CAZyme Information: SPSK_07168-t39_1-p1

Basic Information

• Species: Sporothrix schenckii
• Lineage: Ascomycota; Sordariomycetes; ; Ophiostomataceae; Sporothrix; Sporothrix schenckii
• CAZyme ID: SPSK_07168-t39_1-p1
• CAZy Family: GH5
• CAZyme Description: Multicopper oxidase family protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
686	AXCR01000004|CGC16	74802.56	6.2221

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Sschenckii1099-18	10434	1397361	141	10293

• Gene Location: location=AXCR01000004:2694489-2696610(-)

Full Sequence      

MPDDTSEQGDRLLRPPLDHVHKWKAGEDGPGAQETGSDSDEEQAQWPPASRRPPSRWQRL
CRALATVRQIVMPVLAILTALAVVIALFLLLTGGSLSMPAYDTDTDAPKARPTAKDPVIV
LHPEDHTNREPQTIRLSWNITKSRIAPDGVFRDVILINGEFPGPTIEARTGDTLVVTVTN
SLVDEGLSLHWHGLHMRGANHMDGPVGVTQCAIPANGGSFVYEVPTGDQAGTFWYHSHSE
MQRADGLYGGLVVHAPTDTPATAAAAAAAAVDKEILLLVGDWYQFSGKTVFAEFQDPTSN
GNEPVPGSVLINGRGAFDCGRATKAAPVDCHGVELPPLRLDTQLRYRVRLVNVGVLTGIS
TTVPDARIDVLTVDGGLPVVVPDDAKAVAANSIGVVYPAQRVDYVLSWPDAGATGDGTQL
VVTVDGEYYVGNWQDPPSQTFAIVAAPSTQRRATRPVQRAASPPPSTQATQPTRAIDLRT
VHGTALSTPLPAPDKLYMIFAVVEILSHNKFIPKGYINHTMWVPQERPLLSLDRSAWDSH
QLVPWTGAAPVWVELTINNIDTQGHPFHLHGFDFYVVGSHEGLGGWDYYNPFFVPWKPPR
GGPMNTLDPVLRDTVYVPPYGYVILRFRADNEGIWVLHCHILWHQASGMNMAFQVLGHSE
HGLGGTPQSFRAAEYCRTRNEKHPHL

Enzyme Prediction     

No EC number prediction in SPSK_07168-t39_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	150	650	1.7e-82	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259977	CuRO_3_MCO_like_4	7.91e-60	497	655	1	166	The third cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. 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.
274555	ascorbase	1.22e-58	135	653	3	521	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.
177843	PLN02191	5.28e-55	137	653	27	544	L-ascorbate oxidase
259869	CuRO_1_LCC_like	4.78e-53	135	254	2	120	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.
259926	CuRO_1_Diphenol_Ox	1.17e-51	138	254	5	119	The first cupredoxin domain of fungal laccase, diphenol oxidase. Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which 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. 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
QLI63946.1|AA1	2.86e-140	103	655	63	625
UPX44859.1|AA1	2.16e-139	113	676	72	648
UPK99837.1|AA1	1.46e-138	119	655	84	600
UNI19384.1|AA1	1.48e-133	120	655	172	710
QKD61545.1|AA1	3.84e-133	51	676	27	616

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	7.75e-51	139	653	73	540	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
6F5K_A	1.93e-50	147	653	49	517	Crystal structure of laccase from Myceliophthora thermophila [Thermothelomyces thermophilus]
3SQR_A	2.00e-50	139	653	73	540	Crystal structure of laccase from Botrytis aclada at 1.67 A resolution [Botrytis aclada],4X4K_A Structure of laccase from Botrytis aclada with full copper content [Botrytis aclada]
5Z1X_A	5.96e-47	139	653	9	463	Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z1X_B Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z22_A Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena]
3KW7_A	6.16e-46	140	653	10	470	Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2],3KW7_B Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|K7NCS2|FETC_EPIFE	2.32e-60	133	653	22	493	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|Q55P57|LAC1_CRYNB	4.59e-60	99	670	27	574	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J9VY90|LAC1_CRYNH	3.17e-59	99	648	27	553	Laccase-1 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC1 PE=1 SV=1
sp|J9VQZ4|LAC2_CRYNH	3.66e-54	98	648	26	553	Laccase-2 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC2 PE=3 SV=2
sp|I1RMG9|FET3_GIBZE	1.52e-53	133	653	24	494	Iron transport multicopper oxidase FET3 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FET3 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999891	0.000112

TMHMM  Annotations     

Start	End
70	92