CAZyme Information: MGYG000002524_00617

Basic Information

• Species: Yersinia bercovieri
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Yersinia; Yersinia bercovieri
• CAZyme ID: MGYG000002524_00617
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1815		194654.53	4.9338

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002524	4273500	Isolate	Finland	Europe

• Gene Location: Start: 78780; End: 84227 Strand: +

Full Sequence      

MLQQNRNAGELQLTATDLVCAREILESHKQSKDPGPMYNYLASKGDRYAVLANGVVRGDS
FAGAMAIYYMERTAADHNKPLTEAQIKDIRFDMAGEYIEVLQNRLDISTGTIYGDINHKE
AGQFHEIVFKRHGLPSETWTLEPVFNAIQETSRPTYWQHVLNAAGKPAKELKLSFETYNM
MAQSSMFSPEAIRKTSRRWFSIIDSPSGYWALGKTATNQLFSADDETSIVIPQCNIEIEI
NPTPQATRRIADEDQLQRDVTNGYLVNKPTHSFSFTDGTLDKIDFASVQMGSMASGGVRP
GEIQLDPNVQPSRYLSDYYLEQPAYMLPETGLFDAATLNGLSAQTTFNTYVDPLLLDLSG
RGVKMSGLREGVLFDIDNSGSLKRTGWVGPESGMLVIDNGSGRIDNISQIYSEYYGGTAG
IDGLPGQKLFEHGFAALAEDDSDGNGVIDSADPIWAKLRVWQDISHNGQVDEGELKTLDE
WGISRIDVAATLVGRDDGKGNQIVARGLFTINDKQQEVLAVNFVGSSVSNRVTPLDDGAL
LTSSSDEVTTTAYVSFNHEGEILNAAQLQAKNVYGARGDDDLIASPEGSWLVGRGGRNTY
TGNSGNDVFVISASDDTRYIQGKGGTDTVLITGDQGVGLNMARSGITIAQGGDGDDIIIS
GGNNSVFIQGGNGNSTLVGGGGNDVLSGGRGKNKIIGGSGKAVIYAGPQGDTIYASEQGS
IIHAGGGADRIYGNKSNDVIVAGQGDALIDGGEGINVLALHGSYADYTITRTESGYQLKD
KVAGRDGTLTLKRIQKLNFADIAAVELDARTIIPVNDVLIYGNGNPISRLQSTNIPAQAL
LRNDFCFDPEAELVIAKVSDAVGGTVQLKDDGNVLFTPDSRFTGVMSFKYEVKSATGAPA
LSVLDLSSGESATMRATVLLRSADIPSDPQFIKQSYLNEINVIPIWQEYTGKGVRIGQFE
PGGQFATGPMIFDINHPDLAANVDPSWLATQKRSGVLPEEVSNHATMVAGVMVAAKNHLG
GVGVAHEATLGGHYLSNDGADLTTLGKMSSYDVVNHSWGFKHGFAISNVSSGMINLANTL
NLTLHYAAANGRGGLGTIIVTSGGNQRAQGGSTQGSLMSNSRFAIQVAAMNSKADLSTLQ
THRAPFSNPGSSLLVSAPGSHILSSSQQITAQRGAVFGAQYSTEQGTSFAAPIVSAIAAL
MLQANPNLGYRDVQAILALSARRVKDPTSEWRTNGATRWNGGGMQVSHDYGFGAVDARAA
VRLAESWTHQRSDANQQVLQAKHQFSTGESLLAGMTRAASVILKGEIEVEQVEVDFSANV
GRLGDLTVTLISPNGTQSILLDGAEKKMADSGDDVDTGSEIAGDFNHTFMSTLQRGEHSG
GQWRLVVKNAKNGLPVELKNWSIRLFGNSISRDDTYVYTDEFAALVAQEPTRAFLHDSDD
GVVGGRNTLNMSAVAADVKVNLLTGEATLGDAQLTLRSPARIHNLISGDGNDILIAGRQH
SVLDGGRGLNVLTGGAGKEIFVVRKRASGSDWIVNFDADRGEVIHLIGFADKRFRALRLK
QDGQDVRVQLNDNQHIIVKDREVATLKAHHFHFADTFTPPAGYFDSSIRIDNPQSQPTLL
DKPAAAKQTEIILNGGGGGVSLSFVDNKMVASLVGKVYQRENAKPSIFVVTPQQGEWRYG
NAVQGFRHGIDKIDLSAMGIRNFSELTLIKRSSMVINGLALIQGVDITSAALDFEGKSLE
LAYLDGLDVEQLDAQDFIFADTAVMLSDSPFVHDDMSQLINITADFDRKVRDYEGVFSPP
QTVQRLAPTLTASPF

