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Protein

Alpha-mannosidase 2

Gene

alpha-Man-II

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway (By similarity).By similarity

Catalytic activityi

Hydrolysis of the terminal (1->3)- and (1->6)-linked alpha-D-mannose residues in the mannosyl-oligosaccharide Man5(GlcNAc)3.1 Publication

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi153ZincBy similarity1
Metal bindingi155ZincBy similarity1
Active sitei267NucleophileBy similarity1
Metal bindingi267ZincBy similarity1
Metal bindingi534ZincBy similarity1

GO - Molecular functioni

GO - Biological processi

  • encapsulation of foreign target Source: FlyBase
  • mannose metabolic process Source: GO_Central
  • N-glycan processing Source: FlyBase
  • protein deglycosylation Source: FlyBase
  • rhodopsin biosynthetic process Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.2.1.114. 1994.
ReactomeiR-DME-975578. Reactions specific to the complex N-glycan synthesis pathway.
SABIO-RKQ24451.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGH38. Glycoside Hydrolase Family 38.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-mannosidase 2 (EC:3.2.1.114)
Alternative name(s):
Golgi alpha-mannosidase II
Short name:
AMan II
Short name:
Man II
Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase
Gene namesi
Name:alpha-Man-II
Synonyms:GmII
ORF Names:CG18802
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0011740. alpha-Man-II.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 9CytoplasmicSequence analysis9
Transmembranei10 – 30Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini31 – 1108LumenalSequence analysisAdd BLAST1078

GO - Cellular componenti

  • endoplasmic reticulum Source: FlyBase
  • Golgi membrane Source: GO_Central
  • Golgi stack Source: FlyBase
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002069061 – 1108Alpha-mannosidase 2Add BLAST1108

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ24451.
PRIDEiQ24451.

Expressioni

Inductioni

Inhibited by swainsonine and by copper sulfate.1 Publication

Gene expression databases

BgeeiFBgn0011740.
ExpressionAtlasiQ24451. baseline.
GenevisibleiQ24451. DM.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.By similarity

Protein-protein interaction databases

BioGridi66291. 2 interactors.
DIPiDIP-22953N.
IntActiQ24451. 5 interactors.
MINTiMINT-874970.
STRINGi7227.FBpp0081509.

Chemistry databases

BindingDBiQ24451.

