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Protein

1-phosphatidylinositol-3-phosphate 5-kinase FAB1A

Gene

FAB1A

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 3,5-bisphosphate (By similarity). Plays an important role in maintenance of endomembrane homeostasis including endocytosis, vacuole formation, and vacuolar acidification processes. Required for development of viable pollen. Might mediate recycling of auxin transporters.By similarity3 Publications

Catalytic activityi

ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate.

Cofactori

Mg2+By similarity, Mn2+By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri36 – 10267FYVE-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • 1-phosphatidylinositol-3-phosphate 5-kinase activity Source: TAIR
  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • endomembrane system organization Source: TAIR
  • phosphatidylinositol phosphorylation Source: GOC
  • vacuole organization Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciARA:AT4G33240-MONOMER.
ARA:GQT-2800-MONOMER.
ARA:GQT-2801-MONOMER.
ReactomeiR-ATH-1660514. Synthesis of PIPs at the Golgi membrane.
R-ATH-1660516. Synthesis of PIPs at the early endosome membrane.
R-ATH-1660517. Synthesis of PIPs at the late endosome membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
1-phosphatidylinositol-3-phosphate 5-kinase FAB1A (EC:2.7.1.150)
Short name:
Phosphatidylinositol 3-phosphate 5-kinase
Alternative name(s):
FYVE finger-containing phosphoinositide kinase
PIKfyve
Phosphatidylinositol 3-phosphate 5-kinase type III
Short name:
PIPkin-III
Short name:
Type III PIP kinase
Protein FORMS APLOID AND BINUCLEATE CELLS 1A
Gene namesi
Name:FAB1A
Ordered Locus Names:At4g33240
ORF Names:F4I10.170
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G33240.

Subcellular locationi

GO - Cellular componenti

  • endosome Source: TAIR
  • endosome membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane

Pathology & Biotechi

Disruption phenotypei

Leaf-curling phenotype. Root growth inhibition, root gravitropic response, and hyposensitivity to exogenous auxin. Fab1a and fab1b double mutant displays an abnormal vacuolar phenotype late in pollen development leading to inviable pollen (PubMed:19846542).3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 175717571-phosphatidylinositol-3-phosphate 5-kinase FAB1APRO_0000421870Add
BLAST

Proteomic databases

PaxDbiQ0WUR5.
PRIDEiQ0WUR5.

PTM databases

iPTMnetiQ0WUR5.

Expressioni

Tissue specificityi

Ubiquitous with highest expression levels in pollen, seed, and senescent leaves.1 Publication

Gene expression databases

ExpressionAtlasiQ0WUR5. baseline and differential.
GenevisibleiQ0WUR5. AT.

Interactioni

Subunit structurei

Component of the PI(3,5)P2 regulatory complex at least composed of ATG18, SAC/FIG4, FAB1 and VAC14.By similarity

Protein-protein interaction databases

STRINGi3702.AT4G33240.1.

Structurei

3D structure databases

ProteinModelPortaliQ0WUR5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1395 – 1719325PIPKPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1014 – 108774Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi209 – 2135Poly-Asp

