Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_10430881g0010 |
Family | GH47 |
Protein Properties | Length: 284 Molecular Weight: 31147.1 Isoelectric Point: 4.6858 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH47 | 2 | 276 | 0 |
VQPQSRSGVNNFGGLGASIIDSLDTLYIMGLDEQFQKAKGWVTNSLDFNKDVVASVFETTIRVVGGLLSAYDLAGDSIFLERAKQIADRLLPAWNTPSGI PYNAINLAHGNAHNPGWTGGASILADSGTEQVEFIALSQRTGDPKYQEKVENVIKKLQETFPDDGLLPIYINPNSGQAETYSKITFGAMGDSFYEYLLKV WIQGNKTDGVKHYREMWERSMQGLMKLIRKSSPSSYTYITERSGSALIDKMDELACFAPGMLALGASTDDTDKAA |
Full Sequence |
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Protein Sequence Length: 284 Download |
MVQPQSRSGV NNFGGLGASI IDSLDTLYIM GLDEQFQKAK GWVTNSLDFN KDVVASVFET 60 TIRVVGGLLS AYDLAGDSIF LERAKQIADR LLPAWNTPSG IPYNAINLAH GNAHNPGWTG 120 GASILADSGT EQVEFIALSQ RTGDPKYQEK VENVIKKLQE TFPDDGLLPI YINPNSGQAE 180 TYSKITFGAM GDSFYEYLLK VWIQGNKTDG VKHYREMWER SMQGLMKLIR KSSPSSYTYI 240 TERSGSALID KMDELACFAP GMLALGASTD DTDKAAEYLS LAKE |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR03897 | lanti_2_LanM | 0.002 | 64 | 149 | 95 | + type 2 lantibiotic biosynthesis protein LanM. Members of this family are known generally as LanM, a multifunctional enzyme of lantibiotic biosynthesis. This catalysis by LanM distinguishes the type 2 lantibiotics, such as mersacidin, cinnamycin, and lichenicidin, from LanBC-produced type 1 lantibiotics such as nisin and subtilin. The N-terminal domain contains regions associated with Ser and Thr dehydration. The C-terminal region contains a pfam05147 domain, which catalyzes the formation of the lanthionine bridge [Cellular processes, Toxin production and resistance]. | ||
PTZ00470 | PTZ00470 | 2.0e-111 | 2 | 284 | 289 | + glycoside hydrolase family 47 protein; Provisional | ||
pfam01532 | Glyco_hydro_47 | 2.0e-120 | 2 | 284 | 291 | + 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). |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI18472.1 | 0 | 2 | 284 | 128 | 409 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002310939.1 | 0 | 2 | 284 | 124 | 405 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002325257.1 | 0 | 2 | 284 | 125 | 406 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002519409.1 | 0 | 2 | 284 | 115 | 396 | mannosyl-oligosaccharide alpha-1,2-mannosidase, putative [Ricinus communis] |
RefSeq | XP_002528166.1 | 0 | 2 | 284 | 80 | 362 | mannosyl-oligosaccharide alpha-1,2-mannosidase, putative [Ricinus communis] |
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 | 2 | 284 | 45 | 328 | 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 | 2 | 284 | 35 | 312 | A Chain A, Crystal Structure Of Human Class I Alpha1,2-Mannosidase |
PDB | 1fo3_A | 0 | 2 | 284 | 35 | 312 | A Chain A, Crystal Structure Of Human Class I Alpha1,2-Mannosidase |
PDB | 1fo2_A | 0 | 2 | 284 | 35 | 312 | A Chain A, Crystal Structure Of Human Class I Alpha1,2-Mannosidase In Complex With 1-Deoxymannojirimycin |
PDB | 1x9d_A | 0 | 2 | 284 | 113 | 390 | 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 |
EX435397 | 213 | 72 | 284 | 0 |
EH732594 | 256 | 13 | 268 | 0 |
EX117709 | 284 | 2 | 284 | 0 |
EE645339 | 245 | 12 | 256 | 0 |
ES798011 | 253 | 2 | 254 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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