CAZyme Information: MGYG000004188_02185

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides
• CAZyme ID: MGYG000004188_02185
• CAZy Family: PL35
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
985	MGYG000004188_18|CGC1	112638.51	7.5971

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004188	3351981	MAG	United Kingdom	Europe

• Gene Location: Start: 42318; End: 45275 Strand: +

Full Sequence      

MNNLHEKNKTYYRRAIKPGIIQSILLFLFITLSYTYPTYAQNDWIPQHPRLLFTSNEEIQ
VRKLIKENQEAQELARFLKNRADSLITLAQIPYEMNRYGNMLYTSRAYVERLGILALAYR
LYGEKKYLNAAEQTLQWVCNYPNWDPKHYLDTAEMTTAVAIAYDWLYTALPASTKKLVKK
SIYKNAISRVLQEYEKGGPGSWAKRETNWNVVCNTGMVLGALAVAEDYPQEARTILENAA
RFMPNCLKHFAPDGVCYEGPSYWGYTASYLSLYLKAVTDNGGDKGKIGQLPGIEHTALYY
KRTLSPTGRIFNFANAHEEALNTPAFFLFSKLYHQSEVAEWYRGEIKKTIRQQQPLHQLF
YLSLPWYDNTHPNPLAALPKLEVYHNSINDIIVVNGKRNVQGSIFLTAKGGEPMQAHQQM
DCGTFVLESEGVRWTDDLGSDDYNLPGFWDYKPGGQRWKYFRNNNLSHNTISINHQVQYA
AGKAFVCEEKTDIDQPYAKLDMTSLYKNQAESVFRTFTLTDDQTVEVKDEIKLSDTQSTV
SWSVITKATVETNGNKAHLTHNGKHFYIQIVSPTNATFTSRPAQNTSPKEYPIRNTTILE
ANCTFDQPDATIKVRMSSRPFLEIAHGPYLQEVTTDGATFAFQTSQPSFSFIELKKEGEE
DSNNYAGSQHGLKQADATFFAIRAEELQPNTTYQYRIHAKEIKSFQPYKVVFGDSIASPW
YTFRTIDPKQKGGSIFITSDMHSNPKLLKNLLERCDYKTCTSFFYAGDMMNYMTENGEHP
FTSFIDTSVEMFATSIPFEFVRGNHETRGNMARIFPSFFPKQNGKIYGSYLMGDVMVIML
DTGEDKSDNHPVYAGLTDFDNYRSEQARWLEKVVKSKEFKKAKYRIVISHFPLVVDKDWE
KGTTWKGCQDASRKFLPILNRAGIDLIVAGHTHRFFYHEPEESGNQCPVLEQGAMCATRL
DLADGNIHIKVIGKNGEILLDKNLK

Enzyme Prediction     

No EC number prediction in MGYG000004188_02185.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
PL35	403	574	9.7e-60	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00149	Metallophos	4.25e-13	735	935	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	1.12e-08	796	941	75	225	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	1.20e-08	766	934	40	192	3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms].
cd07402	MPP_GpdQ	6.74e-07	795	936	69	195	Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain. GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 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	3.09e-06	687	935	110	334	probable purple acid phosphatase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRP59764.1	2.90e-283	39	619	18	598
QQT79787.1	2.90e-283	39	619	18	598
ASM65217.1	4.34e-283	39	619	29	609
QUU07041.1	8.26e-283	39	619	18	598
QUT50039.1	3.94e-188	47	617	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
0.029325	0.968779	0.001023	0.000320	0.000259	0.000274

TMHMM  Annotations     

start	end
19	41