CAZyme Information: KIX06539.1

Basic Information

• Species: Rhinocladiella mackenziei
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Rhinocladiella; Rhinocladiella mackenziei
• CAZyme ID: KIX06539.1
• CAZy Family: GH5
• CAZyme Description: Rhinocladiella mackenziei CBS 650.93 unplaced genomic scaffold supercont1.3, whole genome shotgun sequence [Source:UniProtKB/TrEMBL;Acc:A0A0D2ILF5]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
645	KN847477|CGC14	70545.13	5.4425

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_RmackenzieiCBS650.93	11418	1442369	36	11382

• Gene Location: location=KN847477:2770907-2773001(+)

Full Sequence      

MKHGLISALLGSAFVGFALADLGKWMGGGDCPWGGKTASGSHPQRDIPDTGVTRYYDFTV
ARATMAPDGVSVPMIVVNGQFPGPMIEANWGDWIEVNVHNEIYGPEDMTMIHWHGLNQPG
TPYYDGVATVDQCPIVPGSSLTYRFRADEYGTSWYHSHYSAQYSSGVMGPIVIHGPNDVE
YDIDLGPIVVTDWFHDTYDHIVDLVLAPTDTNLPYRPFSDSNLVGGVGQYPCSNITDGTP
CTTVPYAKWEFQPGKKHLLRFINTGATAFETISIDGHTMTVIANDFVPVQPYDTEFVTLG
VSQRVDVVVTANAAPGNYWLRAWNSPQCGDSNAPDGRGIIYYSGGDPAAAPTSSGNPAPE
NRFCQNDNLATTVPQYAIPVANPDTTITLTVTGAPDATGVFHWLFNGVTYVGNLEMPLLL
AAVQAQTAFPPENNVYNTGTNGTVRVVIINNLPAPHPMHLHGHDFQVLAEGSGTWDGSIV
NPSNPQRRDVHMLWAGVGGANAAPPNYIVIQFEQDNPGIWPLHCHMAWHLSAGMSIMILE
RPEELAQIKVPDAVSATCDIFKQWQSAHPTTELDGLKKRNMAERMVEFMKGGKGGHVSHV
DKHRKRGVRGWDHHHIDYEPWTGEKGTGTVERNMIPESLRKRDEV

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	45	357	5.4e-116	0.9647435897435898

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	3.67e-70	53	554	1	535	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.
259923	CuRO_1_MaLCC_like	1.34e-67	51	174	1	122	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	1.98e-63	50	564	20	567	L-ascorbate oxidase
259968	CuRO_3_MaLCC_like	6.53e-63	379	539	2	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.
215324	PLN02604	2.65e-61	53	548	24	554	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIW99529.1|AA1_3	1.13e-183	11	574	87	660
APA07098.1|AA1_3	2.38e-179	32	574	54	593
QFF92555.1|AA1_3	1.12e-176	32	574	54	590
QSZ30962.1|AA1_3	2.39e-176	32	574	54	592
ATZ46043.1|AA1_3	3.17e-176	32	574	54	590

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LM8_A	1.34e-108	32	569	3	533	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.38e-108	32	569	4	534	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	2.12e-108	32	569	31	561	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
3V9E_A	1.39e-106	46	570	60	570	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3DKH_A	3.00e-106	48	574	28	556	L559A mutant of Melanocarpus albomyces laccase [Melanocarpus albomyces],3DKH_B L559A mutant of Melanocarpus albomyces laccase [Melanocarpus albomyces]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A067XMP2|PTAK_PESFW	1.19e-151	32	558	44	566	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|J5JH35|OPS5_BEAB2	8.40e-115	33	564	54	576	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q12570|LAC1_BOTFU	1.89e-111	33	574	47	558	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|P78722|LAC2_PODAS	1.33e-107	48	577	73	606	Laccase-2 OS=Podospora anserina OX=2587412 GN=LAC2 PE=2 SV=1
sp|Q70KY3|LAC1_MELAO	5.48e-107	48	583	78	616	Laccase-1 OS=Melanocarpus albomyces OX=204285 GN=LAC1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000205	0.999777	CS pos: 20-21. Pr: 0.9721

TMHMM  Annotations     

There is no transmembrane helices in KIX06539.1.