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Basic Information | |
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Species | Aquilegia coerulea |
Cazyme ID | Aquca_030_00210.1 |
Family | AA1 |
Protein Properties | Length: 1525 Molecular Weight: 170847 Isoelectric Point: 6.9082 |
Chromosome | Chromosome/Scaffold: 30 Start: 1498531 End: 1518022 |
Description | Tetratricopeptide repeat (TPR)-like superfamily protein |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA1 | 986 | 1510 | 0 |
NVQATPVKRLCKTHNIITVNGQYPGPTLEVNNGDSLEVKVVNRARYNVTIHWHGIRQFRTGWADGPEFVTQCPIRPGQSYTYRFTIEGQEGTLWWHAHSS WLRATVYGALIIHPKAGSSYPFTKPKRETPLMLGEWWDANPIDVVREATRTGAAPNISDAYTINGQPGDLYKCSGKDTVIVPLDSGETNLLRVINSALNQ ELFFTIANHRLTIVAVDASYVKPFTTSVIMIGPGQTTDILITADQPPARYYIAARAYQSAQNAAFDNTTTTAILEYKSAPCPAKKGQSARPILPPLPAYN DTATVTAFTSSLRSPSKVNVPTDIDENLFITVGLGLNPCPRGSRARNCQGPNGTRFTSSMNNVSFVLPSTVSLLQAHQQGIPGVFTTDFPAVPPVKFDYT GNVSRALWSPVRGTKLYKLKYGSTVQIVLQDTTIVTGENHPIHIHGYDFYIIAEGFGNFNSQSDTSKFNLVDPPQRNTVGVPVGGWAVIRFVADNPGVWL MHCHLDVHITWGLAMAFLVENGVGK |
Full Sequence |
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Protein Sequence Length: 1525 Download |
MSSKFGMAGG IPERRVRPIW DAVDSRQFKA ALKLSTALLS KYPKSPYAIA LKGLILERMG 60 KPDEALSVCI DAKERLYSND VVIVDDLTLS TLQIVFARLD RLDLATSCYE YACGKFPNNL 120 ELMMGLFNCY VREYSFVKQQ QTAIKMYKVV GEERFLLWAV CSIQLQVLSG TGGEKLLLLA 180 EGLLKKHVAS HSLHEPEALL LYISILEQQA KYGDALEILS GKLGSLLIIE VDRLRIQGRL 240 LARLCNYAAA ADIFKKILEI CPDDWECFLN YLGCLLEDDS RWCSGTIIDQ LHPSNYVSCK 300 LSHLNNEKFD SQIENASHFM QKIQIENNTD FVRCPYLANL EIERRKRLYG KVEDGQLSDS 360 LLKYFSRFGH MSCFTTDVEM FLQVMSHEEK MTLVEKFNKS CESSTTSQAK KLGQSITIFK 420 IQEAIGTMAN LSSDELECTA SHMADIYCKN LPLSKDLDLQ ENMHGEDLLS MSSNVLVQLF 480 WRTRNVGYLL EAIMVLEFGL TIRRHVWQYK ILLLHLYSHL SAFPLAYEWY KTLDIKNILL 540 ETVVHHILPQ MLVSPLWVDL SDILKDYLKF MDDHFRESAD LTFLAYRHRT YTKAIEFVQF 600 KERLQHSQQY LISRHEAAIL LLKQNADNIE EEESILESSD FGIQLLELSS DVTCKSLTFN 660 DDTRSRPWWT PAPDKNHLLG PFEGKSICHG DYLQKQAEER GANVRKVIER RSLLPRLIYL 720 SIVSASSSIK ESVDSNGSIC DGKNSRELKS LLERYARSLG RSFSEAVVEI VGVSNGQKSV 780 EVFGSNIVDW LNFAVFFNAW KLGSHEVDSS LGDECKSSSW TLVSNLIEKY TMEKLRSMQP 840 LIQSPGVDIS ILVQIVTEPM AWHCIVLQSC IRSILPSGKR KKKSGPTDNS NSPLFQEIQG 900 SVQSLCDMMG EVTKWLNEQL NAPEEDNLVS YLPGRGCNQG PGKVLQVLEA LASSSTDLEH 960 GERISKALCS WRSNDILRKI VIGQRNVQAT PVKRLCKTHN IITVNGQYPG PTLEVNNGDS 1020 LEVKVVNRAR YNVTIHWHGI RQFRTGWADG PEFVTQCPIR PGQSYTYRFT IEGQEGTLWW 1080 HAHSSWLRAT VYGALIIHPK AGSSYPFTKP KRETPLMLGE WWDANPIDVV REATRTGAAP 1140 NISDAYTING QPGDLYKCSG KDTVIVPLDS GETNLLRVIN SALNQELFFT IANHRLTIVA 1200 VDASYVKPFT TSVIMIGPGQ TTDILITADQ PPARYYIAAR AYQSAQNAAF DNTTTTAILE 1260 YKSAPCPAKK GQSARPILPP LPAYNDTATV TAFTSSLRSP SKVNVPTDID ENLFITVGLG 1320 LNPCPRGSRA RNCQGPNGTR FTSSMNNVSF VLPSTVSLLQ AHQQGIPGVF TTDFPAVPPV 1380 KFDYTGNVSR ALWSPVRGTK LYKLKYGSTV QIVLQDTTIV TGENHPIHIH GYDFYIIAEG 1440 FGNFNSQSDT SKFNLVDPPQ RNTVGVPVGG WAVIRFVADN PGVWLMHCHL DVHITWGLAM 1500 AFLVENGVGK LQSLEPPPAD LPVC* 1560 