CAZyme Information: HCAG_07222-t26_1-p1

Basic Information

• Species: Histoplasma capsulatum
• Lineage: Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Histoplasma; Histoplasma capsulatum
• CAZyme ID: HCAG_07222-t26_1-p1
• CAZy Family: GT20
• CAZyme Description: predicted protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
825		91121.68	4.9179

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_HcapsulatumNAm1	9402	339724	89	9313

• Gene Location: location=CH476662:818081-821759(-)

Full Sequence      

MTGEGTYLVSSTIDVYFGSQLIGNANDRPVIKAASSFIGLGVLSTNRYVENGGAGPDGNA
KEWYVTTIRNFRIDITATSRDAYVAALHYQVAQATSLMNVDFIASTDPGTTQQAIFTENG
SGGAISDLTFTGGNFGIYGGNQQFTAQRLKFNNCKTAVQIIWDWGWIWKNIEVTESTTGF
KLMSEDSVPRTGSILVLDSIFRNTETALLTFPASQEKGKGTTGITFDNVAFEAVKYAVVD
NQGKVYLCWERSKSRYMGSWTGMSFSTKREPTLVTDGSTFLPKAPFFERAKPQYEAIPAS
NSSWKPCDRGDVEIQDLLFTTKGPTAGAVLVEWNIKATCSGCASMWDSHVRIGGATGSEL
TSTECPAITSGVNGDGCKSGSLMMHITDSSSAYMENVWLWTADHDIDDPDWQDNNNTLVQ
TSIYTARGLLVESTEATWLYGTSSEHALYYQYNFYKAQNVFAGMIQTESPYYQPTPNPPA
PFESAVGIFSGDPAYQNCHCGSPGNDAAWALRIIESSEIYIAGAGLYSWFSTYTQECIKT
RSCQNSLIQLEGNGGDVRIFNLITIGATNMITSDGNQLTSQDNLAVDYHPYWSQITIIDP
IQKTGPQRLIKQGLHARNEDKCPPVLPEAILPEGKYPTNLSIIDIGGHSDHGYFTLVNGS
PYNWILTSSHSYQMDQWKWHNVPAGESVQCEWQFAQSFNRYDDKGEAYYKIEGTDKTFQI
MARYQDDPNNNFHLRVLYDGLETKDVPKGTSLDFPSRGGLGDMRAMNWVLAGSEEQGYWS
SHKPPIAWMSSILTVIGERKLKHVCMPGSHDAGMSKLNGHTEFFK

Enzyme Prediction     

EC	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH55	307	583	4.3e-97	0.3554054054054054
GH55	4	301	5.8e-71	0.39864864864864863

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
403800	Pectate_lyase_3	5.64e-56	5	181	42	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.
176558	PI-PLCXDc_like_2	2.52e-08	795	821	3	29	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	2.62e-05	796	824	4	32	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSS51941.1|GH55	0.0	4	823	240	1157
QSS69923.1|GH55	0.0	98	823	1	818
UKZ74106.1|GH55	8.57e-217	5	601	243	932
UKZ47543.1|GH55	5.31e-216	5	601	243	932
QPH06534.1|GH55	1.00e-202	5	597	614	1295

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5M5Z_A	1.26e-111	5	576	77	734	Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila],5M60_A Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila]
3EQN_A	4.36e-94	5	583	98	743	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	3.70e-94	5	581	115	859	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	1.61e-87	4	586	119	776	Glucan 1,3-beta-glucosidase OS=Cochliobolus carbonum OX=5017 GN=EXG1 PE=1 SV=1
sp|P53626|E13B_TRIHA	7.64e-20	308	590	479	752	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 OTHER

Other	SP_Sec_SPI	CS Position
0.998601	0.001417

TMHMM  Annotations     

There is no transmembrane helices in HCAG_07222-t26_1-p1.