CAZyme Information: QEL60864.1

Basic Information

• Species: [Candida] auris
• Lineage: Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; [Candida] auris
• CAZyme ID: QEL60864.1
• CAZy Family: GT20
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2100	CP043443|CGC4	238445.98	8.0561

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CaurisB11245	5675	N/A	169	5506

• Gene Location: location=CP043443:2237733-2244557(+)

Full Sequence      

MSHDHSFPKAQRLKEFVGKQFRIGRLHGFAGNFTASALERLRQSPMVADITPDVEIQAFS
VVEQANPPSHLAHISSRDKTTPREKVNVYVVDSGIALDHAEFENRAFPGKDFTNEGSGDT
NGHGTHVAGVIGSQTYGVAKKVRIYELKALNGKGHGSLSGILSALDFAVERRQRKGVPGV
INLSLGAFKSTLLNRAIDAAAKTGLVVVVAAGNTNEDACRYSPASASGAITVGAVDEKQM
ARAFFSNYGSCVDLYAPGVSVSSVHPTSDSPQVLSGTSMAAPAVAGMAASLLSGGVSPGE
IRTELASLSVAAMAPSSVKGYNRVLYNGLDPSEGNSDESSDDETEEDPPIDGDTLTDQFD
LGDTNSDSRGVARTGLQTAVAPLSAFRTPYLDSSHWAGVEGMGHGPDRFFRCYAEEKSSV
KTDITKDADTYPTIDPYPAWNPSDQMPVSRNRIGAIMAHLTKVFGFQEDNMKNMYHYLMK
MLDSRASRMGPYNALRTLHGDYIGGPNSNFRKWYFASEMDIDDAHGWKHVKLDGTIMKSR
EKVASYDRAVDQWYKNMSRFSPTDYVTQISLYLLCWGEANNLRFMPECLCFLFKCCNDYY
YSLEEQEEPESEIPFLDRIITPIYNTYRDQCFSVDGNLVVRTDKDHSSIIGYDDMNQLFW
HRKGIEKIRLKDQTVLMYKSREARYHVLAEVDWSNAFYKTYYESRTWFHIITAFDRVLLI
HFCMFWYYTSFNSKPLYTYDYSIARGNEPPPQATLTVMSLAGSWACLISMVSVSLELFFV
PRKWPGARRVDRRIFWLLLLLIVNTTPTAALFFTSMLRVKDTLAIVITSIQFLFSIGVVL
YLVFKTHADQFGAKPSGRVALACEVFTSDFYKLVYPDKLASYALWICVFTSKFVESYFYL
TLSLKDPLRELFIMRVNRCVGDQWIGSWLCNAQPKVILLLILILDFNLFVLDTYLWYVIW
NTTISVLRSFYLGASIWTPWRNVFSRLPKRIGSKILATTNNNKQNRKISVSKVWNSIIIA
MYREHFLSIEQVHRLIYEISNSDDVEPDMVLREPTFFVSQEDDSLRNTLLQDNSEAQRRI
TFFAQSLSTPMPDIREVKAMPSFTVLIPHYTEKIILSLQEIIKEEDRFSHVTMLEYLKQL
HPSEWANFVWDTKQMAEENDSLDTQPNLTSPEKLDESPYYSVGFKTATPEYVTRTRIWAS
LRSQTLYRTVSGFMNYTRSLKLLSDIEISKDHTSDSNDESKLRLINEMAARKFRIIVSMQ
RYKKFTDEERESTEYLMRAYPELEIAYIDEERDDDGKTTFFSCLVNGTCPVSEKGERSPI
YRIKLSGNPILGDGKSDNQNHALIFVRGEYLQLIDANQDSYIEECLKIRNTLAEFEELRI
PDPYNSQARRAISTNPVAIVGSREYVFSENIGVLGDVAAGKEQTFGTLFARTLSQNGGKL
HYGHPDFLNTIFMCTRGGVSKSQKGLHLNEDIYAGMTAIIRGGRIKHCEYIQCGKGRDLG
FSSISNFITKIGAGMGEQLLSREYFYLGTQLPLDRFLSFYYAHAGFHLNNVCIALSIQMF
LLVGINIAALANDSSICEYNKHKPLTDPRRPHNCLNLVPVIRWLERCIYSIFVVFIISFI
PLGVQEITERGFYKCFTRLGKHIVSLSPLFEVFVCKIYAKSIMRDIAVGGAQYIATGRGF
ATKRESFSSLFTRFANESLGSGAFSLLLVVYISISWWKFPFIYFWMTVLAMLISPFLFNP
NQYSKTEFFLDYLEYLRWLFRGNTQAASESWIIHTKIARSRFTGLKSKLKYGEDDVRFTS
EVKPTRINIIMLNIVPELISLGFVGCAYLFANAQAEARNATPSNAILRILFVSVAPICVN
IGFLLTFFVISVLLGPIITLSFKEFPSLIAATTHILALLNQIFFVELLWVLQNLDVSRTL
LGIACMVLIQRILLRLMNAMMLTREFRHNKSNQAWWSGKWVNAELGWLTLTQPIREFICK
ISELTYFSVDLAVGHIIFYLQLPIIFCPFANTWHSLMLLWVKPGSQIRRQLLSKRQRARQ
RVAVTWSAFVFVVNFLIFAGLIITPLVANKAYNVDLGGLLPDVLQDIRQPEYFRLKRKAW

