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Protein

DNA-directed RNA polymerase I subunit RPA190

Gene

RPA190

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA precursors. Besides, RNA polymerase I has intrinsic RNA cleavage activity. RPA190 and RPA135 both contribute to the polymerase catalytic activity and together form the Pol I active center. In addition, subunit RPA12 contributes a catalytic zinc ribbon that is required for RNA cleavage by Pol I. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA190 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol I by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition.3 Publications

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi62Zinc 1Combined sources1 Publication1
Metal bindingi65Zinc 1Combined sources1 Publication1
Metal bindingi72Zinc 1Combined sources1 Publication1
Metal bindingi75Zinc 1; via tele nitrogenCombined sources1 Publication1
Metal bindingi102Zinc 2Combined sources1 Publication1
Metal bindingi105Zinc 2Combined sources1 Publication1
Metal bindingi233Zinc 2Combined sources1 Publication1
Metal bindingi236Zinc 2Combined sources1 Publication1
Metal bindingi627Magnesium; catalyticBy similarity1
Metal bindingi629Magnesium; catalyticBy similarity1
Metal bindingi631Magnesium; catalyticBy similarity1

GO - Molecular functioni

  • DNA binding Source: InterPro
  • promoter-specific chromatin binding Source: SGD
  • RNA polymerase I activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • ribosome biogenesis Source: UniProtKB-KW
  • transcription from RNA polymerase I promoter Source: UniProtKB
  • transcription of nuclear large rRNA transcript from RNA polymerase I promoter Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Ribosome biogenesis, Transcription

Keywords - Ligandi

Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-33816-MONOMER.
ReactomeiR-SCE-73762. RNA Polymerase I Transcription Initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerase I subunit RPA190 (EC:2.7.7.6)
Alternative name(s):
DNA-directed RNA polymerase I 190 kDa polypeptide
Short name:
A190
DNA-directed RNA polymerase I largest subunit
Gene namesi
Name:RPA190
Synonyms:RPA1, RRN1
Ordered Locus Names:YOR341W
ORF Names:O6276
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR341W.
SGDiS000005868. RPA190.

Subcellular locationi

GO - Cellular componenti

  • DNA-directed RNA polymerase I complex Source: UniProtKB
  • nucleolus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000739301 – 1664DNA-directed RNA polymerase I subunit RPA190Add BLAST1664

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei889PhosphoserineCombined sources1
Modified residuei1636PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP10964.
PRIDEiP10964.
TopDownProteomicsiP10964.

PTM databases

iPTMnetiP10964.

Interactioni

Subunit structurei

Component of the RNA polymerase I (Pol I) complex consisting of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8, RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5, RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43 form the stalk that mediates interactions with transcription initiation factors and newly synthesized RNA.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PRP43P531312EBI-15730,EBI-505
RPA135P221384EBI-15730,EBI-15736
RPC40P077035EBI-15730,EBI-15831
RPO26P204353EBI-15730,EBI-15786

Protein-protein interaction databases

BioGridi34724. 115 interactors.
DIPiDIP-999N.
IntActiP10964. 37 interactors.
MINTiMINT-613626.

