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Protein

Protein farnesyltransferase subunit beta

Gene

Fntb

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential subunit of the farnesyltransferase complex. Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X.4 Publications

Catalytic activityi

Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate.5 Publications

Cofactori

Zn2+12 PublicationsNote: Binds 1 zinc ion per subunit.12 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei102 – 1021Important for selectivity against geranylgeranyl diphosphateBy similarity
Metal bindingi297 – 2971Zinc; catalytic3 Publications
Metal bindingi299 – 2991Zinc; catalytic3 Publications
Metal bindingi362 – 3621Zinc; via tele nitrogen; catalytic3 Publications

GO - Molecular functioni

  1. farnesyltranstransferase activity Source: Ensembl
  2. protein farnesyltransferase activity Source: RGD
  3. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. negative regulation of cell proliferation Source: Ensembl
  2. positive regulation of cell cycle Source: RGD
  3. positive regulation of cell proliferation Source: RGD
  4. positive regulation of fibroblast proliferation Source: Ensembl
  5. positive regulation of nitric-oxide synthase biosynthetic process Source: RGD
  6. protein farnesylation Source: UniProtKB
  7. response to cytokine Source: RGD
  8. response to inorganic substance Source: RGD
  9. response to organic cyclic compound Source: RGD
  10. wound healing Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Prenyltransferase, Transferase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_227662. Inactivation, recovery and regulation of the phototransduction cascade.
SABIO-RKQ02293.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein farnesyltransferase subunit beta (EC:2.5.1.58)
Short name:
FTase-beta
Alternative name(s):
CAAX farnesyltransferase subunit beta
Ras proteins prenyltransferase subunit beta
Gene namesi
Name:Fntb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 6

Organism-specific databases

RGDi620119. Fntb.

Subcellular locationi

GO - Cellular componenti

  1. microtubule associated complex Source: Ensembl
  2. protein complex Source: RGD
  3. protein farnesyltransferase complex Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 437437Protein farnesyltransferase subunit betaPRO_0000119763Add
BLAST

Proteomic databases

PaxDbiQ02293.
PRIDEiQ02293.

PTM databases

PhosphoSiteiQ02293.

Expressioni

Gene expression databases

GenevestigatoriQ02293.

Interactioni

Subunit structurei

Heterodimer of FNTA and FNTB.14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FntaQ0463114EBI-602454,EBI-602447

Protein-protein interaction databases

DIPiDIP-6132N.
IntActiQ02293. 1 interaction.
MINTiMINT-121917.
STRINGi10116.ENSRNOP00000010588.

