CAZyme Information: evm.model.AC2VRR_s00189g103-p1

Basic Information

• Species: Albugo candida
• Lineage: Oomycota; NA; ; Albuginaceae; Albugo; Albugo candida
• CAZyme ID: evm.model.AC2VRR_s00189g103-p1
• CAZy Family: GH81
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
561	Acan2VRR_SC189|CGC2	62536.64	7.2424

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Acandida2VRR	15896	911350	72	15824

• Gene Location: location=Acan2VRR_SC189:194747-196432(-)

Full Sequence      

MKVSVLSSSTWALASILLNVFALKDFQTLIQPKEIASECALATEANRDPKAHFARSTLVI
ELNVTAGRFESTFISFNTRTYNGEIPGKTIKVCMGDKLIVRLWNLLGEGTSNLTNLHVHG
MEVTSKGNGDNVFVPVEPGHLRVYEYAINQSSTTHIYYHPHVHHLVNSQITGLMAGSIFI
VENKFHPSYPRQLREMEEVVMIVQGVCYMNCTNNRDNIHSALINRYVSTELEPNDLNPDI
KIQPSNSMIKDLGQVHLFVNGQYGPTLHMSTKKCKRLRLVNAVANNMVELVVPGCAMYAL
GADGIYRNGSPVKKLVTMLSPGGRSDIALCCEKAGTFWMASDSSASRVEMLGLVNDHRVA
SQKVMKIVVSDCTLDTINATRDFHWKLPYDTQHLVDLRNIPASAIPLKNRYDYELSMDQK
SGFQSPAGVTSAFGINRMPFEENYINHTMVIGQVQEWHISTNIVANNCGSNSVTGSPCRR
VVHPFHLHGFPFQIIAKSQELDPEDLLHEIGQYRDTVLLHGDQKLVIRFIPPAYSLGDIL
THCHISSHSDNGMAQIVRVIE

Enzyme Prediction     

No EC number prediction in evm.model.AC2VRR_s00189g103-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	77	554	8.4e-30	0.9720670391061452

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259922	CuRO_1_Tth-MCO_like	3.69e-40	57	182	1	139	The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus Thermophilus. The subfamily of bacterial laccases includes Tth-MCO and similar proteins. Tth-MCO is a hyperthermophilic multicopper oxidase (MCO) from thermus thermophilus HB27. 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.
225043	SufI	3.75e-37	49	561	22	450	Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis].
259967	CuRO_3_Tth-MCO_like	3.95e-19	422	559	9	123	The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus Thermophilus. The subfamily of bacterial laccases includes Tth-MCO and similar proteins. Tth-MCO is a hyperthermophilic multicopper oxidase (MCO) from thermus thermophilus HB27. 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.
259870	CuRO_3_LCC_like	6.97e-18	426	554	13	128	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.
259957	CuRO_3_CueO_FtsP	1.77e-16	406	557	1	123	The third Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, and similar proteins. CueO is a multicopper oxidase (MCO) that is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CueO is a periplasmic multicopper oxidase that is stimulated by exogenous copper(II). FtsP (also named SufI) is a component of the cell division apparatus. It is involved in protecting or stabilizing the assembly of divisomes under stress conditions. FtsP belongs to the multicopper oxidase superfamily but lacks metal cofactors. The protein is localized at septal rings and may serve as a scaffolding function. Members of this subfamily contain three cupredoxin domains and this model represents the first domain. 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. FtsP does not contain any copper binding sites.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ21019.1|AA1	1.16e-32	112	560	5	469
AWT08580.1|AA1_2	1.15e-16	67	554	35	492
AWU75157.1|AA1_2	1.15e-16	67	554	35	492
QEL59042.1|AA1_2	4.76e-16	82	557	48	510
QEO20037.1|AA1_2	4.76e-16	82	557	48	510

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3ZX1_A	3.29e-27	80	561	74	481	Multicopper oxidase from Campylobacter jejuni: a metallo-oxidase [Campylobacter jejuni subsp. jejuni]
6XIZ_A	1.32e-09	77	561	69	462	Chain A, Copper oxidase [Pediococcus acidilactici],6XIZ_B Chain B, Copper oxidase [Pediococcus acidilactici]
6Z0J_A	4.04e-09	77	561	68	461	Chain A, Putative multicopper oxidase mco [Pediococcus acidilactici 7_4]
6Z0K_A	4.05e-09	77	561	69	462	Chain A, Putative multicopper oxidase mco [Pediococcus acidilactici 7_4]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4LAB0|MCO_STAHJ	2.31e-21	77	559	71	445	Multicopper oxidase mco OS=Staphylococcus haemolyticus (strain JCSC1435) OX=279808 GN=mco PE=3 SV=2
sp|Q8CQF6|MCO_STAES	9.97e-21	77	559	71	445	Multicopper oxidase mco OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=mco PE=3 SV=2
sp|Q6GIX3|MCO_STAAR	5.88e-19	77	559	71	445	Multicopper oxidase mco OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=mco PE=3 SV=2
sp|Q69HT9|MCO_STAAU	1.40e-18	77	559	71	445	Multicopper oxidase mco OS=Staphylococcus aureus OX=1280 GN=mco PE=1 SV=2
sp|Q55P57|LAC1_CRYNB	1.13e-12	82	559	86	560	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.925016	0.074996

TMHMM  Annotations     

There is no transmembrane helices in evm.model.AC2VRR_s00189g103-p1.