CAZyme Information: KAG5416962.1

Basic Information

• Species: Candida metapsilosis
• Lineage: Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; Candida metapsilosis
• CAZyme ID: KAG5416962.1
• CAZy Family: CBM21
• CAZyme Description: FAV3

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
546		58237.38	4.1578

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CmetapsilosisBP57	5743	N/A	17	5726

• Gene Location: location=JAEOAQ010000007:118071-119711(-)

Full Sequence      

MLVFLPFLVTLGATAPVVINTVIVTQTAAGGISQNLQTVAAQNAQVTASAVQNAEVDTPQ
TATSSRFNIFGEIAQLFGFGSTSEASNVATTAPAVVATSSLIATTGQTPITSSPVVASSP
AGAISFPTTSSIASVAPVSSAASLSTSSSAQAGFSSTQANTPSSAQESSQSSNFVLDEAV
PSTPQSGNAYQTTINKLWQRFWENGKWNQEDSICKDNSYQIPSVWDMAVLGKAIADSGDS
NGVETTISRILEYYDQSTGAFSSTPNSPSEIYSDDNSQLLWVFLDAYKMTNKQQYLKYAE
GIMDYLKTQNYQNTGGIIWKKDQSYIASISTTEVALSAMRLYEINGDESLVELAQSCMDF
MFKYLQDSDKLFYDGLDKSTFTPNKGKLTYTVGCAISTLVKLGSSDALSKALELATAATN
QNGAFYTSEGIWNNSLKYVHLLFVGFGDAFAAAGGQFDQFKDEVTRQGNYIYDFVQDPDD
ADLYFDSATSGTPTAYAKYAKVFSTSGATYKPDDDLYCSGSSSGPAPKSLLTNASAGQIL
YQLSKY

Enzyme Prediction     

No EC number prediction in KAG5416962.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH76	188	423	1.8e-28	0.6703910614525139

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
397638	Glyco_hydro_76	1.32e-10	224	397	35	226	Glycosyl hydrolase family 76. Family of alpha-1,6-mannanases.
224250	YyaL	6.24e-04	271	496	408	642	Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin glycosidase-like domains [General function prediction only].
271198	LanC_like	6.47e-04	225	364	59	193	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	8.34e-04	247	384	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.
398697	LANC_like	0.003	243	359	130	253	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCG21685.1|GH0	1.73e-282	1	546	1	538
CCE43726.1|GH0	9.21e-274	1	546	1	532
AOW27063.1|GH0	5.00e-133	184	546	85	447
ABN64243.2|GH0	1.35e-99	188	545	53	417
CCE81418.1|GH0	4.56e-93	189	541	212	571

PDB Hits     

KAG5416962.1 has no PDB hit.

Swiss-Prot Hits     

KAG5416962.1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.655151	0.344847

TMHMM  Annotations     

There is no transmembrane helices in KAG5416962.1.