CAZyme Information: HCEG_04575-t36_1-p1

Basic Information

• Species: Histoplasma capsulatum
• Lineage: Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Histoplasma; Histoplasma capsulatum
• CAZyme ID: HCEG_04575-t36_1-p1
• CAZy Family: GH31
• CAZyme Description: exo-beta-1,3-glucanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2041		224026.72	5.2254

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_HcapsulatumH88	9666	544711	221	9445

• Gene Location: location=DS990638:5574345-5583610(-)

Full Sequence      

MRLGINHIDKEEFLTLYPAAHMEALNENNIKGGFKATGWVPYNPEQVLSHLNTQMHTSSP
PGTSHSSQASWATVTPHNHLDVVYMVPAYVGTSGEDKNWIACIPDERHPTLHTWWTTNTT
TSRLHQTKQPLAGADYKFYRDVVEYGADNTGEKDATEAINAAIGDGDRCGLECGNTFAKG
AIIYFPPGIYKICRPIIQLYYTQFIGDALDPPTIKGCDTFQGIALFDTDPYVPNGNGQNW
YINQNQFFRQIRNFIFDLTEMPLSTADHDQPLVPTGIHWQVSQACSLQNLIFNMPKATDS
NKVTHVGIFMENGSGGFVSDLVFNGGNIGWRAGSQQYTAMNLKFNGCLTAVQMIWDWGFN
WQRIEVDGGAIAFNISGRGGDTGQGVGSVSIIGMFKIHSNVHMNSVGTTVKSEDGDVILD
GTNHVGLWAMGRRYDGYNGTYISGEVDAPQKGKRLLDEDGKLFYRPRPQYKDLKVDEFLI
ATEHDCKNDGTGDNAGDINAFLEKTKKEGKIAYFPAGVYRVGGTVFIPTGSRVQGASWSQ
IQGAGFYFNDIHNPRVLVQIGEKGDVGDMEIVDMMFTAQGATAGAILVEWNVHENSQGSA
AMWDSHVRVGGAFGTDLDIETCPKFEFSDACICASLLFHVTPQASGYFENVWIWLADHDN
DMSVYDSPDKIANQISLYAARGTLIESEGPSWFYGTGSEHTVMYQYQVYGARDIYLGHIQ
TETPYYQPVPIAPLPFSSAKEFPGDPSFEKCKTTGCSAAWGLRIINSEGITLHSSGLYSF
FQEYYQDCVPTHNCQKHILEVKGSKDVALFNTFTVGIVEIGTGINHGAIFQNDSNQSGFT
TEVSIWIPLEGDDEYDIVYVGSEVYDKPSLTCPADCILVFPTSSLSSKTTIDPGKYTTSV
EYGHHSTTIIGGREVPTFYTTVTTITLTIDPITTDGMPYSNINITEGQTSTPLTVLPSVD
IPPIPVPIPDGEGKTTRNITVPPWPAITRGPPESWSNPDASPTDGTKEGVYHTPFVTTVV
ATKPTVSTLSFPSTTTTRPLPVWSTWPPRVVTPIEEEIKKPEPGKTPCKLWFFSFCLNRE
EGETKGLRWNLPPGIYPPGPPPPRAIDLPPSWTIKSPLPPWPPITMGQDRILTYPKEEPT
KCEKKSASVCTTTVFKTTISRGTITSTATSISSRCDTVYGCSASDWDTTTTSTKPSNCPS
SPTARPTGRPPTPPPGCPANALVYPFNMDNVGNIHQILAKYKDKYLEPDVADAFYYERRP
DYGGIRDTKSNGLARANGISNPIEVLNPRSQEGVDHLNSTVVVQDNGDADPMAPDPTTRT
SPYTWDLSQISMPRGLIWRASDSGTVDHNGWYMFHYDRIAGLDQYIYLMDEDKVEEIHPE
MSYHHDIEYLRPDDRYLWVGPIQPNVRHGTGVASKVLGRNLGSCQLCKLIVASLFEGFET
QDESIVTARYLDLLRNIIDDVITKGRMGKAVVNFSHNFEPGVVDMVFIHEFHRLLVELDS
LKVAIVVASGNLASTTPDIDGYPALFGLPGNQYYIPNIIVVGSTDVHGHMSDFSQYADWM
TTFAPGDDVWIPLGNKDYDMTAGTSYSAPFVSGLIGYFRSLQSPWINQLQDPASVKKMIK
IFHRRITVMDGTVVEPTDVKKMKPIIWNGQWGDYSCLSDYRTVDTWDPHGICPRIKLDLA
DETNEGETVAPCDDDFTLFDNSQKQLDGTYCPRLPKAGAGSHTVSFTSKAGVKPTPTCAS
GTGCGGHLCTGFFCSPMPTGVPPDRHDPKDPNASSQVPTTTIGQPTTTKPGNPEPTCNDK
CKLDKGNPCKCNENGCDSESPGCCGNASCPMCECGDNSCSPSSPACCKTETCQWSWTGGG
GGDGSGKPPGPRIGSLLFALDETYRSHPGGDVLTRFWKVFVSELNREADVCNDTPLKLVD
ASSDPENRPHYPPSMEFTVGRGQKCKYTGDSNGAGILKCDGSKHSPCKARGLDDKKTCLV
PLPGSTPSTYYLAVDCKSRLRVAKYEQGLGKEMKTLTQQDSKRRCGFVNLLKMKLNEWLP
G

