CAZyme Information: jhhlp_001539-t41_1-p1

Basic Information

• Species: Lomentospora prolificans
• Lineage: Ascomycota; Sordariomycetes; ; Microascaceae; Lomentospora; Lomentospora prolificans
• CAZyme ID: jhhlp_001539-t41_1-p1
• CAZy Family: AA7
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1058		116223.04	4.5094

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

Full Sequence      

MYQKVLGLLGAPTFLLFAPNILTAQPDAGSLLTSPNGSVEDFIAWERPIALENILCNIGP
ECVDFYTWTRDAALVFKGLVEIFAANQTTDLQTEIHNYIQAQARLQAVENLSGSLRDGSG
LAEPKFHVDSTAFTDNWGRPQRDGPPLRAIAMMAYANWLVEQGEKPLALDKIWPVIQNDL
SYVVQHWNKTGFDLWEEVEGSSFFTTASQYRALIEGGTLAKALGFSCPHCDIVAPQILCF
LQQYWSPSQGYALSNINDHSDRSSKDVNAILASIHSFDPSVGCDGNTFQPCSSRMLATHK
ILADSFKDEYPINSGVAPGKAMAIGRYPEDVYYGGHPWYLATLAAAEQMYDALYVWQENG
YIEVTDVDVPFFHDFSHELQTGKHLNDSAEFAALMNSIANYADGFIDIVAEYIHPNGSIA
EQYTRDTGTPTSARDLTWSYAAFLSAVARRDKQVPRSWLNAQVVTPPNKCVPTSIVGYYA
AADPSPFPLPRGNEKAPGDGQGPGGSCPETRYVVVNFQVRVVTSWGEKIKMVGNTDILGG
WEPGLGVELNAAGYSEEDPIWRVSIVLLAGQEIEYKFVRVGEDGQQVSWESDPNRRYSAP
AECETTATVHPSSPIRIAASPRESPKPRNGLADPTSRHPPAGTAQARPLRTRVVLHHPTL
PLLATSHGRTVTVFSLTSLTPHSTVTNGHERSIRCTAWKPNLDPGRLCLVSGSFDSTAGL
WRWEGASEERDHATDMTARSAAGSDDERREDEDDEEEDTDWQFTLVLEGHDSEIKGVAFS
PSGAHLATCSRDKSVWIWEDVGADEDDDEWETVAVLNEHEGDVKAVAWCPDVPGRNARRS
YSADVLASASYDDTVRIWREDDDGEWVCVAVLSGHEGTVWGIAWEGTERADGAFPRLASC
SADGTIRVWKLKVDDEDDAPTATLGGIPNTMRRSLREDWVCEAVLPKAHTRDIYSVTWSP
RTGLLASTGSDGVIALYREEDEPEPAKAADPGAGGDEAAGSKKWKLVATYDRGHGPYEVN
HVTWCPRYDSEKKPGEEMLVTTGDDGQVRTWRVSVPDA

Enzyme Prediction     

EC	3.2.1.3:94	3.2.1.1:13

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	65	447	2.2e-73	0.8836565096952909
CBM20	513	605	6e-24	0.9777777777777777

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	2.41e-111	48	446	1	415	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
238121	WD40	1.51e-38	657	1052	18	289	WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
99886	CBM20_glucoamylase	1.07e-32	523	612	17	105	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.
293791	7WD40	3.79e-31	777	1051	4	200	WD40 repeats in seven bladed beta propellers. The WD40 repeat is found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing, and cytoskeleton assembly. It typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40. Between the GH and WD dipeptides lies a conserved core. It forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel beta-sheet. The WD40 sequence repeat originally described in literature forms the first three strands of one blade and the last strand in the next blade. The C-terminal WD40 repeat completes the blade structure of the N-terminal WD40 repeat to create the closed ring propeller-structure. The residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands, allowing them to bind either stably or reversibly.
238121	WD40	1.83e-29	766	1053	4	248	WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AEO61583.1|CBM20|GH15|3.2.1.3	AEO61583.1|CBM20|GH15|3.2.1.3	3.33e-204	25	598	16	608
AEO64596.1|CBM20|GH15	AEO64596.1|CBM20|GH15	1.16e-201	38	609	35	632
QSZ31699.1|CBM20|GH15	QSZ31699.1|CBM20|GH15	2.17e-201	38	609	68	671
APA12357.1|CBM20|GH15	APA12357.1|CBM20|GH15	6.51e-201	19	609	52	673
UPK89675.1|CBM20|GH15	UPK89675.1|CBM20|GH15	9.60e-201	39	608	67	663

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VN4_A	2VN4_A	8.08e-194	38	609	1	592	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
6FRV_A	6FRV_A	5.06e-174	65	609	49	611	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
6FHV_A	6FHV_A	1.22e-167	37	603	6	582	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
3EQA_A	3EQA_A	8.39e-153	65	488	49	467	Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]
1AGM_A	1AGM_A	7.74e-150	65	488	49	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	sp|P14804|AMYG_NEUCR	1.31e-193	38	609	36	621	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	sp|P36914|AMYG_ASPOR	7.02e-179	65	609	76	606	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
sp|P69327|AMYG_ASPAW	sp|P69327|AMYG_ASPAW	2.88e-173	34	609	22	635	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
sp|P69328|AMYG_ASPNG	sp|P69328|AMYG_ASPNG	2.88e-173	34	609	22	635	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
sp|P22832|AMYG_ASPUS	sp|P22832|AMYG_ASPUS	7.34e-170	34	609	22	634	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
0.018942	0.981030	CS pos: 24-25. Pr: 0.9385

TMHMM  Annotations     

There is no transmembrane helices in jhhlp_001539-t41_1-p1.