CAZyme Information: POW05603.1

Basic Information

• Species: Puccinia striiformis
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia striiformis
• CAZyme ID: POW05603.1
• CAZy Family: GH16
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1054		116454.53	6.6591

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Pstriiformis93TX-2	14629	N/A	0	14629

• Gene Location: location=PKSM01000169:68875-77942(+)

Full Sequence      

MDLRASRITSYTKTKSESSSYQSSNSSTVTTYNPTNPYFAGSVQVNTPSLVLNREHVVTN
VPQVRRYDWVVANKSASFDGFLRNVFVINNQFPGPLIEANEGDTIVVNVKNELNVPLSIH
WHGIYQRGTQWMDGVSGVTQCPQQPGTTFTYEFTVNDQFGTFWYHAHYGALLADGVSGPL
IIHSPRDPLVRGRDYDNDQILFINDWYHDPSTTITRKLLSTEGYNGTLAAPSPNTALLNG
IGFFNCEKYADGKTCQTNYSPLEIQVPPKQRSRIRLIQAGSHALFKVSVDGHALEVIEAD
ATPVRSSKLFHRVSLHNAERYSVILDTASDSEGDSFHLRAVMDTDCFAPGMDTVEGNTAL
AVVRVSSKPLESGNIRARMPAPTTQDWSDEKDGPCVDLDQSKLAPRINPNLNSNSLGRVY
YNTSFGTIIDRSKKGPSNALGRFFVDNTTYISRESQPLLPQLMSGGSGALNMSEVATQTI
SQPGIWDVVVNNLDQAIDHPIHLHGVDTCVVASGNGTLTEANAHTAEYQLDNPLCRDVHV
VPGGSYLLICRARIPESNMPGPTMAFPGPLIEANEGDTIVVNVKNELTVPLSIHWHGIYQ
RGTQWAHYGALLADGISGPLIVHSKRDPLVRGRDFDNDQIIFMNDWYHDPSTTVTRQLLS
NKGYNGSLAAPSPNTALLNGVGFFNCEKYADGKPCKTNNNPLEIRVPPNQRSRLRLIHAG
SHALFKVSIDDHPLEVIEADATPVQSSTSFHRVNLHNAERYSVILDTRADKEGASFYLRA
SMDTDCYLTVAPGMDTPEGNTALAVVRVSSKPLSMERDQTRIAMPKTKDWKDTLTGPCVD
LDQTKLSPRINPKLNTNSLGRVYFNTSFGTIVDKAHKSPNNTLGRFFVDNTTWISRESDP
LLPKVLSGGSGSVNTSEVATQTINKPGIWDVVINNLDQAIDHPIHLRKNFHSCSRPYQYD
SISARALSESDYILRPYLQSCVVASGKGTLGESNLKSAQYHHDNPLCRDTHVVPGGSYLF
HQHQHQSQLCQILNQDWKVVGDVFLTDWWITLAL

Enzyme Prediction     

EC	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	81	549	1.4e-87	0.9106145251396648
AA1	606	890	1.4e-34	0.5

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259950	CuRO_2_Diphenol_Ox	5.51e-70	639	809	1	164	The second 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 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. Laccase is a multicopper oxidase (MCO) 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.
259950	CuRO_2_Diphenol_Ox	1.71e-69	199	366	1	164	The second 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 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. Laccase is a multicopper oxidase (MCO) 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	2.76e-68	65	183	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	4.12e-56	64	330	1	270	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.
259869	CuRO_1_LCC_like	4.68e-54	65	183	1	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRV98945.1|AA1	1.36e-148	50	549	53	543
QRW13493.1|AA1	3.77e-148	50	549	53	543
QRV91744.1|AA1	1.50e-147	55	549	38	511
QRV76916.1|AA1	1.50e-147	55	549	38	511
QRW05810.1|AA1	4.86e-145	55	549	38	511

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4JHU_A	1.95e-51	68	538	7	424	T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]
3KW7_A	2.21e-51	68	537	7	429	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]
5LM8_A	3.02e-51	59	549	20	474	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	3.08e-51	59	549	21	475	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
6H5Y_A	4.86e-51	68	538	7	424	PM1 mutant, 7D5 [Aspergillus oryzae],6H5Y_B PM1 mutant, 7D5 [Aspergillus oryzae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VQZ4|LAC2_CRYNH	1.27e-117	51	549	48	530	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|J9VY90|LAC1_CRYNH	4.24e-117	52	549	49	530	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|Q55P57|LAC1_CRYNB	6.15e-116	52	549	49	530	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|A0A067XMP2|PTAK_PESFW	5.92e-59	64	549	64	518	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|Q02081|LAC4_THACU	1.80e-51	64	555	22	473	Laccase-4 OS=Thanatephorus cucumeris OX=107832 GN=LCC4 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000028	0.000008

TMHMM  Annotations     

There is no transmembrane helices in POW05603.1.