CAZyme Information: EQL30641.1

Basic Information

• Species: Blastomyces dermatitidis
• Lineage: Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Blastomyces; Blastomyces dermatitidis
• CAZyme ID: EQL30641.1
• CAZy Family: GH13
• CAZyme Description: hypothetical protein, variant

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1494		165060.70	4.9602

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_BdermatitidisATCC26199	9560	447095	380	9180

• Gene Location: location=GL538440:164784-170320(-)

Full Sequence      

MATCHHGLLQSILIWALLSLQVMASFIYPAVTDPLRSAHKHEMGDVVLETQLRLNMAIPS
RVANATRSDIDKARRIVNAAIEKASVLNKARLDHPVRNHYPWKPGFKASRRDASSGDAPP
PLLKISSEIAGASALLAEVEAVAEARDLSKTKRDYSYIDALYNRTAEKQASTFWMEDIER
KGAWPFGNDPSFQVFRNVKDYGAYGDGVHDDTDAIKRAMTDAGTCGERCNGATTKNFILY
FPSGTYLVSSTIETYFGSQLIGDANDRPIIKAASSFVGLGVLSTNHYVEGGGAGPDGNPK
EWYVTTANFYRQIRNFRIDITATNQGAYVAALHYQIAQATSLSNVDFIVSTEPGTTQQAI
FTENGSGGVMSDLTFTGGNFGIYGGNQQFTAQRLKFTNCKTAVQLIWDWGWMWKNIEITG
SATGFKLMSEDSVPRTGSIMVIDSIFRDTDTALLTFPATAEKGRGTTGITLDNVAFEEVR
NAVADNEGKVYLAGSVLSVDTWAIGPVYFDISQRDYTLGMDFTTKRESTLLADQSTSLPK
APFFERQKPQYEAIPASKFVHMKDHAKGDGVTDDTAAFQSVLSQYASSDNIIFVDAGSYI
LTDTITIPVGAKIVGEGWSQLVAFGPNFQDERNPRPLVRVGNDGDHGDVEIQDLLFTTKG
PTAGAVLVEWNIKATCSGCAGMWDSHVRIGGATGTELTSTECPAITSGVNDDGCKSGSLM
MHITRSASAYMENVWLWTADHDIDDPDLQDDNNTLIQTSVYSARGLLVESTEATWLYGTS
SEHAVYYQYNFYKAQKVFAGMIQTESPYYQPTPMPPAPFESAVGIFSGDPNYERCPHGSP
GCDASWALRIIESSEIYIAGAGLYSWFTTYTQECIATRSCQNSMIQLEGNNGRVRIHNLI
SIGATNMIISDGTQVTSEANLAVDYHPYWSQITVVDPIHNTGAQRLIKQGLHTRNEDKCS
VPPDVRVPGGRNPTDLPLVDIGGEADHGYFTLVNGSPYNWILTYNHSYQMDQWKWHDVPA
GESVQCEWQFAESFNRFDDKGEAFYTLEGTNKTFQIWARYYQDDPDNEFHLHVLYDGLET
KDVPKGTSLDYPSRGGIGDMRAINWVLTGSETEGFWSSHKPPIAWMSSILHIIGDRKLKH
VCMPGSHDAGMSKLDGHTQFSNEGNTLTQYLNVYDQLRRGSRYFDVRPAIGNGGKYLTGH
YGYIDILEIGWQGGNGESIQEIVDGINRFTAENPELIIINLDLTLDTDNGYKPFNDEQWS
KTFDLFEGVTHRRGGLQGDLSEKKMNEYIGNGQACVIIIASGGPTRPDKGIYSTRQFPRY
DSYSNTDQIDTMAADQIAKLKGNRNLVPNDGERKDIFHVFSWTLTLTRVFERTIADQSIE
LGYDPLFWRGYHSFTPFSYPSVLYMDFIGSAEQDTKTLEKTTGEVTAMAMAVNMQIASQN
CYVGGGSIEPKKPEPPVSHQPTPGSASPPLRPCLISLISATLLIPLVFFYSCIF

Enzyme Prediction     

No EC number prediction in EQL30641.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH55	165	920	4.9e-254	0.9743243243243244

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
176558	PI-PLCXDc_like_2	1.57e-107	1132	1433	3	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	2.21e-82	195	426	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	1.54e-49	1132	1433	3	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	9.99e-29	1132	1412	3	262	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	6.87e-09	1143	1258	14	119	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
QSS51941.1|GH55	0.0	1	1490	1	1481
QSS69923.1|GH55	0.0	344	1490	2	1142
QBZ61798.1|GH55	0.0	51	1449	56	1431
UKZ47543.1|GH55	0.0	57	938	59	932
UKZ74106.1|GH55	0.0	57	938	59	932

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5M5Z_A	4.45e-172	171	920	4	741	Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila],5M60_A Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila]
3EQN_A	2.51e-162	173	905	26	728	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	1.53e-162	164	912	34	853	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	4.22e-149	123	912	1	764	Glucan 1,3-beta-glucosidase OS=Cochliobolus carbonum OX=5017 GN=EXG1 PE=1 SV=1
sp|P53626|E13B_TRIHA	7.27e-48	168	918	32	743	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
0.000527	0.999440	CS pos: 24-25. Pr: 0.9683

TMHMM  Annotations     

Start	End
7	29
1474	1493