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam09797 | NatB_MDM20 | 4.0e-63 | 307 | 627 | 321 | + N-acetyltransferase B complex (NatB) non catalytic subunit. This is the non-catalytic subunit of the N-terminal acetyltransferase B complex (NatB). The NatB complex catalyzes the acetylation of the amino-terminal methionine residue of all proteins beginning with Met-Asp or Met-Glu and of some proteins beginning with Met-Asn or Met-Met. In Saccharomyces cerevisiae this subunit is called MDM20 and in Schizosaccharomyces pombe it is called Arm1. NatB acetylates the Tpm1 protein and regulates and tropomyocin-actin interactions. This subunit is required by the NatB complex for the N-terminal acetylation of Tpm1. | ||
PLN02191 | PLN02191 | 1.0e-67 | 996 | 1511 | 546 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 2.0e-72 | 996 | 1513 | 556 | + oxidoreductase | ||
TIGR03388 | ascorbase | 2.0e-87 | 996 | 1519 | 555 | + L-ascorbate oxidase, plant type. Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases. | ||
TIGR03389 | laccase | 0 | 986 | 1524 | 544 | + laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate. |
Gene Ontology | |
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GO Term | Description |
GO:0005507 | copper ion binding |
GO:0016491 | oxidoreductase activity |
GO:0055114 | oxidation-reduction process |
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 | CBI15873.1 | 0 | 1 | 1524 | 1 | 1561 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_200653.2 | 0 | 1 | 987 | 64 | 1040 | binding [Arabidopsis thaliana] |
RefSeq | XP_002273069.1 | 0 | 1 | 989 | 1 | 989 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002319956.1 | 0 | 1 | 983 | 1 | 1012 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002516347.1 | 0 | 1 | 998 | 1 | 999 | TPR repeat-containing protein R13F6.10, 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 | 1asq_B | 0 | 996 | 1502 | 19 | 521 | A Chain A, Heme Ligand Mutant Of Recombinant Horseradish Peroxidase In Complex With Benzhydroxamic Acid |
PDB | 1asq_A | 0 | 996 | 1502 | 19 | 521 | A Chain A, Heme Ligand Mutant Of Recombinant Horseradish Peroxidase In Complex With Benzhydroxamic Acid |
PDB | 1asp_B | 0 | 996 | 1502 | 19 | 521 | A Chain A, Heme Ligand Mutant Of Recombinant Horseradish Peroxidase In Complex With Benzhydroxamic Acid |
PDB | 1asp_A | 0 | 996 | 1502 | 19 | 521 | A Chain A, Heme Ligand Mutant Of Recombinant Horseradish Peroxidase In Complex With Benzhydroxamic Acid |
PDB | 1aso_B | 0 | 996 | 1502 | 19 | 521 | A Chain A, Heme Ligand Mutant Of Recombinant Horseradish Peroxidase In Complex With Benzhydroxamic Acid |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO797675 | 510 | 1024 | 1525 | 0 |
DY297248 | 342 | 1163 | 1503 | 0 |
DY263574 | 337 | 987 | 1322 | 0 |
EX658195 | 270 | 987 | 1256 | 0 |
FC900507 | 290 | 1163 | 1452 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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