| Basic Information | |
|---|---|
| Species | Picea abies |
| Cazyme ID | MA_158841g0150 |
| Family | AA1 |
| Protein Properties | Length: 471 Molecular Weight: 52643 Isoelectric Point: 7.4853 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| AA1 | 50 | 287 | 0 |
| GPDTDVWSYGSNVPGPELRVRQGDRIQVQVENRLPEETTVHWHGLRVPNAMDGVAHITQKPIGPGETFTYEFDCLDAGTFWYHPHHHSSAQVARGLYGAL IVDERNPIAVDRDITWVLSDWRLQKDASIKNDFNNLHDVGHNGRIGNTVTVNGRIPGNFDVRAGERIRLRLINAANARIFGLEFEGHTAQVIAIDGHPVE PHAPANNRIVLGPAMRADILLDLRGQPGKRYRVVDAFY | |||
| Full Sequence |
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| Protein Sequence Length: 471 Download |
| MLDRREILLA GASLATTASV LRAAPAPESP IKQFKLIAAP SRQSIIGAHG PDTDVWSYGS 60 NVPGPELRVR QGDRIQVQVE NRLPEETTVH WHGLRVPNAM DGVAHITQKP IGPGETFTYE 120 FDCLDAGTFW YHPHHHSSAQ VARGLYGALI VDERNPIAVD RDITWVLSDW RLQKDASIKN 180 DFNNLHDVGH NGRIGNTVTV NGRIPGNFDV RAGERIRLRL INAANARIFG LEFEGHTAQV 240 IAIDGHPVEP HAPANNRIVL GPAMRADILL DLRGQPGKRY RVVDAFYRHR EYKLLDLAYS 300 DAAQLRDLAD AKPIRLPANP LSEPDLENAE RHDIMLGGGM MGGMISAIMD GQRTNMRTLM 360 HNGLLWSING VAAKGHILDP FLTLKRNQSC RLTLINDTAW HHPMHLHGHV FRVIARNGQP 420 TRRSEWQDTV MMDPRERVEI AFVADNPGDW MFHCHILEHQ SGGMFGLIRV I 480 |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR01480 | copper_res_A | 9.0e-15 | 366 | 470 | 107 | + copper-resistance protein, CopA family. This model represents the CopA copper resistance protein family. CopA is related to laccase (benzenediol:oxygen oxidoreductase) and L-ascorbate oxidase, both copper-containing enzymes. Most members have a typical TAT (twin-arginine translocation) signal sequence with an Arg-Arg pair. Twin-arginine translocation is observed for a large number of periplasmic proteins that cross the inner membrane with metal-containing cofactors already bound. The combination of copper-binding sites and TAT translocation motif suggests a mechansism of resistance by packaging and export [Cellular processes, Detoxification, Transport and binding proteins, Cations and iron carrying compounds]. | ||
| pfam07732 | Cu-oxidase_3 | 5.0e-38 | 53 | 156 | 108 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. | ||
| TIGR01480 | copper_res_A | 1.0e-41 | 33 | 275 | 288 | + copper-resistance protein, CopA family. This model represents the CopA copper resistance protein family. CopA is related to laccase (benzenediol:oxygen oxidoreductase) and L-ascorbate oxidase, both copper-containing enzymes. Most members have a typical TAT (twin-arginine translocation) signal sequence with an Arg-Arg pair. Twin-arginine translocation is observed for a large number of periplasmic proteins that cross the inner membrane with metal-containing cofactors already bound. The combination of copper-binding sites and TAT translocation motif suggests a mechansism of resistance by packaging and export [Cellular processes, Detoxification, Transport and binding proteins, Cations and iron carrying compounds]. | ||
| COG2132 | SufI | 2.0e-87 | 26 | 470 | 448 | + Putative multicopper oxidases [Secondary metabolites biosynthesis, transport, and catabolism] | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| RefSeq | YP_001978352.1 | 0 | 25 | 470 | 2 | 453 | probable multicopper oxidase protein [Rhizobium etli CIAT 652] |
| RefSeq | YP_002289160.1 | 0 | 4 | 471 | 10 | 477 | CumA [Oligotropha carboxidovorans OM5] |
| RefSeq | ZP_00964414.1 | 0 | 9 | 470 | 14 | 482 | multicopper oxidase domain protein [Sulfitobacter sp. NAS-14.1] |
| RefSeq | ZP_01036720.1 | 0 | 25 | 470 | 29 | 481 | multicopper oxidase domain protein [Roseovarius sp. 217] |
| RefSeq | ZP_02186341.1 | 0 | 5 | 470 | 11 | 474 | multicopper oxidase, type 3 [alpha proteobacterium BAL199] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 4f7k_B | 0 | 35 | 470 | 5 | 416 | A Chain A, Characterization And Engineering Of The Bifunctional N- And O-glucosyltransferase Involved In Xenobiotic Metabolism In Plants |
| PDB | 4f7k_A | 0 | 35 | 470 | 5 | 416 | A Chain A, Characterization And Engineering Of The Bifunctional N- And O-glucosyltransferase Involved In Xenobiotic Metabolism In Plants |
| PDB | 3zx1_A | 0 | 19 | 470 | 33 | 479 | A Chain A, Multicopper Oxidase From Campylobacter Jejuni: A Metallo-Oxid |
| PDB | 4ai7_A | 3e-39 | 31 | 470 | 16 | 438 | A Chain A, Multicopper Oxidase From Campylobacter Jejuni: A Metallo-Oxid |
| PDB | 2yar_A | 3e-39 | 31 | 470 | 16 | 438 | A Chain A, Multicopper Oxidase From Campylobacter Jejuni: A Metallo-Oxid |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
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| Hit | Length | Start | End | EValue |
| FG601344 | 133 | 25 | 155 | 8e-35 |
| CX943130 | 193 | 67 | 252 | 2e-26 |
| FL817447 | 237 | 63 | 280 | 9e-25 |
| BX839990 | 244 | 63 | 286 | 4e-24 |
| CX943130 | 89 | 378 | 464 | 0.27 |
| Orthologous Group | |||||
|---|---|---|---|---|---|
| Species | ID | ||||
| Physcomitrella patens | Pp1s9258_1V6.1 | ||||
| Picea abies | MA_159113g0110 | ||||
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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