CAZyme Information: EJT82150.1

Basic Information

• Species: Gaeumannomyces tritici
• Lineage: Ascomycota; Sordariomycetes; ; Magnaporthaceae; Gaeumannomyces; Gaeumannomyces tritici
• CAZyme ID: EJT82150.1
• CAZy Family: GT3
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1442	GL385395|CGC14	155738.79	6.5419

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GtriticiR3-111a-1	14749	644352	291	14458

Full Sequence      

MWWRRRAREPTRALRTSPLPRLLVAMLSHVSFVLAIALLCLWPYSTDALVAPRGVDAASW
NKAGRHLDSFLGPRSPRNQTELESARLLVQAAIAETSVRNKARVLHPLRNTYHADSAAAA
SAMLRERDGDGQNASFTTRMLSPAPPLLQVSDQVASAAALLAELGASGAPASATTVRRAT
TNSSSSDSSVFWMENISRKHYNSSSRQVFRNVRDFGAKGDGRTDDTVAIRRAILSASSGT
QDTEARWPGSDGVRNAVVYLPSGTYLISGTIPALPATQIIGDATNFPVLKAAPSFVGLGV
ISTNELGPGGEASQKRQHYRQIRNLIIDITEASHDAHVSGIHWQASEASSIQHVEVRAAD
PHTAPGGQTTQMGIFTEDGSGGQISDVAVRGGSVGILAGNSQFAAQRIRLSGCTTGVQLL
WDFGGVWKGIDIRESKVGFSLANGNADENNIRNYLGSVYIMDSTFTDVGTAVQNAPVSVE
PGTGTTSVTLDNVLFDRVTNRVFDGEKEYVEGRPSTLDTWTLGPIYLSLPERDLSLGYEF
QTPREPTLLAEYSVTAKNSSGTKSLPKRPFFEKSKPQYTTIPASSWVHMKDFAKGDGKTD
DTIAFQEVLNGKGYIFVDAGDYLLADTVTIHPGTFIVGEAWPKLVAFGPKFSDPRNPRPL
VKVGDEGSVGAVDLQDLLFTTRGATAGAKAIEWNIKADKNGNAGMWDCHVQVGGNSQTKE
TPAACASSSNATCQGAAVLVHITPGASAYLEGLWLRAVDRLLDAPESMENGDKKAEIQFL
SVPRGVLVESQAATWMYGVSVQHSSMYQYNFHNSQKVFVSMLQAESPSTGPESLPTQPRS
DIAVVLPGDAGTPNPRGSWATVVQGTKDVFMAGLGLYSWFSQGSTACISSQSCQDALILM
QNNTNLAIHNLVTIGAKNSIDLSDSGHVTATENLAIDAHPNWSQITVVYPIQNMADAMAC
RDPGSWPATPPNGKFRNADFNDQNRFFVSMINGSPYRLSLTRKNSYQMTEFTYADVDPGF
SPQFSMYYGPGTFVDTNGEAYYRLEGTSKSFQVHGTTNNNDSKYKLRARYVFDGMSANGV
PQGSRYELRSRGGERAVNFVLTGSEKVGYWTSVNPPVAWMNALLPIIGGRKLKHISMLGS
HNAGISFRNGGTIGPEAASLCQGLNIYGQLMAGSRWFDIRPVIGNGGQLLTGHYSGQRAP
VFGINGQALADIVDDINRFTATNPELVIVSLSHAMQTDEGYRDLNDAEWDRVFDALERLD
SRCAGLAGQIPDMTLDSLIGAGRACVVVLSDGGRARPDRGIYRPADSFDLADHWSDSDKV
ADMTADQAGWVRANRNLVSDPGARRDRFLISQHILTVKALNVLVASIEGYAVDVAYDALF
WRVFSAYTPWSFPSVLLMDYVGILYRGDRSPLPEAGEARALVMAVNVGLASRNCWLGGGS
LE

Enzyme Prediction     

No EC number prediction in EJT82150.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH55	181	931	5.5e-185	0.9743243243243244

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
176558	PI-PLCXDc_like_2	3.76e-98	1124	1426	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.
403800	Pectate_lyase_3	2.46e-59	209	439	1	212	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.
176529	PI-PLCXDc_like	9.49e-47	1125	1403	2	277	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.
176500	PI-PLCc_bacteria_like	5.30e-36	1125	1403	2	260	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.
176528	PI-PLCc_BcPLC_like	8.56e-10	1130	1320	8	177	Catalytic domain of Bacillus cereus phosphatidylinositol-specific phospholipases C and similar proteins. This subfamily corresponds to the catalytic domain present in Bacillus cereus phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) and its sequence homologs found in bacteria and 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. Their 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. This family also includes some uncharacterized eukaryotic homologs, which contains a single TIM-barrel type catalytic domain, X domain. They are similar to bacterial PI-PLCs, and distinct from typical eukaryotic PI-PLCs, which have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains, and strictly require Ca2+ for their catalytic activities. The prototype of this family is Bacillus cereus PI-PLC, which has a moderate thermal stability and is active as a monomer.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QBZ61798.1|GH55	QBZ61798.1|GH55	0.0	39	1442	11	1431
QSS51941.1|GH55	QSS51941.1|GH55	0.0	79	1441	63	1445
QSS69923.1|GH55	QSS69923.1|GH55	1.35e-299	363	1441	9	1106
EAA30159.2|GH55	EAA30159.2|GH55	1.55e-195	81	948	88	948
UKZ84316.1|GH55	UKZ84316.1|GH55	1.25e-189	81	971	415	1294

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3EQN_A	3EQN_A	2.80e-115	181	933	16	744	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]
5M5Z_A	5M5Z_A	5.77e-111	191	933	6	742	Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila],5M60_A Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila]
7CHU_A	7CHU_A	6.72e-06	211	294	76	163	Chain A, Putative pectin lyase [Geobacillus virus E2],7CHU_B Chain B, Putative pectin lyase [Geobacillus virus E2],7CHU_C Chain C, Putative pectin lyase [Geobacillus virus E2]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4B0V1|E13B_ARTBC	sp|D4B0V1|E13B_ARTBC	1.03e-108	189	933	41	862	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	sp|P49426|EXG1_COCCA	6.48e-93	160	936	6	776	Glucan 1,3-beta-glucosidase OS=Cochliobolus carbonum OX=5017 GN=EXG1 PE=1 SV=1
sp|P53626|E13B_TRIHA	sp|P53626|E13B_TRIHA	4.41e-37	219	933	70	744	Glucan endo-1,3-beta-glucosidase BGN13.1 OS=Trichoderma harzianum OX=5544 GN=bgn13.1 PE=1 SV=1
sp|Q9ZFG9|ALGE7_AZOVI	sp|Q9ZFG9|ALGE7_AZOVI	4.29e-07	211	389	4	181	Alginate lyase 7 OS=Azotobacter vinelandii OX=354 GN=algE7 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.995222	0.004787

TMHMM  Annotations     

Start	End
21	43