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Protein

Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase

Gene

FTSJ1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs.UniRule annotation

Catalytic activityi

S-adenosyl-L-methionine + cytidine(32)/guanosine(34) in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine(32)/2'-O-methylguanosine(34) in tRNA.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531S-adenosyl-L-methionine; via amide nitrogenUniRule annotation
Binding sitei55 – 551S-adenosyl-L-methionine; via amide nitrogenUniRule annotation
Binding sitei75 – 751S-adenosyl-L-methionineUniRule annotation
Binding sitei91 – 911S-adenosyl-L-methionineUniRule annotation
Binding sitei116 – 1161S-adenosyl-L-methionineUniRule annotation
Active sitei156 – 1561Proton acceptorUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferaseUniRule annotation (EC:2.1.1.205UniRule annotation)
Alternative name(s):
2'-O-ribose RNA methyltransferase TRM7 homologUniRule annotation
Protein ftsJ homolog 1UniRule annotation
Gene namesi
Name:FTSJ1UniRule annotation
ORF Names:JM23
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:13254. FTSJ1.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Mental retardation, X-linked 44 (MRX44)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations.

See also OMIM:309549

Keywords - Diseasei

Mental retardation

Organism-specific databases

MIMi309549. phenotype.
Orphaneti777. X-linked non-syndromic intellectual disability.
PharmGKBiPA28417.

Polymorphism and mutation databases

DMDMi12643879.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 329329Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferasePRO_0000155575Add
BLAST

Proteomic databases

MaxQBiQ9UET6.
PaxDbiQ9UET6.
PRIDEiQ9UET6.

PTM databases

PhosphoSiteiQ9UET6.

Expressioni

Tissue specificityi

Found in fetal brain, lung, liver and kidney. In the adult brain, expressed in amygdala, caudate nucleus, corpus callosum, hippocampus and thalamus.1 Publication

Gene expression databases

BgeeiQ9UET6.
CleanExiHS_FTSJ1.
ExpressionAtlasiQ9UET6. baseline and differential.
GenevisibleiQ9UET6. HS.

Organism-specific databases

HPAiHPA002718.

Interactioni

Protein-protein interaction databases

BioGridi117291. 4 interactions.
IntActiQ9UET6. 1 interaction.
STRINGi9606.ENSP00000326948.

Structurei

3D structure databases

ProteinModelPortaliQ9UET6.
SMRiQ9UET6. Positions 20-201.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family. TRM7 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0293.
GeneTreeiENSGT00730000111146.
HOGENOMiHOG000162368.
HOVERGENiHBG017749.
KOiK14864.
OMAiHFEGQPA.
PhylomeDBiQ9UET6.
TreeFamiTF314897.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01547. RNA_methyltr_E.
MF_03162. RNA_methyltr_E_TRM7.
InterProiIPR028590. RNA_methyltr_E_Trm7.
IPR015507. rRNA-MeTfrase_E.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR10920. PTHR10920. 1 hit.
PfamiPF01728. FtsJ. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9UET6-1) [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
MGRTSKDKRD VYYRLAKENG WRARSAFKLL QLDKEFQLFQ GVTRAVDLCA
60 70 80 90 100
APGSWSQVLS QKIGGQGSGH VVAVDLQAMA PLPGVVQIQG DITQLSTAKE
110 120 130 140 150
IIQHFKGCPA DLVVCDGAPD VTGLHDVDEY MQAQLLLAAL NIATHVLKPG
160 170 180 190 200
GCFVAKIFRG RDVTLLYSQL QVFFSSVLCA KPRSSRNSSI EAFAVCQGYD
210 220 230 240 250
PPEGFIPDLS KPLLDHSYDP DFNQLDGPTR IIVPFVTCGD LSSYDSDRSY
260 270 280 290 300
PLDLEGGSEY KYTPPTQPPI SPPYQEACTL KRKGQLAKEI RPQDCPISRV
310 320
DTFPQPLAAP QCHTLLAPEM EDNEMSCSP
Length:329
Mass (Da):36,079
Last modified:December 1, 2000 - v2
Checksum:i9A85D63A4FA80615
GO
Isoform 2 (identifier: Q9UET6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     219-220: Missing.

Show »
Length:327
Mass (Da):35,867
Checksum:i54417CCDEB515C55
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei219 – 2202Missing in isoform 2. 1 PublicationVSP_041419

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF063015 mRNA. Translation: AAC33734.1.
AJ005892 mRNA. Translation: CAA06749.1.
AK315138 mRNA. Translation: BAG37587.1.
AF196972 Genomic DNA. No translation available.
CH471224 Genomic DNA. Translation: EAW50782.1.
BC023584 mRNA. Translation: AAH23584.1.
CCDSiCCDS14294.1. [Q9UET6-1]
CCDS14295.1. [Q9UET6-2]
RefSeqiNP_001269086.1. NM_001282157.1.
NP_036412.1. NM_012280.3. [Q9UET6-1]
NP_803188.1. NM_177439.2. [Q9UET6-2]
XP_005272652.1. XM_005272595.1. [Q9UET6-2]
UniGeneiHs.23170.

