logo
sublogo
You are browsing environment: FUNGIDB
help

CAZyme Information: CLCR_09486-t43_1-p1

You are here: Home > Sequence: CLCR_09486-t43_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 Cladophialophora carrionii
Lineage Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Cladophialophora; Cladophialophora carrionii
CAZyme ID CLCR_09486-t43_1-p1
CAZy Family GT24
CAZyme Description phosphoribosyl transferase domain protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1164 126425.19 6.7916
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_CcarrioniiKSF 11240 N/A 59 11181
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 1.1.3.-:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA7 305 517 5.1e-44 0.4192139737991266

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
235028 PRK02304 3.43e-27 971 1163 1 175
adenine phosphoribosyltransferase; Provisional
398111 P-mevalo_kinase 2.61e-25 769 887 1 111
Phosphomevalonate kinase. Phosphomevalonate kinase (EC:2.7.4.2) catalyzes the phosphorylation of 5-phosphomevalonate into 5-diphosphomevalonate, an essential step in isoprenoid biosynthesis via the mevalonate pathway. This family represents the animal type of the enzyme. The other is the ERG8 type, found in plants and fungi, and some bacteria (see pfam00288).
396238 FAD_binding_4 6.53e-20 313 453 1 136
FAD binding domain. This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.
223577 Apt 2.15e-19 973 1161 5 177
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide transport and metabolism].
223354 GlcD 5.83e-18 284 520 3 226
FAD/FMN-containing dehydrogenase [Energy production and conversion].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.08e-15 282 505 79 294
2.58e-15 311 752 57 484
4.39e-15 310 753 58 479
1.86e-14 312 500 62 232
1.89e-14 311 505 68 242

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.76e-19 972 1145 3 166
Crystal Structure of Human APRT-Tyr105Phe variant in complex with Adenine, PRPP and Mg2+, 14 hours post crystallization [Homo sapiens],6FD4_B Crystal Structure of Human APRT-Tyr105Phe variant in complex with Adenine, PRPP and Mg2+, 14 hours post crystallization [Homo sapiens],6FD5_A Crystal Structure of Human APRT-Tyr105Phe variant in complex with Adenine, PRPP and Mg2+, 14 days post crystallization (with AMP and PPi products partially generated) [Homo sapiens],6FD5_B Crystal Structure of Human APRT-Tyr105Phe variant in complex with Adenine, PRPP and Mg2+, 14 days post crystallization (with AMP and PPi products partially generated) [Homo sapiens],6FD6_A Crystal Structure of Human APRT-Tyr105Phe variant in complex with Adenine, PRPP and Mg2+, 30 days post crystallization (with AMP and PPi products fully generated) [Homo sapiens],6FD6_B Crystal Structure of Human APRT-Tyr105Phe variant in complex with Adenine, PRPP and Mg2+, 30 days post crystallization (with AMP and PPi products fully generated) [Homo sapiens]
1.76e-19 972 1145 3 166
Crystal Structure of Human APRT wild type in complex with PRPP and Mg2+ [Homo sapiens],6FCH_B Crystal Structure of Human APRT wild type in complex with PRPP and Mg2+ [Homo sapiens],6FCL_A Crystal Structure of Human APRT wild type in complex with AMP [Homo sapiens],6FCL_B Crystal Structure of Human APRT wild type in complex with AMP [Homo sapiens],6HGP_A Crystal Structure of Human APRT wild type in complex with Phosphate ion. [Homo sapiens],6HGP_B Crystal Structure of Human APRT wild type in complex with Phosphate ion. [Homo sapiens],6HGR_A Crystal Structure of Human APRT wild type in complex with IMP [Homo sapiens],6HGR_B Crystal Structure of Human APRT wild type in complex with IMP [Homo sapiens],6HGS_A Crystal Structure of Human APRT wild type in complex with GMP [Homo sapiens],6HGS_B Crystal Structure of Human APRT wild type in complex with GMP [Homo sapiens]
1.81e-19 972 1145 4 167
Crystal Structure of Human APRT wild type in complex with Adenine, PRPP and Mg2+ [Homo sapiens],6FCI_B Crystal Structure of Human APRT wild type in complex with Adenine, PRPP and Mg2+ [Homo sapiens],6FCI_C Crystal Structure of Human APRT wild type in complex with Adenine, PRPP and Mg2+ [Homo sapiens],6FCI_D Crystal Structure of Human APRT wild type in complex with Adenine, PRPP and Mg2+ [Homo sapiens],6HGQ_A Crystal Structure of Human APRT wild type in complex with Hypoxanthine, PRPP and Mg2+ [Homo sapiens],6HGQ_B Crystal Structure of Human APRT wild type in complex with Hypoxanthine, PRPP and Mg2+ [Homo sapiens],6HGQ_C Crystal Structure of Human APRT wild type in complex with Hypoxanthine, PRPP and Mg2+ [Homo sapiens],6HGQ_D Crystal Structure of Human APRT wild type in complex with Hypoxanthine, PRPP and Mg2+ [Homo sapiens]
1.85e-19 972 1145 5 168
Crystal Structure of F173G Mutant of Human APRT [Homo sapiens],4X45_B Crystal Structure of F173G Mutant of Human APRT [Homo sapiens]
1.85e-19 972 1145 5 168
Crystal Structure of Mutant R89Q of human Adenine phosphoribosyltransferase [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.32e-22 972 1145 5 168
Adenine phosphoribosyltransferase OS=Cricetulus griseus OX=10029 GN=APRT PE=3 SV=2
1.47e-21 972 1145 5 168
Adenine phosphoribosyltransferase OS=Rattus norvegicus OX=10116 GN=Aprt PE=1 SV=1
2.21e-21 976 1150 5 166
Adenine phosphoribosyltransferase OS=Roseiflexus castenholzii (strain DSM 13941 / HLO8) OX=383372 GN=apt PE=3 SV=1
2.73e-21 972 1145 5 168
Adenine phosphoribosyltransferase OS=Dipodillus campestris OX=41199 GN=APRT PE=3 SV=1
6.89e-21 972 1145 5 168
Adenine phosphoribosyltransferase OS=Mastomys natalensis OX=10112 GN=APRT PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000044 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in CLCR_09486-t43_1-p1.