Structurei

Secondary structure

11108
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi97 – 99Combined sources3
Beta strandi105 – 107Combined sources3
Helixi108 – 114Combined sources7
Beta strandi123 – 125Combined sources3
Helixi135 – 137Combined sources3
Beta strandi144 – 153Combined sources10
Beta strandi156 – 160Combined sources5
Helixi162 – 168Combined sources7
Helixi170 – 183Combined sources14
Beta strandi189 – 191Combined sources3
Helixi194 – 203Combined sources10
Helixi206 – 217Combined sources12
Beta strandi220 – 225Combined sources6
Beta strandi233 – 235Combined sources3
Helixi238 – 256Combined sources19
Beta strandi262 – 265Combined sources4
Beta strandi268 – 271Combined sources4
Helixi274 – 280Combined sources7
Turni281 – 283Combined sources3
Beta strandi286 – 289Combined sources4
Helixi294 – 302Combined sources9
Beta strandi306 – 310Combined sources5
Beta strandi322 – 326Combined sources5
Helixi334 – 336Combined sources3
Beta strandi338 – 340Combined sources3
Helixi342 – 345Combined sources4
Helixi346 – 348Combined sources3
Helixi350 – 352Combined sources3
Turni371 – 373Combined sources3
Helixi374 – 389Combined sources16
Beta strandi392 – 404Combined sources13
Helixi410 – 429Combined sources20
Helixi431 – 433Combined sources3
Beta strandi435 – 439Combined sources5
Helixi442 – 454Combined sources13
Beta strandi462 – 465Combined sources4
Beta strandi471 – 473Combined sources3
Helixi480 – 482Combined sources3
Helixi486 – 507Combined sources22
Helixi513 – 515Combined sources3
Helixi517 – 531Combined sources15
Turni534 – 538Combined sources5
Helixi543 – 571Combined sources29
Turni575 – 577Combined sources3
Beta strandi586 – 590Combined sources5
Beta strandi592 – 595Combined sources4
Turni597 – 599Combined sources3
Turni610 – 612Combined sources3
Beta strandi613 – 622Combined sources10
Beta strandi624 – 626Combined sources3
Beta strandi628 – 637Combined sources10
Beta strandi641 – 645Combined sources5
Beta strandi653 – 664Combined sources12
Turni665 – 668Combined sources4
Beta strandi669 – 687Combined sources19
Beta strandi691 – 699Combined sources9
Beta strandi707 – 709Combined sources3
Beta strandi711 – 715Combined sources5
Beta strandi732 – 734Combined sources3
Beta strandi739 – 742Combined sources4
Beta strandi748 – 751Combined sources4
Beta strandi757 – 761Combined sources5
Beta strandi763 – 766Combined sources4
Beta strandi769 – 778Combined sources10
Beta strandi782 – 784Combined sources3
Beta strandi794 – 797Combined sources4
Beta strandi808 – 812Combined sources5
Beta strandi817 – 823Combined sources7
Beta strandi826 – 836Combined sources11
Beta strandi838 – 843Combined sources6
