CAZyme Information: P174DRAFT_515722-t37_1-p1

Basic Information

• Species: Aspergillus novofumigatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus novofumigatus
• CAZyme ID: P174DRAFT_515722-t37_1-p1
• CAZy Family: GT71
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1393	MSZS01000009|CGC8	152246.60	5.9282

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=MSZS01000009:493985-498804(-)

Full Sequence      

MWISLSATLSWVYILSYFVLILSSSHAHWDHAAHHQAFISPRGEAAVLPQIQIATAHQIV
REAVAEMTKRNQARLAHPSRNNYSMKPGTKLGKHDNMAAPPPLLNITNQIARAAALVAKL
KAGGLAGRNYTKLYQRAGTFWMEGIEQKGAILADPTGQRDSTAAIQRAIDDGKQCGAACN
GATTKNAIIYFPPEHTLSTSSFVSLGVLSTDVYVNNSGDGPDGNALEWYINTARFYSQIR
NLKIDITASNPGAYMVALHYQVAQATTIKNVKIITDSAMTQQGMYAENGSRGVMLDITFT
SSNFRIYGGSQQFSVTQLTFNSCNTAVKKSIMVKNAKVGFRLYNDANGQIPGSVTIINSV
FSSTKSFAIKMAIPVNYNSDNLILFSGYYKSYVMGATYKENKRSWTNGSKDYDQEPSLLG
PSVAGLDVAPYFERPRNQYADKTAVDFVHLKDEGAAGDGSTDDTDAVQNAFNKYGDGSKI
ILVDAGTYIIKRTVTVPKNVKIIDETWSQFAASGGYFGDASKPAVMLRVGNEGEVGNVEL
QDLILTSKGPTPGVILMEWNVAAESAGSAALWDVHVRLGGATGTELMPTECPPITTGTNP
SSCQVASMLLHVTKRASGYFDNMWLWVADHMIDDPLLDDPLNNMEQLSVYSARGMLIESQ
KATWLYGTASEHSVFYQYNFNGAQNIFTTFLQTESPYYQPTPKPPAPFDQVVGTFDSDPK
YGCDGSDADGCDASWAVIMKNCQNVHIGSAGTYSWFRTYTQDCIDVHGCQKALWLLGSNY
DNNRLQHVIGTGAKNIIVSPDGTTITSAANLAVSSHPSWAHISLYELPSIGAAPKPGDGG
DDQCSNAARQYSSEYVPPGEIELWSNDGTVLNHADDTDGQQSVTIVNLTPYKFIHTAGPE
PYQFSTWQFGDVPSGRALKNNVTYDLGLKNTDKTFAVHVTTHIPDSYERRVVFDLGGMGL
GWRELGFPGERVSVALVISGSEEYGYVTSLQLNNADWMNRMYAIIKDRELRHVVVPGSHD
AGMSSITNSGWNGLGTASNTETQSLDHYNQLRVGVRYFDMRIVSIDGFASFWAAHSLDSL
IAGVNRFTTDYTGEVMVWWVRYMTNLDNGDLTQANRYWSAALANAFYDKLEGINNRCPEP
SDGGKFNRQPLHTFLDAKDGRGCVLIIIDGTLNAGIPKGRAESRIYNTTSFDRDDYWAQE
QYTQQNADKQIAHMKSIARDGGTGDSYYIMQWQCTPSALDVAIPPPTLQLIANQETNPAL
YHYGLNAISPDKFPTVILHDAVGLFHVSDLSAESYNPMMQTLAVGLNLYMVSQNCDVNGG
QNPLAQHATNTRMMLSVGGDRGAGFSTFSGVIFANGTVLETPPPDFCRTCTFNDTGSIDH
PPPTFNATSVKLR

Enzyme Prediction     

No EC number prediction in P174DRAFT_515722-t37_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH55	153	810	1.7e-163	0.9216216216216216

