CAZyme Information: CLUG_05225-t34_1-p1

Basic Information

• Species: Clavispora lusitaniae
• Lineage: Ascomycota; Saccharomycetes; ; Metschnikowiaceae; Clavispora; Clavispora lusitaniae
• CAZyme ID: CLUG_05225-t34_1-p1
• CAZy Family: GT66
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
553	CH408081|CGC2	62836.24	4.5095

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_ClusitaniaeATCC42720	6153	306902	217	5936

• Gene Location: location=CH408081:782291-783952(+)

Full Sequence      

MDPNMSPNALFLQDTLLYTTFVVQQTGTYWYHSHSGSQYSDGLRGIFIIEEKKKDDYPFD
FDVDLPLSVTDYYHEESKNIIKKMLSRYNPTGAEPIPQNALFNETRNVTWEIEPDTTYYL
RVVNMGMFVNQYLYIEDHTFTIVEIDGVYVEPREVDSLHISVAQRYGVLLKTKKNPEQKY
FRFVSILDETMLDFLPQELQVISTNYLQYPGSGKEPRPDTLKSGPREFEKLVNSLHPIDD
FDLRPLDKQVLLDDPDYQIVLNFTMDNLADGVNYAFFNGITYTPPKVPALYTVLSSGDLA
SNPTIYGSNTNTFVLQYGEVIEIVINNMDPGEHPFHLHGHVFQVISRSKGSDDEDDPEMF
DPENPEHTKYPSHPMVRDTVSVNPNGFLVIRFKAENPGVWFFHCHVDWHLEQGLAITLVE
APHEIQKKQNSTDVSHLEACNYFQIPTEGNAAGHRGPSEAHWLDLSGQNVQKKPLPEGFT
TKGYIAFVACALAAIFGLYSIYEYGVEDINTDNAEQVAAKLHKILQEYDGGESSARLIPN
NGATDEEHLASTT

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	13	298	1.3e-105	0.8011869436201781

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259966	CuRO_3_Fet3p	3.39e-88	256	422	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.
259945	CuRO_2_Fet3p_like	5.19e-67	67	209	5	146	The second 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 2 of 3-domain MCOs has lost the ability to bind copper.
225043	SufI	1.78e-63	18	422	117	450	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].
274555	ascorbase	1.44e-53	14	427	85	530	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.
400194	Cu-oxidase_2	1.02e-51	282	424	1	138	Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QFZ52610.1|AA1_2	0.0	21	553	110	642
QFZ46945.1|AA1_2	0.0	21	553	110	642
QFZ41264.1|AA1_2	0.0	21	553	110	642
QFZ29920.1|AA1_2	0.0	21	553	110	642
QFZ35570.1|AA1_2	0.0	21	553	110	642

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	8.14e-157	15	478	88	534	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]
3KW7_A	4.95e-47	14	420	91	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]
2XYB_A	1.14e-45	15	420	92	467	CRYSTAL STRUCTURE OF A FULLY FUNCTIONAL LACCASE FROM THE LIGNINOLYTIC FUNGUS PYCNOPORUS CINNABARINUS [Trametes cinnabarina]
5Z1X_A	1.52e-45	14	450	91	494	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]
5NQ8_A	5.51e-44	15	420	113	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P78591|FET3_CANAX	3.20e-178	14	509	108	582	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1
sp|Q6CII3|FET3_KLULA	4.38e-172	14	515	112	597	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
sp|P38993|FET3_YEAST	7.82e-166	15	548	109	626	Iron transport multicopper oxidase FET3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET3 PE=1 SV=2
sp|Q96WT3|FET3_CANGA	6.07e-165	14	509	104	586	Iron transport multicopper oxidase FET3 OS=Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) OX=284593 GN=FET3 PE=3 SV=1
sp|P43561|FET5_YEAST	1.66e-161	15	527	111	614	Iron transport multicopper oxidase FET5 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET5 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999929	0.000111

TMHMM  Annotations     

Start	End
484	506