Beta strandi851 – 859Combined sources9
Beta strandi866 – 871Combined sources6
Turni872 – 874Combined sources3
Beta strandi875 – 880Combined sources6
Helixi887 – 890Combined sources4
Beta strandi892 – 901Combined sources10
Beta strandi903 – 913Combined sources11
Beta strandi915 – 918Combined sources4
Beta strandi924 – 933Combined sources10
Beta strandi938 – 940Combined sources3
Beta strandi951 – 961Combined sources11
Beta strandi973 – 975Combined sources3
Helixi979 – 989Combined sources11
Beta strandi993 – 997Combined sources5
Beta strandi1007 – 1009Combined sources3
Beta strandi1020 – 1027Combined sources8
Beta strandi1034 – 1044Combined sources11
Helixi1062 – 1064Combined sources3
Beta strandi1065 – 1075Combined sources11
Beta strandi1081 – 1085Combined sources5
Helixi1087 – 1089Combined sources3
Beta strandi1099 – 1107Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HTYX-ray1.40A94-1108[»]
1HWWX-ray1.87A94-1108[»]
1HXKX-ray1.50A94-1108[»]
1PS3X-ray1.80A64-1108[»]
1QWNX-ray1.20A76-1108[»]
1QWUX-ray2.03A76-1108[»]
1QX1X-ray1.30A76-1108[»]
1R33X-ray1.80A76-1108[»]
1R34X-ray1.95A76-1108[»]
1TQSX-ray1.30A76-1108[»]
1TQTX-ray1.90A76-1108[»]
1TQUX-ray2.03A76-1108[»]
1TQVX-ray2.03A76-1108[»]
1TQWX-ray1.20A76-1108[»]
2ALWX-ray1.86A76-1108[»]
2F18X-ray1.30A76-1108[»]
2F1AX-ray1.45A76-1108[»]
2F1BX-ray1.45A76-1108[»]
2F7OX-ray1.43A76-1108[»]
2F7PX-ray1.28A76-1108[»]
2F7QX-ray1.85A76-1108[»]
2F7RX-ray1.35A76-1108[»]
2FYVX-ray1.90A76-1108[»]
2OW6X-ray1.19A76-1108[»]
2OW7X-ray1.77A76-1108[»]
3BLBX-ray1.30A76-1108[»]
3BUBX-ray1.38A76-1108[»]
3BUDX-ray1.85A76-1108[»]
3BUIX-ray1.25A76-1108[»]
3BUPX-ray2.03A76-1108[»]
3BUQX-ray2.01A76-1108[»]
3BVTX-ray1.30A76-1108[»]
3BVUX-ray1.12A76-1108[»]
3BVVX-ray1.30A76-1108[»]
3BVWX-ray1.20A76-1108[»]
3BVXX-ray1.10A76-1108[»]
3CV5X-ray1.60A76-1108[»]
3CZNX-ray1.40A76-1108[»]
3CZSX-ray1.30A76-1108[»]
3D4YX-ray1.52A76-1108[»]
3D4ZX-ray1.39A76-1108[»]
3D50X-ray1.79A76-1108[»]
3D51X-ray1.43A76-1108[»]
3D52X-ray1.60A76-1108[»]
3DDFX-ray1.20A76-1108[»]
3DDGX-ray1.74A76-1108[»]
3DX0X-ray1.70A76-1108[»]
3DX1X-ray1.21A76-1108[»]
3DX2X-ray1.40A76-1108[»]
3DX3X-ray1.42A76-1108[»]
3DX4X-ray1.38A76-1108[»]
3EJPX-ray1.32A76-1108[»]
3EJQX-ray1.45A76-1108[»]
3EJRX-ray1.27A76-1108[»]
3EJSX-ray1.35A76-1108[»]
3EJTX-ray1.35A76-1108[»]
3EJUX-ray1.32A76-1108[»]
ProteinModelPortaliQ24451.
SMRiQ24451.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ24451.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 38 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1959. Eukaryota.
ENOG410XQMZ. LUCA.
GeneTreeiENSGT00510000046304.
InParanoidiQ24451.
KOiK01231.
OrthoDBiEOG091G00YH.
PhylomeDBiQ24451.