Structurei

Secondary structure

11664
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 18Combined sources9
Helixi21 – 27Combined sources7
Helixi52 – 54Combined sources3
Turni63 – 65Combined sources3
Turni69 – 71Combined sources3
Beta strandi77 – 86Combined sources10
Helixi88 – 90Combined sources3
Helixi91 – 100Combined sources10
Turni103 – 105Combined sources3
Beta strandi107 – 110Combined sources4
Helixi112 – 126Combined sources15
Helixi130 – 135Combined sources6
Helixi136 – 138Combined sources3
Helixi175 – 198Combined sources24
Turni199 – 201Combined sources3
Helixi210 – 228Combined sources19
Turni234 – 236Combined sources3
Beta strandi242 – 245Combined sources4
Beta strandi247 – 249Combined sources3
Beta strandi251 – 254Combined sources4
Helixi258 – 266Combined sources9
Turni267 – 270Combined sources4
Helixi317 – 330Combined sources14
Helixi332 – 338Combined sources7
Helixi352 – 355Combined sources4
Beta strandi356 – 362Combined sources7
Helixi365 – 367Combined sources3
Beta strandi371 – 373Combined sources3
Beta strandi376 – 378Combined sources3
Helixi381 – 404Combined sources24
Turni408 – 410Combined sources3
Helixi415 – 438Combined sources24
Helixi440 – 442Combined sources3
Helixi456 – 461Combined sources6
Beta strandi462 – 464Combined sources3
Helixi466 – 470Combined sources5
Beta strandi472 – 486Combined sources15
Beta strandi488 – 490Combined sources3
Beta strandi494 – 497Combined sources4
Helixi499 – 502Combined sources4
Beta strandi506 – 510Combined sources5
Turni513 – 515Combined sources3
Helixi516 – 525Combined sources10
Turni526 – 528Combined sources3
Beta strandi529 – 531Combined sources3
Beta strandi533 – 537Combined sources5
Beta strandi543 – 545Combined sources3
Helixi551 – 558Combined sources8
Turni559 – 562Combined sources4
Helixi568 – 570Combined sources3
Beta strandi576 – 580Combined sources5
Beta strandi586 – 590Combined sources5
Helixi597 – 599Combined sources3
Beta strandi600 – 607Combined sources8
Beta strandi613 – 616Combined sources4
Helixi618 – 620Combined sources3
Helixi621 – 624Combined sources4
Beta strandi628 – 630Combined sources3
Beta strandi632 – 636Combined sources5
Helixi641 – 649Combined sources9
Helixi653 – 656Combined sources4
Turni660 – 662Combined sources3
Helixi672 – 680Combined sources9
Beta strandi686 – 688Combined sources3
Helixi689 – 700Combined sources12
Beta strandi703 – 705Combined sources3
Beta strandi708 – 711Combined sources4
Beta strandi718 – 723Combined sources6
Beta strandi725 – 727Combined sources3
Helixi728 – 739Combined sources12
Beta strandi742 – 744Combined sources3
Beta strandi749 – 752Combined sources4
Helixi757 – 759Combined sources3
Beta strandi768 – 772Combined sources5
Beta strandi775 – 778Combined sources4
Helixi783 – 786Combined sources4
Helixi793 – 824Combined sources32
Helixi830 – 833Combined sources4
Helixi837 – 847Combined sources11
Helixi848 – 850Combined sources3
