CAZyme Information: ASPSYDRAFT_146967-t33_1-p1

Basic Information

• Species: Aspergillus sydowii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus sydowii
• CAZyme ID: ASPSYDRAFT_146967-t33_1-p1
• CAZy Family: PL4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1073		119727.17	5.2102

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AsydowiiCBS593.65	13717	1036612	138	13579

• Gene Location: location=KV878584:1146447-1150917(+)

Full Sequence      

MVSFSFLTEVILLVASCFISAVAGDASYVAVEKLQNAPVGWLRGPAAPPSKMMKFHIAVR
PEKTAEFEQMVLDMSTPGHPNYGQHMKRDEVRDFVRPSDYTMEQVLSWLDSENISKESMK
IRGNWVEVTMPVSQAESLMKTRFYRYTHRATRRNTIRTLDYSVPREMRPYIQTIQPTTHF
EQPNAQVIHPTFRPISMSPSSSHREPTVDCSSQVTPDCLRELYGLYDTEAKPDPRNRLGI
SGYLDQYARYSDFHKFMGMFAPNRTDANFTVETISGGLNTQNSSIGSTEASLDVQYAIAL
AYNPLATYYTTGGRGPFIPEAGESGESESTNEPYLEQLHYLLDLSDDELPAVLSTSYGEA
EQSVPVSYSEASCHLFAQLGARGVSILFSSGDDGVGGSCLTNDGTNRTRFQPIFPASCPF
VTAVGGTYKTDPEIAIDFSGGGFSDRFKRPAYQDASVGSYLEKLGNKWEGLYNPEGRGIP
DVAAQALNYIIVDHGKTYEIGGTSASAPTFAAIVSRLNAERLKDGNPRLGFLNPWLYSLN
QTGFTDIVDGHSSGCANSNIGGPDGYATWNATTGWDPATGLGTPFYNTLVKVARELATFP
RPLRLLSQALLIVGFVFIACQTALNLHTQLNVPPPRTLRPGPLYKLDQAQQSGAHSAPVC
ETFPAAAFAEDGIQVVLKIGAAETDRLMASHVNGSTSCIPNLLVVSDISQTLGQFYAHDV
LADVIHILSEGDRQIYQHQRESYYYWNTGLQPNQAARNLDRYKFLAMVEYAYAQNPSAKW
YVFTETDTTVLWENMAQLLERFNWADPVYIGSPSPGRRWESHFGSRSTFFVYGGSGIVLS
VTAIEKLLQGNRGESGAGDLTSQLLINKYQDLVRDDCCGDSILGYVSFQEGVKIQGQWPM
FNPHPLHKTPLSKAYWCQPAISFHKSDPIAARELWDWEQKWRQERGPDQQQRPILYRDVV
DFFDFASTPVRSDWNNVELDAFDAPTEEAHESFDSCKEACQNHPECFQFTHYRKQCRMSI
IINFGIHAPPSKSDMTEGVHSIAGWDVDKIQKFKIDHDCNEVEWPEPSIERIY

Enzyme Prediction     

No EC number prediction in ASPSYDRAFT_146967-t33_1-p1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173788	Peptidases_S53	4.33e-123	214	584	2	355	Peptidase domain in the S53 family. Members of the peptidases S53 (sedolisin) family include endopeptidases and exopeptidases sedolisin, kumamolysin, and (PSCP) Pepstatin-insensitive Carboxyl Proteinase. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of Asn in subtilisin. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. Characterized sedolisins include Kumamolisin, an extracellular calcium-dependent thermostable endopeptidase from Bacillus. The enzyme is synthesized with a 188 amino acid N-terminal preprotein region which is cleaved after the extraction into the extracellular space with low pH. One kumamolysin paralog, kumamolisin-As, is believed to be a collagenase. TPP1 is a serine protease that functions as a tripeptidyl exopeptidase as well as an endopeptidase. Less is known about PSCP from Pseudomonas which is thought to be an aspartic proteinase.
401284	Pro-kuma_activ	3.51e-47	40	180	2	142	Pro-kumamolisin, activation domain. Members of this family are found in various subtilase propeptides, and adopt a ferredoxin-like fold, with an alpha+beta sandwich. Cleavage of the domain results in activation of the peptide.
206778	Pro-peptidase_S53	1.59e-41	40	177	1	139	Activation domain of S53 peptidases. Members of this family are found in various subtilase propeptides, such as pro-kumamolysin and tripeptidyl peptidase I, and adopt a ferredoxin-like fold, with an alpha+beta sandwich. Cleavage of the domain results in activation of the peptidase.
214928	Pro-kuma_activ	1.34e-30	46	178	5	136	Pro-kumamolisin, activation domain. This domain is found at the N-terminus of peptidases belonging to MEROPS peptidase family S53 (sedolisin, clan SB). The domain adopts a ferredoxin-like fold, with an alpha+beta sandwich. Cleavage of the domain results in activation of the peptidase.
227270	COG4934	1.10e-29	65	589	60	552	Serine protease, subtilase family [Posttranslational modification, protein turnover, chaperones].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS22284.1|GT31	0.0	597	1073	6	488
QRD83812.1|GT31	5.33e-88	652	1073	75	477
QMW32351.1|GT31	5.33e-88	652	1073	75	477
BAE62206.1|GT31	7.38e-88	652	1073	75	477
UDD57328.1|GT31	7.38e-88	652	1073	75	477