Family and domain databases

Gene3Di1.20.1270.50. 1 hit.
2.60.40.1180. 1 hit.
3.20.110.10. 1 hit.
InterProiIPR011013. Gal_mutarotase_SF_dom.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR027291. Glyco_hydro_38/57_N.
IPR011682. Glyco_hydro_38_C.
IPR015341. Glyco_hydro_38_cen.
IPR000602. Glyco_hydro_38_N.
IPR028995. Glyco_hydro_57/38_cen.
IPR013780. Glyco_hydro_b.
[Graphical view]
PfamiPF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view]
SMARTiSM00872. Alpha-mann_mid. 1 hit.
[Graphical view]
SUPFAMiSSF74650. SSF74650. 1 hit.
SSF88688. SSF88688. 1 hit.
SSF88713. SSF88713. 1 hit.

Sequencei

Sequence statusi: Complete.

Q24451-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRIRRRFAL VICSGCLLVF LSLYIILNFA APAATQIKPN YENIENKLHE
60 70 80 90 100
LENGLQEHGE EMRNLRARLA ETSNRDDPIR PPLKVARSPR PGQCQDVVQD
110 120 130 140 150
VPNVDVQMLE LYDRMSFKDI DGGVWKQGWN IKYDPLKYNA HHKLKVFVVP
160 170 180 190 200
HSHNDPGWIQ TFEEYYQHDT KHILSNALRH LHDNPEMKFI WAEISYFARF
210 220 230 240 250
YHDLGENKKL QMKSIVKNGQ LEFVTGGWVM PDEANSHWRN VLLQLTEGQT
260 270 280 290 300
WLKQFMNVTP TASWAIDPFG HSPTMPYILQ KSGFKNMLIQ RTHYSVKKEL
310 320 330 340 350
AQQRQLEFLW RQIWDNKGDT ALFTHMMPFY SYDIPHTCGP DPKVCCQFDF
360 370 380 390 400
KRMGSFGLSC PWKVPPRTIS DQNVAARSDL LVDQWKKKAE LYRTNVLLIP
410 420 430 440 450
LGDDFRFKQN TEWDVQRVNY ERLFEHINSQ AHFNVQAQFG TLQEYFDAVH
460 470 480 490 500
QAERAGQAEF PTLSGDFFTY ADRSDNYWSG YYTSRPYHKR MDRVLMHYVR
510 520 530 540 550
AAEMLSAWHS WDGMARIEER LEQARRELSL FQHHDGITGT AKTHVVVDYE
560 570 580 590 600
QRMQEALKAC QMVMQQSVYR LLTKPSIYSP DFSFSYFTLD DSRWPGSGVE
610 620 630 640 650
DSRTTIILGE DILPSKHVVM HNTLPHWREQ LVDFYVSSPF VSVTDLANNP
660 670 680 690 700
VEAQVSPVWS WHHDTLTKTI HPQGSTTKYR IIFKARVPPM GLATYVLTIS
710 720 730 740 750
DSKPEHTSYA SNLLLRKNPT SLPLGQYPED VKFGDPREIS LRVGNGPTLA
760 770 780 790 800
FSEQGLLKSI QLTQDSPHVP VHFKFLKYGV RSHGDRSGAY LFLPNGPASP
810 820 830 840 850
VELGQPVVLV TKGKLESSVS VGLPSVVHQT IMRGGAPEIR NLVDIGSLDN
860 870 880 890 900
TEIVMRLETH IDSGDIFYTD LNGLQFIKRR RLDKLPLQAN YYPIPSGMFI
910 920 930 940 950
EDANTRLTLL TGQPLGGSSL ASGELEIMQD RRLASDDERG LGQGVLDNKP
960 970 980 990 1000
VLHIYRLVLE KVNNCVRPSE LHPAGYLTSA AHKASQSLLD PLDKFIFAEN
1010 1020 1030 1040 1050
EWIGAQGQFG GDHPSAREDL DVSVMRRLTK SSAKTQRVGY VLHRTNLMQC
1060 1070 1080 1090 1100
GTPEEHTQKL DVCHLLPNVA RCERTTLTFL QNLEHLDGMV APEVCPMETA

