CAZyme Information: EPrPAT00000017047-p1

Basic Information

• Species: Pythium aphanidermatum
• Lineage: Oomycota; NA; ; Pythiaceae; Pythium; Pythium aphanidermatum
• CAZyme ID: EPrPAT00000017047-p1
• CAZy Family: GH16
• CAZyme Description: Ubiquitin carboxyl-terminal hydrolase.

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
974	PaphDAOMBR444_SC0125|CGC2	108846.94	7.9712

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PaphanidermatumDAOMBR444	12363	1223555	58	12305

• Gene Location: location=PaphDAOMBR444_SC0125:45820-49159(-)

Full Sequence      

MPSRDDASATAIGAKRPLALHPDAAQACRHMEILGDATWLSRCLHDTLRRARDSGTLSRA
WLDAVNESAWRRQRVMCLSCDFEGAREHADVPTQCFMTHAIMTDHHYGVLVTKKQLFCAR
CVDFVYLPSPTGPATPSSRLPPSSSPQLRRRLLRSSARRGLVNMGNSCYMNAVLQALAHN
PLLQHEYFVARTHNTTICEQRRRKKQPSGEIADAPVCMGCEMSSLLQMMFPSPRATLTVR
HLTSPVVPQAFLEAFWAYDRTFVGAKQQDAHEFLVSLLNGIHSHTYPLGASASGSLNAPL
VDTEAVHSPRFTPTGTSLCDCVVHQNFAGVFRSEVLCVFCENVTSTYDPFLDVSLSLESE
KKPSQDDSAVAEELSLSLLLERFTHAERLKGANQVYCRRCCRYVDVLKRLVLHKLPNVLV
VHLKRLDFQSCRKRSDAVAFPLRGLDLKAFCVGFEGQRTTPTKNLKLRKSLGLLSPATPP
MGHAGDASYDLAAVVSHHGDAIDGGHFTTFVHTSHDVPLAREGSSETTQWLHVDDCAVTP
VAEAAVRRTQAYLLFYVRRRLFAIEDTAQQKRSLPSAVHVLIGVKTSLVHGASSRRAIRE
TWGSLASPDEARVVFLGCSPDLTQLNASDAERMQREIAQETQRYGDLLVHELVGCRDAYE
ELANKVLAFFQWTTSQRQPRDTKAFVMVVDDDVYLRIDLLLRLLQDPRVDKTRFYGGQVW
AAQYGRAMEPYRKPQHHKYYLSYDQYPMSQLPPFANGPHYIASADIAAFLGSHRDMFHGV
GGHRDGRDGAALDDVSMALWLLAMQIHPMHLPQFQNLRDSMCRNELVSYADISVDGLRHI
HNNLMQNRSFCDGFTYATWLKRSPSNGPATRPDEDLRLSSLTISWHSELDALTDDVHVSL
ELRTIEKSESVRINYVPAQASVFSVCAVAYDLGNAKSVIRDISMNAFCRQFIAALRVAAT
HAPRSRVFCDVSSS

Enzyme Prediction     

EC	2.4.1.122:14

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT31	594	810	1.1e-35	0.984375

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
239125	Peptidase_C19D	1.27e-73	160	557	2	328	A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
395355	UCH	2.80e-64	160	556	2	306	Ubiquitin carboxyl-terminal hydrolase.
239126	Peptidase_C19E	1.84e-56	160	557	3	304	A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
239072	Peptidase_C19	5.95e-45	160	557	1	255	Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
239139	Peptidase_C19R	3.86e-44	160	556	1	229	A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UJR15328.1|CBM21	1.27e-17	160	556	184	492
AHH38393.1|GT31	1.18e-15	594	848	97	326
AWO95575.1|GT31	6.51e-15	594	848	116	345
AWP13074.1|GT31	9.60e-14	594	848	95	324
AAI32529.1|GT31|2.4.1.122	3.04e-13	562	848	65	322

