CAZyme Information: KNZ58169.1

Basic Information

• Species: Puccinia sorghi
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia sorghi
• CAZyme ID: KNZ58169.1
• CAZy Family: GH5
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
912	LAVV01006818|CGC1	99293.07	6.8294

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PsorghiRO10H11247	21769	N/A	691	21078

• Gene Location: location=LAVV01006818:4826-8572(+)

Full Sequence      

MPLPKIPSFGSNFADSFKGRETSQSHSRDTSQAGRFPYISRGNQQASSSHTSESESFPSS
YHERSYASELTPHQRSDQSYGQSFTISSRLKRAFLAPTKFQIAIGSIILIIVVASLVIGL
VLGLRNISLQDKLRNRINTIPVRIPNFNESVIGHIKGEPPQKREFFFVIDERLGSPDGVE
KAMIVANGQYPGPIIEVNQGDEVVVNVKNNLAQPTSIHWQGLFQSGTNYFDGIAGVTECG
IPGCTNFFVLEPAGEQMSYKLHPGSFTGTTFWKAGYGTQAAEGLTGGLVVHPTHSNTTSI
YDEEIMVHLSDLYHENSKALTEKYISVSFLCVASRGRAEGVGGKVGNEPVPDSGTINGVG
QYPHRPNGEIIFPEYHKVVVEKSRRFVRRVSSESLTLCQPLYRLRLVNAGSMAPILFSID
SHNLTVIEADGVEVEPVTFGGGIQIEVGQRYSVVLHAEHEHHEQFWMRATLVTDQFKYDN
PEAVHEILGILAYGEGTEGVPHSQDHAEKIDILDSSRLRPLVPVAPPPATHLFISHYLME
YFLSTSCLLTISPTLCSLSIDRSVGMFNSTTWVPLLPSSSLLANLGDGKDGASVPSPYQF
MLSADKPEVIDMIINNLSGGTSTFSLSGHRPWIIGSGIGSYLGDSSQTLTASPNMTVSTS
TGASMGSSPNITLNNSTSNGPLNASNSNDPHANATASAPSGSSSSAPPEPQTSHPGSPPP
SQTTTSNDQGTSQPNDGSHPGQENPKKSPEEKKQDDGLSSDHAKSYQRPTNYYAAATASA
NSRGVSMHQLEVHEPYKGAYPDYWGKHTSGKYGSKKGWSYPTKRSNRMNFRRQLPKAGNE
VVIQRDTFTIPKDGWVKIRFVTDNPGMWLLADQNQWHLAAGGAMQILSRKAEWPKVPDEV
QKFCSSPEKLMS

Enzyme Prediction     

No EC number prediction in KNZ58169.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	179	881	3.3e-79	0.9748603351955307

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259953	CuRO_2_MCO_like_1	3.93e-57	305	494	1	163	The second 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 oxidise 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 family of MCOs is composed of three cupredoxin domains 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 2 of 3-domain MCOs has lost the ability to bind copper.
259926	CuRO_1_Diphenol_Ox	1.18e-52	163	291	1	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.
274555	ascorbase	2.16e-40	162	493	1	297	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.
215324	PLN02604	1.35e-33	175	473	37	304	oxidoreductase
259923	CuRO_1_MaLCC_like	2.40e-33	163	291	4	122	The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QPL20074.1|AA1	6.04e-90	154	641	107	544
AHA83597.1|AA1	4.46e-86	158	643	94	532
CDR37367.1|AA1	1.69e-82	158	648	99	545
AUS45844.1|AA1	1.35e-63	163	639	123	569
QRC90881.1|AA1	1.15e-60	160	639	101	553

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LM8_A	1.90e-32	163	523	24	333	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.92e-32	163	523	25	334	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
3KW7_A	2.65e-32	175	469	16	261	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]
1HFU_A	2.68e-32	175	469	17	260	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	2.72e-32	175	469	17	260	Chain A, Laccase [Coprinopsis cinerea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VQZ4|LAC2_CRYNH	2.46e-36	160	474	59	339	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|Q55P57|LAC1_CRYNB	2.54e-35	160	471	59	336	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J9VY90|LAC1_CRYNH	2.54e-35	160	471	59	336	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|Q02075|LAC2_THACU	6.38e-35	164	471	23	292	Laccase-2 OS=Thanatephorus cucumeris OX=107832 GN=LCC2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	7.79e-35	163	645	74	498	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000049	0.000000

TMHMM  Annotations     

Start	End
102	124