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Protein

Importin-7

Gene

IPO7

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

Functioni

Functions in nuclear protein import, either by acting as autonomous nuclear transport receptor or as an adapter-like protein in association with the importin-beta subunit KPNB1. Acting autonomously, is thought to serve itself as receptor for nuclear localization signals (NLS) and to promote translocation of import substrates through the nuclear pore complex (NPC) by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In association with KPNB1 mediates the nuclear import of H1 histone and the Ran-binding site of IPO7 is not required but synergizes with that of KPNB1 in importin/substrate complex dissociation. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. In vitro, mediates the nuclear import of HIV-1 reverse transcription complex (RTC) integrase. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev.3 Publications

GO - Molecular functioni

  • GTPase regulator activity Source: ProtInc
  • Ran GTPase binding Source: ProtInc
  • transporter activity Source: ProtInc

GO - Biological processi

  • innate immune response Source: Ensembl
  • protein import into nucleus Source: Ensembl
  • regulation of catalytic activity Source: GOC
  • signal transduction Source: ProtInc
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Importin-7
Short name:
Imp7
Alternative name(s):
Ran-binding protein 7
Short name:
RanBP7
Gene namesi
Name:IPO7
Synonyms:RANBP7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:9852. IPO7.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • membrane Source: UniProtKB
  • nuclear pore Source: ProtInc
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi61 – 611K → A or D: Lowered affinity for RanGTP-binding. 1 Publication

Organism-specific databases

PharmGKBiPA34213.

Polymorphism and mutation databases

BioMutaiIPO7.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10381038Importin-7PRO_0000120750Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine4 Publications
Modified residuei886 – 8861Phosphoserine1 Publication
Modified residuei898 – 8981Phosphothreonine1 Publication
Modified residuei903 – 9031Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO95373.
PaxDbiO95373.
PRIDEiO95373.

PTM databases

PhosphoSiteiO95373.

Expressioni

Gene expression databases

BgeeiO95373.
CleanExiHS_IPO7.
ExpressionAtlasiO95373. baseline and differential.
GenevisibleiO95373. HS.

Organism-specific databases

HPAiHPA019002.
HPA056590.

Interactioni

Subunit structurei

Interacts with H2A, H2B, H3 and H4 histones (By similarity). Forms a heterodimer with KPNB1. Interacts with KPNB1, SNUPN, XPO1, RPL23A, RPS7, RPL5 and HIV-1 reverse transcription complex integrase. Binds directly to nuclear pore complexes (By similarity). Interacts with H2A, H2B, H3 and H4 histones. Binds to HIV-1 Rev.By similarity5 Publications

Protein-protein interaction databases

BioGridi115782. 44 interactions.
DIPiDIP-32574N.
IntActiO95373. 17 interactions.
MINTiMINT-5003960.
STRINGi9606.ENSP00000369042.

Structurei

3D structure databases

ProteinModelPortaliO95373.
SMRiO95373. Positions 2-440.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 10180Importin N-terminalPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi885 – 95773Asp-richAdd
BLAST

