CAZyme Information: PIW_T001816-RA-p1

Basic Information

• Species: Globisporangium iwayamae
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium iwayamae
• CAZyme ID: PIW_T001816-RA-p1
• CAZy Family: AA17
• CAZyme Description: Multicopper oxidase, type 3

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
618		66965.31	7.1524

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GiwayamaeDAOMBR242034	14874	1223558	0	14874

• Gene Location: location=PiwaDAOMBR242034_SC00154:19316-21415(+)

Full Sequence      

MQPRELPSSASQAPALNGNDDHSKLKTSRSTRRSQIARTLGLGTAVLALGLLGTTTFYVS
RAQHHSHHATTGIPIAAINEDTTRLALLNSLVTELDAFKEPIERISVNGELNTTLHVAPL
HFEDGPISFWTRAYEGSVPGPTLRVKPGDVINIELVNDLAPNVPGPWTMNTNHNPNTTNL
HVHGMHVDPTGLADNIFRVVSPGESALTQIHVPRNHPRGLFHYHPHYHGSVFAQMGGGMA
GALVHVLVLQEFRFSGGLGSSAIAVAKASRSRLDLKLKYTIKAALDDVMRELYPGVHQVQ
PSIDIPMAEGLQSRYPAGSSGPPVTDYFTVNGQYIPKIELQPRENRVLRLVNAGGVCALQ
LSVPGCSMTLAATDGIYLTEPRAITTLLLTTGSRADVVVNCEPNSATLEPLRPVQSVRDL
SFDGFLGKTSDVYAGVVAMVHVKGASMEMKPVTKIPAPSSLYGKQASLLQLSALDRELMD
HEPFAFEFSMGGKVQKDGFTYKNYFINGKEFDGESIRDMPLGIVQEWVVVNRHLVDSSVT
TANHPFHLHTNAFQIIAMSHGEGAEYKVGDWRDVISVPTPGNVTIRFRPVDFVGKIVAHC
HVLGHSDGGMIAAVAITH

Enzyme Prediction     

No EC number prediction in PIW_T001816-RA-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	135	610	3.3e-24	0.9553072625698324

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259922	CuRO_1_Tth-MCO_like	1.00e-51	110	244	1	137	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	8.47e-34	131	617	54	449	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	2.20e-33	484	616	8	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	5.67e-25	486	615	4	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.
400194	Cu-oxidase_2	4.18e-20	493	616	11	134	Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ21019.1|AA1	9.77e-182	173	614	2	466
CCO14930.1|AA1	5.33e-31	140	617	19	476
UPL01783.1|AA1_2	1.16e-13	124	612	35	485
QGI84994.1|AA1_2	1.93e-13	124	612	31	480
QGI98645.1|AA1_2	2.55e-13	124	612	31	480

