CAZyme Information: PV06_11743-t43_1-p1

Basic Information

• Species: Exophiala oligosperma
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala oligosperma
• CAZyme ID: PV06_11743-t43_1-p1
• CAZy Family: GT71
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
778		85531.15	4.6868

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EoligospermaCBS72588	11938	N/A	45	11893

• Gene Location: location=KN847389.1:15065-19448(+)

Full Sequence      

MAFWGVITPLFLLTIFASYSLAAPYLNGTTRTYYVAAVEQDWDYMPTGMDMVNAVPIEDS
PQAAAVAGQNGQRIGHVYKKVLFREYTDGGFTAQTPRPSWLGMLGPIIRAEVGDTVKVVF
RNMASHNHTMHPHGFRYAKSSEGLSDAMQMFDGNAVPPGGTWTYIWEAPERSGPGPLDPP
GLAWTYHSDAAGTQDVFSGLVGASIIYRPGELAKHTLDVPAPPGSNLIEEVLTLFLIVDE
NQSYYIDENTLNRTSISEGQLQVNRMDAGFQESNLKHSINGFMFGNLMGINLTAGTQATW
HVEALGNVVNAHTPHWHGNTLMWAQQRIDIVSTFGLLRRTRDGVSREVYLINDQQPGPLI
EADEGDDLEIFVLNNLPVEQTIHWHGLLQRGTPDMDGVPGVTQFPIPPQGNFTYRFSTGS
EYGFYWYHSHFRAYYNDAVRGPLLIRPSPLRRRSFEGFARDSTELDAMLQAERAATPLVL
TDWYHRLSDVVYEEYFTTDAFPQCVDSLLANGFGRVQCLPESVLQAGPGLRLESIVASDP
HDPLSTPVPTASASMSDMPIDTSSGIGTSMETMSSSPLSMDSMSMDISMNMHKRADHATM
TAADSTVSGMTMLSASSTSTSPMETMSGIADMSSLGPKGCSMQMMFKPGFNTSSLPPETC
INTASELFKFDADASQGWAAFHLVNAGAVSRLSVSLDGHSMFVYAADGLYVEPQEVKVLH
ISIGQRYSVMVRLDQEPGAYYLRFASYPYGDMQQVIEDQAILSYQTNGTNKKEYGPSE

Enzyme Prediction     

No EC number prediction in PV06_11743-t43_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	344	518	2e-49	0.4441340782122905

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259862	CuRO_1_ceruloplasmin_like	9.69e-65	31	208	1	176	Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins. This family includes the first, third, and fifth cupredoxin domains of ceruloplasmin and similar proteins including the first, third and fifth cupredoxin domains of unprocessed coagulation factors V and VIII. Ceruloplasmin (ferroxidase) is a multicopper oxidase essential for normal iron homeostasis. It functions in copper transport, amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains and exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. Human Factor VIII facilitates blood clotting by acting as a cofactor for factor IXa. Factor VIII and IXa forms a complex in the presence of Ca+2 and phospholipids that converts factor X to the activated form Xa.
259884	CuRO_1_ceruloplasmin	2.89e-58	31	206	1	180	The first cupredoxin domain of Ceruloplasmin. Ceruloplasmin is a multicopper oxidase essential for normal iron homeostasis and copper transport in blood. It also functions in amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains with six copper centers; three mononuclear sites in domain 2, 4 and 6 and three in the form of trinuclear clusters at the interface of domains 1 and 6. Ceruloplasmin exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the first cupredoxin domain of ceruloplasmin.
259919	CuRO_1_Abr2_like	7.45e-57	342	446	13	117	The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Like other related multicopper oxidases (MCOs), laccase 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.
259886	CuRO_3_ceruloplasmin	5.95e-55	28	215	1	193	The third cupredoxin domain of Ceruloplasmin. Ceruloplasmin is a multicopper oxidase essential for normal iron homeostasis and copper transport in blood. It also functions in amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains with six copper centers; three mononuclear sites in domain 2, 4 and 6 and three in the form of trinuclear clusters at the interface of domains 1 and 6. Ceruloplasmin exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the third cupredoxin domain of ceruloplasmin.
259891	CuRO_1_Ceruloplasmin_like_1	1.24e-53	31	210	1	175	cupredoxin domain of ceruloplasmin homologs. Uncharacterized subfamily of ceruloplasmin homologous proteins. Ceruloplasmin (ferroxidase) is a multicopper oxidase essential for normal iron homeostasis. Ceruloplasmin also functions in copper transport, amine oxidase and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains and exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the first domain of the triplicated units.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPL00042.1|AA1	2.26e-156	342	767	34	430
ATY66532.1|AA1	1.76e-150	333	764	42	434
QOD95012.1|AA1	1.13e-146	338	764	37	426
QPG98040.1|AA1	6.19e-144	339	764	37	430
QLI72976.1|AA1	1.35e-140	339	769	43	446

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5N4L_A	2.15e-51	31	340	707	997	Rat ceruloplasmin trigonal form [Rattus norvegicus],5N4L_B Rat ceruloplasmin trigonal form [Rattus norvegicus]
5N0K_A	2.30e-51	31	340	726	1016	Rat ceruloplasmin orthorhombic form [Rattus norvegicus]
1KCW_A	1.35e-48	31	340	713	1003	X-Ray Crystal Structure Of Human Ceruloplasmin At 3.0 Angstroms [Homo sapiens]
2J5W_A	1.40e-48	31	340	732	1022	Ceruloplasmin revisited: structural and functional roles of various metal cation binding sites [Homo sapiens],4EJX_A Structure of ceruloplasmin-myeloperoxidase complex [Homo sapiens]
4ENZ_A	1.40e-48	31	340	732	1022	Structure of human ceruloplasmin at 2.6 A resolution [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|B3EWZ9|HEPHL_ACRMI	3.50e-65	27	368	728	1066	Hephaestin-like protein OS=Acropora millepora OX=45264 PE=1 SV=1
sp|Q3V1H3|HPHL1_MOUSE	2.82e-60	26	334	21	325	Ferroxidase HEPHL1 OS=Mus musculus OX=10090 GN=Hephl1 PE=2 SV=2
sp|Q6MZM0|HPHL1_HUMAN	5.50e-59	26	379	21	364	Ferroxidase HEPHL1 OS=Homo sapiens OX=9606 GN=HEPHL1 PE=1 SV=2
sp|Q920H8|HEPH_RAT	3.65e-56	19	334	14	326	Hephaestin OS=Rattus norvegicus OX=10116 GN=Heph PE=1 SV=1
sp|Q9BQS7|HEPH_HUMAN	3.66e-56	27	334	22	326	Hephaestin OS=Homo sapiens OX=9606 GN=HEPH PE=1 SV=3

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.116265	0.883693	CS pos: 22-23. Pr: 0.8512

TMHMM  Annotations     

Start	End
2	24