CAZyme Information: CLCR_01625-t43_1-p1

Basic Information

• Species: Cladophialophora carrionii
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Cladophialophora; Cladophialophora carrionii
• CAZyme ID: CLCR_01625-t43_1-p1
• CAZy Family: AA7
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
352	LGRB01000019|CGC5	37569.86	5.2504

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CcarrioniiKSF	11240	N/A	59	11181

• Gene Location: location=LGRB01000019:15456-16514(+)

Full Sequence      

MTVVAADFVPIVPYTTTTLKIANGQRYDVIVEADQIPSSYYVRAVIQSGCPSGGANSGLG
TANAVINYEGATPVTPINNTPITNVTANICQDEPLASLVPFLQKPGGSATAFQASASTIP
AGSVTSVATNDDGTVFQWYINNAVINVNYSQPTLKTLAEGGSNDLISNSIILNQANTWVY
FVIQNQFFASHPMHIHGHDVSVLGTGVGTFTADMISTLNFENPTRRDTVMLQGSAGPGNP
AGYTVIGFETDNPGAWLMHCHIAWHVDGGLALQFVERPGDITTGKYVGDDFKGECSALQE
YESSSPQGAKLSGQSGLKARGYSDELDFGLWNGGAKMNIEQYRKRYAHRHAH

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	1	271	3.3e-36	0.4329608938547486

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259968	CuRO_3_MaLCC_like	1.11e-69	124	275	12	157	The third 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 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
400194	Cu-oxidase_2	5.03e-41	146	280	1	138	Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.
259966	CuRO_3_Fet3p	6.13e-32	129	278	12	160	The third Cupredoxin domain of multicopper oxidase Fet3p. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p 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 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
259977	CuRO_3_MCO_like_4	2.46e-31	178	276	70	166	The third cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
259870	CuRO_3_LCC_like	3.19e-29	129	275	11	132	Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. 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 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Also included in this family are cupredoxin domains 2, 4, and 6 of the 6-domain MCO ceruloplasmin and similar proteins.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAK03309.1|AA1_3	2.82e-95	3	318	464	796
AHZ58327.1|AA1_3	4.73e-66	1	320	280	581
AFG30950.1|AA1_3	8.89e-62	3	302	283	559
AFG30951.1|AA1_3	8.89e-62	3	302	283	559
QQX29064.1|AA1_3	2.51e-60	1	304	308	590

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LM8_A	1.59e-52	1	316	237	543	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.61e-52	1	316	238	544	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	2.52e-52	1	316	265	571	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
3SQR_A	5.14e-48	1	301	285	567	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	9.89e-48	1	301	285	567	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q96UM2|LAC3_BOTFU	4.27e-55	2	274	186	452	Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1
sp|J5JH35|OPS5_BEAB2	1.57e-52	1	307	292	582	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	1.94e-49	1	301	286	568	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q12570|LAC1_BOTFU	2.77e-49	3	306	272	553	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|P06811|LAC1_NEUCR	1.17e-46	1	320	298	613	Laccase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=lacc PE=1 SV=3

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000014	0.000020

TMHMM  Annotations     

There is no transmembrane helices in CLCR_01625-t43_1-p1.