Sequence similaritiesi

Contains 1 FYVE-type zinc finger.PROSITE-ProRule annotation
Contains 1 PIPK domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri36 – 10267FYVE-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG0230. Eukaryota.
COG0459. LUCA.
COG5253. LUCA.
HOGENOMiHOG000241144.
InParanoidiQ0WUR5.
KOiK00921.
OMAiYQVSSKH.
PhylomeDBiQ0WUR5.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.30.800.10. 1 hit.
3.30.810.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027483. PInositol-4-P-5-kinase_C.
IPR002498. PInositol-4-P-5-kinase_core.
IPR027484. PInositol-4-P-5-kinase_N.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
PF01363. FYVE. 1 hit.
PF01504. PIP5K. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 1 hit.
SM00330. PIPKc. 1 hit.
[Graphical view]
SUPFAMiSSF52029. SSF52029. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS51455. PIPK. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q0WUR5-1) [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
MDSQDHKAPG FVDIVKSWIP RKSESSNMSR DFWMPDQSCP VCYECDAQFT
60 70 80 90 100
VFNRRHHCRL CGRVFCAKCA ANSIPSPSDE TKDSHEEPER IRVCNYCYKQ
110 120 130 140 150
WEQGIVPPDN GASIISLHFS SSPSARSVAS TTSNSSNCTI DSTAGPSPRP
160 170 180 190 200
KMNPRASRRV SSNMDSEKSE QQNAKSRRSS DHYGHVLDSS DNQVEFFVNS
210 220 230 240 250
SGRSDGEADD DDDYQSDFAQ SYAQGNDYYG AINLDEVDHI YGSHEAHDVG
260 270 280 290 300
VKIEPNISGF PPDQDLDSLN TETIDKTRQQ ENGWNDVKEG SPPCEESFEP
310 320 330 340 350
EVVDFESDGL LWLPPEPENE EDEREAVLSD DDGDEGDRGD WGYLRPSNSF
360 370 380 390 400
NEKDFHSKDK SSGAMKNVVE GHFRALVAQL LEVDNLPMVN EGDEEGWLDI
410 420 430 440 450
ITSLSWEAAT LLKPDTSKSG GMDPGGYVKV KCIPCGRRSE SMVVKGVVCK
460 470 480 490 500
KNVAHRRMTS KIEKPRLLIL GGALEYQRIS NQLSSFDTLL QQEMDHLKMA
510 520 530 540 550
VAKIDSHNPD ILLVEKSVSR FAQEYLLAKD ISLVLNIKRS LLERISRCTG
560 570 580 590 600
AQIVPSIDQL TSPKLGYCDL FHVEKFVETH VSPCQVAKKM AKTLMFFDGC
610 620 630 640 650
PKPLGCTILL KGAHEDELKK VKHVIQYGVF AAYHLALETS FLADEGASIH
660 670 680 690 700
ELPLQTPITV ALPDKPSMVN RSISTIPGFT VSSAEKSPTT ELRGEPHKAN
710 720 730 740 750
GDLTGNFTSS KTHFQGKLDG NDRIDPSERL LHNLDTVYCK PPETITSKDD
760 770 780 790 800
GLVPTLESRQ LSFHVEEPSV QKDQWSVLSG ATEQVTDGGY TNDSAVIGNQ
810 820 830 840 850
NFNRQEQMES SKGDFHPSAS DHQSILVSLS TRCVWKGSVC ERAHLLRIKY
860 870 880 890 900
YGSFDKPLGR FLRDNLFDQD QCCPSCTMPA EAHIHCYTHR QGSLTISVKK
910 920 930 940 950
LPELLPGQRE GKIWMWHRCL KCPRINGFPP ATRRIVMSDA AWGLSFGKFL
960 970 980 990 1000
ELSFSNHAAA SRVANCGHSL HRDCLRFYGF GRMVACFRYA SINIYAVTLP
1010 1020 1030 1040 1050
PAKLYFNYEN QEWLQKESKE VIKKAEVLFN EVQEALSQIS AKTMGAGSKG
1060 1070 1080 1090 1100
STPNKIKLSL EELAGLLEQR KKEYKDSLQQ MLNVVKDGQP TIDILLINKL
1110 1120 1130 1140 1150
RRLIIFDSYA WDECLAGAAN MVRNNYLEAP KNSAPKVMGR NVSLEKLSDE
1160 1170 1180 1190 1200
KVKSIPTHVA ICNDSLLQDA DYETCLNQGK SFADTSGKFA IPEDVGSDRP
1210 1220 1230 1240 1250
PDCRMEFDPS EGGKDNFVES SQVVKPAHTE SQFQATDLSD TLDAAWIGEQ
1260 1270 1280 1290 1300
TTSENGIFRP PSRAASTNGT QIPDLRLLGS ESELNFKGGP TNDEHTTQVQ
1310 1320 1330 1340 1350
LPSPSFYYSL NKNYSLNSRK HIMAEDRPVY VSSYRELEWR SGARLLLPLG
1360 1370 1380 1390 1400
CNDLVLPVYD DEPTSIIAYA LTSSEYKAQM SGSDKSRDRL DSGGSFSLFD
1410 1420 1430 1440 1450
SVNLLSLNSL SDLSVDMSRS LSSADEQVSQ LLHSSLYLKD LHARISFTDE
1460 1470 1480 1490 1500
GPPGKVKYSV TCYYAKEFEA LRMICCPSET DFIRSLGRCR KWGAQGGKSN
1510 1520 1530 1540 1550
VFFAKSLDDR FIIKQVTKTE LESFIKFGPA YFKYLTESIS TKSPTSLAKI
1560 1570 1580 1590 1600
LGIYQVSSKH LKGGKEFKMD VLVMENLLFK RNFTRLYDLK GSTRARYNPD
1610 1620 1630 1640 1650
TSGSNTVLLD QNLVEAMPTS PIFVGSKAKR LLERAVWNDT SFLASIHVMD
1660 1670 1680 1690 1700
YSLLVGVDEE RNELVLGIID FMRQYTWDKH LETWVKTSGL LGGPKNSTPT
1710 1720 1730 1740 1750
VISPQQYKKR FRKAMTAYFL MVPDQWSPAA VVPSNSSSAE VKEEEEKDNP