Helixi853 – 861Combined sources9
Helixi873 – 884Combined sources12
Helixi886 – 911Combined sources26
Turni912 – 915Combined sources4
Beta strandi916 – 918Combined sources3
Turni920 – 922Combined sources3
Helixi924 – 930Combined sources7
Helixi937 – 944Combined sources8
Helixi976 – 979Combined sources4
Turni986 – 988Combined sources3
Helixi992 – 1011Combined sources20
Helixi1017 – 1027Combined sources11
Beta strandi1036 – 1039Combined sources4
Beta strandi1045 – 1049Combined sources5
Helixi1050 – 1052Combined sources3
Helixi1057 – 1059Combined sources3
Helixi1066 – 1070Combined sources5
Helixi1073 – 1080Combined sources8
Helixi1082 – 1088Combined sources7
Beta strandi1089 – 1092Combined sources4
Helixi1093 – 1107Combined sources15
Beta strandi1109 – 1111Combined sources3
Helixi1113 – 1115Combined sources3
Helixi1123 – 1126Combined sources4
Turni1129 – 1131Combined sources3
Helixi1138 – 1150Combined sources13
Helixi1152 – 1155Combined sources4
Beta strandi1157 – 1160Combined sources4
Helixi1163 – 1175Combined sources13
Helixi1185 – 1194Combined sources10
Helixi1196 – 1200Combined sources5
Helixi1218 – 1226Combined sources9
Beta strandi1237 – 1242Combined sources6
Beta strandi1244 – 1246Combined sources3
Helixi1248 – 1258Combined sources11
Helixi1263 – 1266Combined sources4
Beta strandi1267 – 1275Combined sources9
Beta strandi1288 – 1296Combined sources9
Helixi1299 – 1306Combined sources8
Helixi1310 – 1318Combined sources9
Helixi1320 – 1335Combined sources16
Beta strandi1344 – 1346Combined sources3
Helixi1364 – 1366Combined sources3
Helixi1369 – 1378Combined sources10
Beta strandi1382 – 1384Combined sources3
Helixi1389 – 1394Combined sources6
Helixi1442 – 1452Combined sources11
Beta strandi1454 – 1462Combined sources9
Turni1464 – 1466Combined sources3
Beta strandi1469 – 1476Combined sources8
Helixi1485 – 1493Combined sources9
Beta strandi1497 – 1499Combined sources3
Beta strandi1504 – 1508Combined sources5
Beta strandi1518 – 1523Combined sources6
Helixi1526 – 1529Combined sources4
Helixi1530 – 1532Combined sources3
Turni1533 – 1535Combined sources3
Helixi1538 – 1540Combined sources3
Beta strandi1542 – 1544Combined sources3
Helixi1546 – 1553Combined sources8
Helixi1555 – 1572Combined sources18
Helixi1579 – 1589Combined sources11
Turni1590 – 1592Combined sources3
Helixi1600 – 1603Combined sources4
Helixi1609 – 1613Combined sources5
Helixi1618 – 1627Combined sources10
Helixi1637 – 1643Combined sources7
Helixi1650 – 1652Combined sources3
Beta strandi1653 – 1661Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4C2MX-ray2.80A/P1-1664[»]
4C3HX-ray3.27A1-1664[»]
4C3IX-ray3.0A1-1664[»]
4C3JX-ray3.35A1-1664[»]
4YM7X-ray5.50AA/BA/CA/DA/EA/FA1-1664[»]
5G5Lelectron microscopy4.80A1-1664[»]
ProteinModelPortaliP10964.
SMRiP10964.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni992 – 1004Bridging helixBy similarityAdd BLAST13