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4FIP_A	6.15e-44	76	561	64	475	Structure of the SAGA Ubp8(S144N)/Sgf11(1-72, Delta-ZnF)/Sus1/Sgf73 DUB module [Saccharomyces cerevisiae S288C],4FIP_E Structure of the SAGA Ubp8(S144N)/Sgf11(1-72, Delta-ZnF)/Sus1/Sgf73 DUB module [Saccharomyces cerevisiae S288C],4FK5_A Structure of the SAGA Ubp8(S144N)/Sgf11/Sus1/Sgf73 DUB module [Saccharomyces cerevisiae S288C]
3M99_A	2.52e-43	76	561	59	470	Structure of the Ubp8-Sgf11-Sgf73-Sus1 SAGA DUB module [Saccharomyces cerevisiae],6T9L_K SAGA DUB module bound to a ubiqitinated nucleosome [Saccharomyces cerevisiae S288C]
3MHH_A	2.77e-43	76	561	64	475	Structure of the SAGA Ubp8/Sgf11/Sus1/Sgf73 DUB module [Saccharomyces cerevisiae],3MHS_A Structure of the SAGA Ubp8/Sgf11/Sus1/Sgf73 DUB module bound to ubiquitin aldehyde [Saccharomyces cerevisiae],4FJC_A Structure of the SAGA Ubp8/Sgf11(1-72, Delta-ZnF)/Sus1/Sgf73 DUB module [Saccharomyces cerevisiae S288C],4FJC_E Structure of the SAGA Ubp8/Sgf11(1-72, Delta-ZnF)/Sus1/Sgf73 DUB module [Saccharomyces cerevisiae S288C],4W4U_A Structure of yeast SAGA DUBm with Sgf73 Y57A mutant at 2.8 angstroms resolution [Saccharomyces cerevisiae CEN.PK113-7D],4W4U_D Structure of yeast SAGA DUBm with Sgf73 Y57A mutant at 2.8 angstroms resolution [Saccharomyces cerevisiae CEN.PK113-7D],4WA6_A Structure of yeast SAGA DUBm with Sgf73 N59D mutant at 2.36 angstroms resolution [Saccharomyces cerevisiae S288C],4WA6_D Structure of yeast SAGA DUBm with Sgf73 N59D mutant at 2.36 angstroms resolution [Saccharomyces cerevisiae S288C]
4ZUX_U	3.86e-42	76	561	60	471	SAGA DUB module Ubp8/Sgf11/Sus1/Sgf73 bound to ubiqitinated nucleosome [Saccharomyces cerevisiae S288C],4ZUX_Z SAGA DUB module Ubp8/Sgf11/Sus1/Sgf73 bound to ubiqitinated nucleosome [Saccharomyces cerevisiae S288C],4ZUX_e SAGA DUB module Ubp8/Sgf11/Sus1/Sgf73 bound to ubiqitinated nucleosome [Saccharomyces cerevisiae S288C],4ZUX_j SAGA DUB module Ubp8/Sgf11/Sus1/Sgf73 bound to ubiqitinated nucleosome [Saccharomyces cerevisiae S288C]
6AQR_A	4.16e-42	76	561	64	475	SAGA DUB module Ubp8(C146A)/Sgf11/Sus1/Sgf73 bound to monoubiquitin [Saccharomyces cerevisiae S288C]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P0C8Z3|UBP22_BOVIN	3.62e-48	159	561	165	511	Ubiquitin carboxyl-terminal hydrolase 22 OS=Bos taurus OX=9913 GN=USP22 PE=2 SV=1
sp|Q9UPT9|UBP22_HUMAN	2.74e-47	159	561	176	522	Ubiquitin carboxyl-terminal hydrolase 22 OS=Homo sapiens OX=9606 GN=USP22 PE=1 SV=2
sp|B1AY15|UBP51_MOUSE	9.19e-47	77	559	205	656	Ubiquitin carboxyl-terminal hydrolase 51 OS=Mus musculus OX=10090 GN=Usp51 PE=1 SV=1
sp|Q5DU02|UBP22_MOUSE	1.68e-46	159	561	176	522	Ubiquitin carboxyl-terminal hydrolase 22 OS=Mus musculus OX=10090 GN=Usp22 PE=2 SV=2
sp|Q6GNI6|UB22A_XENLA	7.31e-46	159	561	174	520	Ubiquitin carboxyl-terminal hydrolase 22-A OS=Xenopus laevis OX=8355 GN=usp22-a PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000046	0.000011

TMHMM  Annotations     

There is no transmembrane helices in EPrPAT00000017047-p1.