CAZyme Information: KIX04681.1

Basic Information

• Species: Rhinocladiella mackenziei
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Rhinocladiella; Rhinocladiella mackenziei
• CAZyme ID: KIX04681.1
• CAZy Family: GH2
• CAZyme Description: Rhinocladiella mackenziei CBS 650.93 unplaced genomic scaffold supercont1.4, whole genome shotgun sequence [Source:UniProtKB/TrEMBL;Acc:A0A0D2ING9]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
602	KN847478|CGC13	67206.89	5.3277

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_RmackenzieiCBS650.93	11418	1442369	36	11382

• Gene Location: location=KN847478:1173205-1175698(+)

Full Sequence      

MSISTAQMWLFLLIFTSILQSTLSSNVTYDFNITWVAVNPDGAFTRPTIGVNGQWPPPQI
HANLGDTITVNVLNLLGNQSTSLHFHGLFMNGSTHMDGPAQVSQCAIAPGSSFTYRFRAE
QVGTYWYHSHTQSQYPDGLRAPLIIHDPDNPYAEQFDQELVLTVSDWYHQQMADLIPQYM
KSGHMMSHEPVPDASLLNDTHDLQVGVVPGKTYLVRMVNMAAFAGQYFWIEGHTMTIVEI
DGVYTRATEAEMIYLASGQRCSFLLTTKSQSSHNYPFVASMDQSLFMMAGHVNSDVTGWL
VYDSAHPLPRPKKIDQFNPTDDMTIVPYDEMQLLPKADKSISLNLEMRHSQGATYYMFND
ISYRSPEIPSLYTALTSGNSATDPAVYGISTNPFVLERNDVVELVLYNRHMLRHPFHLHG
HHFQAIYRSEEYGGRYEDSGVTEANLPQKPIRRDTLVLPPGGSMVIRFRADNPGVWLFHC
HMEWHVHTGLVATMIEAPIELQQQRRSQPLPADHIGACVATGTPATENDPGQVDDLLDVQ
NENDPTQGKPEGVSISDAVVSLAAGSVLVMTGLVFLVWFGVKNWGARKAQYAPLAMNVEE
DL

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	46	379	2.3e-133	0.9910979228486647

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259966	CuRO_3_Fet3p	2.61e-78	338	498	1	160	The third Cupredoxin domain of multicopper oxidase Fet3p. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p 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 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	8.75e-75	29	490	4	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.
225043	SufI	1.19e-66	31	499	40	451	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].
259920	CuRO_1_Fet3p	8.53e-66	27	146	1	121	The first Cupredoxin domain of multicopper oxidase Fet3P. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) and a four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the exocellular space and the carboxyl terminus in the cytoplasm. The periplamic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p 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 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
177843	PLN02191	2.13e-64	8	496	5	546	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QOX58957.1|AA1_2	2.87e-238	5	592	4	589
AHZ65140.1|AA1_2	2.41e-235	21	599	4	579
UQC79471.1|AA1_2	4.38e-234	24	600	19	593
AUS45841.1|AA1_2	1.08e-232	17	581	18	582
UPL01783.1|AA1_2	1.25e-230	21	599	15	590

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	5.41e-134	28	543	2	525	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]
5NQ8_A	3.98e-75	30	496	28	488	Crystal structure of laccases from Pycnoporus sanguineus, izoform II [Trametes coccinea],5NQ9_A Crystal structure of laccases from Pycnoporus sanguineus, izoform II, monoclinic [Trametes sanguinea],5NQ9_C Crystal structure of laccases from Pycnoporus sanguineus, izoform II, monoclinic [Trametes sanguinea]
3KW7_A	1.50e-73	30	496	7	472	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]
5NQ7_A	1.59e-73	30	496	28	488	Crystal structure of laccases from Pycnoporus sanguineus, izoform I [Trametes sanguinea]
2XYB_A	7.07e-73	30	518	7	486	CRYSTAL STRUCTURE OF A FULLY FUNCTIONAL LACCASE FROM THE LIGNINOLYTIC FUNGUS PYCNOPORUS CINNABARINUS [Trametes cinnabarina]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|K7NCS2|FETC_EPIFE	4.18e-227	24	583	20	578	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	7.31e-223	29	580	27	576	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|E9R598|FETC_ASPFU	1.27e-208	9	593	5	585	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|P78591|FET3_CANAX	1.27e-143	13	583	9	581	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1
sp|Q6CII3|FET3_KLULA	1.21e-133	21	590	20	595	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 SP

Other	SP_Sec_SPI	CS Position
0.000221	0.999745	CS pos: 24-25. Pr: 0.9786

TMHMM  Annotations     

Start	End
559	581