CAZyme Information: ASPVEDRAFT_50716-t33_1-p1

Basic Information

• Species: Aspergillus versicolor
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus versicolor
• CAZyme ID: ASPVEDRAFT_50716-t33_1-p1
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1005		110440.76	5.1214

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=KV878126:3622978-3626607(+)

Full Sequence      

MGASARLWASLACAVALLGTGSYGRFTTRDDIRTKLAPELSEHAAVYYPDSDVFEDATAR
WSYYHPPNFTVVVEVAVEEDVAKTIRYANAEGLPFLAVNDGHGAISSLANLNHGIEIWLH
KLNSIKIAEDGKTATFGGGTKSVTLIRDLFQQGKQTVHGVCECVSYLGPALGGGHGALQG
KYGMAADQFVSLNIATADGQIITVSEKSDDQDLWWAVRGAGHNFGIVTSVTSKVYDVPDG
GLWAYEQLAFTSDQVEALFEHFNDLADIQPPGFFVWTYLLRIPDLDPKNPVYLANFVREG
VEEIEPELIQPFRDLAATPAAVKKHGLYTDIPTWIDTGVNSRGCAKEGSKVRFPIGFKRF
DIPAQREYFDAFAEGTAGDSQFNTSLTLIEQYSAQGVEAIHEDSTAFPNREDFFLFAPTI
AYSSDTKEVENKAVEFGDQLRDIILKGTGSDNLHSYVNYAAGNEGPRAWYGWEPWRLEKL
QQLEVPPAEPAQEPPKVAVTPCEGLPVRYYFEGGLRRVYPYHYTYNTYCKERWRNRELID
IFTTEFRDREPGYYRKALESGNVTVNGKSAGPNTVLKNGEVVSHTLHRHEPPVTGNDVGI
IEETDDLLVIDKPAGVPVHSTGRYHYNSVMEIIRHNYGGKFVPRPCNRLDRLTSGVMFVG
KTAQGADRMTVSLRERTVQKEYVARVKGKFPDGVLIVDQPIMSISPKVGLNRVRATGKEA
KTKFRRLAYYPPAPPAPQASAAEGEGDEKESGTRPATPPPSYINESEGYSIVHCLPLTGR
THQIRVHLQFLGHPISNDPIYSNRRVFGPELGKNESTADRDDEIIDRLMEMGRTELPETV
SYRTHLTTLPVVPPGTDSSVVQAIMTKEHEAAVEAYQKRKGERLSGKTCDVCGTELYTDP
GVHELGIFLHAVAYSDAGGEWQYRSKMPRWALPPVGMDGPREVPAWEEVEADKETVVGQG
SVPELGGDEDGTTALVEGVGSVDISAARQAQESAAAGAAGAGNGL

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	59	283	1.4e-42	0.48253275109170307

