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Protein

RIMS-binding protein 3A

Gene

RIMBP3

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

Names & Taxonomyi

Protein namesi
Recommended name:
RIMS-binding protein 3A
Short name:
RIM-BP3.A
Alternative name(s):
RIMS-binding protein 3.1
Short name:
RIM-BP3.1
Gene namesi
Name:RIMBP3
Synonyms:KIAA1666, RIMBP3A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:29344. RIMBP3.

Pathology & Biotechi

Polymorphism and mutation databases

BioMutaiRIMBP3.
DMDMi380865484.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16391639RIMS-binding protein 3APRO_0000259597Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei260 – 2601PhosphoserineBy similarity
Modified residuei284 – 2841PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9UFD9.
MaxQBiQ9UFD9.
PaxDbiQ9UFD9.
PRIDEiQ9UFD9.

PTM databases

iPTMnetiQ9UFD9.
PhosphoSiteiQ9UFD9.

Expressioni

Gene expression databases

BgeeiQ9UFD9.
CleanExiHS_RIMBP3.
GenevisibleiQ9UFD9. HS.

Organism-specific databases

HPAiHPA001183.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
AESQ081173EBI-10182375,EBI-717810
AQP1P299723EBI-10182375,EBI-745213
CATSPER1Q8NEC53EBI-10182375,EBI-744545
CREB5Q02930-33EBI-10182375,EBI-10192698
CTBP2Q8IY443EBI-10182375,EBI-10171902
DGCR6LQ9BY273EBI-10182375,EBI-742953
DTX2Q4ZH493EBI-10182375,EBI-10192429
FANCLQ9NW383EBI-10182375,EBI-2339898
NOXA1Q86UR13EBI-10182375,EBI-949814
POLR1CO151603EBI-10182375,EBI-1055079
PPIL1Q9Y3C63EBI-10182375,EBI-2557649
PRKAA1Q131313EBI-10182375,EBI-1181405
PRKAB2O437413EBI-10182375,EBI-1053424
TRAF3IP2O437343EBI-10182375,EBI-744798
ZNF488Q96MN93EBI-10182375,EBI-948288

Protein-protein interaction databases

BioGridi124503. 18 interactions.
IntActiQ9UFD9. 15 interactions.
STRINGi9606.ENSP00000391564.

