caretti G., Schiltz R.L., Dilworth F.J., Di Padova M., Zhao P., Ogryzko V., Fuller-Pace F.V., Hoffman E.P., Tapscott S.J., Sartorelli V.
    Dev. Cell 11:547-560(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDX5.
  12. "Glucocorticoid-induced leucine zipper (GILZ) and long GILZ inhibit myogenic differentiation and mediate anti-myogenic effects of glucocorticoids."
    Bruscoli S., Donato V., Velardi E., Di Sante M., Migliorati G., Donato R., Riccardi C.
    J. Biol. Chem. 285:10385-10396(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TSC22D3.
    Strain: DBA/2.
    Tissue: Myoblast.
  13. Cited for: INTERACTION WITH SETD3.
  14. "Sequential association of myogenic regulatory factors and E proteins at muscle-specific genes."
    Londhe P., Davie J.K.
    Skelet. Muscle 1:14-14(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PROMOTER BINDING.
  15. Cited for: INTERACTION WITH CHD2.
  16. "Crystal structure of MyoD bHLH domain-DNA complex: perspectives on DNA recognition and implications for transcriptional activation."
    Ma P.C.M., Rould M.A., Weintraub H., Pabo C.O.
    Cell 77:451-459(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 102-166.

Entry informationi

Entry nameiMYOD1_MOUSE
AccessioniPrimary (citable) accession number: P10085
Secondary accession number(s): Q8C6B1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 27, 2011
Last modified: July 22, 2015
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.