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3EDY_A	2.32e-68	32	591	7	539	Crystal Structure of the Precursor Form of Human Tripeptidyl-Peptidase 1 [Homo sapiens]
3EE6_A	3.15e-68	18	591	11	558	Crystal Structure Analysis of Tripeptidyl peptidase -I [Homo sapiens],3EE6_B Crystal Structure Analysis of Tripeptidyl peptidase -I [Homo sapiens]
1T1G_A	2.66e-27	350	602	122	364	Chain A, kumamolisin [Bacillus sp. MN-32]
1GT9_1	4.29e-27	350	584	122	346	High resolution crystal structure of a thermostable serine-carboxyl type proteinase, kumamolisin (kscp) [Bacillus subtilis],1GT9_2 High resolution crystal structure of a thermostable serine-carboxyl type proteinase, kumamolisin (kscp) [Bacillus subtilis],1GTG_1 Crystal structure of the thermostable serine-carboxyl type proteinase, kumamolysin (kscp) [Bacillus sp. MN-32],1GTJ_1 Crystal structure of the thermostable serine-carboxyl type proteinase, kumamolisin (KSCP) - complex with Ac-Ile-Ala-Phe-cho [Bacillus sp. MN-32],1GTJ_2 Crystal structure of the thermostable serine-carboxyl type proteinase, kumamolisin (KSCP) - complex with Ac-Ile-Ala-Phe-cho [Bacillus sp. MN-32],1GTL_1 The thermostable serine-carboxyl type proteinase, kumamolisin (KSCP) - complex with Ac-Ile-Pro-Phe-cho [Bacillus sp. MN-32],1GTL_2 The thermostable serine-carboxyl type proteinase, kumamolisin (KSCP) - complex with Ac-Ile-Pro-Phe-cho [Bacillus sp. MN-32]
1SIO_A	6.54e-27	240	602	33	364	Structure of Kumamolisin-As complexed with a covalently-bound inhibitor, AcIPF [Alicyclobacillus sendaiensis],1SIO_B Structure of Kumamolisin-As complexed with a covalently-bound inhibitor, AcIPF [Alicyclobacillus sendaiensis],1SIO_C Structure of Kumamolisin-As complexed with a covalently-bound inhibitor, AcIPF [Alicyclobacillus sendaiensis],1SN7_A Kumamolisin-As, Apoenzyme [Alicyclobacillus sendaiensis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q70GH4|SED3_ASPFU	1.11e-267	1	600	1	596	Tripeptidyl-peptidase sed3 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=sed3 PE=1 SV=1
sp|C5FRX4|SED4_ARTOC	8.00e-201	13	595	19	600	Tripeptidyl-peptidase SED4 OS=Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) OX=554155 GN=SED4 PE=3 SV=1
sp|C5FTQ5|SED3_ARTOC	2.89e-199	27	596	26	595	Tripeptidyl-peptidase SED3 OS=Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) OX=554155 GN=SED3 PE=3 SV=1
sp|D4AIK6|SED4_ARTBC	6.82e-199	31	592	35	597	Probable tripeptidyl-peptidase SED4 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=SED4 PE=1 SV=1
sp|D4D9U2|SED4_TRIVH	6.82e-199	31	592	35	597	Probable tripeptidyl-peptidase SED4 OS=Trichophyton verrucosum (strain HKI 0517) OX=663202 GN=SED4 PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000435	0.999537	CS pos: 23-24. Pr: 0.9818

TMHMM  Annotations     

There is no transmembrane helices in ASPSYDRAFT_146967-t33_1-p1.