Sequence similaritiesi

Belongs to the importin beta family.Curated
Contains 1 importin N-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5656.
GeneTreeiENSGT00550000074736.
HOGENOMiHOG000006586.
HOVERGENiHBG006824.
InParanoidiO95373.
OMAiPIDEYQI.
OrthoDBiEOG7TF787.
PhylomeDBiO95373.
TreeFamiTF300634.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR013713. Cse1.
IPR001494. Importin-beta_N.
[Graphical view]
PfamiPF08506. Cse1. 1 hit.
PF03810. IBN_N. 1 hit.
[Graphical view]
SMARTiSM00913. IBN_N. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
PROSITEiPS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O95373-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPNTIIEAL RGTMDPALRE AAERQLNEAH KSLNFVSTLL QITMSEQLDL
60 70 80 90 100
PVRQAGVIYL KNMITQYWPD RETAPGDISP YTIPEEDRHC IRENIVEAII
110 120 130 140 150
HSPELIRVQL TTCIHHIIKH DYPSRWTAIV DKIGFYLQSD NSACWLGILL
160 170 180 190 200
CLYQLVKNYE YKKPEERSPL VAAMQHFLPV LKDRFIQLLS DQSDQSVLIQ
210 220 230 240 250
KQIFKIFYAL VQYTLPLELI NQQNLTEWIE ILKTVVNRDV PNETLQVEED
260 270 280 290 300
DRPELPWWKC KKWALHILAR LFERYGSPGN VSKEYNEFAE VFLKAFAVGV
310 320 330 340 350
QQVLLKVLYQ YKEKQYMAPR VLQQTLNYIN QGVSHALTWK NLKPHIQGII
360 370 380 390 400
QDVIFPLMCY TDADEELWQE DPYEYIRMKF DVFEDFISPT TAAQTLLFTA
410 420 430 440 450
CSKRKEVLQK TMGFCYQILT EPNADPRKKD GALHMIGSLA EILLKKKIYK
460 470 480 490 500
DQMEYMLQNH VFPLFSSELG YMRARACWVL HYFCEVKFKS DQNLQTALEL
510 520 530 540 550
TRRCLIDDRE MPVKVEAAIA LQVLISNQEK AKEYITPFIR PVMQALLHII
560 570 580 590 600
RETENDDLTN VIQKMICEYS EEVTPIAVEM TQHLAMTFNQ VIQTGPDEEG
610 620 630 640 650
SDDKAVTAMG ILNTIDTLLS VVEDHKEITQ QLEGICLQVI GTVLQQHVLE
660 670 680 690 700
FYEEIFSLAH SLTCQQVSPQ MWQLLPLVFE VFQQDGFDYF TDMMPLLHNY
710 720 730 740 750
VTVDTDTLLS DTKYLEMIYS MCKKVLTGVA GEDAECHAAK LLEVIILQCK
760 770 780 790 800
GRGIDQCIPL FVEAALERLT REVKTSELRT MCLQVAIAAL YYNPHLLLNT
810 820 830 840 850
LENLRFPNNV EPVTNHFITQ WLNDVDCFLG LHDRKMCVLG LCALIDMEQI
860 870 880 890 900
PQVLNQVSGQ ILPAFILLFN GLKRAYACHA EHENDSDDDD EAEDDDETEE
910 920 930 940 950
LGSDEDDIDE DGQEYLEILA KQAGEDGDDE DWEEDDAEET ALEGYSTIID
960 970 980 990 1000
DEDNPVDEYQ IFKAIFQTIQ NRNPVWYQAL THGLNEEQRK QLQDIATLAD
1010 1020 1030
QRRAAHESKM IEKHGGYKFS APVVPSSFNF GGPAPGMN
Length:1,038
Mass (Da):119,517
Last modified:May 1, 1999 - v1
Checksum:i355237CA1DA2D313
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti111 – 1111T → N.
Corresponds to variant rs11042340 [ dbSNP | Ensembl ].
VAR_050003

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF098799 mRNA. Translation: AAC68903.1.
AK312885 mRNA. Translation: BAG35733.1.
AC055845 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68593.1.
BC114929 mRNA. Translation: AAI14930.1.
AJ295844 Genomic DNA. Translation: CAC17609.1.
AL137335 mRNA. Translation: CAB70698.1.
CCDSiCCDS31425.1.
PIRiT46501.
RefSeqiNP_006382.1. NM_006391.2.
UniGeneiHs.744911.

Genome annotation databases

EnsembliENST00000379719; ENSP00000369042; ENSG00000205339.
GeneIDi10527.
KEGGihsa:10527.
UCSCiuc001mho.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF098799 mRNA. Translation: AAC68903.1.
AK312885 mRNA. Translation: BAG35733.1.
AC055845 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68593.1.
BC114929 mRNA. Translation: AAI14930.1.
AJ295844 Genomic DNA. Translation: CAC17609.1.
AL137335 mRNA. Translation: CAB70698.1.
CCDSiCCDS31425.1.
PIRiT46501.
RefSeqiNP_006382.1. NM_006391.2.
UniGeneiHs.744911.

