Species | Penicilliopsis zonata | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Penicilliopsis; Penicilliopsis zonata | |||||||||||
CAZyme ID | ASPZODRAFT_99088-t33_1-p1 | |||||||||||
CAZy Family | GT58 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 103753; End:105146 Strand: - |
MRLCFLFVSP CLAGSVLWSG IFNSTATVED FDLWSWSNEI EPWQWYIHGT GNTSEYLGLS | 60 |
ADYKNPAASD AQGLRITIDG TSFWEDQTME RSELIPQTAE DLGAGHLYYH FSLSTATTNA | 120 |
PNASFEHQIA FFESAFTELQ YGLEDGASGT SDNTLRWLAG GETYWSVQLE AGNWYNFAYD | 180 |
INFDNQTVGL WASNNSDPLV LVVDAVAVTA SSNSEDWHVG ELRLPNGGVN SAAEDWFWSG | 240 |
IYIEEAPLNT EIGSASAAAS TTAASASTAS TSSATSVATS TSTTAPTTST TSTTSVSSTT | 300 |
IPVSTEPAST SVPTSVSTSV PSAVSSSTTV AEISTTVVST SESSAVATAT PTEVSVSTST | 360 |
EVSVATPTAV SISTATASSS TATSTASTST VLPIPSGSAS QILSELHAML TSLLSRAGVH | 420 |
ARDFNGH | 427 |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH131 | 16 | 254 | 1.5e-93 | 0.9921568627450981 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
408085 | GH131_N | 5.24e-65 | 16 | 244 | 1 | 246 | Glycoside hydrolase 131 catalytic N-terminal domain. This is the N-terminal domain found in glycoside hydrolase family 131 (GH131A) protein observed in Coprinopsis cinerea. GH131A exhibits bifunctional exo-beta-1,3-/-1,6- and endo-beta-1,4 activity toward beta-glucan. This domain is catalytic in nature though the catalytic mechanism of C. cinerea GH131A is different from that of typical glycosidases that use a pair of carboxylic acid residues as the catalytic residues. In the case of GH131A, Glu98 and His218 may form a catalytic dyad and Glu98 may activate His218 during catalysis. |
411773 | SP4_N | 0.008 | 308 | 369 | 277 | 338 | N-terminal domain of transcription factor Specificity Protein (SP) 4. Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. Human SP4 is a risk gene of multiple psychiatric disorders including schizophrenia, bipolar disorder, and major depression. SP4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP4. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QMW34786.1|GH131 | 2.46e-130 | 12 | 262 | 15 | 261 |
QRD91104.1|GH131 | 2.46e-130 | 12 | 262 | 15 | 261 |
UDD63765.1|GH131 | 2.46e-130 | 12 | 262 | 15 | 261 |
QMW46856.1|GH131 | 1.99e-129 | 12 | 262 | 15 | 261 |
BAE64574.1|GH131 | 1.99e-129 | 12 | 258 | 15 | 257 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4LE3_A | 5.65e-84 | 14 | 252 | 1 | 240 | Chain A, Beta-glucanase [Podospora anserina],4LE3_B Chain B, Beta-glucanase [Podospora anserina],4LE3_C Chain C, Beta-glucanase [Podospora anserina],4LE3_D Chain D, Beta-glucanase [Podospora anserina],4LE4_A Chain A, Beta-glucanase [Podospora anserina],4LE4_B Chain B, Beta-glucanase [Podospora anserina],4LE4_C Chain C, Beta-glucanase [Podospora anserina],4LE4_D Chain D, Beta-glucanase [Podospora anserina] |
3W9A_A | 8.97e-84 | 14 | 258 | 1 | 237 | Chain A, Crystal structure of the catalytic domain of the glycoside hydrolase family 131 protein from Coprinopsis cinerea [Coprinopsis cinerea okayama7#130],3W9A_B Chain B, Crystal structure of the catalytic domain of the glycoside hydrolase family 131 protein from Coprinopsis cinerea [Coprinopsis cinerea okayama7#130],3W9A_C Chain C, Crystal structure of the catalytic domain of the glycoside hydrolase family 131 protein from Coprinopsis cinerea [Coprinopsis cinerea okayama7#130],3W9A_D Chain D, Crystal structure of the catalytic domain of the glycoside hydrolase family 131 protein from Coprinopsis cinerea [Coprinopsis cinerea okayama7#130] |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.289260 | 0.710700 | CS pos: 13-14. Pr: 0.6695 |
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