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Protein

Glutamine--tRNA ligase

Gene

QARS

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

Functioni

Plays a critical role in brain development.1 Publication

Catalytic activityi

ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln).

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei496ATPBy similarity1

GO - Molecular functioni

GO - Biological processi

  • brain development Source: UniProtKB
  • glutaminyl-tRNA aminoacylation Source: UniProtKB
  • tRNA aminoacylation for protein translation Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS10441-MONOMER.
ReactomeiR-HSA-2408517. SeMet incorporation into proteins.
R-HSA-379716. Cytosolic tRNA aminoacylation.
R-HSA-379726. Mitochondrial tRNA aminoacylation.

Protein family/group databases

MoonProtiP47897.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine--tRNA ligase (EC:6.1.1.18)
Alternative name(s):
Glutaminyl-tRNA synthetase
Short name:
GlnRS
Gene namesi
Name:QARS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:9751. QARS.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: GO_Central
  • mitochondrial matrix Source: Reactome
  • mitochondrion Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Microcephaly, progressive, with seizures and cerebral and cerebellar atrophy (MSCCA)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA severe, autosomal recessive, neurodevelopmental and neurodegenerative disorder characterized by progressive microcephaly, severe seizures in infancy, atrophy of the cerebral cortex and cerebellar vermis, and mild atrophy of the cerebellar hemispheres, resulting in profoundly delayed development and hypotonia.
See also OMIM:615760
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07118945G → V in MSCCA; results in reduced glutaminyl-tRNA aminoacylation activity; does not affect interaction with RARS. 1 PublicationCorresponds to variant rs587777331dbSNPEnsembl.1
Natural variantiVAR_07119057Y → H in MSCCA; results in reduced glutaminyl-tRNA aminoacylation activity; does not affect interaction with RARS. 1 PublicationCorresponds to variant rs587777333dbSNPEnsembl.1
Natural variantiVAR_071191403R → W in MSCCA; results in loss of glutaminyl-tRNA aminoacylation activity; does not interact with RARS; results in reduced protein solubility. 1 PublicationCorresponds to variant rs587777332dbSNPEnsembl.1
Natural variantiVAR_071192515R → W in MSCCA; results in loss of glutaminyl-tRNA aminoacylation activity; results in reduced protein solubility. 1 PublicationCorresponds to variant rs587777334dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Epilepsy, Primary microcephaly

Organism-specific databases

DisGeNETi5859.
MalaCardsiQARS.
MIMi615760. phenotype.
OpenTargetsiENSG00000172053.
Orphaneti404437. Diffuse cerebral and cerebellar atrophy-intractable seizures-progressive microcephaly syndrome.
PharmGKBiPA34093.

Chemistry databases

ChEMBLiCHEMBL3054.
DrugBankiDB00130. L-Glutamine.

Polymorphism and mutation databases

DMDMi1351170.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001958602 – 775Glutamine--tRNA ligaseAdd BLAST774

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei70PhosphoserineCombined sources1
Modified residuei309N6-acetyllysineCombined sources1
Modified residuei495PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP47897.
MaxQBiP47897.
PaxDbiP47897.
PeptideAtlasiP47897.
PRIDEiP47897.

PTM databases

iPTMnetiP47897.
PhosphoSitePlusiP47897.
SwissPalmiP47897.

Expressioni

Tissue specificityi

Highly expressed in fetal cerebral cortex, particularly in the ventricular zone, inner subventricular zone, outer subventricular zone, and cortical plate.1 Publication

Gene expression databases

BgeeiENSG00000172053.
CleanExiHS_QARS.
ExpressionAtlasiP47897. baseline and differential.
GenevisibleiP47897. HS.

Organism-specific databases

HPAiHPA036986.
HPA036987.

Interactioni

Subunit structurei

Part of a multisubunit complex that groups tRNA ligases for Arg, Asp, Glu, Gln, Ile, Leu, Lys, Met and Pro. Interacts with RARS.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AESQ081173EBI-347462,EBI-717810
DTX2Q86UW93EBI-10209725,EBI-740376
KLC3Q6P5973EBI-10209725,EBI-1643885
LZTS2Q9BRK45EBI-347462,EBI-741037
RNF11Q9Y3C54EBI-347462,EBI-396669
TCF12Q990813EBI-347462,EBI-722877
TRAF4Q9BUZ45EBI-347462,EBI-3650647
TRIP13Q156455EBI-347462,EBI-358993
VPS37BQ9H9H43EBI-10209725,EBI-4400866

Protein-protein interaction databases

BioGridi111797. 124 interactors.
IntActiP47897. 80 interactors.
MINTiMINT-5004268.
STRINGi9606.ENSP00000307567.