Sequence similaritiesi

Belongs to the RNA polymerase beta' chain family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000074861.
HOGENOMiHOG000205401.
InParanoidiP10964.
KOiK02999.
OMAiIREINHV.
OrthoDBiEOG092C19ZG.

Family and domain databases

InterProiIPR015699. DNA-dir_RNA_pol1_lsu.
IPR000722. RNA_pol_asu.
IPR006592. RNA_pol_N.
IPR007080. RNA_pol_Rpb1_1.
IPR007066. RNA_pol_Rpb1_3.
IPR007083. RNA_pol_Rpb1_4.
IPR007081. RNA_pol_Rpb1_5.
[Graphical view]
PANTHERiPTHR19376:SF11. PTHR19376:SF11. 3 hits.
PfamiPF04997. RNA_pol_Rpb1_1. 1 hit.
PF00623. RNA_pol_Rpb1_2. 1 hit.
PF04983. RNA_pol_Rpb1_3. 1 hit.
PF05000. RNA_pol_Rpb1_4. 1 hit.
PF04998. RNA_pol_Rpb1_5. 1 hit.
[Graphical view]
SMARTiSM00663. RPOLA_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10964-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDISKPVGSE ITSVDFGILT AKEIRNLSAK QITNPTVLDN LGHPVSGGLY
60 70 80 90 100
DLALGAFLRN LCSTCGLDEK FCPGHQGHIE LPVPCYNPLF FNQLYIYLRA
110 120 130 140 150
SCLFCHHFRL KSVEVHRYAC KLRLLQYGLI DESYKLDEIT LGSLNSSMYT
160 170 180 190 200
DDEAIEDNED EMDGEGSKQS KDISSTLLNE LKSKRSEYVD MAIAKALSDG
210 220 230 240 250
RTTERGSFTA TVNDERKKLV HEFHKKLLSR GKCDNCGMFS PKFRKDGFTK
260 270 280 290 300
IFETALNEKQ ITNNRVKGFI RQDMIKKQKQ AKKLDGSNEA SANDEESFDV
310 320 330 340 350
GRNPTTRPKT GSTYILSTEV KNILDTVFRK EQCVLQYVFH SRPNLSRKLV
360 370 380 390 400
KADSFFMDVL VVPPTRFRLP SKLGEEVHEN SQNQLLSKVL TTSLLIRDLN
410 420 430 440 450
DDLSKLQKDK VSLEDRRVIF SRLMNAFVTI QNDVNAFIDS TKAQGRTSGK
460 470 480 490 500
VPIPGVKQAL EKKEGLFRKH MMGKRVNYAA RSVISPDPNI ETNEIGVPPV
510 520 530 540 550
FAVKLTYPEP VTAYNIAELR QAVINGPDKW PGATQIQNED GSLVSLIGMS
560 570 580 590 600
VEQRKALANQ LLTPSSNVST HTLNKKVYRH IKNRDVVLMN RQPTLHKASM
610 620 630 640 650
MGHKVRVLPN EKTLRLHYAN TGAYNADFDG DEMNMHFPQN ENARAEALNL
660 670 680 690 700
ANTDSQYLTP TSGSPVRGLI QDHISAGVWL TSKDSFFTRE QYQQYIYGCI
710 720 730 740 750
RPEDGHTTRS KIVTLPPTIF KPYPLWTGKQ IITTVLLNVT PPDMPGINLI
760 770 780 790 800
SKNKIKNEYW GKGSLENEVL FKDGALLCGI LDKSQYGASK YGIVHSLHEV
810 820 830 840 850
YGPEVAAKVL SVLGRLFTNY ITATAFTCGM DDLRLTAEGN KWRTDILKTS
860 870 880 890 900
VDTGREAAAE VTNLDKDTPA DDPELLKRLQ EILRDNNKSG ILDAVTSSKV
910 920 930 940 950
NAITSQVVSK CVPDGTMKKF PCNSMQAMAL SGAKGSNVNV SQIMCLLGQQ
960 970 980 990 1000
ALEGRRVPVM VSGKTLPSFK PYETDAMAGG YVKGRFYSGI KPQEYYFHCM
1010 1020 1030 1040 1050
AGREGLIDTA VKTSRSGYLQ RCLTKQLEGV HVSYDNSIRD ADGTLVQFMY
1060 1070 1080 1090 1100
GGDAIDITKE SHMTQFEFCL DNYYALLKKY NPSALIEHLD VESALKYSKK
1110 1120 1130 1140 1150
TLKYRKKHSK EPHYKQSVKY DPVLAKYNPA KYLGSVSENF QDKLESFLDK
1160 1170 1180 1190 1200
NSKLFKSSDG VNEKKFRALM QLKYMRSLIN PGEAVGIIAS QSVGEPSTQM
1210 1220 1230 1240 1250
TLNTFHFAGH GAANVTLGIP RLREIVMTAS AAIKTPQMTL PIWNDVSDEQ
1260 1270 1280 1290 1300
ADTFCKSISK VLLSEVIDKV IVTETTGTSN TAGGNAARSY VIHMRFFDNN
1310 1320 1330 1340 1350
EYSEEYDVSK EELQNVISNQ FIHLLEAAIV KEIKKQKRTT GPDIGVAVPR
1360 1370 1380 1390 1400
LQTDVANSSS NSKRLEEDND EEQSHKKTKQ AVSYDEPDED EIETMREAEK
1410 1420 1430 1440 1450
SSDEEGIDSD KESDSDSEDE DVDMNEQINK SIVEANNNMN KVQRDRQSAI
1460 1470 1480 1490 1500
ISHHRFITKY NFDDESGKWC EFKLELAADT EKLLMVNIVE EICRKSIIRQ
1510 1520 1530 1540 1550
IPHIDRCVHP EPENGKRVLV TEGVNFQAMW DQEAFIDVDG ITSNDVAAVL
1560 1570 1580 1590 1600
KTYGVEAARN TIVNEINNVF SRYAISVSFR HLDLIADMMT RQGTYLAFNR
1610 1620 1630 1640 1650
QGMETSTSSF MKMSYETTCQ FLTKAVLDNE REQLDSPSAR IVVGKLNNVG
1660
TGSFDVLAKV PNAA
Length:1,664
Mass (Da):186,432
Last modified:November 1, 1997 - v2
Checksum:iDF65A7AA459D5E6D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti158N → T in AAA34890 (PubMed:2830265).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03530 Genomic DNA. Translation: AAA34890.1.
X95720 Genomic DNA. Translation: CAA65029.1.
Z75249 Genomic DNA. Translation: CAA99665.1.
BK006948 Genomic DNA. Translation: DAA11102.1.
PIRiS67250.
RefSeqiNP_014986.3. NM_001183761.3.

