CAZyme Information: KAG1709253.1

Basic Information

• Species: Phytophthora capsici
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora capsici
• CAZyme ID: KAG1709253.1
• CAZy Family: GT71
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
626	JADEVP010000005|CGC2	70092.46	4.5041

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PcapsiciLT1534	28579	763924	5206	23373

• Gene Location: location=JADEVP010000005:247742-249622(-)

Full Sequence      

MRLSICVFFAFAIAVVTAVHDYQPLRQPTVYQSDCAKQWSKLSSGSSSDVDDRSTITSRT
GELRINLAVKLARFTSDYVDFNTRTYNGHVPAPTIKVCPGDRLVVTLTNSLGAGVNNNTN
LHLHGVHVPPVGDADNVMPNVKPGGQRRYTYEIRPDHPAGTFWYHPHSHGNVNSQLNGLM
AGALIIVDRPADFPAELAAMDDQVMLLQSICVENCFNIYDNLEDAIENKFSSSKKMDKEK
IEWLTDLEIVEDDADVPLNDTSLPTVYVNGQYLPTLDLAVGEYKRLRFVNAIANNVAELV
TSHGSGCSLEVVAMDGIYFKKPTAKEVIVIPPGGRADVALMCAEIGEFYLETDCASSRNK
LLGLVNQHRVPSQPIVKLKVSKSEDEDDDDDVGEEESVKFMRLPTTLPKRPAYMEDTLGT
PDSRPIIEESNKYDFEFSVWMDKGIKYGVNHEELDVSNINYSMPVNELQQWELSIKDYRK
PAIWDCDLDDESSGVERQLKKKKSSNCRTMSHPFHMHSTHFQISDMDDITDPENVMFDVG
EWRDTLPLFRGGVQIRFTPREYMVGSIFAHCHIASHVDAGMAQLVNVYDSDTRPNGDEKT
ASFSADSDPEEDEEEESDAAEEVEIR

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	82	582	1.5e-35	0.9720670391061452

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259922	CuRO_1_Tth-MCO_like	7.85e-59	62	186	1	138	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	2.62e-39	57	582	27	443	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].
259869	CuRO_1_LCC_like	8.11e-29	66	186	4	119	Cupredoxin domain 1 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 1 of 3-domain MCOs contains 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 1, 3, and 5 of the 6-domain MCO ceruloplasmin and similar proteins.
400195	Cu-oxidase_3	2.35e-28	85	190	19	118	Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.
259930	CuRO_1_CumA_like	1.98e-21	55	186	4	118	The first cupredoxin domain of CumA like multicopper oxidase. This multicopper oxidase (MCO) subfamily includes CumA from Pseudomonas putida, which is involved in the oxidation of Mn(II). However, the cumA gene has been identified in a variety of bacterial species, including both Mn(II)-oxidizing and non-Mn(II)-oxidizing strains. Thus, the proteins in this family may catalyze the oxidation of other substrates. MCO catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water and has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ21019.1|AA1	1.41e-38	117	591	5	472
CCO14930.1|AA1	1.86e-23	93	580	20	468
CAB4112911.1|AA1	6.14e-10	85	582	46	532
CAK44017.1|AA1	2.57e-09	87	203	107	218
UCK81628.1|AA1	5.31e-09	83	192	106	209

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3ZX1_A	3.82e-26	85	581	74	473	Multicopper oxidase from Campylobacter jejuni: a metallo-oxidase [Campylobacter jejuni subsp. jejuni]
2XU9_A	7.08e-23	85	587	39	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	7.14e-23	85	587	40	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	8.69e-23	85	587	62	461	Chain A, Laccase [Thermus thermophilus HB27],6WCP_A Chain A, Laccase [Thermus thermophilus HB27]
3NSY_A	1.05e-15	64	581	19	482	The multi-copper oxidase CueO with six Met to Ser mutations (M358S,M361S,M362S,M364S,M366S,M368S) [Escherichia coli]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q8X947|CUEO_ECO57	5.22e-14	64	581	47	510	Multicopper oxidase CueO OS=Escherichia coli O157:H7 OX=83334 GN=cueO PE=3 SV=1
sp|P36649|CUEO_ECOLI	6.91e-14	64	581	47	510	Multicopper oxidase CueO OS=Escherichia coli (strain K12) OX=83333 GN=cueO PE=1 SV=2
sp|Q96WT3|FET3_CANGA	1.47e-09	85	230	43	175	Iron transport multicopper oxidase FET3 OS=Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) OX=284593 GN=FET3 PE=3 SV=1
sp|Q03966|LAC1_CRYPA	1.84e-09	19	581	25	544	Laccase OS=Cryphonectria parasitica OX=5116 GN=LAC-1 PE=3 SV=1
sp|I6WZK7|MMCO_MYCTU	6.48e-09	82	343	84	326	Multicopper oxidase MmcO OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=mmcO PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000213	0.999768	CS pos: 18-19. Pr: 0.9796

TMHMM  Annotations     

There is no transmembrane helices in KAG1709253.1.