Genome annotation databases

EnsembliENST00000019019; ENSP00000019019; ENSG00000068438. [Q9UET6-2]
ENST00000348411; ENSP00000326948; ENSG00000068438.
GeneIDi24140.
KEGGihsa:24140.
UCSCiuc004djn.1. human. [Q9UET6-2]
uc004djo.1. human. [Q9UET6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF063015 mRNA. Translation: AAC33734.1.
AJ005892 mRNA. Translation: CAA06749.1.
AK315138 mRNA. Translation: BAG37587.1.
AF196972 Genomic DNA. No translation available.
CH471224 Genomic DNA. Translation: EAW50782.1.
BC023584 mRNA. Translation: AAH23584.1.
CCDSiCCDS14294.1. [Q9UET6-1]
CCDS14295.1. [Q9UET6-2]
RefSeqiNP_001269086.1. NM_001282157.1.
NP_036412.1. NM_012280.3. [Q9UET6-1]
NP_803188.1. NM_177439.2. [Q9UET6-2]
XP_005272652.1. XM_005272595.1. [Q9UET6-2]
UniGeneiHs.23170.

3D structure databases

ProteinModelPortaliQ9UET6.
SMRiQ9UET6. Positions 20-201.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117291. 4 interactions.
IntActiQ9UET6. 1 interaction.
STRINGi9606.ENSP00000326948.

PTM databases

PhosphoSiteiQ9UET6.

Polymorphism and mutation databases

DMDMi12643879.

Proteomic databases

MaxQBiQ9UET6.
PaxDbiQ9UET6.
PRIDEiQ9UET6.

Protocols and materials databases

DNASUi24140.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000019019; ENSP00000019019; ENSG00000068438. [Q9UET6-2]
ENST00000348411; ENSP00000326948; ENSG00000068438.
GeneIDi24140.
KEGGihsa:24140.
UCSCiuc004djn.1. human. [Q9UET6-2]
uc004djo.1. human. [Q9UET6-1]

Organism-specific databases

CTDi24140.
GeneCardsiGC0XP048334.
HGNCiHGNC:13254. FTSJ1.
HPAiHPA002718.
MIMi300499. gene.
309549. phenotype.
neXtProtiNX_Q9UET6.
Orphaneti777. X-linked non-syndromic intellectual disability.
PharmGKBiPA28417.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0293.
GeneTreeiENSGT00730000111146.
HOGENOMiHOG000162368.
HOVERGENiHBG017749.
KOiK14864.
OMAiHFEGQPA.
PhylomeDBiQ9UET6.
TreeFamiTF314897.

Miscellaneous databases

ChiTaRSiFTSJ1. human.
GeneWikiiFTSJ1.
GenomeRNAii24140.
NextBioi46813.
PROiQ9UET6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UET6.
CleanExiHS_FTSJ1.
ExpressionAtlasiQ9UET6. baseline and differential.
GenevisibleiQ9UET6. HS.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01547. RNA_methyltr_E.
MF_03162. RNA_methyltr_E_TRM7.
InterProiIPR028590. RNA_methyltr_E_Trm7.
IPR015507. rRNA-MeTfrase_E.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR10920. PTHR10920. 1 hit.
PfamiPF01728. FtsJ. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A human and yeast gene involved in cell division."
    Pengue G., Lutfiyya L.L., Mazzarella R.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "Transcription map in Xp11.23."
    Strom T.M., Nyakatura G., Hellebrand H., Drescher B., Rosenthal A., Meindl A.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  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 1).
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Lymph.
  7. "Mutations in the FTSJ1 gene coding for a novel S-adenosylmethionine-binding protein cause nonsyndromic X-linked mental retardation."
    Freude K., Hoffmann K., Jensen L.-R., Delatycki M.B., des Portes V., Moser B., Hamel B.C.J., van Bokhoven H., Moraine C., Fryns J.-P., Chelly J., Gecz J., Lenzner S., Kalscheuer V.M., Ropers H.-H.
    Am. J. Hum. Genet. 75:305-309(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MRX44, TISSUE SPECIFICITY.
  8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTRM7_HUMAN
AccessioniPrimary (citable) accession number: Q9UET6
Secondary accession number(s): B2RCJ0, O75670
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: July 22, 2015
This is version 132 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 X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  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.