CAZyme Information: PV07_05315-t44_1-p1

Basic Information

• Species: Cladophialophora immunda
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Cladophialophora; Cladophialophora immunda
• CAZyme ID: PV07_05315-t44_1-p1
• CAZy Family: GH16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1005	KN847042.1|CGC18	103815.37	4.5051

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CimmundaCBS83496	12879	N/A	49	12830

• Gene Location: location=KN847042.1:2436157-2439300(-)

Full Sequence      

MRSLLYAAAFLPLQTLAWFGKASDIDEIVVVTTTRTITVCPITEAWTCGPDYPTAPWQDW
TGTPTSTGSEVSPTSKGNGNGGHNHSGSPSSSSPTGHHSSGPHSSVQATWTSSSSPAGSP
SSSGPYVGPSSSTSHGGPSSSGPYGSPSSSSPAGSPTSTSDYGTPTSSSSAPGDSSSSTD
PPAGGSSTTSPSASSTSTDPPVDPPTSSSTTSGLPVDPATTSSSASSTSSDPPVDPPTTS
SSATSTSSDPPVDPPTTSSSVTSTTSDLPVDPATTSSSASTTSSDPPVGPGTTSSTTSSA
ADPPAGTSTSTSSGSSTSSADPAGTSTSSSSSTSSDPPTSSTSSASTTSSSADPTSTTTS
SSVDPVTTSSSTTITTTATLTSTTSRSATTTSSSTCAPSQTLSALPEQTSCPDNTADDRS
QWCGKSVSDDTLVPYSSGQTKSFTLTITDADIDFDGTVRPAFAINGGTPGPAIEVNWGDE
VVITVINLLTDNATTIHWHGIRQFGTNDQDGVPGVTECAIPPNGGQRTYTWIASTYGTGW
YHSHTLSQYGGGIRGPIIIHGPATAEYDYDMGHVMIDEVFSQTIFQMAWNIARLRGPLPA
AVNYMVNGQNKSPDGTAGKATEWTVEPGKKHLFRIINSSAQSSFIVHFDYHQMTVISSDY
TPIVPYTTTSLYVNPGQRYNVIVEMDQTPGAYYMRAITQTGCGEQNVNTGLGIANPVFTY
KGSCGTPTSETLSITPASDCRDEPLASLVPFVSKNGGSVDDFSDTAKLLPGGNGGSQVFD
GYGSIIRWYFGGLLDLNGNSASVLGNQTVSVDFENPTLKTMAELPTLSFNSSKYSNAVVL
DGPAGDWVYFVIQNNFQTSHPIHLHGHDFSVLGQGKGVFTADQVTSLNFANPCRRDTALL
YGFAGPGGVAQSGWTVIGFQTDNPGAWIMHCHIIWHADGGMGLQYIEQPDAINANGYWTS
SGFQDECNAYSSYQNGGGEGKLTYEAGIKRDLERHRYALKHKGKH

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	436	735	2.2e-102	0.9583333333333334

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259923	CuRO_1_MaLCC_like	8.29e-55	438	549	1	111	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.
259968	CuRO_3_MaLCC_like	1.32e-52	804	946	28	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.
274555	ascorbase	1.01e-48	455	947	16	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.
259947	CuRO_2_MaLCC_like	2.87e-48	571	731	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.
177843	PLN02191	3.20e-48	463	952	46	551	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAK03309.1|AA1_3	6.52e-285	398	995	208	802
AFG30950.1|AA1_3	1.66e-119	399	974	29	559
AFG30951.1|AA1_3	1.66e-119	399	974	29	559
QIX00022.1|AA1_3|CBM20	7.86e-115	407	973	81	615
AHZ58330.1|AA1_3	1.04e-112	400	952	26	555

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	5.35e-105	401	973	28	567	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.45e-104	401	973	28	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]
5LM8_A	1.90e-97	441	973	24	528	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.95e-97	441	973	25	529	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	4.12e-97	441	973	52	556	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q12570|LAC1_BOTFU	1.35e-109	403	973	29	548	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|J5JH35|OPS5_BEAB2	2.54e-105	437	949	70	553	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96UM2|LAC3_BOTFU	2.00e-102	469	945	1	452	Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1
sp|Q96WM9|LAC2_BOTFU	8.07e-102	414	973	41	568	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q03966|LAC1_CRYPA	7.94e-100	407	973	32	577	Laccase OS=Cryphonectria parasitica OX=5116 GN=LAC-1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000498	0.999447	CS pos: 22-23. Pr: 0.9009

TMHMM  Annotations     

There is no transmembrane helices in PV07_05315-t44_1-p1.