CAZyme Information: MGYG000001170_01811

Basic Information

• Species: UMGS1603 sp900759005
• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; UMGS1603; UMGS1603 sp900759005
• CAZyme ID: MGYG000001170_01811
• CAZy Family: GH0
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
761	MGYG000001170_180|CGC1	86097.34	5.7355

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001170	2224944	MAG	Austria	Europe

• Gene Location: Start: 3657; End: 5942 Strand: -

Full Sequence      

MQIKKVILVFKTHFDIGFTKLSREVLDDYAGKMLDRVAETCDATRDMGALKYVWTMPAWP
LKTMRDRADEAHAKKVDELIARNQLAWHALPYTSHYDFCGVEDALWGLKNAKELSERYHL
PLKRAAKMTDVPGHGRFLAEMLADAGVRLLHLGCNEFAMPPSLPEIFWWEAPSGKRVLTM
YNSGYGTGLFPPENWRFDTWMALMNTNDNSGPQSAEIVKSDYERLHARFPEAEIVCGTLD
DMWNALKNEDLSDLPIVKSDLADTWIHGTASYPRESAQIRRLRARLNRVQRAWLSHPDDP
ELRKAVARAYDAMALYAEHTWGLDVKIWLGAIPDYESFDEYRKTSEKCARMEESWREQIE
RAEKATAACEEAEKRLGIRLPAEFKFEGGETLSGEQTLSGARYALRFSADTGKIHALTDL
VRGCELLSERGETSVFSYRYDRFGADDMTEYLRAYAHRFSDWGIFDNGRINYPECAHAVR
VPEFVSCRQNGRTVQFVYRASAGERLGDAETVNLYVTVPDTDAPVHIRVELKSKKATPYI
ESGALCMPLGAKNPAYFINKTGSVLRPETDIARNANHAFYALEHFAAASDDRAMIAIVSH
DAPLVSLGENGVHKFRAEYEPHAPEMRFCLFNNMWGTNFPQWIEGDMAFEFDVFSENANA
VDSAYARACALAANPNGETPIEIPFTLSEGLRLTGVYPEKNGVLLHIQNLKSAAQSGTIC
AQGWTFEEEDLLGRKLGDEWKNAVSTEFAPYDLRAFRAKRV

Enzyme Prediction     

No EC number prediction in MGYG000001170_01811.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10791	GH38N_AMII_like_1	3.76e-51	5	267	1	254	N-terminal catalytic domain of mainly uncharacterized eukaryotic proteins similar to alpha-mannosidases; glycoside hydrolase family 38 (GH38). The subfamily of mainly uncharacterized eukaryotic proteins shows sequence homology with class II alpha-mannosidases (AlphaAMIIs). AlphaAMIIs possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyze the degradation of N-linked oligosaccharides. The N-terminal catalytic domain of alphaMII adopts a structure consisting of parallel 7-stranded beta/alpha barrel. This subfamily belongs to the GH38 family of retaining glycosyl hydrolases, which employ a two-step mechanism involving the formation of a covalent glycosyl enzyme complex; two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst.
pfam16477	DUF5054	2.04e-11	279	469	8	226	Domain of unknown function (DUF5054). This family consists of Glycosyl hydrolase family 38 proteins around 700 residues in length and is mainly found in various Clostridium and Rhizobium species. The function of this family is unknown.
cd10814	GH38N_AMII_SpGH38_like	4.84e-05	167	263	157	269	N-terminal catalytic domain of SPGH38, a putative alpha-mannosidase of Streptococcus pyogenes, and its prokaryotic homologs; glycoside hydrolase family 38 (GH38). The subfamily is represented by SpGH38 of Streptococcus pyogenes, which has been assigned as a putative alpha-mannosidase, and is encoded by ORF spy1604. SpGH38 appears to exist as an elongated dimer and display alpha-1,3 mannosidase activity. It is active on disaccharides and some aryl glycosides. SpGH38 can also effectively deglycosylate human N-glycans in vitro. A divalent metal ion, such as a zinc ion, is required for its activity. SpGH38 is inhibited by swainsonine. The absence of any secretion signal peptide suggests that SpGH38 may be intracellular.
cd04171	SelB	0.006	113	163	38	92	SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome. SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AUS95533.1	5.86e-135	8	654	9	740
AIA19246.1	1.14e-124	3	653	5	715
AQT68768.1	6.57e-93	3	757	243	1100
AOW10779.1	7.72e-85	2	723	41	853
SDS35267.1	9.66e-82	8	645	39	757

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

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
1.000053	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001170_01811.