Structurei

Secondary structure

1
437
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 263Combined sources
Helixi28 – 336Combined sources
Helixi43 – 6523Combined sources
Helixi75 – 8511Combined sources
Helixi91 – 966Combined sources
Helixi100 – 11314Combined sources
Helixi120 – 13314Combined sources
Beta strandi138 – 1436Combined sources
Helixi150 – 16314Combined sources
Helixi166 – 1716Combined sources
Helixi174 – 18411Combined sources
Beta strandi191 – 1944Combined sources
Helixi201 – 21313Combined sources
Turni219 – 2246Combined sources
Helixi225 – 2328Combined sources
Beta strandi237 – 2393Combined sources
Helixi249 – 26113Combined sources
Helixi265 – 2673Combined sources
Helixi270 – 2789Combined sources
Turni283 – 2853Combined sources
Beta strandi287 – 2915Combined sources
Helixi300 – 3034Combined sources
Turni304 – 3063Combined sources
Helixi307 – 31711Combined sources
Beta strandi321 – 3233Combined sources
Beta strandi325 – 3273Combined sources
Helixi332 – 34211Combined sources
Beta strandi348 – 3503Combined sources
Beta strandi352 – 3554Combined sources
Helixi360 – 37415Combined sources
Beta strandi375 – 3784Combined sources
Beta strandi381 – 3844Combined sources
Helixi390 – 3923Combined sources
Turni399 – 4013Combined sources
Helixi405 – 41511Combined sources
Helixi424 – 4263Combined sources
Helixi434 – 4363Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D8DX-ray2.00B1-437[»]
1D8EX-ray3.00B1-437[»]
1FPPX-ray2.75B1-437[»]
1FT1X-ray2.25B1-437[»]
1FT2X-ray3.40B22-422[»]
1FTImodel-B22-422[»]
1HZ7model-B41-406[»]
1JCRX-ray2.00B1-437[»]
1JCSX-ray2.20B1-437[»]
1KZOX-ray2.20B1-437[»]
1KZPX-ray2.10B1-437[»]
1KZRmodel-B17-423[»]
1N94X-ray3.50B22-418[»]
1N95X-ray2.30B22-423[»]
1N9AX-ray3.20B22-423[»]
1NI1X-ray2.30B22-423[»]
1NL4X-ray2.70B23-423[»]
1O1RX-ray2.30B1-427[»]
1O1SX-ray2.30B1-427[»]
1O1TX-ray2.10B1-427[»]
1O5MX-ray2.30B1-437[»]
1QBQX-ray2.40B1-437[»]
1QE2model-B41-406[»]
1SA5X-ray2.60B1-437[»]
1TN7X-ray2.30B1-437[»]
1TN8X-ray2.25B1-437[»]
1X81X-ray3.50B22-418[»]
2BEDX-ray2.70B23-423[»]
2FTImodel-B22-422[»]
2R2LX-ray2.23B23-423[»]
2ZIRX-ray2.40B1-437[»]
2ZISX-ray2.60B1-437[»]
3DPYX-ray2.70B1-437[»]
3E30X-ray2.45B1-437[»]
3E32X-ray2.45B1-437[»]
3E33X-ray1.90B1-437[»]
3E34X-ray2.05B1-437[»]
3EU5X-ray2.80B1-427[»]
3EUVX-ray2.75B1-427[»]
3FTImodel-B22-422[»]
3KSLX-ray2.05B1-437[»]
3KSQX-ray2.10B1-437[»]
4GTMX-ray2.20B1-427[»]
4GTOX-ray2.15B1-427[»]
4GTPX-ray2.75B1-427[»]
4GTQX-ray2.60B1-427[»]
4GTRX-ray2.20B1-427[»]
ProteinModelPortaliQ02293.
SMRiQ02293. Positions 22-437.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02293.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati123 – 16442PFTB 1Add
BLAST
Repeati174 – 21542PFTB 2Add
BLAST
Repeati222 – 26342PFTB 3Add
BLAST
Repeati270 – 31243PFTB 4Add
BLAST
Repeati332 – 37443PFTB 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni248 – 2514Farnesyl diphosphate binding
Regioni291 – 2944Farnesyl diphosphate binding
Regioni300 – 3034Farnesyl diphosphate binding

Sequence similaritiesi

Contains 5 PFTB repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5029.
GeneTreeiENSGT00550000075042.
HOGENOMiHOG000190594.
HOVERGENiHBG008173.
InParanoidiQ02293.
KOiK05954.
OMAiPIHPLYN.
OrthoDBiEOG7P02HV.
PhylomeDBiQ02293.
TreeFamiTF353162.

Family and domain databases

Gene3Di1.50.10.20. 1 hit.
InterProiIPR026872. FTB.
IPR001330. Prenyltrans.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PANTHERiPTHR11774:SF6. PTHR11774:SF6. 1 hit.
PfamiPF00432. Prenyltrans. 2 hits.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 1 hit.

Sequencei

Sequence statusi: Complete.

Q02293-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSSSFTYY CPPSSSPVWS EPLYSLRPEH ARERLQDDSV ETVTSIEQAK
60 70 80 90 100
VEEKIQEVFS SYKFNHLVPR LVLQREKHFH YLKRGLRQLT DAYECLDASR
110 120 130 140 150
PWLCYWILHS LELLDEPIPQ IVATDVCQFL ELCQSPDGGF GGGPGQYPHL
160 170 180 190 200
APTYAAVNAL CIIGTEEAYN VINREKLLQY LYSLKQPDGS FLMHVGGEVD
210 220 230 240 250
VRSAYCAASV ASLTNIITPD LFEGTAEWIA RCQNWEGGIG GVPGMEAHGG
260 270 280 290 300
YTFCGLAALV ILKKERSLNL KSLLQWVTSR QMRFEGGFQG RCNKLVDGCY
310 320 330 340 350
SFWQAGLLPL LHRALHAQGD PALSMSHWMF HQQALQEYIL MCCQCPAGGL
360 370 380 390 400
LDKPGKSRDF YHTCYCLSGL SIAQHFGSGA MLHDVVMGVP ENVLQPTHPV
410 420 430
YNIGPDKVIQ ATTHFLQKPV PGFEECEDAV TSDPATD
Length:437
Mass (Da):48,673
Last modified:April 1, 1993 - v1
Checksum:i41A9D6D79CD319A8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M69056 mRNA. Translation: AAA41176.1.
BC087675 mRNA. Translation: AAH87675.1.
PIRiA40037.
RefSeqiNP_742031.1. NM_172034.2.
UniGeneiRn.8873.

