CAZyme Information: ALNC14_036700:RNA-p1

Basic Information

• Species: Albugo laibachii
• Lineage: Oomycota; NA; ; Albuginaceae; Albugo; Albugo laibachii
• CAZyme ID: ALNC14_036700:RNA-p1
• CAZy Family: CBM48
• CAZyme Description: conserved hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
562		63008.92	7.0505

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AlaibachiiNc14	14629	890382	180	14449

• Gene Location: location=FR824081:83990-85678(+)

Full Sequence      

MRASVVAISTLASILHTNFALNDFQALIQPKIIASECALAMEANRDPEAQFKKGTLVVDL
NVTAGRFESAYISFNTRTYNGQIPGKTIKVCEGDTLVVNLWNHLGEGSSNLTNLHVHGME
VSSMGQSDNVFVAVEPRQFRRYEYAIEQSITDHIYYHPHVHLLVSSQISGLMGGNIFIVE
NKYHPSYPRQLREMEEVVLLLQGVCYQNCTNNRDNIFNAIISRYGVSEQSLLPNELNPNI
KIRPENSMIQDTKQVHIFVNGQYGPELHMSTNKCKRLRWTNALANNVVELVMPGCMMYAM
GVDGIYRKGSPVQKAVNIISPGGRSDIALCCEKAGTYWMSSDSSSSRLGQLGFVNDHRAA
TQKVMKIIVSENATQEVNLIADFTWKLPYDTQHLVDLRTIPASSIPPANMYSYELSMDIK
NMFVDAKGVKFAFGVNQKTYDDNYINHTMVVGQVQQWQISTKTVSDACDANPPSTTRCRE
MVHPFHLHGFPFQIVSKSENFDPDDLLHEIGEYRDTVLLRSGLKILIRFIPPAYAVGEIL
THCHIASHSDNGMAQKVRVIRA

Enzyme Prediction     

No EC number prediction in ALNC14_036700:RNA-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	75	554	9e-32	0.9720670391061452

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259922	CuRO_1_Tth-MCO_like	4.59e-47	55	180	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	5.90e-34	76	559	54	448	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	1.87e-23	423	559	10	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.
259969	CuRO_3_McoC_like	1.66e-19	433	559	21	125	The third cupredoxin domain of a multicopper oxidase McoC and similar proteins. This family includes bacteria multicopper oxidases (MCOs) represented by McoC from pathogenic bacterium Campylobacter jejuni. McoC is a periplasmic multicopper oxidase, which has been characterized to be associated with copper homeostasis. McoC may also function to protect against oxidative stress as it may convert metallic ions into their less toxic form. MCOs are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. They are capable of oxidizing a vast range of substrates, varying from aromatic compunds to inorganic compounds such as metals. Most MCOs 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.
400195	Cu-oxidase_3	4.29e-19	78	182	19	117	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	6.48e-31	110	560	5	469
UQC83005.1|AA1_2	7.00e-13	80	553	54	493
CCO14930.1|AA1	1.38e-12	85	552	19	468
AGZ90172.1|AA1_3	4.69e-12	61	556	85	553
QYT05468.1|AA1	6.55e-12	6	559	71	616

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2XU9_A	7.21e-23	54	553	15	432	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	7.28e-23	54	553	16	433	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	8.77e-23	54	553	38	455	Chain A, Laccase [Thermus thermophilus HB27],6WCP_A Chain A, Laccase [Thermus thermophilus HB27]
6EVG_A	7.24e-13	57	559	36	507	Structural and Functional Characterisation of a Bacterial Laccase-like Multi-copper Oxidase CueO from Lignin-Degrading Bacterium Ochrobactrum sp. with Oxidase Activity towards Lignin Model Compounds and Lignosulfonate [Ochrobactrum]
2YXV_A	3.16e-11	58	553	20	434	Chain A, Blue copper oxidase cueO [Escherichia coli],2YXV_B Chain B, Blue copper oxidase cueO [Escherichia coli],2YXW_A Chain A, Blue copper oxidase cueO [Escherichia coli],2YXW_B Chain B, Blue copper oxidase cueO [Escherichia coli]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q69HT9|MCO_STAAU	1.88e-18	75	561	71	447	Multicopper oxidase mco OS=Staphylococcus aureus OX=1280 GN=mco PE=1 SV=2
sp|Q6GIX3|MCO_STAAR	2.51e-18	75	561	71	447	Multicopper oxidase mco OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=mco PE=3 SV=2
sp|Q4LAB0|MCO_STAHJ	4.50e-17	75	559	71	445	Multicopper oxidase mco OS=Staphylococcus haemolyticus (strain JCSC1435) OX=279808 GN=mco PE=3 SV=2
sp|Q8CQF6|MCO_STAES	2.53e-16	75	559	71	445	Multicopper oxidase mco OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=mco PE=3 SV=2
sp|Q941X2|LAC3_ORYSJ	2.78e-10	75	554	46	542	Laccase-3 OS=Oryza sativa subsp. japonica OX=39947 GN=LAC3 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.002711	0.997274	CS pos: 20-21. Pr: 0.9286

TMHMM  Annotations     

There is no transmembrane helices in ALNC14_036700:RNA-p1.