CAZyme Information: CPAR2_213690-T-p1

Basic Information

• Species: Candida parapsilosis
• Lineage: Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; Candida parapsilosis
• CAZyme ID: CPAR2_213690-T-p1
• CAZy Family: GH47
• CAZyme Description: Has domain(s) with predicted catalytic activity and role in carbohydrate metabolic process

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
532	Contig005809_C_parapsilosis_CDC317|CGC8	57577.34	4.0569

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CparapsilosisCDC317	5984	578454	147	5837

• Gene Location: location=Contig005809_C_parapsilosis_CDC317:2916927-2918525(+)

Full Sequence      

MLVLLPFIFTLGATAPVVINTVIVTQTYGANQNLQTAQTKNVQTTPSPVQASQIQAQQTA
STSSFNIFGEIAQLFGFGSTSEASNVANTSPAAVTATSPAVTTTPVAGTATPTPTTFSAI
SSIASSPSSESPFTTTQLQTDTPSTQTNSASSAIESSQSSNFVLDEAVSSTPQSGNAYLT
TVNKIWQRFWENGKWNQEDSICQDDSYQIPSVWDMAVLGKAIADSGDTNGVETTISRILE
YYDSNTGAFSSTPNSSSEIYSDDNSQLLWVFLDAYKMTNKEQYLKYAEGIMDYLKTQNYQ
NTGGIIWKRDQSYIASISTTEVALSAMRLYEFNNDESLVELAQNCMDFMFNHLQDSDSLF
FDGLDKETFSVNKGKLTYTVGCAISTLVKLGTQDALNKALDLATAATNTDGAFYTSEGIW
NNSLQYVHLLFVGFGDAFGTGKFDKFKDEVTRQGNYIYEFVQDPDDANLYFDSATSGTPS
TYAKYAKVFSTSGATYKPNEDLYCSGSSSGPAPKSLLTNASAGQILYQLANY

Enzyme Prediction     

No EC number prediction in CPAR2_213690-T-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH76	175	408	1.9e-28	0.6536312849162011

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
397638	Glyco_hydro_76	4.41e-10	212	437	35	291	Glycosyl hydrolase family 76. Family of alpha-1,6-mannanases.
398697	LANC_like	1.92e-05	231	359	130	267	Lanthionine synthetase C-like protein. Lanthionines are thioether bridges that are putatively generated by dehydration of Ser and Thr residues followed by addition of cysteine residues within the peptide. This family contains the lanthionine synthetase C-like proteins 1 and 2 which are related to the bacterial lanthionine synthetase components C (LanC). LANCL1 (P40 seven-transmembrane-domain protein) and LANCL2 (testes-specific adriamycin sensitivity protein) are thought to be peptide-modifying enzyme components in eukaryotic cells. Both proteins are produced in large quantities in the brain and testes and may have role in the immune surveillance of these organs. Lanthionines are found in lantibiotics, which are peptide-derived, post-translationally modified antimicrobials produced by several bacterial strains. This region contains seven internal repeats.
271198	LanC_like	2.27e-04	235	372	31	155	Cyclases involved in the biosynthesis of lantibiotics, and similar proteins. LanC is the cyclase enzyme of the lanthionine synthetase. Lanthionine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as a precursor peptide and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans), in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. A related domain is also present in LanM and other pro- and eukaryotic proteins with poorly characterized functions.
271198	LanC_like	0.002	267	351	105	192	Cyclases involved in the biosynthesis of lantibiotics, and similar proteins. LanC is the cyclase enzyme of the lanthionine synthetase. Lanthionine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as a precursor peptide and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans), in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. A related domain is also present in LanM and other pro- and eukaryotic proteins with poorly characterized functions.
224250	YyaL	0.008	263	304	274	315	Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin glycosidase-like domains [General function prediction only].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCE43726.1|GH0	0.0	1	532	1	532
CCG21685.1|GH0	1.59e-293	1	532	1	538
AOW27063.1|GH0	1.96e-134	172	532	85	447
ABN64243.2|GH0	2.85e-101	176	530	53	416
CCE81418.1|GH0	1.51e-89	177	527	212	571

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4C1S_A	4.55e-07	248	403	94	265	Glycoside hydrolase family 76 (mannosidase) Bt3792 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],4C1S_B Glycoside hydrolase family 76 (mannosidase) Bt3792 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482]
4MU9_A	9.83e-06	260	434	116	300	Crystal structure of a putative glycosylhydrolase (BT_3782) from Bacteroides thetaiotaomicron VPI-5482 at 1.89 A resolution [Bacteroides thetaiotaomicron VPI-5482],4MU9_B Crystal structure of a putative glycosylhydrolase (BT_3782) from Bacteroides thetaiotaomicron VPI-5482 at 1.89 A resolution [Bacteroides thetaiotaomicron VPI-5482]

Swiss-Prot Hits     

CPAR2_213690-T-p1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.685508	0.314493

TMHMM  Annotations     

There is no transmembrane helices in CPAR2_213690-T-p1.