Genome annotation databases

EnsembliENSRNOT00000010588; ENSRNOP00000010588; ENSRNOG00000007660.
GeneIDi64511.
KEGGirno:64511.
UCSCiRGD:620119. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M69056 mRNA. Translation: AAA41176.1.
BC087675 mRNA. Translation: AAH87675.1.
PIRiA40037.
RefSeqiNP_742031.1. NM_172034.2.
UniGeneiRn.8873.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D8DX-ray2.00B1-437[»]
1D8EX-ray3.00B1-437[»]
1FPPX-ray2.75B1-437[»]
1FT1X-ray2.25B1-437[»]
1FT2X-ray3.40B22-422[»]
1FTImodel-B22-422[»]
1HZ7model-B41-406[»]
1JCRX-ray2.00B1-437[»]
1JCSX-ray2.20B1-437[»]
1KZOX-ray2.20B1-437[»]
1KZPX-ray2.10B1-437[»]
1KZRmodel-B17-423[»]
1N94X-ray3.50B22-418[»]
1N95X-ray2.30B22-423[»]
1N9AX-ray3.20B22-423[»]
1NI1X-ray2.30B22-423[»]
1NL4X-ray2.70B23-423[»]
1O1RX-ray2.30B1-427[»]
1O1SX-ray2.30B1-427[»]
1O1TX-ray2.10B1-427[»]
1O5MX-ray2.30B1-437[»]
1QBQX-ray2.40B1-437[»]
1QE2model-B41-406[»]
1SA5X-ray2.60B1-437[»]
1TN7X-ray2.30B1-437[»]
1TN8X-ray2.25B1-437[»]
1X81X-ray3.50B22-418[»]
2BEDX-ray2.70B23-423[»]
2FTImodel-B22-422[»]
2R2LX-ray2.23B23-423[»]
2ZIRX-ray2.40B1-437[»]
2ZISX-ray2.60B1-437[»]
3DPYX-ray2.70B1-437[»]
3E30X-ray2.45B1-437[»]
3E32X-ray2.45B1-437[»]
3E33X-ray1.90B1-437[»]
3E34X-ray2.05B1-437[»]
3EU5X-ray2.80B1-427[»]
3EUVX-ray2.75B1-427[»]
3FTImodel-B22-422[»]
3KSLX-ray2.05B1-437[»]
3KSQX-ray2.10B1-437[»]
4GTMX-ray2.20B1-427[»]
4GTOX-ray2.15B1-427[»]
4GTPX-ray2.75B1-427[»]
4GTQX-ray2.60B1-427[»]
4GTRX-ray2.20B1-427[»]
ProteinModelPortaliQ02293.
SMRiQ02293. Positions 22-437.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6132N.
IntActiQ02293. 1 interaction.
MINTiMINT-121917.
STRINGi10116.ENSRNOP00000010588.

Chemistry

BindingDBiQ02293.
ChEMBLiCHEMBL2095197.

PTM databases

PhosphoSiteiQ02293.

Proteomic databases

PaxDbiQ02293.
PRIDEiQ02293.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000010588; ENSRNOP00000010588; ENSRNOG00000007660.
GeneIDi64511.
KEGGirno:64511.
UCSCiRGD:620119. rat.

Organism-specific databases

CTDi2342.
RGDi620119. Fntb.

Phylogenomic databases

eggNOGiCOG5029.
GeneTreeiENSGT00550000075042.
HOGENOMiHOG000190594.
HOVERGENiHBG008173.
InParanoidiQ02293.
KOiK05954.
OMAiPIHPLYN.
OrthoDBiEOG7P02HV.
PhylomeDBiQ02293.
TreeFamiTF353162.

Enzyme and pathway databases

ReactomeiREACT_227662. Inactivation, recovery and regulation of the phototransduction cascade.
SABIO-RKQ02293.

Miscellaneous databases

EvolutionaryTraceiQ02293.
NextBioi613294.
PROiQ02293.

Gene expression databases

GenevestigatoriQ02293.