Chemistry databases

BindingDBiP47897.

Structurei

Secondary structure

1775
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 12Combined sources7
Helixi17 – 25Combined sources9
Helixi27 – 42Combined sources16
Turni43 – 45Combined sources3
Helixi50 – 62Combined sources13
Helixi66 – 68Combined sources3
Helixi69 – 77Combined sources9
Helixi84 – 94Combined sources11
Helixi104 – 110Combined sources7
Helixi119 – 140Combined sources22
Helixi141 – 143Combined sources3
Helixi147 – 154Combined sources8
Helixi162 – 177Combined sources16
Helixi220 – 223Combined sources4
Helixi226 – 229Combined sources4
Helixi237 – 239Combined sources3
Helixi249 – 260Combined sources12
Beta strandi265 – 268Combined sources4
Helixi278 – 293Combined sources16
Beta strandi297 – 302Combined sources6
Helixi312 – 324Combined sources13
Beta strandi330 – 334Combined sources5
Helixi335 – 338Combined sources4
Helixi339 – 351Combined sources13
Beta strandi354 – 358Combined sources5
Turni374 – 377Combined sources4
Helixi380 – 391Combined sources12
Beta strandi401 – 404Combined sources4
Beta strandi416 – 420Combined sources5
Turni426 – 428Combined sources3
Beta strandi433 – 436Combined sources4
Helixi438 – 448Combined sources11
Beta strandi452 – 457Combined sources6
Helixi464 – 473Combined sources10
Beta strandi480 – 484Combined sources5
Beta strandi487 – 489Combined sources3
Helixi496 – 504Combined sources9
Beta strandi507 – 510Combined sources4
Helixi519 – 524Combined sources6
Helixi529 – 539Combined sources11
Beta strandi546 – 548Combined sources3
Helixi551 – 564Combined sources14
Beta strandi570 – 576Combined sources7
Beta strandi578 – 581Combined sources4
Beta strandi592 – 594Combined sources3
Helixi599 – 601Combined sources3
Beta strandi603 – 606Combined sources4
Beta strandi613 – 615Combined sources3
Turni616 – 618Combined sources3
Beta strandi647 – 650Combined sources4
Beta strandi654 – 656Combined sources3
Beta strandi661 – 663Combined sources3
Beta strandi681 – 683Combined sources3
Beta strandi685 – 692Combined sources8
Beta strandi695 – 700Combined sources6
Turni702 – 705Combined sources4
Turni711 – 714Combined sources4
Beta strandi720 – 722Combined sources3
Beta strandi725 – 728Combined sources4
Beta strandi732 – 734Combined sources3
Beta strandi740 – 743Combined sources4
Turni744 – 746Combined sources3
Beta strandi747 – 751Combined sources5
Beta strandi757 – 759Combined sources3
Beta strandi761 – 766Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3ZX-ray4.03C1-775[»]
4YE6X-ray2.40A1-775[»]
4YE8X-ray3.30A1-775[»]
4YE9X-ray2.70A1-775[»]
ProteinModelPortaliP47897.
SMRiP47897.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi270 – 280"HIGH" regionAdd BLAST11
Motifi493 – 497"KMSKS" region5

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1148. Eukaryota.
COG0008. LUCA.
GeneTreeiENSGT00550000074972.
HOGENOMiHOG000259233.
HOVERGENiHBG000889.
InParanoidiP47897.
KOiK01886.
OMAiFNAFKIL.
OrthoDBiEOG091G026F.
PhylomeDBiP47897.
TreeFamiTF105683.