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2XU9_A	1.45e-33	97	616	3	438	Crystal structure of Laccase from Thermus thermophilus HB27 [Thermus thermophilus HB27],2XUW_A Crystal Structure of Apolaccase from Thermus thermophilus HB27 [Thermus thermophilus HB27],2XVB_A Crystal structure of Laccase from Thermus thermophilus HB27 complexed with Hg, crystal of the apoenzyme soaked for 5 min. in 5 mM HgCl2 at 278 K. [Thermus thermophilus HB27],2YAE_A X-ray induced reduction of laccase from Thermus thermophilus HB27(0.0- 12.5 percent dose) [Thermus thermophilus HB27],2YAF_A X-ray induced reduction of laccase from Thermus thermophilus HB27 (12. 5-25.0 percent dose) [Thermus thermophilus HB27],2YAH_A X-ray induced reduction of laccase from Thermus thermophilus HB27 (25. 0-37.5 percent dose) [Thermus thermophilus HB27],2YAM_A X-ray induced reduction of laccase from Thermus thermophilus HB27 (37. 5-50.0 percent dose) [Thermus thermophilus HB27],2YAO_A X-ray induced reduction of laccase from Thermus thermophilus HB27 (50. 0-62.5 percent dose) [Thermus thermophilus HB27],2YAP_A X-ray induced reduction of laccase from Thermus thermophilus HB27 (62. 5-75.0 percent dose) [Thermus thermophilus HB27],2YAQ_A X-ray induced reduction of laccase from Thermus thermophilus HB27 (75. 0-87.5 percent dose) [Thermus thermophilus HB27],2YAR_A X-ray induced reduction of laccase from Thermus thermophilus HB27 (87. 5-100.0 percent dose) [Thermus thermophilus HB27],4AI7_A Crystal structure of Laccase from Thermus thermophilus HB27 complexed with Hg, crystal of the apoenzyme soaked for 2 h in 5 mM HgCl2 at 278 K. [Thermus thermophilus HB27],5AFA_A Crystal structure of Laccase from Thermus thermophilus HB27 complexed with Ag, crystal of the holoenzyme soaked for 30 m in 5 mM AgNO3 at 278 K. [Thermus thermophilus HB27],5G3B_A Preserving metallic sites affected by radiation damage: the CuT2 case in Thermus thermophilus multicopper oxidase [Thermus thermophilus],5G3C_A Preserving Metallic sites affected by radiation damage the CuT2 case in thermus termophilus multicopper oxidase [Thermus thermophilus],5G3D_A preserving Metallic Sites Affected by Radiation Damage the CuT2 cCase in Thermus Thermophilus Multicopper Oxidase [Thermus thermophilus],5G3E_A Preserving Metallic Sites Affected by Radiation DAmage the CuT2 CAse in THermus Thermophilus Multicopper Oxidase [Thermus thermophilus],5G3F_A Preserving Metallic Sites Affected by Radiation Damage the CuT2 CAse in Thermus Thermophilus Multicopper Oxidase [Thermus thermophilus],5G3G_A Preserving MEtallic Sites Affected by Radiation Damage the CuT2 case in Thermus Thermophilus multicopper Oxidase [Thermus thermophilus],5G3H_A Preserving Metallic Sites Affected by Radiation Damage the CuT2 Case in Thermus Thermophilus Multicopper oxidase [Thermus thermophilus],5JRR_A Crystal structure of native laccase from Thermus thermophilus HB27 [Thermus thermophilus HB27],5JX9_A Crystal structure of laccase from Thermus thermophilus HB27 (Cu(II)-cyclophanes, 5 min) [Thermus thermophilus HB27],5K0D_A Crystal structure of laccase from Thermus thermophilus HB27 (Cu(II)-cyclophanes, 3 min) [Thermus thermophilus HB27],5K15_A Crystal structure of laccase from Thermus thermophilus HB27 (Cu2PO, 8 min) [Thermus thermophilus HB27],5K3K_A Crystal structure of laccase from Thermus thermophilus HB27 (CuSO4, 20 min) [Thermus thermophilus HB27],5K5K_A Crystal structure of laccasse from Thermus thermophilus HB27 (ascorbic acid 10 min) [Thermus thermophilus HB27],5K7A_A Crystal structure of laccase fron Thermus thermophilus HB27 (sodium nitrate 1.5 min) [Thermus thermophilus HB27],5K84_A Crystal structure of laccase from Thermus thermophilus HB27 (sodium nitrate 10 min) [Thermus thermophilus HB27],6Q29_A Chain A, Laccase [Thermus thermophilus HB27],6TYR_A Chain A, Laccase [Thermus thermophilus HB27]
6W2K_A	1.47e-33	97	616	4	439	Chain A, Laccase [Thermus thermophilus HB27],6W2K_B Chain B, Laccase [Thermus thermophilus HB27],6W9X_A Chain A, Laccase [Thermus thermophilus HB27],6WCG_A Chain A, Laccase [Thermus thermophilus HB27],6WCH_A Chain A, Laccase [Thermus thermophilus HB27],6WCL_A Chain A, Laccase [Thermus thermophilus HB27],6WCM_A Chain A, Laccase [Thermus thermophilus HB27]
6WCN_A	2.03e-33	97	616	26	461	Chain A, Laccase [Thermus thermophilus HB27],6WCP_A Chain A, Laccase [Thermus thermophilus HB27]
3ZX1_A	1.77e-21	134	616	75	479	Multicopper oxidase from Campylobacter jejuni: a metallo-oxidase [Campylobacter jejuni subsp. jejuni]
6IM7_A	5.79e-16	131	616	38	488	CueO-12.1 multicopper oxidase [Escherichia coli K-12]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q6GIX3|MCO_STAAR	1.26e-14	131	617	72	446	Multicopper oxidase mco OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=mco PE=3 SV=2
sp|Q69HT9|MCO_STAAU	1.67e-14	131	617	72	446	Multicopper oxidase mco OS=Staphylococcus aureus OX=1280 GN=mco PE=1 SV=2
sp|Q4LAB0|MCO_STAHJ	6.95e-14	131	617	72	446	Multicopper oxidase mco OS=Staphylococcus haemolyticus (strain JCSC1435) OX=279808 GN=mco PE=3 SV=2
sp|Q8CQF6|MCO_STAES	8.95e-13	108	617	48	446	Multicopper oxidase mco OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=mco PE=3 SV=2
sp|Q8ZBK0|CUEO_YERPE	1.17e-12	101	617	38	532	Multicopper oxidase CueO OS=Yersinia pestis OX=632 GN=cueO PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.996565	0.003415

TMHMM  Annotations     

Start	End
36	58