CAZyme Information: SAPIO_CDS1160-t41_1-p1

Basic Information

• Species: Scedosporium apiospermum
• Lineage: Ascomycota; Sordariomycetes; ; Microascaceae; Scedosporium; Scedosporium apiospermum
• CAZyme ID: SAPIO_CDS1160-t41_1-p1
• CAZy Family: AA7
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1114		123786.09	4.9465

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SapiospermumIHEM14462	10920	N/A	2544	8376

• Gene Location: location=JOWA01000044:1167439-1172604(-)

Full Sequence      

MLIHICRARRLLIAVLLIIGLIILFSRDHGIPERRLSDGPEEVLNSTLGFGKIFVVNLPE
RTDRRDLMTLAAAVTGLDFTYIDGVRGANIPEKVLPPSPREKNVNWSGKTGSWRAHMNVL
QRIVQENLTSALIMEDDADWDIRLKSQAQAFALASQAYLQPLQNDPSHNLASLFPALSKT
LQEDAYVQELQNTPATKKPSTTSSPYGDDWDVIWLGHVGSHLPSDWTSRELNSNHAPLSL
LTILIPNDETVADKRHLKRHPFADRIDDFAARFEPHTRVVHEARGTAGIQAYAVSRRGAR
KLLLKFGLEEFTSSYDLMLRDWCDGAYEGERPVCITTQPPLMSQYYSKGGSDIHGIGGGY
FKKSGSTYIRYSVMLNLRKLVARRTDAGLAHIEGLADQWPDEGAILGHAPDAEDYLNHDL
KTRSDPNSPNYGNHLSPEEVLQFFEPSEDRVKAVTEWLVSEGISASRISRSRNKQWIQFD
ATVEEIEALFYADFHIYEHEDTGTVNVACSGYYLPESVRDHIDYITPGIRLMPEDSLVQP
QQKRTYEREVSPKDKQSRWRRHLGSDVLIKGRLPFANKSPGKSWSGKSKAVAGSEGTNQR
DGAEPEVEEPEVIPPYNDCIYSVTPECIRAQYDIPEGTKNRSDNKLGIFQGLNIRYWQGD
LDRYFHAVAPWVPKGSHPQNNLVNGAIGETSNRSESGAEAVMDFQLGMSLVWPQETVLWH
VDDPWYEEQHTQEPLIYKGYFNSWFPFSLYPAYNQTGNCLDPECLDPTYPNSNPGGYDGP
LACGTFEPTNIISISYSGSEASLPASYLRRQCAEIMKLALQGVTVVVSSGDYGVGSNRRD
PPPVGCLGENYDVFNPNFPGNCPYVLTVGSTEWRRVESEDDEGDEGDERTGRGGRGGDDG
RGEEEGRGGGGGDDDDDRGTKKPNLDQLQRFTGPYEETATTFFSSGGGFSNVYPVPEYQL
AHQKAYFSTLAASNITLDVEGYHGGRTDYETIGSDGLNFNLEGRGYPDLSAIGDNIYVVH
RGHPVLMMGTSASAPIVASMLNLVNEERLAVGKSTVGWVHPVIYSHPEIFEDITKGENPN
CLSRGFPAVKGWDPVTGLGTPKYPKLLEVFMSLP

Enzyme Prediction     

No EC number prediction in SAPIO_CDS1160-t41_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT25	52	313	7.2e-27	0.9502762430939227

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173788	Peptidases_S53	4.66e-87	622	1107	1	361	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	7.80e-37	424	531	37	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	3.14e-30	424	527	36	138	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.
133474	Glyco_transf_25	1.57e-26	52	141	1	96	Glycosyltransferase family 25 [lipooligosaccharide (LOS) biosynthesis protein] is a family of glycosyltransferases involved in LOS biosynthesis. The members include the beta(1,4) galactosyltransferases: Lgt2 of Moraxella catarrhalis, LgtB and LgtE of Neisseria gonorrhoeae and Lic2A of Haemophilus influenzae. M. catarrhalis Lgt2 catalyzes the addition of galactose (Gal) to the growing chain of LOS on the cell surface. N. gonorrhoeae LgtB and LgtE link Gal-beta(1,4) to GlcNAc (N-acetylglucosamine) and Glc (glucose), respectively. The genes encoding LgtB and LgtE are two genes of a five gene locus involved in the synthesis of gonococcal LOS. LgtE is believed to perform the first step in LOS biosynthesis.
214928	Pro-kuma_activ	4.09e-25	424	527	34	134	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VBB79661.1|GT25	4.16e-103	28	403	32	397
QBZ63647.1|GT25	2.00e-99	10	400	5	391
AEO59316.1|GT25	4.63e-95	42	403	36	393
CAP61640.1|GT25	2.50e-94	28	401	32	387
CDP27993.1|GT25	2.50e-94	28	401	32	387

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3EDY_A	7.43e-35	424	1112	50	543	Crystal Structure of the Precursor Form of Human Tripeptidyl-Peptidase 1 [Homo sapiens]
3EE6_A	1.02e-34	424	1112	69	562	Crystal Structure Analysis of Tripeptidyl peptidase -I [Homo sapiens],3EE6_B Crystal Structure Analysis of Tripeptidyl peptidase -I [Homo sapiens]
1GT9_1	2.93e-16	770	1111	101	356	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]
1T1G_A	3.16e-16	770	1111	101	356	Chain A, kumamolisin [Bacillus sp. MN-32]
1T1I_A	1.01e-15	770	1111	101	356	Chain A, kumamolisin [Bacillus sp. MN-32]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q70DX9|SED1_ASPFU	3.59e-148	418	1114	65	644	Tripeptidyl-peptidase sed1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=sed1 PE=1 SV=1
sp|Q8NK92|AORSN_ASPOR	3.60e-121	424	1114	72	652	Aorsin OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=aorO PE=1 SV=2
sp|C5FHK0|SED1_ARTOC	6.34e-74	412	1113	63	669	Tripeptidyl-peptidase SED1 OS=Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) OX=554155 GN=SED1 PE=3 SV=1
sp|F8W2M8|TPP1_DANRE	4.29e-41	420	1112	61	557	Tripeptidyl-peptidase 1 OS=Danio rerio OX=7955 GN=tpp1 PE=1 SV=2
sp|C5FBW2|SED2_ARTOC	1.04e-39	424	1109	71	594	Tripeptidyl-peptidase SED2 OS=Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) OX=554155 GN=SED2 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999082	0.000933

TMHMM  Annotations     

Start	End
12	31