CAZyme Information: EAQ82906.1

Basic Information

• Species: Chaetomium globosum
• Lineage: Ascomycota; Sordariomycetes; ; Chaetomiaceae; Chaetomium; Chaetomium globosum
• CAZyme ID: EAQ82906.1
• CAZy Family: AA1
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
745		81316.15	5.0631

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CglobosumCBS148.51	11232	306901	184	11048

• Gene Location: location=CH408038:105983-109458(+)

Full Sequence      

MFPAGPAGPTGPKSPCHRALVHEPVQGLGPKEPYEAPIGGRIGHVQEILDSDTGHGLATA
REGLLYDTRQGCASTHLTGNPDGWGRLCVQTFRPLPTVLNPIDIPEVTGSTHAGPSSLPA
KSLRGTAKITIATTPICTALRLLMRDSGDSAHEGRRGNVGDVPSAAAHPARRTPRLEARG
QEEPVLPTMKFRGRRLERERDTLTSKMRQSIFSLLATFTGTFALSIPLAPDGLLQPRQAG
CENTAESRNCWGEYDIDTNYYDVFPENPGPPKEFWLSVEEGPCSLDGFERSCMTFNGTVP
GPTIIADWGDEVIIHVTNNMASNGTSIHWHGLRMLNNALNDGVPGVTQCGLAPGETMTYR
FRVTQYGSTWYHSHFSLQYAEGLFGGMILRGPATQNYDEDLGLLFLQDWAHVEAFTNWHV
AKLGAPPTMPNGLINGTNTFDCSGSDNARCVGGGKKFEMVFEQNKKYLIRLVNVAVDGAF
QFSIDGHSLTVIAHDLVPIKPYTTDSVQITIGQRYDVIVEANAQPGDYWLRGGWNTNCGI
NTNAADITGIVRYDASSTADPQTESSVDPAKDCIGEAPWKTVPHLEVDVGNMRGGVVYEE
MGTKFDDYFKWTINTSSLYLDWADPTMGQIFEGKNLFPTEYNVVPVNVGMFDGDTSKFNT
TGTSRRDVATLPANGYLAIAFKLDNPGAWLVHCHIAWHASQGLSLEFVESQSDIQTDAVS
RQVFDDVCASWKAWSPVWPQDDSGI

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	258	573	1.4e-126	0.9935897435897436

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259947	CuRO_2_MaLCC_like	1.20e-68	401	565	1	161	The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Laccase is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.
259923	CuRO_1_MaLCC_like	1.04e-64	269	389	1	121	The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
177843	PLN02191	3.98e-59	272	714	24	551	L-ascorbate oxidase
274555	ascorbase	3.18e-57	284	709	14	523	L-ascorbate oxidase, plant type. Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases.
274556	laccase	1.56e-52	290	708	22	518	laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AGZ62514.1|AA1_3	4.16e-232	207	745	1	576
CAP64719.1|AA1_3	1.06e-227	207	745	1	597
CDP30116.1|AA1_3	1.06e-227	207	745	1	597
VBB81961.1|AA1_3	1.51e-227	207	745	1	597
AFC76164.1|AA1_3|1.10.3.2	3.54e-224	213	745	9	580

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	1.22e-225	213	745	9	580	Crystal structure of laccase from Botrytis aclada at 1.67 A resolution [Botrytis aclada],4X4K_A Structure of laccase from Botrytis aclada with full copper content [Botrytis aclada]
3V9E_A	2.46e-225	213	745	9	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LWX_A	1.52e-120	243	739	23	561	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	3.97e-119	251	739	4	533	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	4.09e-119	251	739	5	534	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q96WM9|LAC2_BOTFU	1.71e-222	213	745	9	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q12570|LAC1_BOTFU	1.87e-187	207	745	1	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|J5JH35|OPS5_BEAB2	1.03e-160	241	745	44	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q0CCX6|GEDJ_ASPTN	1.13e-112	239	745	26	605	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1
sp|Q4WQY8|TPCJ_ASPFU	4.40e-109	236	745	23	609	Oxidoreductase tpcJ OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=tpcJ PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000052	0.000002

TMHMM  Annotations     

There is no transmembrane helices in EAQ82906.1.