CAZyme Information: MGYG000000652_00394

Basic Information

• Species: Bacteroides togonis
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides togonis
• CAZyme ID: MGYG000000652_00394
• CAZy Family: PL35
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
987	MGYG000000652_2|CGC3	112274.11	6.8517

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000652	3410500	MAG	Germany	Europe

• Gene Location: Start: 127386; End: 130349 Strand: -

Full Sequence      

MNSTQKHLENNATLCRFLKTNIKNCILLLLLFTLLMPTCTILAQTDWQSHPRLLFTPNEE
IQVKELIKQNQDVRKLAYYLKNRADSLATLAQIPYEMNRYGNMLYTSRAYVDRLGTLALA
YRLYGEKKYLDAADQALQWVCNFPDWDPNHYLDTAEMTTAVAIAYDWLYKSLPASTRKLI
KNSIYRNAIARVLKEYEKGGPGSWAKRETNWNVVCNTGMVLGALAVAEDYPQEARTILEN
AARYMPNCLKHFAPDGVCYEGPSYWGYTASYLSLYLKAVTDNGGDKGKIGQLPGIENTAL
YYKRTLSPSGRVFNFANAHDEALNTPAFFLFSRLYSQAEVAEWYRKEIGKVIQGQQPLHQ
LFFLSLPWYDNAQPNPQSSLPKLEVYHNTINDIIILNGKRDVQGSIFLTAKGGEPMQAHQ
QMDCGTFVLESEGIRWTDDLGSDDYNLPGFWDYKPNGQRWKYFRNNNLSHNTISIDHQIQ
YAAGEAFVCEEKTDIAQPYAKLDMTSLYKDQAESVFRTFTLIDDQTVEVTDEIKLTNAQS
TVSWSVITKADVETDGKTAHLTLNGKHFYMQIISPTNATFTSRLAQNTSPKEYPIRNTTI
IEANCTFGQPDATIKVRMSSRPFLEIAHGPYLQEVTTNGATFAFQTSNPSFSFIELKKKG
EIQSNNYSGSQHGLKQADATFFAIRAEELQPNTTYQYRIHAKEIKSFQPYKVVFGDSIAS
TWYTFRTIDPEQEGGSIFITSDMHSNPKLLKNLLERCDYQTCTSFFYAGDMMNYMTENGE
HPFTSFIDTSVELFATSIPFEFVRGNHETRGNMARIFPSFFPKQNGKIYGSYLMGDVMVI
MLDTGEDKSDTHPVYAGLTDFDNYRSEQARWLEKIVKSKEFKKAKYRIVISHFPLVADKE
WEKGTTWKGCQDASQKFLPILNRAGIDLIVAGHTHRFFYHEPGESGNQCPVLEQGAMCAT
RLDLTDGNIHIKVIGKNGEALLNKTLK

Enzyme Prediction     

No EC number prediction in MGYG000000652_00394.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
PL35	405	576	1.7e-58	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00149	Metallophos	4.48e-14	737	937	3	191	Calcineurin-like phosphoesterase. This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.
cd07378	MPP_ACP5	4.55e-08	798	935	75	217	Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain. Acid phosphatase 5 (ACP5) removes the mannose 6-phosphate recognition marker from lysosomal proteins. The exact site of dephosphorylation is not clear. Evidence suggests dephosphorylation may take place in a prelysosomal compartment as well as in the lysosome. ACP5 belongs to the metallophosphatase (MPP) superfamily. 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 MPP superfamily 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). 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.
COG1409	CpdA	3.66e-07	768	936	40	192	3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms].
cd00839	MPP_PAPs	4.00e-07	790	975	61	236	purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain. Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs belong to the metallophosphatase (MPP) superfamily. 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 MPP superfamily 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). 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.
PLN02533	PLN02533	1.48e-06	689	937	110	334	probable purple acid phosphatase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRP59764.1	4.08e-281	34	621	10	598
QQT79787.1	4.08e-281	34	621	10	598
ASM65217.1	6.09e-281	34	621	21	609
QUU07041.1	2.33e-280	34	621	10	598
QUT50039.1	8.47e-194	49	619	34	604

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

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
0.110497	0.882365	0.006168	0.000352	0.000273	0.000324

TMHMM  Annotations     

start	end
25	47