AYVSSHSS
Length:1,108
Mass (Da):126,721
Last modified:June 16, 2003 - v2
Checksum:i55E370EC8CAC6D4A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti71E → K in CAA54732 (PubMed:7890162).Curated1
Sequence conflicti305 – 306QL → HV in CAA10755 (PubMed:10504337).Curated2
Sequence conflicti397L → V in CAA10755 (PubMed:10504337).Curated1
Sequence conflicti970E → K in CAA54732 (PubMed:7890162).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77652 mRNA. Translation: CAA54732.1.
AJ132715 Genomic DNA. Translation: CAA10755.1.
AE014297 Genomic DNA. Translation: AAF54375.1.
AY119464 mRNA. Translation: AAM50118.1.
PIRiJC4037.
RefSeqiNP_524291.2. NM_079567.3.
UniGeneiDm.2459.

Genome annotation databases

EnsemblMetazoaiFBtr0082031; FBpp0081509; FBgn0011740.
GeneIDi41126.
KEGGidme:Dmel_CG18802.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77652 mRNA. Translation: CAA54732.1.
AJ132715 Genomic DNA. Translation: CAA10755.1.
AE014297 Genomic DNA. Translation: AAF54375.1.
AY119464 mRNA. Translation: AAM50118.1.
PIRiJC4037.
RefSeqiNP_524291.2. NM_079567.3.
UniGeneiDm.2459.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HTYX-ray1.40A94-1108[»]
1HWWX-ray1.87A94-1108[»]
1HXKX-ray1.50A94-1108[»]
1PS3X-ray1.80A64-1108[»]
1QWNX-ray1.20A76-1108[»]
1QWUX-ray2.03A76-1108[»]
1QX1X-ray1.30A76-1108[»]
1R33X-ray1.80A76-1108[»]
1R34X-ray1.95A76-1108[»]
1TQSX-ray1.30A76-1108[»]
1TQTX-ray1.90A76-1108[»]
1TQUX-ray2.03A76-1108[»]
1TQVX-ray2.03A76-1108[»]
1TQWX-ray1.20A76-1108[»]
2ALWX-ray1.86A76-1108[»]
2F18X-ray1.30A76-1108[»]
2F1AX-ray1.45A76-1108[»]
2F1BX-ray1.45A76-1108[»]
2F7OX-ray1.43A76-1108[»]
2F7PX-ray1.28A76-1108[»]
2F7QX-ray1.85A76-1108[»]
2F7RX-ray1.35A76-1108[»]
2FYVX-ray1.90A76-1108[»]
2OW6X-ray1.19A76-1108[»]
2OW7X-ray1.77A76-1108[»]
3BLBX-ray1.30A76-1108[»]
3BUBX-ray1.38A76-1108[»]
3BUDX-ray1.85A76-1108[»]
3BUIX-ray1.25A76-1108[»]
3BUPX-ray2.03A76-1108[»]
3BUQX-ray2.01A76-1108[»]
3BVTX-ray1.30A76-1108[»]
3BVUX-ray1.12A76-1108[»]
3BVVX-ray1.30A76-1108[»]
3BVWX-ray1.20A76-1108[»]
3BVXX-ray1.10A76-1108[»]
3CV5X-ray1.60A76-1108[»]
3CZNX-ray1.40A76-1108[»]
3CZSX-ray1.30A76-1108[»]
3D4YX-ray1.52A76-1108[»]
3D4ZX-ray1.39A76-1108[»]
3D50X-ray1.79A76-1108[»]
3D51X-ray1.43A76-1108[»]
3D52X-ray1.60A76-1108[»]
3DDFX-ray1.20A76-1108[»]
3DDGX-ray1.74A76-1108[»]
3DX0X-ray1.70A76-1108[»]
3DX1X-ray1.21A76-1108[»]
3DX2X-ray1.40A76-1108[»]
3DX3X-ray1.42A76-1108[»]
3DX4X-ray1.38A76-1108[»]
3EJPX-ray1.32A76-1108[»]
3EJQX-ray1.45A76-1108[»]
3EJRX-ray1.27A76-1108[»]
3EJSX-ray1.35A76-1108[»]
3EJTX-ray1.35A76-1108[»]
3EJUX-ray1.32A76-1108[»]
ProteinModelPortaliQ24451.
SMRiQ24451.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66291. 2 interactors.
DIPiDIP-22953N.
IntActiQ24451. 5 interactors.
MINTiMINT-874970.
STRINGi7227.FBpp0081509.

Chemistry databases

BindingDBiQ24451.

Protein family/group databases

CAZyiGH38. Glycoside Hydrolase Family 38.

Proteomic databases

PaxDbiQ24451.
PRIDEiQ24451.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0082031; FBpp0081509; FBgn0011740.
GeneIDi41126.
KEGGidme:Dmel_CG18802.

Organism-specific databases

CTDi41126.
FlyBaseiFBgn0011740. alpha-Man-II.

Phylogenomic databases

eggNOGiKOG1959. Eukaryota.
ENOG410XQMZ. LUCA.
GeneTreeiENSGT00510000046304.
InParanoidiQ24451.
KOiK01231.
OrthoDBiEOG091G00YH.
PhylomeDBiQ24451.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi3.2.1.114. 1994.
ReactomeiR-DME-975578. Reactions specific to the complex N-glycan synthesis pathway.
SABIO-RKQ24451.

Miscellaneous databases

ChiTaRSialpha-Man-II. fly.
EvolutionaryTraceiQ24451.
GenomeRNAii41126.
PROiQ24451.

Gene expression databases

BgeeiFBgn0011740.
ExpressionAtlasiQ24451. baseline.
GenevisibleiQ24451. DM.

Family and domain databases

Gene3Di1.20.1270.50. 1 hit.
2.60.40.1180. 1 hit.
3.20.110.10. 1 hit.
InterProiIPR011013. Gal_mutarotase_SF_dom.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR027291. Glyco_hydro_38/57_N.
IPR011682. Glyco_hydro_38_C.
IPR015341. Glyco_hydro_38_cen.
IPR000602. Glyco_hydro_38_N.
IPR028995. Glyco_hydro_57/38_cen.
IPR013780. Glyco_hydro_b.
[Graphical view]
PfamiPF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view]
SMARTiSM00872. Alpha-mann_mid. 1 hit.
[Graphical view]
SUPFAMiSSF74650. SSF74650. 1 hit.
SSF88688. SSF88688. 1 hit.
SSF88713. SSF88713. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMAN2_DROME
AccessioniPrimary (citable) accession number: Q24451
Secondary accession number(s): Q9TYG5, Q9VHD8, Q9VHD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 16, 2003
Last modified: November 30, 2016
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.