CAZyme Information: CAP94137:RNA-p1

Basic Information

• Species: Penicillium rubens
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Penicillium; Penicillium rubens
• CAZyme ID: CAP94137:RNA-p1
• CAZy Family: GH37
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
651	Pc00c16|CGC1	72388.04	6.7274

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PrubensWisconsin54-1255	14021	500485	1464	12557

• Gene Location: location=Pc00c16:3522833-3525133(+)

Full Sequence      

MQRQYSRDRKTAPISELLAPRPMPGLSGRPWPIAGCSLAACLLIGLMYLLQSSIFFGPLI
LPGRHHQNIQEDEAIIARPRIELHPEDHVYRAPATQYLDWRVTSEFRRPDGVLKRVYLIN
GLFPGPTVEARPGDTLIINVTSALPDEPIALHWHGLHVTNAMDGAVGISQCPITSGGHFV
YNLTIPSDQSGTFWYHAHSGVSRADGLYGGLVVHAPASKSTASSLMPRRRDNLPRYTYDR
ELLLLVGDWYHRTAGDVLEWYMDPGNFGNEPVPDSMLINGVGHFDCMMAVPARPVDCIDQ
QVNNSFINLDPHASYRIRVVNTGALAGISLVFDNHLLDLLQVDSVDVARSKERNVNSIGV
LLPGQRMDFILRPLLQTSEKQSHMRIQFDQDSFKYANPALTPDQTFAINYRSDAVDGPPL
KANYLNIGEAPSAPSILRSIPPIAQQTHVVYTKIQKMARHSNKPFGYFNQTTWKPQQDPP
VPLTSIPRAKWDANQFAITTGPEPVWIDLVINNLDEGSHPFHLHGHHFFVLAVHQAEFGW
GSYNPFVDKIPPHLGPESDALRNHTDDVNNPSTGYNTGLYDTSRAALRDTVQIPSRGYAV
LRFRADNPGVWLFHCHMLWHSATGMAMLIDVQGDPAGLNAHADSGESCPAF

Enzyme Prediction     

No EC number prediction in CAP94137:RNA-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	112	626	7.4e-91	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259977	CuRO_3_MCO_like_4	3.50e-61	449	631	2	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	7.73e-61	95	625	1	517	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	3.18e-59	88	628	17	543	L-ascorbate oxidase
225043	SufI	1.72e-54	91	632	31	449	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].
215324	PLN02604	5.53e-53	100	630	29	545	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPX44859.1|AA1	5.22e-268	4	649	12	649
QMW37919.1|AA1	7.18e-236	31	631	20	598
QRD88142.1|AA1	2.13e-234	31	631	37	615
QMW25836.1|AA1	2.13e-234	31	631	37	615
CAK44017.1|AA1	6.37e-215	30	631	13	586

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	3.51e-49	95	642	2	489	Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_B Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_C Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_D Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_E Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_F Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae]
1AOZ_A	5.51e-47	96	628	4	520	Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1AOZ_B Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1ASO_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASO_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASP_A X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASP_B X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASQ_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASQ_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo]
5LM8_A	1.50e-44	110	629	38	502	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.53e-44	110	629	39	503	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	3.09e-44	110	629	66	530	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|I1RMG9|FET3_GIBZE	4.67e-61	94	625	23	490	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
sp|K7NCS2|FETC_EPIFE	5.77e-58	92	625	19	489	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|E9R598|FETC_ASPFU	8.53e-57	94	626	21	487	Iron transport multicopper oxidase fetC OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=fetC PE=2 SV=1
sp|Q55P57|LAC1_CRYNB	7.45e-56	93	647	59	573	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|Q6CII3|FET3_KLULA	5.71e-55	95	629	34	503	Iron transport multicopper oxidase FET3 OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=FET3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999978	0.000011

TMHMM  Annotations     

Start	End
33	55