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Protein

Guanylate kinase

Gene

GUK1

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

Functioni

Essential for recycling GMP and indirectly, cGMP.

Catalytic activityi

ATP + GMP = ADP + GDP.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei44 – 441By similarity
Active sitei137 – 1371By similarity
Active sitei148 – 1481By similarity
Binding sitei171 – 1711ATPBy similarity
Binding sitei172 – 1721ATP; via carbonyl oxygenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 188ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. guanylate kinase activity Source: UniProtKB

GO - Biological processi

  1. ATP metabolic process Source: Ensembl
  2. dATP metabolic process Source: Ensembl
  3. dGDP biosynthetic process Source: Ensembl
  4. dGMP metabolic process Source: Ensembl
  5. drug metabolic process Source: Reactome
  6. GDP biosynthetic process Source: Ensembl
  7. GDP-mannose metabolic process Source: Ensembl
  8. glycoprotein transport Source: Ensembl
  9. GMP metabolic process Source: Ensembl
  10. nucleobase-containing small molecule interconversion Source: Reactome
  11. nucleobase-containing small molecule metabolic process Source: Reactome
  12. purine nucleotide metabolic process Source: UniProtKB
  13. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS07104-MONOMER.
BRENDAi2.7.4.8. 2681.
ReactomeiREACT_121388. Abacavir metabolism.
REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
SABIO-RKQ16774.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanylate kinase (EC:2.7.4.8)
Alternative name(s):
GMP kinase
Gene namesi
Name:GUK1
Synonyms:GMK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:4693. GUK1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29072.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 197196Guanylate kinasePRO_0000170651Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ16774.
PaxDbiQ16774.
PRIDEiQ16774.

PTM databases

PhosphoSiteiQ16774.

Expressioni

Gene expression databases

BgeeiQ16774.
CleanExiHS_GUK1.
ExpressionAtlasiQ16774. baseline and differential.
GenevestigatoriQ16774.

Organism-specific databases

HPAiHPA048587.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi109242. 8 interactions.
IntActiQ16774. 2 interactions.
STRINGi9606.ENSP00000317659.

Structurei

3D structure databases

ProteinModelPortaliQ16774.
SMRiQ16774. Positions 5-193.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 186183Guanylate kinase-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the guanylate kinase family.Curated
Contains 1 guanylate kinase-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0194.
GeneTreeiENSGT00730000110700.
HOGENOMiHOG000037640.
HOVERGENiHBG003344.
InParanoidiQ16774.
KOiK00942.
OrthoDBiEOG7J1814.
PhylomeDBiQ16774.
TreeFamiTF314473.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR017665. Guanylate_kinase.
IPR020590. Guanylate_kinase_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00625. Guanylate_kin. 1 hit.
[Graphical view]
SMARTiSM00072. GuKc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR03263. guanyl_kin. 1 hit.
PROSITEiPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q16774-1) [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
MSGPRPVVLS GPSGAGKSTL LKRLLQEHSG IFGFSVSHTT RNPRPGEENG
60 70 80 90 100
KDYYFVTREV MQRDIAAGDF IEHAEFSGNL YGTSKVAVQA VQAMNRICVL
110 120 130 140 150
DVDLQGVRNI KATDLRPIYI SVQPPSLHVL EQRLRQRNTE TEESLVKRLA
160 170 180 190
AAQADMESSK EPGLFDVVII NDSLDQAYAE LKEALSEEIK KAQRTGA
Length:197
Mass (Da):21,726
Last modified:January 23, 2007 - v2
Checksum:iC49573212A0DA825
GO
Isoform 2 (identifier: Q16774-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLRRPLAGLAAAALGRAPPDGM

Show »
Length:218
Mass (Da):23,782
Checksum:i6972858284006BB2
GO
Isoform 3 (identifier: Q16774-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLRRPLAGLAAAALGRAPPDGM
     159-197: SKEPGLFDVV...EIKKAQRTGA → RNQESSKDRR...CCPCGWNILG

Note: Gene prediction based on EST data.

Show »
Length:241
Mass (Da):26,596
Checksum:i418604D9B391F864
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MLRRPLAGLAAAALGRAPPD GM in isoform 2 and isoform 3. 1 PublicationVSP_043778
Alternative sequencei159 – 19739SKEPG…QRTGA → RNQESSKDRRLRLAVCSRHP GPIQDQGSSIEPPPWQAIRQ LCALGQHVEWRRCCPCGWNI LG in isoform 3. CuratedVSP_047372Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L76200 mRNA. Translation: AAC37598.1.
U66895 mRNA. Translation: AAC50659.1.
AK303845 mRNA. Translation: BAG64788.1.
AL359510 Genomic DNA. No translation available.
CH471098 Genomic DNA. Translation: EAW69856.1.
BC006249 mRNA. Translation: AAH06249.1.
BC009914 mRNA. Translation: AAH09914.1.
CCDSiCCDS1568.1. [Q16774-1]
CCDS53481.1. [Q16774-2]
CCDS55689.1. [Q16774-3]
PIRiS68864.
RefSeqiNP_000849.1. NM_000858.5. [Q16774-1]
NP_001152862.1. NM_001159390.1. [Q16774-2]
NP_001152863.1. NM_001159391.1. [Q16774-1]
NP_001229768.1. NM_001242839.1. [Q16774-1]
NP_001229769.1. NM_001242840.1. [Q16774-3]
UniGeneiHs.376933.