Enzyme Prediction     

EC	2.4.1.34:56

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT48	1070	1840	2.7e-289	0.9891745602165088

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396784	Glucan_synthase	0.0	1073	1878	5	819	1,3-beta-glucan synthase component. This family consists of various 1,3-beta-glucan synthase components including Gls1, Gls2 and Gls3 from yeast. 1,3-beta-glucan synthase EC:2.4.1.34 also known as callose synthase catalyzes the formation of a beta-1,3-glucan polymer that is a major component of the fungal cell wall. The reaction catalyzed is:- UDP-glucose + {(1,3)-beta-D-glucosyl}(N) <=> UDP + {(1,3)-beta-D-glucosyl}(N+1).
173790	Peptidases_S8_PCSK9_ProteinaseK_like	2.37e-94	70	279	2	221	Peptidase S8 family domain in ProteinaseK-like proteins. The peptidase S8 or Subtilase clan of proteases have a Asp/His/Ser catalytic triad that is not homologous to trypsin. This CD contains several members of this clan including: PCSK9 (Proprotein convertase subtilisin/kexin type 9), Proteinase_K, Proteinase_T, and other subtilisin-like serine proteases. PCSK9 posttranslationally regulates hepatic low-density lipoprotein receptors (LDLRs) by binding to LDLRs on the cell surface, leading to their degradation. The binding site of PCSK9 has been localized to the epidermal growth factor-like repeat A (EGF-A) domain of the LDLR. Characterized Proteinases K are secreted endopeptidases with a high degree of sequence conservation. Proteinases K are not substrate-specific and function in a wide variety of species in different pathways. It can hydrolyze keratin and other proteins with subtilisin-like specificity. The number of calcium-binding motifs found in these differ. Proteinase T is a novel proteinase from the fungus Tritirachium album Limber. The amino acid sequence of proteinase T as deduced from the nucleotide sequence is about 56% identical to that of proteinase K.
173803	Peptidases_S8_Subtilisin_subset	2.96e-51	86	279	2	198	Peptidase S8 family domain in Subtilisin proteins. This group is composed of many different subtilisins: Pro-TK-subtilisin, subtilisin Carlsberg, serine protease Pb92 subtilisin, and BPN subtilisins just to name a few. Pro-TK-subtilisin is a serine protease from the hyperthermophilic archaeon Thermococcus kodakaraensis and consists of a signal peptide, a propeptide, and a mature domain. TK-subtilisin is matured from pro-TK-subtilisin upon autoprocessing and degradation of the propeptide. Unlike other subtilisins though, the folding of the unprocessed form of pro-TK-subtilisin is induced by Ca2+ binding which is almost completed prior to autoprocessing. Ca2+ is required for activity unlike the bacterial subtilisins. The propeptide is not required for folding of the mature domain unlike the bacterial subtilases because of the stability produced from Ca2+ binding. Subtilisin Carlsberg is extremely similar in structure to subtilisin BPN'/Novo thought it has a 30% difference in amino acid sequence. The substrate binding regions are also similar and 2 possible Ca2+ binding sites have been identified recently. Subtilisin Carlsberg possesses the highest commercial importance as a proteolytic additive for detergents. Serine protease Pb92, the serine protease from the alkalophilic Bacillus strain PB92, also contains two calcium ions and the overall folding of the polypeptide chain closely resembles that of the subtilisins. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. 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.
173810	Peptidases_S8_Thermitase_like	1.67e-48	86	279	30	225	Peptidase S8 family domain in Thermitase-like proteins. Thermitase is a non-specific, trypsin-related serine protease with a very high specific activity. It contains a subtilisin like domain. The tertiary structure of thermitase is similar to that of subtilisin BPN'. It contains a Asp/His/Ser catalytic triad. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53 the it follows glutamic acid, while in S8 it precedes histidine. 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. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.
173787	Peptidases_S8_S53	6.82e-45	86	279	1	210	Peptidase domain in the S8 and S53 families. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) family include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. 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. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QEL60864.1|GT48	0.0	1	2100	1	2100
QRG37581.1|GT48	0.0	1	2100	1	2115
QWW23750.1|GT48	0.0	1	2100	36	2166
QEO20591.1|GT48	0.0	1	2100	1	2118
QWU87677.1|GT48	0.0	1	1843	36	1889

