CAZyme Information: CPAR2_304050-T-p1

Basic Information

• Species: Candida parapsilosis
• Lineage: Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; Candida parapsilosis
• CAZyme ID: CPAR2_304050-T-p1
• CAZy Family: GH72
• CAZyme Description: Ortholog(s) have role in meiotic cell cycle, synaptonemal complex organization

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
613	Contig005806_C_parapsilosis_CDC317|CGC4	69765.41	4.7756

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CparapsilosisCDC317	5984	578454	147	5837

• Gene Location: location=Contig005806_C_parapsilosis_CDC317:970064-971905(+)

Full Sequence      

MLFQVTLLLSFLYSLVASKTHTYNWDIGYVKANPDGMHERRMIGINNQWPNPTIRVKQHD
RVIVNLYNGLPDRNASLHFHGLMQRGFNGEDGPEMVTQCPIGPGSTITYDFNVGNQTGTY
WYHSHSGTQYGDGLRGMIIIEYADKEDEPYLYDEDVSLTVNDHYHLESPEIIKQFLSRFN
PTGAEPIPQNSLFNETKNVTWYVKPDTTYLLRIVNMGLFVSQYLYIEDHKFVIVEIDGVA
VEPYEVDSIYITVGQRYVALVKTKSRSDVNYRFINALDAEMLDFLPEDLQLVSTNYLVYD
KDAAKPKHYPYYDFEKFTNSLKGFNDFDLKPLSGEKLLPEPDITIQVNFSMEVLGNGVTY
ALFNDKSYVPPKVPILYTVLSSGALSTNPEIYGSNTNTFVLQGNETVELILNNHDPGKHA
FHLHGHNFQVISRSPGTDDEDHPVEFNPNNDTMTDYPEYPMIRDTVEVNSNGYFVLRFKA
DNPGVWFFHCHVDWHLEQGLALVLVEAPEEIQAHQKHISANHVQVCRNVSVPVQGNAAAN
MDFLDLSGQNLQQPPLPEGFTAKGYFAMALCTLIALYGIWSIYKYGIEDVSKDNSAEVIE
RLYKILDEHDGGR

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	39	383	2e-140	0.9910979228486647

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225043	SufI	4.14e-83	9	509	24	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].
274555	ascorbase	2.60e-81	23	511	4	528	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.
259966	CuRO_3_Fet3p	1.82e-80	342	508	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	2.02e-72	154	301	1	148	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.
177843	PLN02191	3.61e-69	11	511	7	551	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCG24206.1|AA1_2	0.0	3	613	4	614
CAX41429.1|AA1_2	1.55e-311	15	610	17	620
AOW29490.1|AA1_2	2.56e-310	15	610	17	619
ABN68144.2|AA1_2	2.47e-270	16	606	17	610
QFZ52610.1|AA1_2	1.71e-268	16	612	15	620

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	4.09e-191	19	559	1	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]
1V10_A	2.90e-62	26	506	27	489	Chain A, Laccase [Rigidoporus microporus]
5Z1X_A	4.42e-60	21	513	9	472	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]
5NQ7_A	1.41e-59	32	515	36	498	Crystal structure of laccases from Pycnoporus sanguineus, izoform I [Trametes sanguinea]
3KW7_A	2.68e-59	27	506	10	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P78591|FET3_CANAX	2.52e-229	7	607	10	594	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1
sp|Q6CII3|FET3_KLULA	1.23e-203	20	602	27	602	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	6.17e-200	2	603	5	598	Iron transport multicopper oxidase FET3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET3 PE=1 SV=2
sp|Q96WT3|FET3_CANGA	1.78e-196	4	590	2	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	3.18e-191	10	610	5	616	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 SP

Other	SP_Sec_SPI	CS Position
0.000213	0.999751	CS pos: 18-19. Pr: 0.9751

TMHMM  Annotations     

Start	End
564	583