Structurei

Secondary structure

1
1639
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1572 – 15787Combined sources
Turni1582 – 15854Combined sources
Beta strandi1589 – 15913Combined sources
Beta strandi1602 – 16076Combined sources
Beta strandi1614 – 16218Combined sources
Beta strandi1623 – 16275Combined sources
Turni1628 – 16303Combined sources
Beta strandi1631 – 16333Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EGENMR-A1572-1639[»]
ProteinModelPortaliQ9UFD9.
SMRiQ9UFD9. Positions 833-900, 1572-1639.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UFD9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini832 – 89968SH3 1PROSITE-ProRule annotationAdd
BLAST
Domaini995 – 108389Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini1088 – 118497Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini1452 – 152069SH3 2PROSITE-ProRule annotationAdd
BLAST
Domaini1569 – 163668SH3 3PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili21 – 143123Sequence analysisAdd
BLAST
Coiled coili409 – 44234Sequence analysisAdd
BLAST
Coiled coili480 – 619140Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi30 – 137108Arg-richAdd
BLAST
Compositional biasi312 – 36655Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the RIMBP family.Curated
Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 3 SH3 domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG3632. Eukaryota.
ENOG410XZ8W. LUCA.
GeneTreeiENSGT00390000017228.
HOGENOMiHOG000090231.
HOVERGENiHBG096074.
InParanoidiQ9UFD9.
OMAiWETMSST.
PhylomeDBiQ9UFD9.
TreeFamiTF316230.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF07653. SH3_2. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 3 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
SSF50044. SSF50044. 3 hits.
PROSITEiPS50853. FN3. 2 hits.
PS50002. SH3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UFD9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKDSPSPLG ASPKKPGCSS PAAAVLENQR RELEKLRAEL EAERAGWRAE
60 70 80 90 100
RRRFAARERQ LREEAERERR QLADRLRSKW EAQRSRELRQ LQEEMQRERE
110 120 130 140 150
AEIRQLLRWK EAEQRQLQQL LHRERDGVVR QARELQRQLA EELVNRGHCS
160 170 180 190 200
RPGASEVSAA QCRCRLQEVL AQLRWQTDGE QAARIRYLQA ALEVERQLFL
210 220 230 240 250
KYILAHFRGH PALSGSPDPQ AVHSLEEPLP QTSSGSCHAP KPACQLGSLD
260 270 280 290 300
SLSAEVGVRS RSLGLVSSAC SSSPDGLLST HASSLDCFAP ACSRSLDSTR
310 320 330 340 350
SLPKASKSEE RPSSPDTSTP GSRRLSPPPS PLPPPPPPSA HRKLSNPRGG
360 370 380 390 400
EGSESQPCEV LTPSPPGLGH HELIKLNWLL AKALWVLARR CYTLQAENKQ
410 420 430 440 450
LRRAGCPYQA DEKVKRLKVK RAELTGLARR LADRARKLQE TNLRAVSAPI
460 470 480 490 500
PGESCAGLEL CQVFARQRAR DLSEQASAPL AKDKQIEELR QECHLLQARV
510 520 530 540 550
ASGPCSDLHT GRGGPCTQWL NVRDLDRLQR ESQREVLRLQ RQLMLQQGNG
560 570 580 590 600
GAWPEAGGQS ATCEEVRRQM LALERELDQR RRECQELGAQ AAPARRRGEE
610 620 630 640 650
AETQLQAALL KNAWLAEENG RLQAKTDWVR KVEAENSEVR GHLGRACQER
660 670 680 690 700
DASGLIAEQL LQQAARGQDR QQQLQRDPQK ALCDLHPSWK EIQALQCRPG
710 720 730 740 750
HPPEQPWETS QMPESQVKGS RRPKFHARPE DYAVSQPNRD IQEKREASLE
760 770 780 790 800
ESPVALGESA SVPQVSETVP ASQPLSKKTS SQSNSSSEGS MWATVPSSPT
810 820 830 840 850
LDRDTASEVD DLEPDSVSLA LEMGGSAAPA APKLKIFMAQ YNYNPFEGPN
860 870 880 890 900
DHPEGELPLT AGDYIYIFGD MDEDGFYEGE LEDGRRGLVP SNFVEQIPDS
910 920 930 940 950
YIPGCLPAKS PDLGPSQLPA GQDEALEEDS LLSGKAQGVV DRGLCQMVRV
960 970 980 990 1000
GSKTEVATEI LDTKTEACQL GLLQSMGKQG LSRPLLGTKG VLRMAPMQLH
1010 1020 1030 1040 1050
LQNVTATSAN ITWVYSSHRH PHVVYLDDRE HALTPAGVSC YTFQGLCPGT
1060 1070 1080 1090 1100
HYRARVEVRL PRDLLQVYWG TMSSTVTFDT LLAGPPYPPL DVLVERHASP
1110 1120 1130 1140 1150
GVLVVSWLPV TIDSAGSSNG VQVTGYAVYA DGLKVCEVAD ATAGSTLLEF
1160 1170 1180 1190 1200
SQLQVPLTWQ KVSVRTMSLC GESLDSVPAQ IPEDFFMCHR WPETPPFSYT
1210 1220 1230 1240 1250
CGDPSTYRVT FPVCPQKLSL APPSAKASPH NPGSCGEPQA KFLEAFFEEP
1260 1270 1280 1290 1300
PRRQSPVSNL GSEGECPSSG AGSQAQELAE AWEGCRKDLL FQKSPQNHRP
1310 1320 1330 1340 1350
PSVSDQPGEK ENCSQHMGTS KSPAPGFIHL RTECGPRKEP CQEKAALERV
1360 1370 1380 1390 1400
LRQKQDAQGF TPPQLGASQQ YASDFHNVLK EEQEALCLDL WGTERREERR
1410 1420 1430 1440 1450
EPEPHSRQGQ ALGVKRGCQL HEPSSALCPA PSAKVIKMPR GGPQQLGTGA
1460 1470 1480 1490 1500
NTPARVFVAL SDYNPLVMSA NLKAAEEELV FQKRQLLRVW GSQDTHDFYL
1510 1520 1530 1540 1550
SECNRQVGNI PGRLVAEMEV GTEQTDRRWR SPAQGNLPSV AHLEDFQGLT
1560 1570 1580 1590 1600
IPQGSSLVLQ GNSKRLPLWT PKIMIAALDY DPGDGQMGGQ GKGRLALRAG
1610 1620 1630
DVVMVYGPMD DQGFYYGELG GHRGLVPAHL LDHMSLHGH
Length:1,639
Mass (Da):180,717
Last modified:March 21, 2012 - v4
Checksum:iB1A465ECFDBE7903
GO

