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CAZyme Information: ASPZODRAFT_99088-t33_1-p1

You are here: Home > Sequence: ASPZODRAFT_99088-t33_1-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

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
Protein Length CGC Molecular Weight Isoelectric Point
427 KV878345|CGC4 44575.34 3.8262
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PzonataCBS506.65 10027 1073090 158 9869
Gene Location Start: 103753; End:105146  Strand: -

Full Sequence      Download help

MRLCFLFVSP  CLAGSVLWSG  IFNSTATVED  FDLWSWSNEI  EPWQWYIHGT  GNTSEYLGLS60
ADYKNPAASD  AQGLRITIDG  TSFWEDQTME  RSELIPQTAE  DLGAGHLYYH  FSLSTATTNA120
PNASFEHQIA  FFESAFTELQ  YGLEDGASGT  SDNTLRWLAG  GETYWSVQLE  AGNWYNFAYD180
INFDNQTVGL  WASNNSDPLV  LVVDAVAVTA  SSNSEDWHVG  ELRLPNGGVN  SAAEDWFWSG240
IYIEEAPLNT  EIGSASAAAS  TTAASASTAS  TSSATSVATS  TSTTAPTTST  TSTTSVSSTT300
IPVSTEPAST  SVPTSVSTSV  PSAVSSSTTV  AEISTTVVST  SESSAVATAT  PTEVSVSTST360
EVSVATPTAV  SISTATASSS  TATSTASTST  VLPIPSGSAS  QILSELHAML  TSLLSRAGVH420
ARDFNGH427

Enzyme Prediction      help

No EC number prediction in ASPZODRAFT_99088-t33_1-p1.

CAZyme Signature Domains help

Created with Snap214264851061281491701922132342562772983203413623844051254GH131
Family Start End Evalue family coverage
GH131 16 254 1.5e-93 0.9921568627450981

CDD Domains      download full data without filtering help

Created with Snap2142648510612814917019221323425627729832034136238440516244GH131_N308369SP4_N
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.

CAZyme Hits      help

Created with Snap2142648510612814917019221323425627729832034136238440512262QMW34786.1|GH13112262QRD91104.1|GH13112262UDD63765.1|GH13112262QMW46856.1|GH13112258BAE64574.1|GH131
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

PDB Hits      download full data without filtering help

Created with Snap21426485106128149170192213234256277298320341362384405142524LE3_A142583W9A_A
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]

Swiss-Prot Hits      help

ASPZODRAFT_99088-t33_1-p1 has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.289260 0.710700 CS pos: 13-14. Pr: 0.6695

TMHMM  Annotations      help

There is no transmembrane helices in ASPZODRAFT_99088-t33_1-p1.