CAZyme Information: EDK45895.1

Basic Information

• Species: Lodderomyces elongisporus
• Lineage: Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Lodderomyces; Lodderomyces elongisporus
• CAZyme ID: EDK45895.1
• CAZy Family: GT34
• CAZyme Description: conserved hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
429		49454.82	9.1461

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_LelongisporusNRRLYB-4239	5908	379508	109	5799

• Gene Location: location=CH981528:1066563-1067852(+)

Full Sequence      

MEMKALFSSLRILVTKIISFVLVPLAFLQSLYSDFPGEYVFDRAYYLADRYLIKALFFAV
FAYKLRYRKQIYLHNGFPLQRYQGYNVYLRFKCGCPKALKKKGTPLTRPMIDSAFKVPAT
DPNYILQVQFAIKDIFAVNHEVGSLAPIFFKLAWYCCATYDANTLLSGSSGGSSGGSSGA
TIRFEPEFFDKEIMVLNVARNALEQVKCNFPEISYADLWTLAGKLAIEEMGGPTIKWLPG
RSDYVNTEYVAPQGLLPFGNKNTDHIISIRRTFTRLGLDDQETVALIGAHGLGRCYKYTG
DCEGQWNRGLLRFSNEFFRVLISESWHQEIVPEAGGVQYYNIDNSLRMLNTDMELLRDPS
YKIWVQEYAKDENRYFKDFAEAYAKLLDLRIRRDAKGTVILQESYKYKQRRSKRESRDDR
NRTDIVDKI

Enzyme Prediction     

No EC number prediction in EDK45895.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA2	132	388	1.1e-39	0.9529411764705882

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173825	ascorbate_peroxidase	3.03e-85	131	389	9	248	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	8.40e-48	117	389	3	242	L-ascorbate peroxidase
178467	PLN02879	1.79e-42	146	389	34	245	L-ascorbate peroxidase
173823	plant_peroxidase_like	2.09e-41	131	386	2	253	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.
166005	PLN02364	1.84e-38	146	389	33	245	L-ascorbate peroxidase 1

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QPC69144.1|AA2	8.64e-68	120	406	14	294
QPC78013.1|AA2	7.98e-67	120	406	8	288
QKD61761.1|AA2	9.51e-67	119	406	13	294
QNP98603.1|AA2	1.89e-66	128	397	9	267
QKX59578.1|AA2	5.08e-66	133	400	12	280

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5AMM_A	9.35e-51	132	389	15	257	Structure of Leishmania major peroxidase D211N mutant [Leishmania major],5AMM_B Structure of Leishmania major peroxidase D211N mutant [Leishmania major]
4GED_A	1.24e-50	132	389	15	257	Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex [Leishmania major]
3RIV_A	1.35e-50	132	389	16	258	The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin],3RIV_B The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin]
5AL9_A	1.84e-50	132	389	15	257	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	3.99e-49	132	389	16	258	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	3.57e-95	139	394	45	289	Putative heme-binding peroxidase OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=CCP2 PE=3 SV=2
sp|Q6BIB1|CCPR2_DEBHA	9.25e-88	77	400	107	422	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|Q6CAB5|CCPR2_YARLI	3.36e-67	128	397	9	267	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	1.32e-66	122	406	16	294	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
sp|Q5B1Z0|CCPR2_EMENI	4.62e-65	139	406	22	284	Putative heme-binding peroxidase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=AN5440 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000025	0.000001

TMHMM  Annotations     

Start	End
7	29
44	63