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
176558	PI-PLCXDc_like_2	1.33e-113	1002	1307	1	300	Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins. This subfamily corresponds to the catalytic domain present in a group of uncharacterized hypothetical proteins found in bacteria and fungi, which are similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs.
176529	PI-PLCXDc_like	5.90e-53	1002	1307	1	288	Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing and similar proteins. This family corresponds to the catalytic domain present in phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD) which are bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) sequence homologs mainly found in eukaryota. The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs and their bacterial homologs contain a single TIM-barrel type catalytic domain, X domain, which is more closely related to that of bacterial PI-PLCs. Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may be distinct from that of typical eukaryotic PI-PLCs.
403800	Pectate_lyase_3	2.24e-38	153	341	9	213	Pectate lyase superfamily protein. This family of proteins possesses a beta helical structure like Pectate lyase. This family is most closely related to glycosyl hydrolase family 28.
176500	PI-PLCc_bacteria_like	1.86e-30	1002	1283	1	259	Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar proteins. This subfamily corresponds to the catalytic domain present in bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) and their sequence homologs found in eukaryota. Bacterial PI-PLCs participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although their precise physiological function remains unclear, bacterial PI-PLCs may function as virulence factors in some pathogenic bacteria. Bacterial PI-PLCs contain a single TIM-barrel type catalytic domain. Its catalytic mechanism is based on general base and acid catalysis utilizing two well conserved histidines, and consists of two steps, a phosphotransfer and a phosphodiesterase reaction. Eukaryotic homologs in this family are named as phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD). They are distinct from the typical eukaryotic phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11), which have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, which is closely related to that of bacterial PI-PLCs. Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may be distinct from that of typical eukaryotic PI-PLCs. This family also includes a distinctly different type of eukaryotic PLC, glycosylphosphatidylinositol-specific phospholipase C (GPI-PLC), an integral membrane protein characterized in the protozoan parasite Trypanosoma brucei. T. brucei GPI-PLC hydrolyzes the GPI-anchor on the variant specific glycoprotein (VSG), releasing dimyristyl glycerol (DMG), which may facilitate the evasion of the protozoan to the host's immune system. It does not require Ca2+ for its activity and is more closely related to bacterial PI-PLCs, but not mammalian PI-PLCs.
176555	PI-PLCXD1c	1.06e-08	1001	1077	1	94	Catalytic domain of phosphatidylinositol-specific phospholipase C, X domain containing 1. This subfamily corresponds to the catalytic domain present in a group of phosphatidylinositol-specific phospholipase C X domain containing 1 (PI-PLCXD1), 2 (PI-PLCXD2) and 3 (PI-PLCXD3), which are bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) sequence homologs found in vertebrates. The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, members in this group contain a single TIM-barrel type catalytic domain, X domain, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UNI16537.1|GH55	7.25e-307	53	834	61	909
BCS22830.1|GH55	1.16e-300	53	834	62	892
EAA60060.1|GH55	5.87e-295	50	831	59	898
QSS51941.1|GH55	2.96e-260	50	1320	63	1443
QPH06534.1|GH55	3.33e-228	52	825	450	1296

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5M5Z_A	2.76e-114	157	810	40	741	Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila],5M60_A Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila]
3EQN_A	2.68e-102	140	781	26	716	Chain A, Glucan 1,3-beta-glucosidase [Phanerodontia chrysosporium],3EQN_B Chain B, Glucan 1,3-beta-glucosidase [Phanerodontia chrysosporium],3EQO_A Chain A, Glucan 1,3-beta-glucosidase [Phanerodontia chrysosporium],3EQO_B Chain B, Glucan 1,3-beta-glucosidase [Phanerodontia chrysosporium]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4B0V1|E13B_ARTBC	3.78e-107	122	770	25	824	Probable glucan endo-1,3-beta-glucosidase ARB_02077 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02077 PE=1 SV=1
sp|P49426|EXG1_COCCA	2.24e-85	157	763	82	721	Glucan 1,3-beta-glucosidase OS=Cochliobolus carbonum OX=5017 GN=EXG1 PE=1 SV=1
sp|P53626|E13B_TRIHA	2.36e-37	235	825	159	760	Glucan endo-1,3-beta-glucosidase BGN13.1 OS=Trichoderma harzianum OX=5544 GN=bgn13.1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000282	0.999726	CS pos: 27-28. Pr: 0.9729

TMHMM  Annotations     

Start	End
7	29