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Basic Information | |
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Species | Brassica rapa |
Cazyme ID | Bra014291 |
Family | GH47 |
Protein Properties | Length: 659 Molecular Weight: 75089 Isoelectric Point: 6.3221 |
Chromosome | Chromosome/Scaffold: 08 Start: 1881537 End: 1885510 |
Description | alpha-mannosidase 1 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH47 | 202 | 634 | 0 |
AMLHAWSSYEKYAWGKDELQPRTKDGTDSFGGLGATMIDSLDTLYIMGLHEQFQKAREWVATSLDFDKDYDASMFETTIRVVGGLLSTYDLSGDKLFLDK AKDIADRLLPAWNTPTGIPYNIINLRSGSAHNPSWAAGGASILADSGTEQLEFIALSQRTGDPKYQQKVEKVITELNKNFPADGLLPIYINPDNGNPSYS TTTFGAMGDSFYEYLLKVWVQGNKTSEVKLYREMWEKSMKGLLSLINKSTPSSFTYIREKNGNNFIDKMDELACFAPGMLALGASGYGPDDEKKFLTLAE ELAWTCYNFYQSTPTKLAGENYFFNAGQDMSVGTSWNILRPETVESLFYLWRLTGNKTYQEWGWNIFQAFEKNSRIESGYVGLKDVNTGAKDNKMQSFFL AETLKYLYLLFSPPSVISLDEWVFNTEAHPLKI |
Full Sequence |
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Protein Sequence Length: 659 Download |
MRYLFVGATP RQNRRLNMSE DPTSATSNGE RWQLGEVGSD EQRLRKENRD EEPEHRRLEK 60 ERADSKVDTF TLSSSSVSWN LIPQFVSVSS AECVCVREMA RGRSITSSGI WRYLNPAYYL 120 RRPKRLALLF FVFVSVSMVV WDRMNLAREH EVEVYKLNEE VSRLEQMLEE LKGVGNGKTL 180 MIQKDVPQNP VDMERRQKVK EAMLHAWSSY EKYAWGKDEL QPRTKDGTDS FGGLGATMID 240 SLDTLYIMGL HEQFQKAREW VATSLDFDKD YDASMFETTI RVVGGLLSTY DLSGDKLFLD 300 KAKDIADRLL PAWNTPTGIP YNIINLRSGS AHNPSWAAGG ASILADSGTE QLEFIALSQR 360 TGDPKYQQKV EKVITELNKN FPADGLLPIY INPDNGNPSY STTTFGAMGD SFYEYLLKVW 420 VQGNKTSEVK LYREMWEKSM KGLLSLINKS TPSSFTYIRE KNGNNFIDKM DELACFAPGM 480 LALGASGYGP DDEKKFLTLA EELAWTCYNF YQSTPTKLAG ENYFFNAGQD MSVGTSWNIL 540 RPETVESLFY LWRLTGNKTY QEWGWNIFQA FEKNSRIESG YVGLKDVNTG AKDNKMQSFF 600 LAETLKYLYL LFSPPSVISL DEWVFNTEAH PLKIVARNEQ RKPTITLRQR RFGGIIKG* 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd04434 | LanC_like | 0.003 | 285 | 399 | 123 | + LanC-like proteins. LanC is the cyclase enzyme of the lanthionine synthetase. Lanthionine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as a precursor peptide and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans), in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. A related domain is also present in LanM and other pro- and eukaryotic proteins of unknown function. | ||
pfam01532 | Glyco_hydro_47 | 0 | 202 | 634 | 452 | + Glycosyl hydrolase family 47. Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2). | ||
PTZ00470 | PTZ00470 | 0 | 192 | 634 | 454 | + glycoside hydrolase family 47 protein; Provisional |
Gene Ontology | |
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GO Term | Description |
GO:0004571 | mannosyl-oligosaccharide 1,2-alpha-mannosidase activity |
GO:0005509 | calcium ion binding |
GO:0016020 | membrane |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAK92711.1 | 0 | 99 | 657 | 1 | 571 | putative mannosidase [Arabidopsis thaliana] |
DDBJ | BAB01459.1 | 0 | 99 | 657 | 1 | 580 | alpha 1,2-mannosidase-like protein [Arabidopsis thaliana] |
RefSeq | NP_001031171.1 | 0 | 203 | 656 | 1 | 454 | mannosyl-oligosaccharide 1,2-alpha-mannosidase, putative [Arabidopsis thaliana] |
RefSeq | NP_175570.1 | 0 | 99 | 656 | 1 | 558 | mannosyl-oligosaccharide 1,2-alpha-mannosidase, putative [Arabidopsis thaliana] |
RefSeq | NP_566675.1 | 0 | 99 | 657 | 1 | 571 | mannosyl-oligosaccharide 1,2-alpha-mannosidase, putative [Arabidopsis thaliana] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1nxc_A | 0 | 182 | 642 | 7 | 471 | A Chain A, Structure Of Mouse Golgi Alpha-1,2-Mannosidase Ia Reveals The Molecular Basis For Substrate Specificity Among Class I Enzymes (Family 47 Glycosidases) |
PDB | 1fmi_A | 0 | 188 | 634 | 2 | 456 | A Chain A, Crystal Structure Of Human Class I Alpha1,2-Mannosidase |
PDB | 1fo3_A | 0 | 188 | 634 | 2 | 456 | A Chain A, Crystal Structure Of Human Class I Alpha1,2-Mannosidase |
PDB | 1fo2_A | 0 | 188 | 634 | 2 | 456 | A Chain A, Crystal Structure Of Human Class I Alpha1,2-Mannosidase In Complex With 1-Deoxymannojirimycin |
PDB | 1x9d_A | 0 | 189 | 634 | 81 | 534 | A Chain A, Crystal Structure Of Human Class I Alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO780776 | 264 | 339 | 601 | 0 |
HO780776 | 175 | 118 | 283 | 0 |
HO780776 | 60 | 280 | 339 | 0 |
EX117709 | 296 | 220 | 515 | 0 |
HO780776 | 49 | 591 | 639 | 0.000000000000003 |
Sequence Alignments (This image is cropped. Click for full image.) |
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