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CAZyme Information: HCEG_02398-t36_1-p1
You are here: Home > Sequence: HCEG_02398-t36_1-p1
Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Histoplasma capsulatum | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Histoplasma; Histoplasma capsulatum | |||||||||||
| CAZyme ID | HCEG_02398-t36_1-p1 | |||||||||||
| CAZy Family | CE4 | |||||||||||
| CAZyme Description | glucoamylase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 2479370; End:2484677 Strand: - | |||||||||||
Full Sequence Download help
| MDYVMPLTKA LLANIGAEGA KVKGAVAGIV VASPSKEDPD YFYTWTRDAS LVFKGLVDAF | 60 |
| ISGDTSLQSK IHEFISAQAH LQTISNPSGG LSSGGLGEPK FDVNMSSFNG NWGRPQRDGP | 120 |
| ALRATAMISY GKWLIANGYA NTARMIVWPV VQNDLSYVAQ FWSSPGFDLW EEVDGMSFFT | 180 |
| TAVQHRALVE GSRFARQIGL RCPSCESQAP QVLCFMQNYW TGSYINSNTG GDRSGKDTNS | 240 |
| ILASIHTFDP EASCDDLTFQ PCSAKSLANH KVVTDSFRSI YPLNHGVSAG SAVAVGRYPE | 300 |
| DVYFGGNPWY LSTFAAAEQL YDAIYQWQRL GSILVTDVSI HFFKDIYASA VVGTYPSSST | 360 |
| TFKSIIEAVR DYADGYLAVA QKYTPVSGEL AEQFSRDDGT PLSASDLTWS YASFLTAVSR | 420 |
| RNSSVPDPWG QTAASSIPST CQITSATGPY RTATNTKWPS DLTSISRTTS FSNGLTETKI | 480 |
| TTTSTTTSTS PCVTPDSIRV TFNEVATTTP GQRIFIIGSV PELGSWDVLS AIALSADQYT | 540 |
| DDNRLWHRTI QLGAGLDFEY KYIRLSMRTE ANAIMQKPAC LRISCFCEKH SSQMPHRMSW | 600 |
| SAVSTPFQKW EILCHKWMML PVPMSWAKHS VTAFSVPKCR PLRGCLEHET EVSPPTRRLL | 660 |
| ILALQDDKAR CIHFSRIAWR LVDIASVNYL QTTMSFSDSL PVSDTSQELF GSAEWLLSPP | 720 |
| AFVAQKGDHG PAQVTFPPPG AESETGFRTR QRVSLACLPC RNRHVKCDSG LPICSRCKFD | 780 |
| GRQCKYMQSR RGGHNKIVSS DTRAPVTQSP TRGSEFSHRS SGDRTSTRVG DSDSAGMVET | 840 |
| GTSSESAATT GSASLDRPFE CYYTFFHESH PMVLPKQHFT ARLDVDPESL EVVAAIMRYI | 900 |
| GSLYGHCPSP EFFKSLSESL LFCNQLPRNG FSVQALMLYS IATHWNNDKP RAREILDVAT | 960 |
| TMALEIGMNS CQFAYQHGEG NLVLEETWRR TWWLLYIVDS LYAGIRHSPG FALWSVNSNV | 1020 |
| DLPCEEEDFH SGNIPKPKTL VEFDDRQFDT VDVVFSSFAY LIDASRILGT TLAVGLDDSN | 1080 |
| PVDPEVDYAD SGLVAWSLHL PDIKRELVTN KGNVDPILFL AHMLIHTTTI YLHRPRSKLL | 1140 |
| YNNAENISKC APPPPPERLT HAAQEAYQMH TVKVLTASEK ISSLLALPTP LVKQSQFIIC | 1200 |
| MVALSTIAQL SACIFDTNID TSRAIKERIR LNIGALKAHE KIWPLGRKTL YEVKLIARQV | 1260 |
| FALPNLDCQA ISDLMDQAHE ISNHSGNSVM IDESFPTAIF GDSCFLSPVP PPL | 1313 |
Enzyme Prediction help
| EC | 3.2.1.3:94 | 1.14.99.55:4 |
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CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH15 | 12 | 418 | 9.9e-78 | 0.9833795013850416 |
| CBM20 | 498 | 567 | 6.5e-17 | 0.7222222222222222 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 395586 | Glyco_hydro_15 | 3.00e-133 | 9 | 417 | 5 | 415 | Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits. |
| 99886 | CBM20_glucoamylase | 6.43e-35 | 492 | 564 | 1 | 73 | Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Glucoamylases are inverting, exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1,4-glycosidic bonds but also have some activity towards 1,6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications, where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain, a C-terminal CBM20 domain, and a highly O-glycosylated linker region that connects the two. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch. |
