CAZyme Information: CNK03190-t26_1-p1

Basic Information

• Species: Cryptococcus neoformans
• Lineage: Arthropoda; Insecta; ; Eriococcidae; Cryptococcus; Cryptococcus neoformans
• CAZyme ID: CNK03190-t26_1-p1
• CAZy Family: GT32
• CAZyme Description: carbohydrate binding protein, putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
940	AE017351.1|CGC1	104007.13	5.5536

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CneoformansJEC21	7004	214684	372	6632

• Gene Location: location=AE017351.1:948333-951791(+)

Full Sequence      

MLSSRTIWIWLAPCLCLSNLLGVWGMTDARRIQLRDETAALFRHGYEGYIKYAYPADELR
PLSCAPLRRSKNAADFGINDLHANVSLTLLDVLSSLPLLHPHALPSALERITTQVSFDQD
VKVQVFEMTIRALGGLLSMYQYLDDLPDSPYEQARVLGVVREGKEGWLGLGLGAQEKVDK
VDVKKYKPRILELAEDLGRRMLPAFNTKTGLPYARVNLKHGIEKGESVETCTAGAGSLIL
EFSLLSRLTGDDRYEQLARNAYYSIWNRRSDHNLLGNTIGATHGHWLMPGLSGVGAGMDS
FFEYGVKAGIMLGDDSFYDIFYDSYAAIQTHVRTTDGFIYRPIHTRLLQIPSPTTIDSLS
AFLPAIQVLAGDIPSAIRSHLVFWNLWRKFGALPESWRWQERRIEWAGWPGRPEFIESTY
YLYQATKDPFYLRVGERVLKDLARRTKTSCGFATIKNVLTSELEDRMESFMLSETLKYLY
LLFSDTPFPNQNKVFTTEGHPLYIPQPLLQPSTNARKSLHKGEWLTCPAYQSPFAIGGID
FHGTDKVGNRVEKVGITVGIEGTSEYEYARALVFGWGEEGLKVEDQKRMWFDGGVCSIQE
VPKFAFDIVLTSPFNETFPEDPSPGSDKVYQNTTTGDYVISNIAGIRLGVRWRLDGQGYD
VSSIGPHRVRTGQQVTVIDSSMRNHFPLPSLAPGPPQPQYEPTEVILRFVFLSPVVVKDK
HVEASTVFLHALGATATFGKDFGASATSPRMEDQQGWQLSGGALPILVLPNPSDGCSPLT
LSTPDYPFILLLDRGNCTFAEKAQNAETIGASGLLIVGYPHPPEGGVTQGDQTVYAAPEE
GLVRPSAEPNEAEGLDSMGIVYMEHLVGELVRNASQKGEIGAAIMRIEGVGEEAAGSSGF
PQAGSGATKKHWESDSRIREGRLAVGDWEICNLVVVDTSV

Enzyme Prediction     

EC	3.2.1.113:6

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	42	503	4e-129	0.9932735426008968

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	1.38e-121	41	502	1	451	Glycosyl hydrolase family 47. Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2).
240427	PTZ00470	9.61e-58	30	507	72	521	glycoside hydrolase family 47 protein; Provisional
239047	PA_GO-like	3.57e-12	733	817	21	90	PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on protein GRO10. This group contains various PA domain-containing proteins similar to the functionally uncharacterized Arabidopsis GRO10. The PA domain may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.
240122	PA_subtilisin_1	8.28e-10	741	834	4	91	PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. A subgroup of PA domain-containing subtilisin-like proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following subtilisin-like proteases: i) melon cucumisin, ii) Arabidopsis thaliana Ara12, iii) Alnus glutinosa ag12, iv) members of the tomato P69 family, and v) tomato LeSBT2. However, these proteins belong to other subtilisin-like subgroups. Relatively little is known about proteins in this subgroup.
239037	PA_GRAIL_like	1.26e-09	766	816	34	90	PA _GRAIL_like: Protease-associated (PA) domain GRAIL-like. This group includes PA domain containing E3 (ubiquitin ligases) similar to human GRAIL (gene related to anergy in lymphocytes) protein. Proteins in this group contain a C3H2C3 RING finger. E3 ubiquitin ligase is part of an enzymic cascade, the end result of which is the ubiquitination of proteins. In this cascade, E1 activates the ubiquitin, the activated ubiquitin is carried by E2, and E3 recognizes the acceptor protein as well as catalyzes the transfer of the activated ubiquitin from E2 to this acceptor. GRAIL, a transmembrane protein localized in the endosomes, controls the development of T cell clonal anergy, and may ubiquitinate membrane-associated targets for T cell activation. GRAIL1 is associated with, and regulated by, two isoforms of otubain 1 (the ubiquitin-specific protease). Additional E3s belonging to this group include human (h)Goliath and Xenopus GREUL1 (Goliath Related E3 Ubiquitin Ligase 1). hGoliath and GRAIL both have the property of self-ubiquitination. hGoliath is expressed in leukocytes; its expression and localization is not modified in leukemia. GREUL1 may play a role in the generation of anterior ectoderm. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AAW46395.2|GH47	0.0	1	940	1	940
AUB28289.1|GH47	0.0	1	940	1	940
AFR98181.1|GH47	0.0	1	940	1	940
KNX50001.2|GH47	0.0	1	940	1	940
UOH84003.1|GH47	0.0	26	940	1	870

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KIJ_A	1.10e-35	41	504	12	451	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
1FMI_A	1.21e-35	41	504	17	456	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
1FO2_A	1.25e-35	41	504	17	456	Crystal Structure Of Human Class I Alpha1,2-Mannosidase In Complex With 1-Deoxymannojirimycin [Homo sapiens],1FO3_A Crystal Structure Of Human Class I Alpha1,2-Mannosidase In Complex With Kifunensine [Homo sapiens]
1X9D_A	3.83e-35	41	504	95	534	Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue [Homo sapiens]
5KK7_A	5.12e-35	41	504	12	451	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase T688A mutant and Thio-disaccharide substrate analog complex [Homo sapiens],5KK7_B Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase T688A mutant and Thio-disaccharide substrate analog complex [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|O94726|MNL1_SCHPO	1.34e-110	23	500	24	473	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mnl1 PE=3 SV=2
sp|Q92611|EDEM1_HUMAN	7.68e-108	31	500	127	582	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Homo sapiens OX=9606 GN=EDEM1 PE=1 SV=1
sp|Q925U4|EDEM1_MOUSE	9.73e-107	31	500	122	577	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Mus musculus OX=10090 GN=Edem1 PE=1 SV=1
sp|Q9SXC9|MNS5_ARATH	2.18e-98	28	504	31	478	Alpha-mannosidase I MNS5 OS=Arabidopsis thaliana OX=3702 GN=MNS5 PE=1 SV=1
sp|Q6GQB9|EDEM3_XENLA	6.10e-98	9	817	14	721	ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Xenopus laevis OX=8355 GN=edem3 PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.013592	0.986360	CS pos: 25-26. Pr: 0.9227

TMHMM  Annotations     

Start	End
7	26