CAZyme Information: KLU87058.1

Basic Information

• Species: Magnaporthiopsis poae
• Lineage: Ascomycota; Sordariomycetes; ; Magnaporthaceae; Magnaporthiopsis; Magnaporthiopsis poae
• CAZyme ID: KLU87058.1
• CAZy Family: GH2
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1425	GL876970|CGC15	156325.18	5.0609

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_MpoaeATCC64411	12363	644358	200	12163

• Gene Location: location=GL876970:557873-562588(+)

Full Sequence      

MAVLNKARLDKPFRNRYKQSSASRTAKRTDTVDAPLPLLNITEEIASAAALIAEAEALSS
NDTGLLNSTASLNRRASPFWMEGLARKGTVPWGNDPNYKVFRNVVTHYQADPTGQRDSTA
AIQKAIDDGKRCGEKCNGSTTKNAIVYLPPGRYLVSSTLKLNFGTQLIGDANDWPRIVAS
SSFVGLGVLSTDIYTENGGNGPDGNPLQWYINTARFYSQIRNLRVDITATDPEAYICAVH
YQVAQATTIENVELIAKTGTTQQGMFAENGSGGVMSDITFTGGNFGFYGGSQQFSASRMT
FNGCKTAAQIIWDWGWVWKGVSVNDVEVGFRLISDDGSGAIGSVSFVDSSFTNIKMAAIY
TATPTDKPGSGVTGLILDNVYLEASILNPVGKRILGRGYYKTFIIGPTYTNNKRTFLNGQ
PMDYTREKSLLAASPGSLRGLQVAPYFDRPRNQYLDKSSADFVHLKDGGAKGDGSTDDTK
AVQDFFNQYGDGSKIIFVDAGTYILTDTVTIPKDAKIVGETWSQFAASGSRFADLNSPRV
MLKVGNDGDVGTVEMQDLILTTKGGTAGAVLMEWNVKASSAGAAALWDVHARVGGATGTD
LTPAECPPITSGTNPSRCQAASMLLHITKKASGYFDNMWLWVADHIIDDPLLEDPMNNME
QISVYSARGVLIESQTATWLYGTSSEHNVFYQYNFHQARNIYTTMIQTESPYYQPTPKPP
APFESAVGNFVGDPNYDCRGGDFDGCDESWAVIMTGSQEVHIGAAGTYSWFSTYSQDCID
SQTCQKALWLIDNNYDNNRIDHIIGIGAKNVMVSGGEAITAADNLSVSKHPSWSQISVFE
VDSKGQAPDENQCLPSDEMFSKETMPSGNSMPWHLMGPENAAASTKYYVTIVNLTPYRFV
KDRQHSYQFDVFDFGDVPSGKSRQNTLVYTTDVKANPVDDNGEAYYSIQGTDKKFTIRGT
THIPDNYPKRAVIDLTGMGQPQREYGFPEQEVPVTLVITGSEEYGYITSVVFGPDNWMHQ
LYDVIKDRELRHLVMPGSHDAGMSTISYAWDGAGTPGNSQNQGLNIYDQLRVGSRWFDMR
LVSVKGGGFWAAHVNDEVANVPVGATGESLDDIIAGINRFTSESPGEIIIWWVKYMVDLN
LNVPAGTGRRWSEQKANEFYTALEKINNRCPDLGNNVKFDRLKAQTLLDKNNGAGCVLIM
TDGRLDQGITPDRPSSGIYRGRQYMDRDDYWAEKTNEVDNSAAQVSHMEKITRSGDNGDS
FYIMQWQPTPDIYSSTFLYGLQRIALMPTNPALYWRALNSMKPNIWPTVIMQDYIGLLHL
NEVGFPDQLGAEIRVLCIGLNLYMVSQNCKVSKTKHPLLQRGSMMSIFGEPDQSKDVIYA
NGTVVNQVPAGFHLGRAPVLKAGTSFGNGTILAVDTLNPDFGAEL

Enzyme Prediction     

No EC number prediction in KLU87058.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH55	70	824	8.7e-237	0.977027027027027

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
176558	PI-PLCXDc_like_2	3.50e-95	1022	1341	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	5.04e-74	101	331	1	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.
176529	PI-PLCXDc_like	2.88e-43	1022	1341	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.
176500	PI-PLCc_bacteria_like	1.64e-30	1022	1316	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.
176557	PI-PLCXDc_like_1	5.75e-11	1026	1315	5	266	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UNI16537.1|GH55	0.0	1	848	75	909
EAA60060.1|GH55	0.0	1	846	76	899
BCS22830.1|GH55	0.0	1	848	76	892
QSS51941.1|GH55	0.0	2	1351	81	1440
UKZ84316.1|GH55	4.01e-311	4	845	433	1274

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5M5Z_A	8.76e-155	77	824	4	742	Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila],5M60_A Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila]
3EQN_A	1.93e-151	53	796	2	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	4.03e-151	73	819	37	856	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	1.88e-124	62	778	31	721	Glucan 1,3-beta-glucosidase OS=Cochliobolus carbonum OX=5017 GN=EXG1 PE=1 SV=1
sp|P53626|E13B_TRIHA	5.08e-45	68	790	26	711	Glucan endo-1,3-beta-glucosidase BGN13.1 OS=Trichoderma harzianum OX=5544 GN=bgn13.1 PE=1 SV=1
sp|Q55DH0|Y1320_DICDI	9.21e-06	994	1119	213	351	PI-PLC X domain-containing protein DDB_G0269228 OS=Dictyostelium discoideum OX=44689 GN=DDB_G0269228 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000056	0.000001

TMHMM  Annotations     

There is no transmembrane helices in KLU87058.1.