QAVGNKS
Note: A number of isoforms are produced. According to EST sequences.
Length:1,757
Mass (Da):196,193
Last modified:September 5, 2006 - v1
Checksum:i0F7AF38EE610CD5A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti279 – 2791Q → H in CAB36798 (PubMed:10617198).Curated
Sequence conflicti279 – 2791Q → H in CAB80041 (PubMed:10617198).Curated
Sequence conflicti285 – 2851N → T in CAB36798 (PubMed:10617198).Curated
Sequence conflicti285 – 2851N → T in CAB80041 (PubMed:10617198).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL035525 Genomic DNA. Translation: CAB36798.1.
AL161583 Genomic DNA. Translation: CAB80041.1.
CP002687 Genomic DNA. Translation: AEE86194.1.
AK227081 mRNA. Translation: BAE99133.1.
PIRiT05204.
RefSeqiNP_195050.6. NM_119478.6. [Q0WUR5-1]
UniGeneiAt.28052.

Genome annotation databases

EnsemblPlantsiAT4G33240.1; AT4G33240.1; AT4G33240. [Q0WUR5-1]
GeneIDi829460.
KEGGiath:AT4G33240.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL035525 Genomic DNA. Translation: CAB36798.1.
AL161583 Genomic DNA. Translation: CAB80041.1.
CP002687 Genomic DNA. Translation: AEE86194.1.
AK227081 mRNA. Translation: BAE99133.1.
PIRiT05204.
RefSeqiNP_195050.6. NM_119478.6. [Q0WUR5-1]
UniGeneiAt.28052.

3D structure databases

ProteinModelPortaliQ0WUR5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G33240.1.

PTM databases

iPTMnetiQ0WUR5.

Proteomic databases

PaxDbiQ0WUR5.
PRIDEiQ0WUR5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G33240.1; AT4G33240.1; AT4G33240. [Q0WUR5-1]
GeneIDi829460.
KEGGiath:AT4G33240.

Organism-specific databases

TAIRiAT4G33240.

Phylogenomic databases

eggNOGiKOG0230. Eukaryota.
COG0459. LUCA.
COG5253. LUCA.
HOGENOMiHOG000241144.
InParanoidiQ0WUR5.
KOiK00921.
OMAiYQVSSKH.
PhylomeDBiQ0WUR5.

Enzyme and pathway databases

BioCyciARA:AT4G33240-MONOMER.
ARA:GQT-2800-MONOMER.
ARA:GQT-2801-MONOMER.
ReactomeiR-ATH-1660514. Synthesis of PIPs at the Golgi membrane.
R-ATH-1660516. Synthesis of PIPs at the early endosome membrane.
R-ATH-1660517. Synthesis of PIPs at the late endosome membrane.

Miscellaneous databases

PROiQ0WUR5.

Gene expression databases

ExpressionAtlasiQ0WUR5. baseline and differential.
GenevisibleiQ0WUR5. AT.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.30.800.10. 1 hit.
3.30.810.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027483. PInositol-4-P-5-kinase_C.
IPR002498. PInositol-4-P-5-kinase_core.
IPR027484. PInositol-4-P-5-kinase_N.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
PF01363. FYVE. 1 hit.
PF01504. PIP5K. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 1 hit.
SM00330. PIPKc. 1 hit.
[Graphical view]
SUPFAMiSSF52029. SSF52029. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS51455. PIPK. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Inositol phospholipid metabolism in Arabidopsis. Characterized and putative isoforms of inositol phospholipid kinase and phosphoinositide-specific phospholipase C."
    Mueller-Roeber B., Pical C.
    Plant Physiol. 130:22-46(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, REVIEW.
  5. "Arabidopsis FAB1/PIKfyve proteins are essential for development of viable pollen."
    Whitley P., Hinz S., Doughty J.
    Plant Physiol. 151:1812-1822(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  6. "Loss-of-function and gain-of-function mutations in FAB1A/B impair endomembrane homeostasis, conferring pleiotropic developmental abnormalities in Arabidopsis."
    Hirano T., Matsuzawa T., Takegawa K., Sato M.H.
    Plant Physiol. 155:797-807(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
  7. "Arabidopsis FAB1A/B is possibly involved in the recycling of auxin transporters."
    Hirano T., Sato M.H.
    Plant Signal. Behav. 6:583-585(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiFAB1A_ARATH
AccessioniPrimary (citable) accession number: Q0WUR5
Secondary accession number(s): Q9SMY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2013
Last sequence update: September 5, 2006
Last modified: June 8, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. 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.