CAZyme Information: CTMYA2_042850.t1-p1

Basic Information

• Species: Candida tropicalis
• Lineage: Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; Candida tropicalis
• CAZyme ID: CTMYA2_042850.t1-p1
• CAZy Family: GT22
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
254		29114.52	7.4110

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CtropicalisMYA3404-2020	6136	N/A	0	6136

• Gene Location: location=CP047871:2499340-2500186(-)

Full Sequence      

MIREFIYRLFKPRQIFIIPLPIEQIIHEIVNLMPSKFDDGSLAPIFVRLAWHCCATYDVA
TNTGGSNGATMRFEPELTDDGNTGLFVAMLALSQVKVKYPMISYADLWTLAGKVAIEYMG
RPHAGHIRTTFTRLGFNDQQTVVLVGAHGVGRCHKKFSGWDGKWTHDPLVFDNEFYKVLL
SETWSQDVVPETGKVQYYNGDRSLIMLNTDMELIRDSRYRQWVEVYAKNKERFLNDFAAA
FSKLLELGVKRSCE

Enzyme Prediction     

EC	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA2	125	249	2.3e-23	0.49019607843137253
AA2	33	123	6.5e-20	0.35294117647058826

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173825	ascorbate_peroxidase	7.81e-105	22	250	13	251	Ascorbate peroxidases and cytochrome C peroxidases. Ascorbate peroxidases are a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Along with related catalase-peroxidases, ascorbate peroxidases belong to class I of the plant superfamily. Ascorbate peroxidases are found in the chloroplasts and/or cytosol of algae and plants, where they have been shown to control the concentration of lethal hydrogen peroxide molecules. The yeast cytochrome c peroxidase is a divergent member of the family; it forms a complex with cytochrome c to catalyze the reduction of hydrogen peroxide to water.
178218	PLN02608	1.90e-57	41	250	29	245	L-ascorbate peroxidase
173823	plant_peroxidase_like	3.64e-50	29	246	7	255	Heme-dependent peroxidases similar to plant peroxidases. Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX), which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions. Several sub-families can be identified. Class I includes intracellular peroxidases present in fungi, plants, archaea and bacteria, called catalase-peroxidases, that can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. Catalase-peroxidases are typically comprised of two homologous domains that probably arose via a single gene duplication event. Class II includes ligninase and other extracellular fungal peroxidases, while class III is comprised of classic extracellular plant peroxidases, like horseradish peroxidase.
178467	PLN02879	8.51e-50	43	248	34	246	L-ascorbate peroxidase
166005	PLN02364	1.13e-46	43	248	33	246	L-ascorbate peroxidase 1

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BDA47129.1|AA2	6.39e-76	23	249	89	346
QKD61761.1|AA2	1.11e-73	19	254	16	284
QNP98097.1|AA2	1.13e-73	28	248	46	296
QNP98603.1|AA2	1.78e-72	35	251	20	263
QGI94677.1|AA2	1.79e-72	19	254	16	284

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4GED_A	4.73e-64	19	250	5	260	Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex [Leishmania major]
3RIV_A	5.18e-64	19	250	6	261	The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin],3RIV_B The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin]
5AMM_A	2.85e-63	19	250	5	260	Structure of Leishmania major peroxidase D211N mutant [Leishmania major],5AMM_B Structure of Leishmania major peroxidase D211N mutant [Leishmania major]
5AL9_A	8.07e-63	19	250	5	260	Structure of Leishmania major peroxidase D211R mutant (high res) [Leishmania major],5ALA_A Structure of Leishmania major peroxidase D211R mutant (low res) [Leishmania major],5ALA_B Structure of Leishmania major peroxidase D211R mutant (low res) [Leishmania major]
3RIW_A	1.66e-62	19	250	6	261	The Crystal Structure of Leishmania major Peroxidase mutant C197T [Leishmania major strain Friedlin],3RIW_B The Crystal Structure of Leishmania major Peroxidase mutant C197T [Leishmania major strain Friedlin]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q59X94|CCPR2_CANAL	4.38e-119	23	251	31	288	Putative heme-binding peroxidase OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=CCP2 PE=3 SV=2
sp|Q6BIB1|CCPR2_DEBHA	1.77e-100	22	251	157	415	Putative heme-binding peroxidase OS=Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968) OX=284592 GN=DEHA2G12166g PE=3 SV=3
sp|Q6C7U1|CCPR3_YARLI	2.00e-74	28	248	46	296	Putative heme-binding peroxidase OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=YALI0D25366g PE=3 SV=1
sp|Q6CAB5|CCPR2_YARLI	3.17e-73	35	251	20	263	Putative cytochrome c peroxidase, mitochondrial OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=YALI0D04268g PE=3 SV=1
sp|Q4HWQ2|CCPR2_GIBZE	7.21e-72	28	254	25	284	Putative heme-binding peroxidase OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FGRRES_10606 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000059	0.000002

TMHMM  Annotations     

There is no transmembrane helices in CTMYA2_042850.t1-p1.