Family and domain databases

Gene3Di1.10.1160.10. 1 hit.
2.40.240.10. 2 hits.
3.40.50.620. 2 hits.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR004514. Gln-tRNA-synth.
IPR007638. Gln-tRNA-synth_Ib_RNA-bd_2.
IPR007639. Gln-tRNA-synth_Ib_RNA-bd_N.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
PF04558. tRNA_synt_1c_R1. 1 hit.
PF04557. tRNA_synt_1c_R2. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF50715. SSF50715. 1 hit.
TIGRFAMsiTIGR00440. glnS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 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: P47897-1) [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
MAALDSLSLF TSLGLSEQKA RETLKNSALS AQLREAATQA QQTLGSTIDK
60 70 80 90 100
ATGILLYGLA SRLRDTRRLS FLVSYIASKK IHTEPQLSAA LEYVRSHPLD
110 120 130 140 150
PIDTVDFERE CGVGVIVTPE QIEEAVEAAI NRHRPQLLVE RYHFNMGLLM
160 170 180 190 200
GEARAVLKWA DGKMIKNEVD MQVLHLLGPK LEADLEKKFK VAKARLEETD
210 220 230 240 250
RRTAKDVVEN GETADQTLSL MEQLRGEALK FHKPGENYKT PGYVVTPHTM
260 270 280 290 300
NLLKQHLEIT GGQVRTRFPP EPNGILHIGH AKAINFNFGY AKANNGICFL
310 320 330 340 350
RFDDTNPEKE EAKFFTAICD MVAWLGYTPY KVTYASDYFD QLYAWAVELI
360 370 380 390 400
RRGLAYVCHQ RGEELKGHNT LPSPWRDRPM EESLLLFEAM RKGKFSEGEA
410 420 430 440 450
TLRMKLVMED GKMDPVAYRV KYTPHHRTGD KWCIYPTYDY THCLCDSIEH
460 470 480 490 500
ITHSLCTKEF QARRSSYFWL CNALDVYCPV QWEYGRLNLH YAVVSKRKIL
510 520 530 540 550
QLVATGAVRD WDDPRLFTLT ALRRRGFPPE AINNFCARVG VTVAQTTMEP
560 570 580 590 600
HLLEACVRDV LNDTAPRAMA VLESLRVIIT NFPAAKSLDI QVPNFPADET
610 620 630 640 650
KGFHQVPFAP IVFIERTDFK EEPEPGFKRL AWGQPVGLRH TGYVIELQHV
660 670 680 690 700
VKGPSGCVES LEVTCRRADA GEKPKAFIHW VSQPLMCEVR LYERLFQHKN
710 720 730 740 750
PEDPTEVPGG FLSDLNLASL HVVDAALVDC SVALAKPFDK FQFERLGYFS
760 770
VDPDSHQGKL VFNRTVTLKE DPGKV
Length:775
Mass (Da):87,799
Last modified:February 1, 1996 - v1
Checksum:iADDE23E6C442FF73
GO
Isoform 2 (identifier: P47897-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     78-89: SKKIHTEPQLSA → T

Show »
Length:764
Mass (Da):86,579
Checksum:iBA9B1C92EE0C2F72
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07118945G → V in MSCCA; results in reduced glutaminyl-tRNA aminoacylation activity; does not affect interaction with RARS. 1 PublicationCorresponds to variant rs587777331dbSNPEnsembl.1
Natural variantiVAR_07119057Y → H in MSCCA; results in reduced glutaminyl-tRNA aminoacylation activity; does not affect interaction with RARS. 1 PublicationCorresponds to variant rs587777333dbSNPEnsembl.1
Natural variantiVAR_071191403R → W in MSCCA; results in loss of glutaminyl-tRNA aminoacylation activity; does not interact with RARS; results in reduced protein solubility. 1 PublicationCorresponds to variant rs587777332dbSNPEnsembl.1
Natural variantiVAR_071192515R → W in MSCCA; results in loss of glutaminyl-tRNA aminoacylation activity; results in reduced protein solubility. 1 PublicationCorresponds to variant rs587777334dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_05510778 – 89SKKIH…PQLSA → T in isoform 2. 1 PublicationAdd BLAST12

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76013 mRNA. Translation: CAA53600.1.
AK301559 mRNA. Translation: BAG63054.1.
AC135506 Genomic DNA. No translation available.
BC000394 mRNA. Translation: AAH00394.1.
BC001567 mRNA. Translation: AAH01567.1.
BC029739 mRNA. Translation: AAH29739.1.
CCDSiCCDS2788.1. [P47897-1]
CCDS63633.1. [P47897-2]
PIRiI37422.
RefSeqiNP_001259002.1. NM_001272073.1. [P47897-2]
NP_005042.1. NM_005051.2. [P47897-1]
UniGeneiHs.79322.