Enzyme Prediction     

No EC number prediction in HCEG_04575-t36_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH55	112	846	3.8e-227	0.9824324324324324

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
403800	Pectate_lyase_3	1.05e-74	139	374	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.
173787	Peptidases_S8_S53	8.38e-19	1378	1620	14	239	Peptidase domain in the S8 and S53 families. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) family include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.
173790	Peptidases_S8_PCSK9_ProteinaseK_like	1.56e-12	1503	1620	147	250	Peptidase S8 family domain in ProteinaseK-like proteins. The peptidase S8 or Subtilase clan of proteases have a Asp/His/Ser catalytic triad that is not homologous to trypsin. This CD contains several members of this clan including: PCSK9 (Proprotein convertase subtilisin/kexin type 9), Proteinase_K, Proteinase_T, and other subtilisin-like serine proteases. PCSK9 posttranslationally regulates hepatic low-density lipoprotein receptors (LDLRs) by binding to LDLRs on the cell surface, leading to their degradation. The binding site of PCSK9 has been localized to the epidermal growth factor-like repeat A (EGF-A) domain of the LDLR. Characterized Proteinases K are secreted endopeptidases with a high degree of sequence conservation. Proteinases K are not substrate-specific and function in a wide variety of species in different pathways. It can hydrolyze keratin and other proteins with subtilisin-like specificity. The number of calcium-binding motifs found in these differ. Proteinase T is a novel proteinase from the fungus Tritirachium album Limber. The amino acid sequence of proteinase T as deduced from the nucleotide sequence is about 56% identical to that of proteinase K.
173810	Peptidases_S8_Thermitase_like	2.32e-12	1503	1608	154	246	Peptidase S8 family domain in Thermitase-like proteins. Thermitase is a non-specific, trypsin-related serine protease with a very high specific activity. It contains a subtilisin like domain. The tertiary structure of thermitase is similar to that of subtilisin BPN'. It contains a Asp/His/Ser catalytic triad. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53 the it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.
173799	Peptidases_S8_Subtilisin_like	5.19e-12	1503	1619	149	254	Peptidase S8 family domain in Subtilisin-like proteins. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSS48832.1|GH55	0.0	125	1997	42	2044
QSS50317.1|GH55	0.0	125	1475	74	1547
QSS62360.1|GH55	0.0	403	1997	1	1568
QSS52973.1|GH55	0.0	125	1098	115	1190
VBB73332.1|GH55	0.0	129	1859	106	2022

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5M5Z_A	7.15e-167	114	844	6	751	Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila],5M60_A Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila]
3EQN_A	5.55e-160	136	846	46	755	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]
1DBI_A	8.28e-06	1454	1600	113	241	Crystal Structure Of A Thermostable Serine Protease [Bacillus sp. Ak1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4B0V1|E13B_ARTBC	3.01e-160	103	846	28	873	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	1.14e-132	135	817	66	756	Glucan 1,3-beta-glucosidase OS=Cochliobolus carbonum OX=5017 GN=EXG1 PE=1 SV=1
sp|P53626|E13B_TRIHA	5.02e-47	135	798	60	708	Glucan endo-1,3-beta-glucosidase BGN13.1 OS=Trichoderma harzianum OX=5544 GN=bgn13.1 PE=1 SV=1
sp|Q9Y778|SMP1_MAGPO	2.10e-15	1325	1632	109	391	Subtilisin-like proteinase Mp1 OS=Magnaporthiopsis poae OX=148304 PE=1 SV=1
sp|A1CIA7|ORYZ_ASPCL	3.62e-13	1325	1619	118	378	Alkaline protease 1 OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=alp1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000075	0.000000

TMHMM  Annotations     

There is no transmembrane helices in HCEG_04575-t36_1-p1.