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4DZT_A	7.57e-52	64	329	3	276	Aqualysin I: the crystal structure of a serine protease from an extreme thermophile, Thermus aquaticus YT-1 [Thermus aquaticus]
5WSL_A	3.75e-49	86	330	33	279	Structural studies of keratinase from Meiothermus taiwanensis WR-220 [Meiothermus taiwanensis WR-220],5WSL_B Structural studies of keratinase from Meiothermus taiwanensis WR-220 [Meiothermus taiwanensis WR-220],5WSL_C Structural studies of keratinase from Meiothermus taiwanensis WR-220 [Meiothermus taiwanensis WR-220]
2B6N_A	6.09e-46	86	326	33	275	The 1.8 A crystal structure of a Proteinase K like enzyme from a psychrotroph Serratia species [Serratia sp. GF96]
3F7O_A	8.44e-45	63	291	4	240	Crystal structure of Cuticle-Degrading Protease from Paecilomyces lilacinus (PL646) [Purpureocillium lilacinum],3F7O_B Crystal structure of Cuticle-Degrading Protease from Paecilomyces lilacinus (PL646) [Purpureocillium lilacinum]
3F7M_A	2.15e-43	88	328	36	277	Crystal structure of apo Cuticle-Degrading Protease (ver112) from Verticillium psalliotae [Lecanicillium psalliotae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q04952|FKS3_YEAST	0.0	437	2090	15	1755	1,3-beta-glucan synthase component FKS3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FKS3 PE=1 SV=1
sp|P38631|FKS1_YEAST	0.0	435	2090	146	1843	1,3-beta-glucan synthase component FKS1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FKS1 PE=1 SV=2
sp|P40989|FKS2_YEAST	0.0	435	2090	165	1862	1,3-beta-glucan synthase component GSC2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=GSC2 PE=1 SV=2
sp|O93927|FKS1_CRYNH	0.0	413	2081	114	1790	1,3-beta-glucan synthase component FKS1 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=FKS1 PE=3 SV=3
sp|A2QLK4|FKS1_ASPNC	0.0	435	2077	179	1857	1,3-beta-glucan synthase component FKS1 OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=fksA PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000050	0.000000

TMHMM  Annotations     

Start	End
760	782
795	817
822	844
938	960
1545	1567
1607	1624
1690	1712
1719	1738
1809	1831
1851	1873
1888	1910
1917	1934
1999	2021
2042	2064