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
211331	PseudoU_synth_ScRIB2	1.72e-100	583	803	1	187	Pseudouridine synthases similar to Saccharomyces cerevisiae RIB2. Pseudouridine synthase, Saccharomyces cerevisiae RIB2_like. This group is comprised of eukaryotic and bacterial proteins similar to Saccharomyces cerevisiae RIB2, S. cerevisiae Pus6p and human hRPUDSD2. S. cerevisiae RIB2 displays two distinct catalytic activities. The N-terminal domain of RIB2 is RNA:psi-synthase which makes psi32 on cytoplasmic tRNAs. Psi32 is highly phylogenetically conserved. The C-terminal domain of RIB2 has a DRAP deaminase activity which catalyses the formation of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate from 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate during riboflavin biosynthesis. S. cerevisiae Pus6p makes the psi31 of cytoplasmic and mitochondrial tRNAs.
161659	rluA_subfam	9.93e-83	531	814	1	257	pseudouridine synthase, RluA family. In E. coli, RluD (SfhB) modifies uridine to pseudouridine at 23S RNA U1911, 1915, and 1917, RluC modifies 955, 2504 and 2580, and RluA modifies U746 and tRNA U32. An additional homolog from E. coli outside this family, TruC (SP|Q46918), modifies uracil-65 in transfer RNAs to pseudouridine. [Protein synthesis, tRNA and rRNA base modification]
223638	RluA	3.11e-61	552	807	28	255	Pseudouridylate synthase, 23S rRNA- or tRNA-specific [Translation, ribosomal structure and biogenesis].
211346	PseudoU_synth_RluA_like	1.24e-46	607	812	1	174	Pseudouridine synthase, RluA family. This group is comprised of eukaryotic, bacterial and archeal proteins similar to eight site specific Escherichia coli pseudouridine synthases: RsuA, RluA, RluB, RluC, RluD, RluE, RluF and TruA. Pseudouridine synthases catalyze the isomerization of specific uridines in a n RNA molecule to pseudouridines (5-ribosyluracil, psi) requiring no cofactors. E. coli RluC for example makes psi955, 2504 and 2580 in 23S RNA. Some psi sites such as psi1917 in 23S RNA made by RluD are universally conserved. Other psi sites occur in a more restricted fashion, for example psi2819 in 21S mitochondrial ribosomal RNA made by S. cerevisiae Pus5p is only found in mitochondrial large subunit rRNAs from some other species and in gram negative bacteria. The E. coli counterpart of this psi residue is psi2580 in 23S rRNA. psi2604in 23S RNA made by RluF has only been detected in E.coli.
376401	PseudoU_synth_2	2.27e-27	607	789	1	150	RNA pseudouridylate synthase. Members of this family are involved in modifying bases in RNA molecules. They carry out the conversion of uracil bases to pseudouridine. This family includes RluD, a pseudouridylate synthase that converts specific uracils to pseudouridine in 23S rRNA. RluA from E. coli converts bases in both rRNA and tRNA.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRC92907.1|AA7	3.09e-18	73	271	79	268
UNI23960.1|AA7	4.78e-18	56	483	29	456
QLI74064.1|AA7	2.48e-17	29	481	37	474
QRW22693.1|AA7	3.83e-17	68	228	60	220
QUC19098.1|AA7	6.16e-17	72	484	51	453

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2BVF_A	3.31e-31	32	285	2	257	Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 3 (P1) [Paenarthrobacter nicotinovorans],2BVF_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 3 (P1) [Paenarthrobacter nicotinovorans],2BVG_A Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_C Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_D Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVH_A Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_C Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_D Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans]
3W8W_A	5.07e-22	21	484	1	448	The crystal structure of EncM [Streptomyces maritimus],3W8W_B The crystal structure of EncM [Streptomyces maritimus],3W8X_A The complex structure of EncM with trifluorotriketide [Streptomyces maritimus],3W8X_B The complex structure of EncM with trifluorotriketide [Streptomyces maritimus],3W8Z_A The complex structure of EncM with hydroxytetraketide [Streptomyces maritimus],3W8Z_B The complex structure of EncM with hydroxytetraketide [Streptomyces maritimus]
6FYD_A	1.55e-21	31	484	7	444	The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_B The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_C The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_D The crystal structure of EncM T139V mutant [Streptomyces maritimus]
6FYE_A	2.76e-21	31	484	7	444	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYB_A	3.69e-21	31	484	7	444	The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_B The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_C The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_D The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYC_A The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus],6FYC_B The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|B6HLP5|CHYH_PENRW	1.39e-129	8	484	12	484	FAD-linked oxidoreductase chyH OS=Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) OX=500485 GN=chyH PE=3 SV=1
sp|I1S3L1|CHRY5_GIBZE	4.08e-126	28	484	23	490	FAD-linked oxidoreductase chry5 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=chry5 PE=3 SV=1
sp|Q09709|YA32_SCHPO	7.60e-112	509	932	15	381	Pseudouridylate synthase C18B11.02c OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPAC18B11.02c PE=3 SV=1
sp|Q12362|RIB2_YEAST	3.93e-102	512	934	75	434	Bifunctional protein RIB2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=RIB2 PE=1 SV=1
sp|Q12069|PUS9_YEAST	1.89e-101	512	932	102	460	tRNA pseudouridine(32) synthase, mitochondrial OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=PUS9 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.002669	0.997279	CS pos: 24-25. Pr: 0.9675

TMHMM  Annotations     

Start	End
7	26