Sequence cautioni

The sequence AAH35246.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB33336.1 differs from that shown. Reason: Frameshift at position 652. Curated
The sequence CAB61362.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti396 – 3961A → E in BAB33336 (PubMed:11258795).Curated
Sequence conflicti437 – 4371K → E in BAB33336 (PubMed:11258795).Curated
Sequence conflicti653 – 6531S → P in BAB33336 (PubMed:11258795).Curated
Sequence conflicti882 – 8821E → D in BAB33336 (PubMed:11258795).Curated
Sequence conflicti1307 – 13071P → T in AAH35246 (PubMed:15489334).Curated
Sequence conflicti1314 – 13141S → Y in CAB61362 (PubMed:17974005).Curated
Sequence conflicti1314 – 13141S → Y in AAH35246 (PubMed:15489334).Curated
Sequence conflicti1391 – 13911W → R in AAH35246 (PubMed:15489334).Curated
Sequence conflicti1484 – 14841R → K in BAB33336 (PubMed:11258795).Curated
Sequence conflicti1536 – 15361N → H in BAB33336 (PubMed:11258795).Curated
Sequence conflicti1536 – 15361N → H in CAB55970 (PubMed:17974005).Curated
Sequence conflicti1536 – 15361N → H in AAH35246 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1513 – 15131R → C.2 Publications
Corresponds to variant rs374395444 [ dbSNP | Ensembl ].
VAR_028969

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC023490 Genomic DNA. No translation available.
AB051453 mRNA. Translation: BAB33336.1. Frameshift.
AL117509 mRNA. Translation: CAB55970.1.
AL133030 mRNA. Translation: CAB61362.2. Different initiation.
BC035246 mRNA. Translation: AAH35246.2. Different initiation.
CCDSiCCDS46665.1.
PIRiT17280.
T42704.
RefSeqiNP_056487.1. NM_015672.1.
UniGeneiHs.115429.

Genome annotation databases

EnsembliENST00000619918; ENSP00000483386; ENSG00000275793.
GeneIDi85376.
KEGGihsa:85376.
UCSCiuc002zsd.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC023490 Genomic DNA. No translation available.
AB051453 mRNA. Translation: BAB33336.1. Frameshift.
AL117509 mRNA. Translation: CAB55970.1.
AL133030 mRNA. Translation: CAB61362.2. Different initiation.
BC035246 mRNA. Translation: AAH35246.2. Different initiation.
CCDSiCCDS46665.1.
PIRiT17280.
T42704.
RefSeqiNP_056487.1. NM_015672.1.
UniGeneiHs.115429.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EGENMR-A1572-1639[»]
ProteinModelPortaliQ9UFD9.
SMRiQ9UFD9. Positions 833-900, 1572-1639.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124503. 18 interactions.
IntActiQ9UFD9. 15 interactions.
STRINGi9606.ENSP00000391564.

PTM databases

iPTMnetiQ9UFD9.
PhosphoSiteiQ9UFD9.

Polymorphism and mutation databases

BioMutaiRIMBP3.
DMDMi380865484.

Proteomic databases

EPDiQ9UFD9.
MaxQBiQ9UFD9.
PaxDbiQ9UFD9.
PRIDEiQ9UFD9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000619918; ENSP00000483386; ENSG00000275793.
GeneIDi85376.
KEGGihsa:85376.
UCSCiuc002zsd.5. human.

Organism-specific databases

CTDi85376.
GeneCardsiRIMBP3.
H-InvDBHIX0016277.
HIX0041402.
HIX0197170.
HGNCiHGNC:29344. RIMBP3.
HPAiHPA001183.
MIMi612699. gene.
neXtProtiNX_Q9UFD9.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3632. Eukaryota.
ENOG410XZ8W. LUCA.
GeneTreeiENSGT00390000017228.
HOGENOMiHOG000090231.
HOVERGENiHBG096074.
InParanoidiQ9UFD9.
OMAiWETMSST.
PhylomeDBiQ9UFD9.
TreeFamiTF316230.

Miscellaneous databases

EvolutionaryTraceiQ9UFD9.
GenomeRNAii85376.
PROiQ9UFD9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UFD9.
CleanExiHS_RIMBP3.
GenevisibleiQ9UFD9. HS.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF07653. SH3_2. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 3 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
SSF50044. SSF50044. 3 hits.
PROSITEiPS50853. FN3. 2 hits.
PS50002. SH3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Identification of novel transcribed sequences on human chromosome 22 by expressed sequence tag mapping."
    Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O.
    DNA Res. 8:1-9(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 50-1639, VARIANT CYS-1513.
    Tissue: Brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 473-1639.
    Tissue: Testis.
  4. "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] OF 753-1639, VARIANT CYS-1513.
    Tissue: Testis.
  5. "Solution structure of the third SH3 domain from human KIAA1666 protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (AUG-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1572-1639.

Entry informationi

Entry nameiRIM3A_HUMAN
AccessioniPrimary (citable) accession number: Q9UFD9
Secondary accession number(s): Q8IYP7, Q9BY94, Q9UFQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: March 21, 2012
Last modified: June 8, 2016
This is version 118 of the entry and version 4 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, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.