CAZyme Information: CXQ85_002345-t46_1-p1

Basic Information

• Species: [Candida] haemuloni
• Lineage: Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; [Candida] haemuloni
• CAZyme ID: CXQ85_002345-t46_1-p1
• CAZy Family: GH72|CBM43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2785	PKFO01000003|CGC14	312566.22	5.0578

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_ChaemulonisB11899	5409	N/A	160	5249

• Gene Location: location=PKFO01000003:1592585-1601118(-)

Full Sequence      

MATDIEKVIANFDKEEATEYASELYLLLKNYAEAEDDLNYQDIWSQLTRLIHAYCNLKDN
EGDTKNKAKAIEDNEKFRSMGSLNLFKLISRNLIIVLGKLTNKIYDTANDLFPYLTLTDN
GHLSFSGKAASVVLIDLFENYPHHLTSLLSFGATVAYKLIKKNSSIDSNIIYLLASILKN
ASKADVDDKFQAKLVKIFSKNILSSALKNNAADSEANNSSVLQVEYYILGLKNLLIMSSA
SHYEQLLEFSASSTSGSKLKPEAIMTQQHQFQIGLLNNHKKVIQFGFSSQFPQVRHATVA
LLSHLLHNFVDTGKFNAIEYLIEAYPFPSSSTWNNQAHHRIENEVELGFPSRKDHNIIST
HNSEALIDSKINLKNLQYGYVESMVMYMQLQQFQDWSFYASSITAIFDLILSKFSGLNHA
PHVPTSEWNVVLAQWTIVVEFLIKESGASIHEVVAQYIVNRFSASADSEDFSRSASPDPR
SSKPRRQEASLFRFKSTKKTKAKSMDNSHITPYTNPYQASLLLSVVNLLVPYAINFTSID
NSQPEDSKVDGEAAEEGDETTNKVLDGETALPARGNDYISNLLLSLLVNDSEQIRNHATS
SLLLYANVNKSQSNSLILQLFQSVTSELNSDLRSESSSEKNVSGFQAVRLFSNSLALSSL
IKQADSTLLQNSTIAKILSFCTQNLKHSSNANKKFLTNAACWIIMSSLVTFNETSEFVKL
NSSQFLVFWKNLLTSQFISADIGNMSDNAQLSEVMNNLTLRSLSLICLHNYIDSAQSSNE
LSRQLQFLLVKSYNYLTYLESTFESIGLLTSFNAQSFNESEFNPNLVGNLIFSNFNTATS
LPAQNRLTSLILHNKKVVLSGFIKLAPTLKRDVNSSLVVFLTRVFADAKCFSRLPVTDAL
KEKAKSSKSKSSTTKVAHENASLVKLEEEYNYDFGLTSKFRYVESNVISEPETVAANAEP
SGEGDLRGWASSFEERVNDGSYFAFDNDPAVFLLKGSSETPTRSRGIITSIVDKSIELFQ
YVFPNLTFKIQFSLLEQLRASLTQKNSDPLRHTAIQINDSVALNGLLKYYTAIGGFMDGQ
ILNAVLDTVEKINSDNIEVNLLNAETVGMVSKMLSKDDVDGTVARYINDIVKQSEPSARG
KLLIYLASIFKFTHSGFSNILDVVLQLMKDPNPIMAYYSSKASAILLENALGNEHLVKEL
IHQVYLNTLNDDFGLNLDNGFLANLRASYKFHAVYSRIVSYSVTSLGPALKSCDKELKVE
IRNLLILFANGVGSYDSDEYVNVVRDVLVTFQEILIFDLSFVPEFSKWFHSEAVDVIKGN
AKIGVGVLGPTSPCHESIFPVSTCFGLYELAFASLLEMTKVGISTLQKENVNLAWIAMEI
HPCDSLKQLIKYWVDSNPEMVWFAQVNALFKSSTRKLTGPFVEHNYQVKLLPLTQRQKKK
NTGGIDLKDDEVRNIVNEDQDTEDKNEPITWEFRSFLYDLIIQILSAAEKKPVLMSSLTN
KIQEVVRMSFLGTTSPIPAINLKGVALLDNALSLFGHLEDPLYPGISILEQQQAQIISAL
VPCYGPQSNAELIVNAISVSSKFINLPRIKFYSKQRILKTLVCLLEEVSSNKFLKFTYLE
AMSEFSRKAIQLSILDCWASVRIDIQQHAEDGSDEFGAILSKYSELLISLWILALNDLSS
LRYTQPTSREVGLYSDCWLDFVEVLTIELEEDSTRVTKLLQDDSKDFFFVLFCQCAESLI
KNQNTTRVLSSVKRLVSIPELVEHLLADDIFGEVIDLLDRLILVEEETESKIEVIDIVST
LAKVHSGKVKNEENNEKLLELLRVAMLPLFSIFVFLREDFNHEDVTQQVALKRCSSASNL
LILKKSLSAAIGILKCFQGEVKSNICSCLFYLFAKFYEHDDDNLIGVILPYLKLVVNELG
DDKTETVQSFFQILKRQGFFSATRNKNNHVITVVLLLTNSDIKLDADESKILANAILRLI
EDSEYASAGIQSIKSLLRQSDSPLQSLIVKQIVQTLLLQLAGDGKDVKIDLRLAFEIIIV
FSQSEGVKNDTSKIVPLYAALIPLLVKHDVAGTIDGDYLHGKTVLLLTKNPEAFKTVVNE
YLDESQKATAEKLVKKTRGHTQVDSTNDSTIELKTFGHKYMMLHNLGKLTFSFLCLLPLA
LQAHAKTHEYNFDASLIKHNPDGVFEREVIGINGQWPLPIIRVAKHDRVVIHLTNSMTDR
NTSLHFHGLFMNNTNAMDGPENLTQCPIPPGHTFTYDFTVDAQAGTYWYHSHSGSQYSDG
LRAMFIIEEESPDLYPFKFDEEVPLTICDWYHSESSDIMKQFLSRYNPTGAEPIPQNSLF
NDTKNVTWNVEPDTTYFLRIVNMGMFVSQYLYIEDHTFTIVEVDGVYVEPVETSSLYITV
AQRYGVLVKTKKDVSNKAFRFVNVLDEPMLDLIPDDLQMISTNYVQYGHGDVEKPDPLEN
GKGKFDELEATLDPYDDFKLIPVRRDPLYAEHDLQIVLNFEMDNLGDGVNYAFFNGITYT
APKVPTLFSVLSAGEHANNAAIYGSNTNTYVLQPGEIVEIVLNNMDAGKHPFHLHGHVFQ
TVFRSEGTDDDDNPEVYDPSNPDHDKHPEFPMLRDTVMVHPNGFVKLRFKADNPGVWFFH
CHVDWHLEQGLAIVLVEDPQSIQENQQDIPKSHLEACSKLDIPVKGNAAGNYGDTEASWL
DLSGENVQMKPLPPGFTPKGYVAIVVCALAALFGIYTIYVYGMEDVNTEDAEHMVQKLYQ
ILGENDQAEPEERERLTEPSASANE