Genome annotation databases

EnsembliENST00000312726; ENSP00000317659; ENSG00000143774. [Q16774-1]
ENST00000366716; ENSP00000355677; ENSG00000143774. [Q16774-1]
ENST00000366718; ENSP00000355679; ENSG00000143774. [Q16774-1]
ENST00000366726; ENSP00000355687; ENSG00000143774. [Q16774-1]
ENST00000366728; ENSP00000355689; ENSG00000143774. [Q16774-3]
ENST00000366730; ENSP00000355691; ENSG00000143774. [Q16774-1]
ENST00000391865; ENSP00000375738; ENSG00000143774. [Q16774-2]
GeneIDi2987.
KEGGihsa:2987.
UCSCiuc001hsh.3. human. [Q16774-1]
uc001hsi.3. human. [Q16774-2]

Polymorphism databases

DMDMi2497498.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L76200 mRNA. Translation: AAC37598.1.
U66895 mRNA. Translation: AAC50659.1.
AK303845 mRNA. Translation: BAG64788.1.
AL359510 Genomic DNA. No translation available.
CH471098 Genomic DNA. Translation: EAW69856.1.
BC006249 mRNA. Translation: AAH06249.1.
BC009914 mRNA. Translation: AAH09914.1.
CCDSiCCDS1568.1. [Q16774-1]
CCDS53481.1. [Q16774-2]
CCDS55689.1. [Q16774-3]
PIRiS68864.
RefSeqiNP_000849.1. NM_000858.5. [Q16774-1]
NP_001152862.1. NM_001159390.1. [Q16774-2]
NP_001152863.1. NM_001159391.1. [Q16774-1]
NP_001229768.1. NM_001242839.1. [Q16774-1]
NP_001229769.1. NM_001242840.1. [Q16774-3]
UniGeneiHs.376933.

3D structure databases

ProteinModelPortaliQ16774.
SMRiQ16774. Positions 5-193.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109242. 8 interactions.
IntActiQ16774. 2 interactions.
STRINGi9606.ENSP00000317659.

Chemistry

ChEMBLiCHEMBL4989.

PTM databases

PhosphoSiteiQ16774.

Polymorphism databases

DMDMi2497498.

Proteomic databases

MaxQBiQ16774.
PaxDbiQ16774.
PRIDEiQ16774.

Protocols and materials databases

DNASUi2987.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312726; ENSP00000317659; ENSG00000143774. [Q16774-1]
ENST00000366716; ENSP00000355677; ENSG00000143774. [Q16774-1]
ENST00000366718; ENSP00000355679; ENSG00000143774. [Q16774-1]
ENST00000366726; ENSP00000355687; ENSG00000143774. [Q16774-1]
ENST00000366728; ENSP00000355689; ENSG00000143774. [Q16774-3]
ENST00000366730; ENSP00000355691; ENSG00000143774. [Q16774-1]
ENST00000391865; ENSP00000375738; ENSG00000143774. [Q16774-2]
GeneIDi2987.
KEGGihsa:2987.
UCSCiuc001hsh.3. human. [Q16774-1]
uc001hsi.3. human. [Q16774-2]

Organism-specific databases

CTDi2987.
GeneCardsiGC01P228327.
HGNCiHGNC:4693. GUK1.
HPAiHPA048587.
MIMi139270. gene.
neXtProtiNX_Q16774.
PharmGKBiPA29072.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0194.
GeneTreeiENSGT00730000110700.
HOGENOMiHOG000037640.
HOVERGENiHBG003344.
InParanoidiQ16774.
KOiK00942.
OrthoDBiEOG7J1814.
PhylomeDBiQ16774.
TreeFamiTF314473.

Enzyme and pathway databases

BioCyciMetaCyc:HS07104-MONOMER.
BRENDAi2.7.4.8. 2681.
ReactomeiREACT_121388. Abacavir metabolism.
REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
SABIO-RKQ16774.

Miscellaneous databases

ChiTaRSiGUK1. human.
GeneWikiiGUK1.
GenomeRNAii2987.
NextBioi11844.
PROiQ16774.
SOURCEiSearch...

Gene expression databases

BgeeiQ16774.
CleanExiHS_GUK1.
ExpressionAtlasiQ16774. baseline and differential.
GenevestigatoriQ16774.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR017665. Guanylate_kinase.
IPR020590. Guanylate_kinase_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00625. Guanylate_kin. 1 hit.
[Graphical view]
SMARTiSM00072. GuKc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR03263. guanyl_kin. 1 hit.
PROSITEiPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human guanylate kinase (GUK1): cDNA sequence, expression and chromosomal localisation."
    Fitzgibbon J., Katsanis N., Wells D., Delhanty J., Vallins W., Hunt D.M.
    FEBS Lett. 385:185-188(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Retina.
  2. "Cloning, characterization, and modeling of mouse and human guanylate kinases."
    Brady W.A., Kokoris M.S., Fitzgibbon M., Black M.E.
    J. Biol. Chem. 271:16734-16740(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Ovary.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung.
  7. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiKGUA_HUMAN
AccessioniPrimary (citable) accession number: Q16774
Secondary accession number(s): B1ANH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 131 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

Miscellaneous

In addition to phosphorylating GMP, antiviral prodrugs such as acyclovir, ganciclovir, and carbovir and anticancer prodrugs such as the thiopurines are dependent on GMPK for their activation.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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.