Genome annotation databases

EnsemblFungiiYOR341W; YOR341W; YOR341W.
GeneIDi854519.
KEGGisce:YOR341W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03530 Genomic DNA. Translation: AAA34890.1.
X95720 Genomic DNA. Translation: CAA65029.1.
Z75249 Genomic DNA. Translation: CAA99665.1.
BK006948 Genomic DNA. Translation: DAA11102.1.
PIRiS67250.
RefSeqiNP_014986.3. NM_001183761.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4C2MX-ray2.80A/P1-1664[»]
4C3HX-ray3.27A1-1664[»]
4C3IX-ray3.0A1-1664[»]
4C3JX-ray3.35A1-1664[»]
4YM7X-ray5.50AA/BA/CA/DA/EA/FA1-1664[»]
5G5Lelectron microscopy4.80A1-1664[»]
ProteinModelPortaliP10964.
SMRiP10964.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34724. 115 interactors.
DIPiDIP-999N.
IntActiP10964. 37 interactors.
MINTiMINT-613626.

PTM databases

iPTMnetiP10964.

Proteomic databases

MaxQBiP10964.
PRIDEiP10964.
TopDownProteomicsiP10964.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR341W; YOR341W; YOR341W.
GeneIDi854519.
KEGGisce:YOR341W.

Organism-specific databases

EuPathDBiFungiDB:YOR341W.
SGDiS000005868. RPA190.

Phylogenomic databases

GeneTreeiENSGT00550000074861.
HOGENOMiHOG000205401.
InParanoidiP10964.
KOiK02999.
OMAiIREINHV.
OrthoDBiEOG092C19ZG.

Enzyme and pathway databases

BioCyciYEAST:G3O-33816-MONOMER.
ReactomeiR-SCE-73762. RNA Polymerase I Transcription Initiation.

Miscellaneous databases

PROiP10964.

Family and domain databases

InterProiIPR015699. DNA-dir_RNA_pol1_lsu.
IPR000722. RNA_pol_asu.
IPR006592. RNA_pol_N.
IPR007080. RNA_pol_Rpb1_1.
IPR007066. RNA_pol_Rpb1_3.
IPR007083. RNA_pol_Rpb1_4.
IPR007081. RNA_pol_Rpb1_5.
[Graphical view]
PANTHERiPTHR19376:SF11. PTHR19376:SF11. 3 hits.
PfamiPF04997. RNA_pol_Rpb1_1. 1 hit.
PF00623. RNA_pol_Rpb1_2. 1 hit.
PF04983. RNA_pol_Rpb1_3. 1 hit.
PF05000. RNA_pol_Rpb1_4. 1 hit.
PF04998. RNA_pol_Rpb1_5. 1 hit.
[Graphical view]
SMARTiSM00663. RPOLA_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRPA1_YEAST
AccessioniPrimary (citable) accession number: P10964
Secondary accession number(s): D6W336, Q99330
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 168 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2840 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

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.