| 213391 | fungal_TF_MHR | 4.03e-33 | 859 | 1253 | 10 | 401 | fungal transcription factor regulatory middle homology region. This domain is present in the large family of fungal zinc cluster transcription factors that contain an N-terminal GAL4-like C6 zinc binuclear cluster DNA-binding domain. Examples of members of this large fungal group are the following Saccharomyces cerevisiae transcription factors, GAL4, STB5, DAL81, CAT8, RDR1, HAL9, PUT3, PPR1, ASG1, RSF2, PIP2, as well as the C-terminal domain of the Cep3, a subunit of the yeast centromere-binding factor 3. It has been suggested that this region plays a regulatory role. |
| 395557 | CBM_20 | 4.44e-24 | 498 | 566 | 1 | 68 | Starch binding domain. |
| 99883 | CBM20_alpha_amylase | 1.38e-18 | 500 | 564 | 3 | 63 | Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QSS49369.1|CBM20|GH15 | 0.0 | 9 | 564 | 56 | 611 |
| QSS67842.1|CBM20|GH15 | 0.0 | 9 | 564 | 56 | 611 |
| QSS60609.1|CBM20|GH15 | 3.36e-310 | 9 | 564 | 99 | 582 |
| CAC28076.1|CBM20|GH15|3.2.1.3 | 6.46e-248 | 11 | 564 | 47 | 583 |
| ABH92242.1|CBM20|GH15|3.2.1.3 | 6.46e-248 | 11 | 564 | 47 | 583 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6FRV_A | 3.48e-222 | 10 | 565 | 17 | 582 | Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger] |
| 1AGM_A | 3.56e-208 | 10 | 460 | 17 | 467 | Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. x100 to 2.4 angstroms resolution [Aspergillus awamori],1DOG_A REFINED STRUCTURE FOR THE COMPLEX OF 1-DEOXYNOJIRIMYCIN WITH GLUCOAMYLASE FROM (ASPERGILLUS AWAMORI) VAR. X100 TO 2.4 ANGSTROMS RESOLUTION [Aspergillus awamori],1GLM_A REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 [Aspergillus awamori],3GLY_A REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 [Aspergillus awamori] |
| 1GAH_A | 3.69e-208 | 10 | 460 | 17 | 467 | GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE [Aspergillus awamori] |
| 1GAI_A | 3.83e-208 | 10 | 460 | 17 | 467 | GLUCOAMYLASE-471 COMPLEXED WITH D-GLUCO-DIHYDROACARBOSE [Aspergillus awamori] |
| 3EQA_A | 6.12e-206 | 10 | 460 | 17 | 468 | Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| sp|P36914|AMYG_ASPOR | 8.88e-237 | 9 | 565 | 43 | 579 | Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2 |
| sp|P0DN29|AMYG_ARTBC | 2.18e-227 | 9 | 564 | 40 | 576 | Glucoamylase ARB_02327-1 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02327-1 PE=1 SV=1 |
| sp|P22832|AMYG_ASPUS | 2.38e-226 | 10 | 565 | 41 | 605 | Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1 |
| sp|P23176|AMYG_ASPKA | 2.30e-223 | 10 | 565 | 41 | 605 | Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1 |
| sp|P69327|AMYG_ASPAW | 4.12e-221 | 10 | 565 | 41 | 606 | Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 1.000040 | 0.000000 |