Genome annotation databases

EnsembliENST00000306125; ENSP00000307567; ENSG00000172053. [P47897-1]
ENST00000414533; ENSP00000390015; ENSG00000172053. [P47897-2]
GeneIDi5859.
KEGGihsa:5859.
UCSCiuc003cvx.5. human. [P47897-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76013 mRNA. Translation: CAA53600.1.
AK301559 mRNA. Translation: BAG63054.1.
AC135506 Genomic DNA. No translation available.
BC000394 mRNA. Translation: AAH00394.1.
BC001567 mRNA. Translation: AAH01567.1.
BC029739 mRNA. Translation: AAH29739.1.
CCDSiCCDS2788.1. [P47897-1]
CCDS63633.1. [P47897-2]
PIRiI37422.
RefSeqiNP_001259002.1. NM_001272073.1. [P47897-2]
NP_005042.1. NM_005051.2. [P47897-1]
UniGeneiHs.79322.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3ZX-ray4.03C1-775[»]
4YE6X-ray2.40A1-775[»]
4YE8X-ray3.30A1-775[»]
4YE9X-ray2.70A1-775[»]
ProteinModelPortaliP47897.
SMRiP47897.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111797. 124 interactors.
IntActiP47897. 80 interactors.
MINTiMINT-5004268.
STRINGi9606.ENSP00000307567.

Chemistry databases

BindingDBiP47897.
ChEMBLiCHEMBL3054.
DrugBankiDB00130. L-Glutamine.

Protein family/group databases

MoonProtiP47897.

PTM databases

iPTMnetiP47897.
PhosphoSitePlusiP47897.
SwissPalmiP47897.

Polymorphism and mutation databases

DMDMi1351170.

Proteomic databases

EPDiP47897.
MaxQBiP47897.
PaxDbiP47897.
PeptideAtlasiP47897.
PRIDEiP47897.

Protocols and materials databases

DNASUi5859.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000306125; ENSP00000307567; ENSG00000172053. [P47897-1]
ENST00000414533; ENSP00000390015; ENSG00000172053. [P47897-2]
GeneIDi5859.
KEGGihsa:5859.
UCSCiuc003cvx.5. human. [P47897-1]

Organism-specific databases

CTDi5859.
DisGeNETi5859.
GeneCardsiQARS.
HGNCiHGNC:9751. QARS.
HPAiHPA036986.
HPA036987.
MalaCardsiQARS.
MIMi603727. gene.
615760. phenotype.
neXtProtiNX_P47897.
OpenTargetsiENSG00000172053.
Orphaneti404437. Diffuse cerebral and cerebellar atrophy-intractable seizures-progressive microcephaly syndrome.
PharmGKBiPA34093.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1148. Eukaryota.
COG0008. LUCA.
GeneTreeiENSGT00550000074972.
HOGENOMiHOG000259233.
HOVERGENiHBG000889.
InParanoidiP47897.
KOiK01886.
OMAiFNAFKIL.
OrthoDBiEOG091G026F.
PhylomeDBiP47897.
TreeFamiTF105683.

Enzyme and pathway databases

BioCyciZFISH:HS10441-MONOMER.
ReactomeiR-HSA-2408517. SeMet incorporation into proteins.
R-HSA-379716. Cytosolic tRNA aminoacylation.
R-HSA-379726. Mitochondrial tRNA aminoacylation.

Miscellaneous databases

ChiTaRSiQARS. human.
GeneWikiiQARS.
GenomeRNAii5859.
PROiP47897.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000172053.
CleanExiHS_QARS.
ExpressionAtlasiP47897. baseline and differential.
GenevisibleiP47897. HS.

Family and domain databases

Gene3Di1.10.1160.10. 1 hit.
2.40.240.10. 2 hits.
3.40.50.620. 2 hits.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR004514. Gln-tRNA-synth.
IPR007638. Gln-tRNA-synth_Ib_RNA-bd_2.
IPR007639. Gln-tRNA-synth_Ib_RNA-bd_N.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
PF04558. tRNA_synt_1c_R1. 1 hit.
PF04557. tRNA_synt_1c_R2. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF50715. SSF50715. 1 hit.
TIGRFAMsiTIGR00440. glnS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSYQ_HUMAN
AccessioniPrimary (citable) accession number: P47897
Secondary accession number(s): B4DWJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 30, 2016
This is version 168 of the entry and version 1 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.