| Basic Information | |
|---|---|
| Species | Chlamydomonas reinhardtii |
| Cazyme ID | Cre07.g331150.t1.2 |
| Family | AA2 |
| Protein Properties | Length: 1378 Molecular Weight: 150219 Isoelectric Point: 6.9839 |
| Chromosome | Chromosome/Scaffold: 7 Start: 2716643 End: 2727658 |
| Description | Cupredoxin superfamily protein |
| 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 |
| AA2 | 194 | 345 | 1e-21 |
| EKRLASFFMRAAFHDSLAVDVSQCPGPNCGGADASLVLSLEEMARPENAEDNFAELAGRAAKKIASFYDVSVADTLAVCAAVAPEVLSKGRIKILTGSGK GVLRVGRLDSVVPAPPGNLPAANTTLEQFAAFWAARGISATEATALMGSHAL | |||
| Full Sequence |
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| Protein Sequence Length: 1378 Download |
| MLAATPAGPW RSPGALQASA WTVFAGALQG HTRLPSARLA SLQAYGASST SRLHPLTRAQ 60 QQRADPPQPP SSLLPNCPFR AAVNAQTRTS ALGPIPDAIA AALGVQDGAL TTAAGAAVDP 120 APLAAKLSAR IQCSARLCVD MTKYAWHTDL ADVNARVLLW SPKVPTMRAG QTYDPRGKDW 180 VSVVAMCREL FKYEKRLASF FMRAAFHDSL AVDVSQCPGP NCGGADASLV LSLEEMARPE 240 NAEDNFAELA GRAAKKIASF YDVSVADTLA VCAAVAPEVL SKGRIKILTG SGKGVLRVGR 300 LDSVVPAPPG NLPAANTTLE QFAAFWAARG ISATEATALM GSHALIDDQA CFQGKGMSDY 360 CNPATADCSN VRMFRWENHY YKDICSPTLT VRTEKPGELD PVETPIVGMT DPEIDAEARR 420 ETCKFTSKEG RTMAMNRLAL MRCGLMPEPV EPEDGVTVTW TYKNCRDGAA YGINVAEQCP 480 HAHLWFYTPN DAYLGLACQG VGTSAAAAEV RSATRAFIKS QDEWDKAFSS AYIKMVTAFA 540 LWPDADGSDR KAAYLINGGE CATGLHLEAA CAQGAAGPAS ADVRALHAAT YVPPSSKLRD 600 SCKSCSQGVC PEPKQCEQCV KQFRADRRPK TNPLVTEANC CGCATLSRSL TYNATKDANG 660 NTYVIKTDFG VRWPDVMPFV LPPQPLPAAA ACPVPERQLD TFTFDDNVAP TVTIRPAGSN 720 PPVAPEGDIS DLCPAADGTI VEVRGYPSSP FRWKPFTQTY VAPPRAQVAA SYARPGTNLT 780 VDAYEIDIFT TARNIGCPGG RPTWFLSYNG SVPGPSFRVL KGRQTLVRFN NRLTPANLSG 840 TPFSLQFDPC EGTRSGRPIT VHLHGSSSLA PYDGWAEDST CGAETKDYYY PNWRAGFLWY 900 HDHQLDITSE NAYFGLSGMY TVHDRAAEGG CGEPWNLDAL PDWDMQFKDG VLDRHCQLYY 960 DRAGPHRNNL YGDINFVNGI PWPVATMEPR WQRFRWLVSS VSRPYKLRFV DAATGADVGG 1020 SKCHVIAGDG GIRRTPATFP AAGLFVAVAE RYEVVCDFRD FNGRSLYLLN AFDDDRMKDV 1080 PFFCNSHLVM KIDVRCNGTG CLASPPPVNA IFTPLVPAQP AIDRVLSQTD INAALTLARN 1140 RQCTRTFRFG RRNGQWVING ETWHTVRIAA GDVGHNTWEV WCLETGGGWF HPIHIHLVDF 1200 YVLTRNREEA QVREYERFTP KDMVQLDPGA EVSVLVRFGA HRGEFMFHCH NLMHEDFEMM 1260 RSFHVVPTPG SRTAATALPL QAQPSIVQNL NVVYDLYDDP VYGPARPRPS AGLTPLRVPS 1320 VQTTAALSFP IDNALYRIYY PNGAPNVNPL LANAAINPWI VDICQPQRAQ QVQEQQV* 1380 |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK10883 | PRK10883 | 2.0e-13 | 799 | 1269 | 496 | + FtsI repressor; Provisional | ||
| pfam00141 | peroxidase | 7.0e-14 | 188 | 344 | 164 | + Peroxidase. | ||
| pfam07731 | Cu-oxidase_2 | 4.0e-15 | 1162 | 1267 | 109 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. | ||
| cd00314 | plant_peroxidase_like | 3.0e-35 | 189 | 422 | 244 | + Heme-dependent peroxidases similar to plant peroxidases. Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX), which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions. Several sub-families can be identified. Class I includes intracellular peroxidases present in fungi, plants, archaea and bacteria, called catalase-peroxidases, that can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. Catalase-peroxidases are typically comprised of two homologous domains that probably arose via a single gene duplication event. Class II includes ligninase and other extracellular fungal peroxidases, while class III is comprised of classic extracellular plant peroxidases, like horseradish peroxidase. | ||
| COG2132 | SufI | 2.0e-39 | 769 | 1267 | 510 | + 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 |
| EMBL | CAB75422.1 | 0 | 725 | 1292 | 45 | 571 | polyphenol oxidase [Acremonium murorum] |
| RefSeq | XP_001690431.1 | 0 | 75 | 1366 | 27 | 1319 | hypothetical protein CHLREDRAFT_169463 [Chlamydomonas reinhardtii] |
| RefSeq | XP_001690611.1 | 0 | 77 | 1369 | 29 | 1302 | hypothetical protein CHLREDRAFT_188467 [Chlamydomonas reinhardtii] |
| RefSeq | XP_001795063.1 | 0 | 763 | 1266 | 40 | 490 | hypothetical protein SNOG_04650 [Phaeosphaeria nodorum SN15] |
| RefSeq | XP_001938088.1 | 0 | 749 | 1266 | 26 | 488 | blue copper oxidase cueO precursor [Pyrenophora tritici-repentis Pt-1C-BFP] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3abg_B | 0 | 756 | 1281 | 11 | 491 | A Chain A, X-Ray Crystal Analysis Of Bilirubin Oxidase From Myrothecium Verrucaria At 2.3 Angstrom Resolution Using A Twin Crystal |
| PDB | 3abg_A | 0 | 756 | 1281 | 11 | 491 | A Chain A, X-Ray Crystal Analysis Of Bilirubin Oxidase From Myrothecium Verrucaria At 2.3 Angstrom Resolution Using A Twin Crystal |
| PDB | 2xll_D | 0 | 756 | 1281 | 11 | 491 | A Chain A, X-Ray Crystal Analysis Of Bilirubin Oxidase From Myrothecium Verrucaria At 2.3 Angstrom Resolution Using A Twin Crystal |
| PDB | 2xll_C | 0 | 756 | 1281 | 11 | 491 | A Chain A, X-Ray Crystal Analysis Of Bilirubin Oxidase From Myrothecium Verrucaria At 2.3 Angstrom Resolution Using A Twin Crystal |
| PDB | 2xll_B | 0 | 756 | 1281 | 11 | 491 | A Chain A, X-Ray Crystal Analysis Of Bilirubin Oxidase From Myrothecium Verrucaria At 2.3 Angstrom Resolution Using A Twin Crystal |
| Hydropathy |
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