CAZyme Information: P174DRAFT_463658-t37_1-p1

Basic Information

• Species: Aspergillus novofumigatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus novofumigatus
• CAZyme ID: P174DRAFT_463658-t37_1-p1
• CAZy Family: GH76
• CAZyme Description: putative oligoxyloglucan-reducing end-specific xyloglucanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
815	MSZS01000008|CGC5	87644.83	6.0358

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=MSZS01000008:806115-808562(+)

Full Sequence      

MKYWLQQLGLTVLCALSAAARTAEHAYEFKSVAITGGGYITGIVGHPTEKNLLYARTDIG
STYRWEQGLNKWIPLTDFLGPEDENLLGTESVAMDPTDPNRLYLAQGRYLSSNNSAFFVS
DDRGATFTRYRAPFPMGANELGRNNGERLAVNPFKPNELWMGTRNAGLMRSSDRAKTWTN
VTNFPDAAANGIGITFVIFDPKHEGAIYVGASIPGGLYYTTDGGENWKSLPGQPMQWDPS
LLVYPNETQPQSAGPQPMKAVLASNGVLYVTYADYPGPWGVAYGAVHVYNTTASTWMDIT
PNANNTSPKPYTPQAFPAGGYCGLSVAADDPDTVVVVSLDRDPGPALDSMYLSRDGGKSW
KDVSQLSTPPGSGGYWGHPIAEAALANGTKVPWLSFNWGPQWGGYGAPSPVKGLTKVGWW
MTAVLIDPSNPDHVLYGTGATIWATDTIAQADKNSTPKWYIQAQGIEETVTLAMISPREG
AHLLSGAGDINGFRHDDLDTPQPMFGLPVFSNLNTLDWAGQRPEVIVRGGPCGHQYPDGC
GQAAYSTDGGSEWTKFQTCIKGVNTSSTNPGVMAIDASGKYVVWTSAMYVVSPSVQAVTP
AANDSGPYASNDWGKTWASPRGLTVQTPYISADRVQPKTFYAFSGGVWYVSTDGGLSYDA
FNATKLGLPAHTGAVPVVSVDRAGEIWLALGSNGVYHTTDFGKRWKRITHKGTVADLITV
GAATHGSKKPALFIRGSQGDPKKSNYGIYRSDDNGSTWDRVDDDTHRYGGFNLIQGDPRV
YGRVYLGTGGRGLLYADIVPERSDKEGNVLGTGGI

Enzyme Prediction     

EC	3.2.1.151:27	3.2.1.150:4	3.2.1.151:5

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH74	82	189	2.5e-18	0.463519313304721

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
271234	Sialidase_non-viral	3.88e-09	545	758	51	293	Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
406353	Sortilin-Vps10	3.91e-06	115	230	1	112	Sortilin, neurotensin receptor 3,. Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1.
406353	Sortilin-Vps10	6.18e-06	72	230	13	164	Sortilin, neurotensin receptor 3,. Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1.
406353	Sortilin-Vps10	9.37e-06	608	764	4	167	Sortilin, neurotensin receptor 3,. Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1.
405545	PSII_BNR	8.23e-05	18	228	55	268	Photosynthesis system II assembly factor YCF48. YCF48 is one of several assembly factors of the photosynthesis system II. The photosynthesis system II occurs in Cyanobacteria that are Gram-negative bacteria performing oxygenic photosynthesis. One of the three membranes surrounding these bacteria is the inner thylakoid membrane (TM) system that is localized within the cell and houses the large pigment-protein complexes of the photosynthetic electron transfer chain, i.e. Photosystem (PS) II, PSI, the cytochrome b6f complex, and the ATP synthase. YCF48 is necessary for efficient assembly and repair of the PSII. YCF48 is found predominantly in the thykaloid membrane. It is a BNR repeat protein.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBG67009.1|GH74	0.0	1	815	1	815
EAA64249.1|GH74|3.2.1.150	0.0	18	798	26	808
BCS21231.1|GH74	0.0	8	798	8	796
BAC22065.1|GH74|3.2.1.150	7.39e-316	9	806	10	793
CAF02212.1|GH74|3.2.1.150	7.39e-316	9	806	10	793

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1SQJ_A	4.26e-315	24	806	2	770	Crystal Structure Analysis of Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH) [Geotrichum sp. M128],1SQJ_B Crystal Structure Analysis of Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH) [Geotrichum sp. M128]
2EBS_A	2.44e-314	24	806	2	770	Chain A, Oligoxyloglucan reducing end-specific cellobiohydrolase [Geotrichum sp. M128],2EBS_B Chain B, Oligoxyloglucan reducing end-specific cellobiohydrolase [Geotrichum sp. M128]
3A0F_A	2.72e-240	28	796	11	758	The crystal structure of Geotrichum sp. M128 xyloglucanase [Geotrichum sp. M128]
4LGN_A	2.01e-133	27	806	7	743	The structure of Acidothermus cellulolyticus family 74 glycoside hydrolase [Acidothermus cellulolyticus 11B]
7KN8_A	6.02e-133	27	797	10	713	Chain A, Cellulase [Xanthomonas campestris pv. campestris str. ATCC 33913],7KN8_B Chain B, Cellulase [Xanthomonas campestris pv. campestris str. ATCC 33913]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A1DAU0|XGCA_NEOFI	0.0	1	815	1	815	Probable oligoxyloglucan-reducing end-specific xyloglucanase OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=xgcA PE=3 SV=1
sp|Q5BD38|XGCA_EMENI	0.0	18	798	26	808	Oligoxyloglucan-reducing end-specific xyloglucanase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=xgcA PE=1 SV=1
sp|Q8J0D2|CBHRE_GEOS1	1.31e-316	9	806	10	793	Oligoxyloglucan reducing end-specific cellobiohydrolase OS=Geotrichum sp. (strain M128) OX=203496 PE=1 SV=1
sp|Q3MUH7|XG74_PAESP	8.05e-146	2	815	8	783	Xyloglucanase OS=Paenibacillus sp. OX=58172 GN=xeg74 PE=1 SV=1
sp|A3DFA0|XG74_ACET2	1.46e-123	15	797	27	757	Xyloglucanase Xgh74A OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=xghA PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000357	0.999620	CS pos: 20-21. Pr: 0.9730

TMHMM  Annotations     

There is no transmembrane helices in P174DRAFT_463658-t37_1-p1.