3D structure databases

ProteinModelPortaliO95373.
SMRiO95373. Positions 2-440.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115782. 44 interactions.
DIPiDIP-32574N.
IntActiO95373. 17 interactions.
MINTiMINT-5003960.
STRINGi9606.ENSP00000369042.

PTM databases

PhosphoSiteiO95373.

Polymorphism and mutation databases

BioMutaiIPO7.

Proteomic databases

MaxQBiO95373.
PaxDbiO95373.
PRIDEiO95373.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379719; ENSP00000369042; ENSG00000205339.
GeneIDi10527.
KEGGihsa:10527.
UCSCiuc001mho.3. human.

Organism-specific databases

CTDi10527.
GeneCardsiGC11P009362.
HGNCiHGNC:9852. IPO7.
HPAiHPA019002.
HPA056590.
MIMi605586. gene.
neXtProtiNX_O95373.
PharmGKBiPA34213.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5656.
GeneTreeiENSGT00550000074736.
HOGENOMiHOG000006586.
HOVERGENiHBG006824.
InParanoidiO95373.
OMAiPIDEYQI.
OrthoDBiEOG7TF787.
PhylomeDBiO95373.
TreeFamiTF300634.

Miscellaneous databases

ChiTaRSiIPO7. human.
GeneWikiiIPO7.
GenomeRNAii10527.
NextBioi39938.
PROiO95373.
SOURCEiSearch...

Gene expression databases

BgeeiO95373.
CleanExiHS_IPO7.
ExpressionAtlasiO95373. baseline and differential.
GenevisibleiO95373. HS.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR013713. Cse1.
IPR001494. Importin-beta_N.
[Graphical view]
PfamiPF08506. Cse1. 1 hit.
PF03810. IBN_N. 1 hit.
[Graphical view]
SMARTiSM00913. IBN_N. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
PROSITEiPS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import of ribosomal proteins in mammalian cells."
    Jaekel S., Goerlich D.
    EMBO J. 17:4491-4502(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RPL23A; RPS7; RPL5 AND KPNB1.
  2. "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].
    Tissue: Uterus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-11, ACETYLATION AT MET-1.
    Tissue: Platelet.
  7. "Comparative sequencing of a 1 Mb region in man (chromosome 11p15) and mouse (chromosome 7)."
    Cichutek A., Winterpacht A., Hankeln T., Schmidt E.R., Zabel B.U.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-1038.
    Tissue: Blood.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 831-1038.
    Tissue: Testis.
  9. Cited for: CHARACTERIZATION.
  10. "The importin beta/importin 7 heterodimer is a functional nuclear import receptor for histone H1."
    Jaekel S., Albig W., Kutay U., Bischoff F.R., Schwamborn K., Doenecke D., Goerlich D.
    EMBO J. 18:2411-2423(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH H1 HISTONE AND KPNB1, MUTAGENESIS OF LYS-61.
  11. Cited for: IDENTIFICATION IN AN EXPORT RECEPTOR COMPLEX, INTERACTION WITH KPNB1; SNUPN AND XPO1.
  12. "Nuclear import of HIV-1 intracellular reverse transcription complexes is mediated by importin 7."
    Fassati A., Goerlich D., Harrison I., Zaytseva L., Mingot J.-M.
    EMBO J. 22:3675-3685(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH INTEGRASE OF HIV-1 REVERSE TRANSCRIPTION COMPLEX.
  13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Multiple importins function as nuclear transport receptors for the Rev protein of human immunodeficiency virus type 1."
    Arnold M., Nath A., Hauber J., Kehlenbach R.H.
    J. Biol. Chem. 281:20883-20890(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 REV.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886; THR-898 AND SER-903, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiIPO7_HUMAN
AccessioniPrimary (citable) accession number: O95373
Secondary accession number(s): A6NNM5
, B2R786, Q1RMF7, Q9H177, Q9NTE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: May 1, 1999
Last modified: July 22, 2015
This is version 131 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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

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.