CAZyme Information: ASPTUDRAFT_107715-t33_1-p1

Basic Information

• Species: Aspergillus tubingensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus tubingensis
• CAZyme ID: ASPTUDRAFT_107715-t33_1-p1
• CAZy Family: PL4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
818	KV878208|CGC10	87330.84	5.9206

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AtubingensisCBS134.48	12592	767770	274	12318

• Gene Location: location=KV878208:1730647-1733810(+)

Full Sequence      

AAQSPAIDVAGIAADPTPHGPTMSGTPADCNRWFTIKKGDTCYDLEKAFGLTPQQFQQWN
PAVSRDCLVNFWPGYAYCVGVGPVAIPTSADTAPHAPTMTGIAANCNRWYTAQKGDNCYA
VEKAFGLTPQQFQQWNPAWNPAVSLDCLVNLWPGYAYCVGVGPAANGPHGPTMPGIAPNC
VQFYTAKKGDTCYAVEKAFGITPQQFQQWNPAVSLDCLVNFWADYVYCVGVGPVAPTSTS
TVTATATSASTTTSSTTLTTSTTSTTALTTSTTSTAWTTGATWTTGTSTTSTSLSPTTVF
TTFTTTLTLTTTLTSNGQTTVIVTTTVTTTVSPSTTLGTSTTLTTALPPSGTSSTTTSTS
SVPTTSTSSASTTLTTSTTLSTPKPSTTSNPPTSTPSTPVTPTTPRTSTSTIPRSPSITP
NPSSRPPISPFPSTMVTTNATYSTRNPITSYNQTITPIDTAWPPTKTHPGQPKDCDKWYL
VAPGDTCRSIYQRHGNSITMDELLEWNPDLKADCDYPIAGYWVCVGIKRPALTIIYPTTN
DTVPDPTPWTPRPTPTETSVYPPTKTQPGLAPSCSAFYEAQPSDTCDQILASNPMLKFPL
LLEWNPALKADCSGILPGYSYCIAAYNDTNRPSPPTVTTQPYPLKPGTAKNCTAWYKKDD
GDTCDLIVEMFGTFDKAQFVAWNPDIGVHCYGLENGYYYCVADPSTPKTRTRPVITAMTF
PTARPRRQPGVTKDCNKWWLVSIHDDCYDIMQFNGITMADLYTWNPALSGKRNCLEGLVP
DTEVCVGIMSSSSTTDTAAPSSTVPGASFRTGLVTVRG

Enzyme Prediction     

EC	-	-

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
212030	LysM	2.46e-09	477	523	1	45	Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
212030	LysM	6.30e-09	182	218	1	37	Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
212030	LysM	4.01e-08	35	68	4	37	Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
212030	LysM	1.05e-06	108	141	1	34	Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
180536	PRK06347	2.48e-06	34	214	408	580	1,4-beta-N-acetylmuramoylhydrolase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAK42252.1|CBM50	0.0	1	818	19	792
BCS02341.1|CBM50	1.21e-264	458	818	24	383
BCS14019.1|CBM50	1.21e-264	458	818	24	383
BCS14018.1|CBM50	4.04e-148	1	225	19	315
BCS02340.1|CBM50	4.04e-148	1	225	19	315

PDB Hits     

ASPTUDRAFT_107715-t33_1-p1 has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4ALG0|LYSM1_ARTBC	3.96e-23	563	789	144	374	LysM domain-containing protein ARB_05157 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05157 PE=1 SV=1
sp|D4AVW3|LYSM5_ARTBC	1.30e-20	16	161	355	536	LysM domain-containing protein ARB_00327 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_00327 PE=3 SV=2
sp|D4AZ68|LYSM3_ARTBC	2.53e-10	574	701	268	406	LysM domain-containing protein ARB_01488 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_01488 PE=3 SV=1
sp|D4B5F9|PGDA_ARTBC	2.52e-08	700	788	339	437	Probable peptidoglycan-N-acetylglucosamine deacetylase ARB_03699 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_03699 PE=1 SV=2
sp|D4AY86|LYSM6_ARTBC	3.89e-07	20	159	263	419	LysM domain-containing protein ARB_01155/01156 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_01155/01156 PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000054	0.000000

TMHMM  Annotations     

There is no transmembrane helices in ASPTUDRAFT_107715-t33_1-p1.