CAZyme Information: P174DRAFT_425759-t37_1-p1

Basic Information

• Species: Aspergillus novofumigatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus novofumigatus
• CAZyme ID: P174DRAFT_425759-t37_1-p1
• CAZy Family: GH17
• CAZyme Description: fibronectin type III domain protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1110	MSZS01000012|CGC3	120868.95	4.8033

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnovofumigatusIBT16806	11729	1392255	197	11532

• Gene Location: location=MSZS01000012:283634-287578(-)

Full Sequence      

MYGQLWHGLAAIATLGSCALANPLVYWDGRGNASMNYEHFMARDTADFDQSDLSFITRMA
AIGDSYSAGIGAGNRIQTDADWACSRYDHSYPYLIHNDPQLGDPAACTFQFVSCSGAVTA
DVLDKQIPQISGSQQVILLSVGGNDAELSSILNQCIFGWAALAPETVKSAKEAALKHPEF
AWAANFDWDSLGHGCEKQLARTRDIIAGNTFSRSLDSVIEAAKKKLSPDGMIYYTGYAKF
FAERSITGKIASLFQGAQKLTRANRKIMNDLVDAANAQISAAVKRAGSQVKFVDYDSWVG
HFNGRFCENGVDESTVESNTRTGLMFYELNTMDPFGTNPWKRSDKQPFEGTFEGTVNQLA
EITRLMDPDAKFSEQAFISDAGTASIASFDVKLVNSASVLGLTIPNLLPDGYGRVFHPQI
LLHELIASLVIYEMVNKNEQDHGFPAIPETLTLDSCPSYGNNNGAGDGQQIALASYVNPL
ADPVAWDRMIAYPSSKVSVLVANVLNGPDTTVNEDWAKVINRAHTSGKRILGYVRTGYLG
QSQQAFETRLGSTDLADWVSQIQTDVDLWYQLYPGKIGGIFFDEGWNDCGPDNLYADLYR
FITDATKRKHPGAFTVLNPGATMPQCFEHSADTLMTFEQSYDTYMNNYVPNPGWTPKDPR
KLWHIIYGVPEADAGKVAALALKRGAGLIHITNDLLPNPYDTLPDEAYMKAITDTIKGGG
PDVADPTPYPAGGHAAFPPGPLLVTASDYSSVSLKWDISNREPPHAYAVYRDGNEVARLP
GTMSRVTIGNISPGSSMSFTVRAIGTDGKETGDSNSVAATTQSLPNNQAVTNVRVSKSAT
STTIQADFLVPYAFMRVYLTDPDTHCQMPAWPINFNAGNFICTHYMVENEVLYEYSGANL
TEGQTNYPWAWSSKGAAPVKRDGYTFTWTLPVGTDTTDSSYFSVQAQGYGPLTNVFHPCP
SEWHDSTAGAGAFCTGSSPYDCKGETLCSTTNVKWCDKAVNQMNRGQTIYTSNAEALALS
GNCWANNAGFGCSVKIRGTDQNGNNCKITGDEMWEAYQDIRNIGGCGKCGTKHFGNGCMV
SVDYYYGCDNRDKGVQLMADFAETNLTDSM

Enzyme Prediction     

No EC number prediction in P174DRAFT_425759-t37_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH135	473	704	2.6e-21	0.9493670886075949

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
403383	Spherulin4	5.05e-48	476	712	1	238	Spherulation-specific family 4. This protein is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 250 and 398 amino acids in length. There is a conserved NPG sequence motif and there are two completely conserved G residues that may be functionally important. Starvation will often induce spherulation - the production of spores - and this process may involve DNA-methylation. Changes in the methylation of spherulin4 are associated with the formation of spherules, but these changes are probably transient. Methylation of the gene accompanies its transcriptional activation, and spherulin4 mRNA is only detectable in late spherulating cultures and mature spherules. It is a spherulation-specific protein.
238861	SEST_like	2.31e-34	58	310	2	224	SEST_like. A family of secreted SGNH-hydrolases similar to Streptomyces scabies esterase (SEST), a causal agent of the potato scab disease, which hydrolyzes a specific ester bond in suberin, a plant lipid. The tertiary fold of this enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxylic acid.
406036	MU117	1.87e-30	981	1088	1	104	Meiotically up-regulated gene family. This protein was identified as being up-regulated during meiosis in S.pombe. This family of proteins is found in largely in plants and fungi. Proteins in this family are typically between 128 and 920 amino acids in length.
404371	Lipase_GDSL_2	1.57e-05	61	146	1	74	GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657.
400568	ChitinaseA_N	3.55e-04	743	832	30	130	Chitinase A, N-terminal domain. This domain is found in a number of bacterial chitinases and similar viral proteins. It is organized into a fibronectin III module domain-like fold, comprising only beta strands. Its function is not known, but it may be involved in interaction with the enzyme substrate, chitin. It is separated by a hinge region from the catalytic domain (pfam00704); this hinge region is probably mobile, allowing the N-terminal domain to have different relative positions in solution.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS11365.1|GH0	0.0	1	1095	1	1114
BCR99052.1|GH0	0.0	1	1095	1	1114
UNO38501.1|CE3|GH0	3.13e-139	458	974	486	1000
CCT67685.1|CE0	1.21e-120	4	463	3	463
QGI80975.1|CE0	1.23e-120	4	463	3	463

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4HYQ_A	1.73e-15	61	280	7	176	Crystal structure of phospholipase A1 from Streptomyces albidoflavus NA297 [Streptomyces albidoflavus]
5MAL_A	3.15e-12	57	281	2	179	Crystal structure of extracelular lipase from Streptomyces rimosus at 1.7A resolution [Streptomyces rimosus],5MAL_B Crystal structure of extracelular lipase from Streptomyces rimosus at 1.7A resolution [Streptomyces rimosus]
5C5G_A	5.92e-07	466	675	5	211	Crystal Structure of Aspergillus clavatus Sph3 [Aspergillus clavatus NRRL 1]
5D6T_A	6.96e-07	466	675	23	229	Crystal Structure of Aspergillus clavatus Sph3 in complex with GalNAc [Aspergillus clavatus NRRL 1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9S2A5|LIP1_STRCO	7.63e-13	61	282	40	213	Lipase 1 OS=Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) OX=100226 GN=SCO1725 PE=1 SV=1
sp|Q93MW7|LIP_STRRM	2.71e-11	57	281	36	213	Lipase OS=Streptomyces rimosus OX=1927 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000291	0.999669	CS pos: 21-22. Pr: 0.9709

TMHMM  Annotations     

Start	End
5	27