CAZyme Information: ASPVEDRAFT_49868-t33_1-p1

Basic Information

• Species: Aspergillus versicolor
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus versicolor
• CAZyme ID: ASPVEDRAFT_49868-t33_1-p1
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1141	KV878126|CGC4	124187.14	7.5253

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AversicolorCBS583.65	13364	1036611	142	13222

• Gene Location: location=KV878126:751428-754853(-)

Full Sequence      

MATLDSVKHALRHIADTSRPAVHQILSDALYSSAFDLLLQGPGWTSYRDFIIPQLSKLLD
PVFDSHDHVSVLEIGPGPQSILGHLSDRARRKITKYAAYEPNEVFNSKMREWLCPSSQAE
HPLPCLEKPPDIHQAPFMPAQYAGFGAHSHNEQFDIILFCHSLYGIKHKADIVKLAVNML
REKPEGAMVVVFHRDAGLRELGSLVCHRTASLPTGIIRIPNTDEALDQFSSFIAGFAVQD
GTIRDKWRAKCRSLGHSDDAHPGQLEFRSPEIMVTFTRHAASLQELTAQLPLVERQRTIK
NRDARLHQRAAIIRPTEVGHIQACVQWALKHGASLTVIGGGHSGHCLWPSVVGVDMSAFN
QVHTATATEDQTDGSTPCSIIVAGAGCTSIDIIRAAKATGITVPLGTRPSVGAGLWLQGG
IGHLARMYGLACDSIVGAVLVCVHTSQVLCIGHVPNEHRPADAVRPEKEADLLWAIRGAG
TNIGIVVSVTFKTYTAPTYSVQTWIVPLNNSLAARCKLRDFDQGIAGKLPRSSSADAYLY
TEAGKLHLGVAMFEALSTDPEMISERTLTTGRHILGRETSSKVVDCIGLFEVDMYISGMH
GGHGGGKTSSFKRCLFLKDIGQPSMVDALTAAVTTAPSPFCYLHLLHGGGAVGEVPPDAT
AFGCRDWDFACVITGVWPRDLDQTHFARGVVDWVYHVANSLLPLSCGVYGADLGPDPRDT
PLAARAFGPNLSRLANLKQRVDPQNVLAYACPLPKNTLLSNPKLIVVVTGVAGAGKDYCA
EIWASLLGTEMGRTARTASISYVAKQEYAAASGADFTRLLHDRVYKEQHRQALTAFFQAQ
VWNEPWLPAERFMRTVDESRDVDVLLITGMRDNAPVPSFAHLVPTRRLLEVQIASGDETR
RTRRGFFDHGLANNPLGCSPNFTFNNEKPGEEAAKAFARRHLVPFLHEDLQRLADMVRLV
PEFPRPGIEFRHVLNIAQHPGGLALCTSLLRSHFAGDWAKVNVVACCEAGGFVYASPLAS
QVDKPLALIREAGKLPPPTVSVQRSTSHIGASGPTNPTDTRIELSRDAIPRGASVVVVDD
VLATGNTLCAVLHLLREASVRIEDMSVMVVAEFPVHRGRELLRLRGFGRVNVQSLLVYDG
V

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	310	504	2.1e-38	0.38209606986899564

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
235028	PRK02304	4.68e-36	948	1140	1	175	adenine phosphoribosyltransferase; Provisional
223577	Apt	1.00e-25	950	1140	5	179	Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide transport and metabolism].
177930	PLN02293	8.91e-23	950	1137	14	180	adenine phosphoribosyltransferase
398111	P-mevalo_kinase	1.24e-21	768	884	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	4.89e-19	310	441	2	129	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRC92907.1|AA7	1.81e-14	310	746	64	483
UDD61931.1|AA7	2.89e-14	310	745	49	463
UQC87672.1|AA7	7.49e-14	310	749	71	491
QMW42271.1|AA7	1.19e-13	310	746	49	464
CAE7214923.1|AA7	1.28e-13	315	746	69	482

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4X45_A	1.56e-18	949	1139	5	180	Crystal Structure of F173G Mutant of Human APRT [Homo sapiens],4X45_B Crystal Structure of F173G Mutant of Human APRT [Homo sapiens]
6FCH_A	2.02e-18	949	1139	3	178	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]
6FCI_A	2.08e-18	949	1139	4	179	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]
1ORE_A	2.13e-18	949	1139	5	180	Human Adenine Phosphoribosyltransferase [Homo sapiens],1ZN7_A Human Adenine Phosphoribosyltransferase Complexed with PRPP, ADE and R5P [Homo sapiens],1ZN7_B Human Adenine Phosphoribosyltransferase Complexed with PRPP, ADE and R5P [Homo sapiens],1ZN8_A Human Adenine Phosphoribosyltransferase Complexed with AMP, in Space Group P1 at 1.76 A Resolution [Homo sapiens],1ZN8_B Human Adenine Phosphoribosyltransferase Complexed with AMP, in Space Group P1 at 1.76 A Resolution [Homo sapiens],1ZN9_A Human Adenine Phosphoribosyltransferase in Apo and AMP Complexed Forms [Homo sapiens],1ZN9_B Human Adenine Phosphoribosyltransferase in Apo and AMP Complexed Forms [Homo sapiens]
4X44_A	2.13e-18	949	1139	5	180	Crystal Structure of Mutant R89Q of human Adenine phosphoribosyltransferase [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|C5CIH1|APT_KOSOT	1.73e-22	953	1138	3	170	Adenine phosphoribosyltransferase OS=Kosmotoga olearia (strain ATCC BAA-1733 / DSM 21960 / TBF 19.5.1) OX=521045 GN=apt PE=3 SV=1
sp|Q64427|APT_MASNA	5.72e-22	949	1139	5	180	Adenine phosphoribosyltransferase OS=Mastomys natalensis OX=10112 GN=APRT PE=3 SV=1
sp|P47952|APT_CRIGR	5.72e-22	949	1139	5	180	Adenine phosphoribosyltransferase OS=Cricetulus griseus OX=10029 GN=APRT PE=3 SV=2
sp|P36972|APT_RAT	7.78e-22	949	1139	5	180	Adenine phosphoribosyltransferase OS=Rattus norvegicus OX=10116 GN=Aprt PE=1 SV=1
sp|A7NG77|APT_ROSCS	1.59e-21	953	1122	5	161	Adenine phosphoribosyltransferase OS=Roseiflexus castenholzii (strain DSM 13941 / HLO8) OX=383372 GN=apt PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000080	0.000000

TMHMM  Annotations     

There is no transmembrane helices in ASPVEDRAFT_49868-t33_1-p1.