CAZyme Information: jhhlp_004829-t41_1-p1

Basic Information

• Species: Lomentospora prolificans
• Lineage: Ascomycota; Sordariomycetes; ; Microascaceae; Lomentospora; Lomentospora prolificans
• CAZyme ID: jhhlp_004829-t41_1-p1
• CAZy Family: GH15|CBM20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
625		67269.80	4.9491

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_LprolificansJHH5317	8768	N/A	208	8560

• Gene Location: location=NLAX01000094:453866-455964(-)

Full Sequence      

MRAYTSLALVLSALRGIAACPVTSNPAIDDFVTSETEVSLHKLLCNIGSDGCEASGVAAG
VVVASPSKSDPDYWYTWTRDSALVFKTVIEQFASGDYDASLQKKIQEYIVAQAKLQGVDN
PSGSLVDGSGLGEPKFYVDLTQFTGAWGRPQHDGPALRAIAMAQYAKWLIDNGYPKTAQE
VVWPVIRNDLYYTAQYCRIRNNTGFDLWEEVSGASFFTTISQYRALVEGSNLASQLQTTC
KSCDEIAPQILCFVQNYWSNSGYIVSNIHNNAGRSGKDGNSILASIHSYDPRLGCDATTF
QPCSDKALSNHKAVTDSFRSWPINNGIPQGTAVAVGRYIEDVYYNGNPWYLLTLAAAEQL
YDAVAVWKAQGSVTVTSTSLGFFKDLVPSIATGTYQNGTTTYDSIIDAVFTYADGYLNVV
KTYMHTDGSMPEQFSKNDGTPLAARDLTWSYSAFLTAAAARSQAHSPQFGWLATAPKLPS
TCSALTADGSYVSATAVSFPASQTPGGTETITTTAPEPTSTVCLHKVTFNSVTQTVWGDS
VKVVGSIKELGSWNPANARPLSADAYTDSNPLWRATISVPAGSSFQYKFIKVNDAGAVTW
ESDPNRSYSASTQCSSTGNAGGNWQ

Enzyme Prediction     

EC	3.2.1.3:94	1.14.99.55:4

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	47	458	4.3e-75	0.9750692520775623
CBM20	526	615	3.9e-27	0.9555555555555556

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	8.26e-133	37	458	1	416	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	9.38e-41	518	624	3	106	Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Glucoamylases are inverting, exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1,4-glycosidic bonds but also have some activity towards 1,6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications, where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain, a C-terminal CBM20 domain, and a highly O-glycosylated linker region that connects the two. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.
395557	CBM_20	1.19e-36	527	617	3	92	Starch binding domain.
99883	CBM20_alpha_amylase	1.37e-30	527	619	3	91	Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.
215006	CBM_2	1.53e-27	526	608	2	84	Starch binding domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AAE15057.1|CBM20|GH15|3.2.1.3	6.80e-260	27	625	36	626
AAE15056.1|CBM20|GH15|3.2.1.3	6.80e-260	27	625	36	626
CAB91426.1|CBM20|GH15|3.2.1.3	1.37e-259	27	625	36	626
UPK89675.1|CBM20|GH15	2.28e-259	9	625	47	669
CAA47707.1|CBM20|GH15|3.2.1.3	5.02e-257	27	625	36	625

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VN4_A	1.19e-237	27	608	1	580	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
6FRV_A	1.81e-208	28	614	3	604	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
6FHV_A	2.99e-183	31	625	11	593	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
3EQA_A	2.61e-181	28	500	3	467	Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]
1AGM_A	7.43e-181	28	500	3	466	Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. x100 to 2.4 angstroms resolution [Aspergillus awamori],1DOG_A REFINED STRUCTURE FOR THE COMPLEX OF 1-DEOXYNOJIRIMYCIN WITH GLUCOAMYLASE FROM (ASPERGILLUS AWAMORI) VAR. X100 TO 2.4 ANGSTROMS RESOLUTION [Aspergillus awamori],1GLM_A REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 [Aspergillus awamori],3GLY_A REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 [Aspergillus awamori]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P14804|AMYG_NEUCR	2.43e-260	27	625	36	626	Glucoamylase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=gla-1 PE=1 SV=3
sp|P36914|AMYG_ASPOR	3.59e-214	28	614	30	600	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
sp|P69328|AMYG_ASPNG	2.61e-208	11	614	6	628	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
sp|P69327|AMYG_ASPAW	2.61e-208	11	614	6	628	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
sp|P22832|AMYG_ASPUS	4.08e-207	11	614	6	627	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000277	0.999687	CS pos: 19-20. Pr: 0.9661

TMHMM  Annotations     

There is no transmembrane helices in jhhlp_004829-t41_1-p1.