| Basic Information | |
|---|---|
| Species | Setaria italica |
| Cazyme ID | Si004323m |
| Family | AA1 |
| Protein Properties | Length: 587 Molecular Weight: 64698.9 Isoelectric Point: 6.4412 |
| Chromosome | Chromosome/Scaffold: 5 Start: 7252282 End: 7254265 |
| Description | Cupredoxin superfamily protein |
| View CDS | |
| External Links |
|---|
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| AA1 | 103 | 368 | 5.9e-25 |
| TFPGPTIEALQGVPLWVTWENHLPDRHILPWDPTVPVAIPRAGGVPTVVHLHGGVHPPQSDGHANAWFTAGFRERGPTWTTPTYAYPNAQSPGGVLWYHD HALGLTRANLLAGLLGAYVIRNPAAEAPLGLPCGDALDRVLVLADRSFYADGSLYMNCTGDNPGVHPQWQPEYFGDAVTVNGKAWPFLPVARRRYRFRII NASNARFFNLSLSNGLPFHVIGSDASYLPRPVAVTHLLVAVAEAFDVVVDFSESSEAELEVVNTAP | |||
| Full Sequence |
|---|
| Protein Sequence Length: 587 Download |
| MVPVRAEVAA LLLLLLVAAV GVAAGFRPGP PVSEDTLEKV AASLEMYVDL LPQMPKVLGY 60 SLKYGRPAPT HLTIGMYQKK WKFHRDLPVT TVFAFGTSAE SATFPGPTIE ALQGVPLWVT 120 WENHLPDRHI LPWDPTVPVA IPRAGGVPTV VHLHGGVHPP QSDGHANAWF TAGFRERGPT 180 WTTPTYAYPN AQSPGGVLWY HDHALGLTRA NLLAGLLGAY VIRNPAAEAP LGLPCGDALD 240 RVLVLADRSF YADGSLYMNC TGDNPGVHPQ WQPEYFGDAV TVNGKAWPFL PVARRRYRFR 300 IINASNARFF NLSLSNGLPF HVIGSDASYL PRPVAVTHLL VAVAEAFDVV VDFSESSEAE 360 LEVVNTAPYP YPDGDSPDHL TGKVMKFVVA PARLWDDHSR VPARLLDYVK VAEEEAAQRR 420 YIVMYEYEDE ATGNPTHLYI NGKRPEDPAT ETPRAGTTEV WEVINLTADN HPLHLHLATF 480 QAVRVRGLVE LEEFKRCMER LNDAARCGVA RHAVGEEVAV PEHERTWKNV VKLAPGFVTT 540 VVVKFLMVDT GRAYPFDAAA EPGYVYHCHI LDHEDNAMIR PLKLIR* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK10965 | PRK10965 | 2.0e-5 | 440 | 578 | 143 | + multicopper oxidase; Provisional | ||
| pfam07732 | Cu-oxidase_3 | 1.0e-10 | 103 | 226 | 127 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. | ||
| PRK10883 | PRK10883 | 2.0e-15 | 194 | 339 | 151 | + FtsI repressor; Provisional | ||
| PRK10965 | PRK10965 | 3.0e-20 | 94 | 339 | 260 | + multicopper oxidase; Provisional | ||
| COG2132 | SufI | 1.0e-39 | 67 | 582 | 527 | + Putative multicopper oxidases [Secondary metabolites biosynthesis, transport, and catabolism] | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0005507 | copper ion binding |
| GO:0016491 | oxidoreductase activity |
| GO:0055114 | oxidation-reduction process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | EAZ10376.1 | 0 | 30 | 570 | 28 | 566 | hypothetical protein OsJ_00212 [Oryza sativa Japonica Group] |
| GenBank | EAZ22879.1 | 0 | 67 | 586 | 65 | 582 | hypothetical protein OsJ_06565 [Oryza sativa Japonica Group] |
| RefSeq | NP_001041895.1 | 0 | 30 | 586 | 28 | 582 | Os01g0126100 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | XP_002455264.1 | 0 | 31 | 585 | 33 | 587 | hypothetical protein SORBIDRAFT_03g007440 [Sorghum bicolor] |
| RefSeq | XP_002457447.1 | 0 | 25 | 586 | 23 | 589 | hypothetical protein SORBIDRAFT_03g007480 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3zdw_A | 0 | 43 | 584 | 2 | 508 | A Chain A, Crystal Structure Of The Dipicolinate Synthase Chain B From Bacillus Cereus. Northeast Structural Genomics Consortium Target Bcr215. |
| PDB | 2x88_A | 0 | 43 | 584 | 2 | 508 | A Chain A, Crystal Structure Of The Dipicolinate Synthase Chain B From Bacillus Cereus. Northeast Structural Genomics Consortium Target Bcr215. |
| PDB | 2x87_A | 0 | 43 | 584 | 2 | 508 | A Chain A, Crystal Structure Of The Reconstituted Cota |
| PDB | 2bhf_A | 0 | 43 | 584 | 2 | 508 | A Chain A, Crystal Structure Of The Reconstituted Cota |
| PDB | 1w8e_A | 0 | 43 | 584 | 2 | 508 | A Chain A, Crystal Structure Of The Reconstituted Cota |
