CAZyme Information: MGYG000001522_00804

Basic Information

• Species: Pauljensenia radingae_A
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Pauljensenia; Pauljensenia radingae_A
• CAZyme ID: MGYG000001522_00804
• CAZy Family: GH125
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
440	MGYG000001522_4|CGC10	48817.41	4.4178

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001522	2458350	Isolate	not provided	not provided

• Gene Location: Start: 622576; End: 623898 Strand: +

Full Sequence      

MARADSTWMEHIIATVKERVDARVGEVFEDCFVNTISSTIERYDDGSAFVLTGDIPAMWL
RDSTWQMIPYVHFSGDYPEIAELIGGVLQRQLMYIDMDPYANAFNAEPNGAGHHDDLTEM
SPWIWERKYEVDSLSAPLFLAGHLWDRTHEDAHLGGLEKALETVVDVFAREQRHETSDYR
FERPGAQVATETLSHGGKGAPVGYTGMTWSGFRPSDDANSYGYNVPGNAFAVVVLRTAAR
VLEQMNAATGATSSPVISRARDLADQISAGIYEHGVIDHPQWGKVFAYEVDGLGQTLIMD
DANMPSLLSLPYIGFLEADDPIYLNTRAMVLSDTNPFYFNGSRAQGIGSPHTPHEYIWPI
ALAVQALTSTSAHEVDQIIDTLIHTTGGTGLMHESFHKDDDALFTREWFSWANAMFCELV
LAYCSLTQSNDISRKEASNG

Enzyme Prediction     

No EC number prediction in MGYG000001522_00804.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH125	23	421	1.8e-156	0.9925373134328358

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3538	COG3538	0.0	6	424	11	423	Meiotically up-regulated gene 157 (Mug157) protein (function unknown) [Function unknown].
pfam06824	Glyco_hydro_125	0.0	21	421	1	416	Metal-independent alpha-mannosidase (GH125). This family, which contains bacterial and fungal glycoside hydrolases, is also known as GH125. They function as metal-independent alpha-mannosidases, with specificity for alpha-1,6-linked non-reducing terminal mannose residues. Structurally this family is part of the 6 hairpin glycosidase superfamily.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SDT94338.1	0.0	1	440	1	440
AIQ18384.1	7.90e-152	23	426	27	426
ASS66075.1	1.53e-151	6	426	8	426
AWV34210.1	1.60e-151	9	424	1	414
AIQ74892.1	3.21e-151	9	424	1	414

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3QT3_A	3.19e-136	21	420	25	419	Analysisof a New Family of Widely Distributed Metal-independent alpha-Mannosidases Provides Unique Insight into the Processing of N-linked Glycans, Clostridium perfringens CPE0426 apo-structure [Clostridium perfringens],3QT9_A Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Clostridium perfringens CPE0426 complexed with alpha-1,6-linked 1-thio-alpha-mannobiose [Clostridium perfringens]
6RQK_A	4.16e-136	21	420	25	419	Crystalstructure of GH125 1,6-alpha-mannosidase from Clostridium perfringens in complex with mannoimidazole [Clostridium perfringens str. 13],6RQK_B Crystal structure of GH125 1,6-alpha-mannosidase from Clostridium perfringens in complex with mannoimidazole [Clostridium perfringens str. 13]
5M7I_A	2.37e-135	21	420	25	419	Crystalstructure of GH125 1,6-alpha-mannosidase mutant from Clostridium perfringens in complex with 1,6-alpha-mannobiose [Clostridium perfringens str. 13],5M7Y_A Crystal structure of GH125 1,6-alpha-mannosidase mutant from Clostridium perfringens in complex with 1,6-alpha-mannotriose [Clostridium perfringens str. 13]
2NVP_A	2.02e-131	21	420	25	419	X-RayCrystal Structure of Protein CPF_0428 from Clostridium perfringens. Northeast Structural Genomics Consortium Target CpR63. [Clostridium perfringens]
3QPF_A	3.43e-130	8	426	11	425	Analysisof a New Family of Widely Distributed Metal-independent alpha-Mannosidases Provides Unique Insight into the Processing of N-linked Glycans, Streptococcus pneumoniae SP_2144 apo-structure [Streptococcus pneumoniae],3QPF_B Analysis of a New Family of Widely Distributed Metal-independent alpha-Mannosidases Provides Unique Insight into the Processing of N-linked Glycans, Streptococcus pneumoniae SP_2144 apo-structure [Streptococcus pneumoniae],3QRY_A Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Streptococcus pneumoniae SP_2144 1-deoxymannojirimycin complex [Streptococcus pneumoniae],3QRY_B Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Streptococcus pneumoniae SP_2144 1-deoxymannojirimycin complex [Streptococcus pneumoniae],3QSP_A Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Streptococcus pneumoniae SP_2144 non-productive substrate complex with alpha-1,6-mannobiose [Streptococcus pneumoniae],3QSP_B Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Streptococcus pneumoniae SP_2144 non-productive substrate complex with alpha-1,6-mannobiose [Streptococcus pneumoniae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q10449	7.70e-92	9	421	64	494	Meiotically up-regulated gene 157 protein OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mug157 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000049	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001522_00804.