CAZyme Information: MGYG000003819_01614

Basic Information

• Species: UMGS1872 sp900555795
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; UMGS1872; UMGS1872 sp900555795
• CAZyme ID: MGYG000003819_01614
• CAZy Family: CE7
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1049	MGYG000003819_24|CGC1	109748.55	4.0309

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003819	2286303	MAG	United States	North America

• Gene Location: Start: 20629; End: 23778 Strand: -

Full Sequence      

MRKWNKLLALLLAMVMAFSTMSTALADGEEAAADAEAPAAETEAPVAETEAPAEDAEAGA
YNGTIVILHTNDVHGAIAGYAKVAALAAKYEAEGAYVLIMDAGDFSQGEAEVSVSEGATA
VEMMDMAGYDVVTLGNHEFDYGYTNLLENFKEADFQVTAANVTYEGVAAFENYVVFEAPG
GTKVGVFGLSTPETATKAHPAKIKGVTFAAGEDMYAIAQTQVDALTAAGCDVIVTLAHLG
IDEGSAGNRSTDLLEHVTGIDVLIDGHSHSTEEDVAAATNADRKVGETVVTSTGTKLENI
GVITIKDGAITTNTVASESITVAEDDAIVARAAEIAAEIEADYGTVFAKTEVKLSGDRAP
GVRTQETPLGNLIADAILWYATKDGELPVPAENVIALTNGGGIRATIEAGDITKKDVNTV
LPFGNTVAYITITGAALLEALEASTYAAPDALGGFPQVSGINFTVNTMKKFDAGDLYEGS
TYSKPNSINRVTIDSVNGKAFDPAATYAIVTNDFTAAGGDTYYAFSVATVVDTGAPLDEV
VMAYITEVLGGVVTAEKYGETAGRITIKGYSDVSGQNWFYDAAVYATEKGLIDGLTETTF
GPSENMTRAGLVTALYRLAGSPEVTAENPFSDVADDAAYKNAVIWANENGVVTGKTETTF
DPNGSILRQEIAALLYRYVSGQGYDVSIGEKTNILSYTDAQTISEYAIPAIQWMCGVGLF
QGNADGSIQPKATATRAQVATILMRFDALKLTPVEETPAEPAAAYIETEITFEVAEQEGV
PAHTVTGILTVPTAATKAAPVPGVVMLHGTGSNLHEVLGAYDTAAQEMAKKGIATLRFNF
QGIGDGKEAEYVNYSYTSANIDAKAAADYLAKLETVDGEKLGVMGWSQGGTNALLAAAAY
PETFKAVVTWAGALDLTGLFADFDAAAAEAAEKGFVNLVQDWRTDLPHGAKWFEDVKNTD
VLAKAKTITAPILTINGEKDDVVDPASGAEIVKDAANSLSKNVIIPNCDHTMNMFVEGAT
EINTVIANTADFFVQAFAAMEEATVEAAA

Enzyme Prediction     

No EC number prediction in MGYG000003819_01614.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE7	769	987	1e-18	0.7156549520766773

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0737	UshA	1.30e-76	51	545	13	496	2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
PRK09558	ushA	8.83e-70	56	565	26	548	bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed
PRK09419	PRK09419	1.63e-68	46	552	648	1135	multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
cd00845	MPP_UshA_N_like	8.89e-53	65	306	1	237	Escherichia coli UshA-like family, N-terminal metallophosphatase domain. This family includes the bacterial enzyme UshA, and related enzymes including SoxB, CpdB, YhcR, and CD73. All members have a similar domain architecture which includes an N-terminal metallophosphatase domain and a C-terminal nucleotidase domain. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.
cd07408	MPP_SA0022_N	5.16e-47	65	320	1	254	Staphylococcus aureus SA0022 and related proteins, N-terminal metallophosphatase domain. SA0022 is an uncharacterized Staphylococcus aureus UshA-like protein with two putative domains, an N-terminal metallophosphatase domain and a C-terminal nucleotidase domain. SA0022 also contains a putative C-terminal cell wall anchor domain. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCJ95849.1	1.04e-89	63	548	39	495
AGA59602.1	1.09e-80	64	545	34	488
ABW18467.1	1.17e-80	65	548	60	517
AEI45885.1	3.02e-79	64	574	48	527
QQY79959.1	3.97e-79	65	567	39	510

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2Z1A_A	4.33e-39	64	547	29	516	Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8]
7D0V_A	1.09e-30	65	523	5	485	ChainA, Snake venom 5'-nucleotidase [Naja atra],7D0V_B Chain B, Snake venom 5'-nucleotidase [Naja atra]
5H7W_A	4.62e-30	65	523	5	485	Crystalstructure of 5'-nucleotidase from venom of Naja atra [Naja atra],5H7W_B Crystal structure of 5'-nucleotidase from venom of Naja atra [Naja atra]
1OI8_A	4.77e-30	65	545	9	505	5'-Nucleotidase(E. coli) with an Engineered Disulfide Bridge (P90C, L424C) [Escherichia coli],1OI8_B 5'-Nucleotidase (E. coli) with an Engineered Disulfide Bridge (P90C, L424C) [Escherichia coli]
1HO5_A	5.92e-30	65	545	9	505	5'-Nucleotidase(E. Coli) In Complex With Adenosine And Phosphate [Escherichia coli],1HO5_B 5'-Nucleotidase (E. Coli) In Complex With Adenosine And Phosphate [Escherichia coli],1HPU_A 5'-Nucleotidase (Closed Form), Complex With Ampcp [Escherichia coli],1HPU_B 5'-Nucleotidase (Closed Form), Complex With Ampcp [Escherichia coli],1HPU_C 5'-Nucleotidase (Closed Form), Complex With Ampcp [Escherichia coli],1HPU_D 5'-Nucleotidase (Closed Form), Complex With Ampcp [Escherichia coli]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A9BJC1	2.46e-46	65	522	24	458	Mannosylglucosyl-3-phosphoglycerate phosphatase OS=Petrotoga mobilis (strain DSM 10674 / SJ95) OX=403833 GN=mggB PE=1 SV=1
O34313	1.83e-43	65	529	669	1142	Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
B6EWW8	1.84e-32	65	523	44	524	Snake venom 5'-nucleotidase OS=Gloydius brevicaudus OX=259325 PE=2 SV=1
F8S0Z7	4.38e-32	65	523	44	524	Snake venom 5'-nucleotidase OS=Crotalus adamanteus OX=8729 PE=1 SV=2
A0A2I4HXH5	2.53e-29	65	523	5	485	Snake venom 5'-nucleotidase (Fragment) OS=Naja atra OX=8656 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000583	0.998320	0.000351	0.000278	0.000237	0.000195

TMHMM  Annotations     

start	end
7	26