Family and domain databases

Gene3Di1.50.10.20. 1 hit.
InterProiIPR026872. FTB.
IPR001330. Prenyltrans.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PANTHERiPTHR11774:SF6. PTHR11774:SF6. 1 hit.
PfamiPF00432. Prenyltrans. 2 hits.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and expression of the peptide-binding beta subunit of rat p21ras farnesyltransferase, the counterpart of yeast DPR1/RAM1."
    Chen W.-J., Andres D.A., Goldstein J.L., Russell D.W., Brown M.S.
    Cell 66:327-334(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Brain.
  2. "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].
    Tissue: Brain.
  3. "Crystal structure of protein farnesyltransferase at 2.25-A resolution."
    Park H.-W., Boduluri S.R., Mooomaw J.F., Casey P.J., Beese L.S.
    Science 275:1800-1804(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH ZINC.
  4. Erratum
    Park H.-W., Boduluri S.R., Mooomaw J.F., Casey P.J., Beese L.S.
    Science 276:21-21(1997)
  5. "Protein farnesyltransferase: structure and implications for substrate binding."
    Dunten P., Kammlott U., Crowther R., Weber D., Palermo R., Birktoft J.
    Biochemistry 37:7907-7912(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC IONS, SUBUNIT, COFACTOR.
  6. "Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate."
    Long S.B., Casey P.J., Beese L.S.
    Biochemistry 37:9612-9618(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC IONS, COFACTOR, SUBUNIT.
  7. "Crystal structure of farnesyl protein transferase complexed with a CaaX peptide and farnesyl diphosphate analogue."
    Strickland C.L., Windsor W.T., Syto R., Wang L., Bond R., Wu Z., Schwartz J., Le H.V., Beese L.S., Weber P.C.
    Biochemistry 37:16601-16611(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH FNTA; ZINC IONS AND FARNESYL DIPHOSPHATE ANALOG, COFACTOR, SUBUNIT.
  8. "The basis for K-Ras4B binding specificity to protein farnesyltransferase revealed by 2 A resolution ternary complex structures."
    Long S.B., Casey P.J., Beese L.S.
    Structure 8:209-222(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FNTA AND KRAS, INTERACTION WITH KRAS, CATALYTIC ACTIVITY, COFACTOR, FUNCTION, SUBUNIT.
  9. "The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics."
    Long S.B., Hancock P.J., Kral A.M., Hellinga H.W., Beese L.S.
    Proc. Natl. Acad. Sci. U.S.A. 98:12948-12953(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH FNTA AND GERANYLGERANYL DIPHOSPHATE, SUBUNIT.
  10. "Reaction path of protein farnesyltransferase at atomic resolution."
    Long S.B., Casey P.J., Beese L.S.
    Nature 419:645-650(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC IONS, SUBUNIT, COFACTOR.
  11. "Biochemical and structural studies with prenyl diphosphate analogues provide insights into isoprenoid recognition by protein farnesyl transferase."
    Turek-Etienne T.C., Strickland C.L., Distefano M.D.
    Biochemistry 42:3716-3724(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-427 IN COMPLEX WITH FNTA; GERANYLGERANYL DIPHOSPHATE AND ZINC IONS, COFACTOR, SUBUNIT.
  12. "Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity."
    Reid T.S., Terry K.L., Casey P.J., Beese L.S.
    J. Mol. Biol. 343:417-433(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH FNTA AND ZINC IONS, COFACTOR, SUBUNIT.
  13. "Caged protein prenyltransferase substrates: tools for understanding protein prenylation."
    DeGraw A.J., Hast M.A., Xu J., Mullen D., Beese L.S., Barany G., Distefano M.D.
    Chem. Biol. Drug Des. 72:171-181(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC, COFACTOR, CATALYTIC ACTIVITY, SUBUNIT.
  14. "Structural basis for binding and selectivity of antimalarial and anticancer ethylenediamine inhibitors to protein farnesyltransferase."
    Hast M.A., Fletcher S., Cummings C.G., Pusateri E.E., Blaskovich M.A., Rivas K., Gelb M.H., Van Voorhis W.C., Sebti S.M., Hamilton A.D., Beese L.S.
    Chem. Biol. 16:181-192(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC IONS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, SUBUNIT.
  15. Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1-427 IN COMPLEX WITH FNTA AND ZINC IONS, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, FUNCTION.
  16. Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC, SUBUNIT, COFACTOR.
  17. Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-427 IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC IONS, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, FUNCTION.

Entry informationi

Entry nameiFNTB_RAT
AccessioniPrimary (citable) accession number: Q02293
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: January 7, 2015
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.