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	2186	2535	2.6e-146	0.9940652818991098

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225043	SufI	2.44e-86	2191	2659	56	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].
259966	CuRO_3_Fet3p	1.92e-83	2492	2659	2	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	9.21e-82	2167	2677	1	538	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.
259945	CuRO_2_Fet3p_like	2.49e-72	2301	2449	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.
215324	PLN02604	1.81e-70	2148	2657	4	546	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QWW22201.1|AA1_2	0.0	1	2764	2	2702
QWU86473.1|AA1_2	0.0	2152	2782	4	634
QRG36491.1|AA1_2	0.0	2149	2776	4	631
QEL59042.1|AA1_2	0.0	2149	2776	4	631
QEO20037.1|AA1_2	0.0	2149	2776	4	631

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	1.16e-183	2166	2715	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]
2QT6_A	1.65e-69	2181	2681	17	491	Chain A, Laccase [Lentinus tigrinus],2QT6_B Chain B, Laccase [Lentinus tigrinus]
5NQ7_A	3.58e-67	2180	2681	37	511	Crystal structure of laccases from Pycnoporus sanguineus, izoform I [Trametes sanguinea]
3KW7_A	1.09e-66	2181	2681	17	495	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]
5NQ8_A	3.40e-65	2180	2681	37	511	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	6.73e-208	2165	2746	21	582	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1
sp|Q6CII3|FET3_KLULA	3.63e-196	2163	2752	23	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|Q96WT3|FET3_CANGA	2.16e-192	2164	2746	16	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|P38993|FET3_YEAST	3.06e-192	2163	2755	19	593	Iron transport multicopper oxidase FET3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET3 PE=1 SV=2
sp|P43561|FET5_YEAST	3.48e-182	2149	2766	2	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 OTHER

Other	SP_Sec_SPI	CS Position
1.000034	0.000000

TMHMM  Annotations     

Start	End
2720	2742