Enzyme Prediction     

No EC number prediction in MGYG000002524_00617.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04059	Peptidases_S8_Protein_convertases_Kexins_Furin-like	1.08e-64	926	1222	1	297	Peptidase S8 family domain in Protein convertases. Protein convertases, whose members include furins and kexins, are members of the peptidase S8 or Subtilase clan of proteases. They have an Asp/His/Ser catalytic triad that is not homologous to trypsin. Kexins are involved in the activation of peptide hormones, growth factors, and viral proteins. Furin cleaves cell surface vasoactive peptides and proteins involved in cardiovascular tissue remodeling in the TGN, at cell surface, or in endosomes but rarely in the ER. Furin also plays a key role in blood pressure regulation though the activation of transforming growth factor (TGF)-beta. High specificity is seen for cleavage after dibasic (Lys-Arg or Arg-Arg) or multiple basic residues in protein convertases. There is also strong sequence conservation.
cd07498	Peptidases_S8_15	2.94e-30	972	1217	10	239	Peptidase S8 family domain, uncharacterized subfamily 15. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
pfam00082	Peptidase_S8	1.91e-28	972	1229	13	280	Subtilase family. Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see pfam00089). Structure is an alpha/beta fold containing a 7-stranded parallel beta sheet, order 2314567.
cd00306	Peptidases_S8_S53	1.88e-24	972	1220	10	241	Peptidase domain in the S8 and S53 families. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) family include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.
cd07477	Peptidases_S8_Subtilisin_subset	1.66e-21	972	1218	11	227	Peptidase S8 family domain in Subtilisin proteins. This group is composed of many different subtilisins: Pro-TK-subtilisin, subtilisin Carlsberg, serine protease Pb92 subtilisin, and BPN subtilisins just to name a few. Pro-TK-subtilisin is a serine protease from the hyperthermophilic archaeon Thermococcus kodakaraensis and consists of a signal peptide, a propeptide, and a mature domain. TK-subtilisin is matured from pro-TK-subtilisin upon autoprocessing and degradation of the propeptide. Unlike other subtilisins though, the folding of the unprocessed form of pro-TK-subtilisin is induced by Ca2+ binding which is almost completed prior to autoprocessing. Ca2+ is required for activity unlike the bacterial subtilisins. The propeptide is not required for folding of the mature domain unlike the bacterial subtilases because of the stability produced from Ca2+ binding. Subtilisin Carlsberg is extremely similar in structure to subtilisin BPN'/Novo thought it has a 30% difference in amino acid sequence. The substrate binding regions are also similar and 2 possible Ca2+ binding sites have been identified recently. Subtilisin Carlsberg possesses the highest commercial importance as a proteolytic additive for detergents. Serine protease Pb92, the serine protease from the alkalophilic Bacillus strain PB92, also contains two calcium ions and the overall folding of the polypeptide chain closely resembles that of the subtilisins. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SBW81129.1	2.50e-215	231	1596	267	1678
SDU86200.1	3.23e-213	231	1596	271	1682
AOH85652.1	2.77e-15	352	489	44	185
AEE95448.1	2.77e-09	926	1320	149	485
AIY26234.1	6.52e-09	918	1291	120	491

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1P8J_A	4.36e-32	926	1409	6	467	CrystalStructure Of The Proprotein Convertase Furin [Mus musculus],1P8J_B Crystal Structure Of The Proprotein Convertase Furin [Mus musculus],1P8J_C Crystal Structure Of The Proprotein Convertase Furin [Mus musculus],1P8J_D Crystal Structure Of The Proprotein Convertase Furin [Mus musculus],1P8J_E Crystal Structure Of The Proprotein Convertase Furin [Mus musculus],1P8J_F Crystal Structure Of The Proprotein Convertase Furin [Mus musculus],1P8J_G Crystal Structure Of The Proprotein Convertase Furin [Mus musculus],1P8J_H Crystal Structure Of The Proprotein Convertase Furin [Mus musculus]
6YD3_A	4.98e-32	926	1409	6	467	ChainA, Furin [Homo sapiens],6YD4_A Chain A, Furin [Homo sapiens],6YD7_A Chain A, Furin [Homo sapiens],7O1U_A Chain A, Furin [Homo sapiens],7O1W_A Chain A, Furin [Homo sapiens],7O1Y_A Chain A, Furin [Homo sapiens],7O20_A Chain A, Furin [Homo sapiens],7O22_A Chain A, Furin [Homo sapiens],7QXY_A Chain A, Furin [Homo sapiens],7QXZ_A Chain A, Furin [Homo sapiens],7QY0_A Chain A, Furin [Homo sapiens],7QY1_A Chain A, Furin [Homo sapiens],7QY2_A Chain A, Furin [Homo sapiens]
4OMC_A	5.13e-32	926	1409	6	467	X-raystructure of human furin in complex with the competitive inhibitor meta-guanidinomethyl-Phac-RVR-Amba [Homo sapiens],4OMC_B X-ray structure of human furin in complex with the competitive inhibitor meta-guanidinomethyl-Phac-RVR-Amba [Homo sapiens],4OMC_C X-ray structure of human furin in complex with the competitive inhibitor meta-guanidinomethyl-Phac-RVR-Amba [Homo sapiens],4OMC_D X-ray structure of human furin in complex with the competitive inhibitor meta-guanidinomethyl-Phac-RVR-Amba [Homo sapiens],4OMC_E X-ray structure of human furin in complex with the competitive inhibitor meta-guanidinomethyl-Phac-RVR-Amba [Homo sapiens],4OMC_F X-ray structure of human furin in complex with the competitive inhibitor meta-guanidinomethyl-Phac-RVR-Amba [Homo sapiens],4OMD_A X-ray structure of human furin in complex with the competitive inhibitor Phac-RVR-Amba [Homo sapiens],4OMD_B X-ray structure of human furin in complex with the competitive inhibitor Phac-RVR-Amba [Homo sapiens],4OMD_C X-ray structure of human furin in complex with the competitive inhibitor Phac-RVR-Amba [Homo sapiens],4OMD_D X-ray structure of human furin in complex with the competitive inhibitor Phac-RVR-Amba [Homo sapiens],4OMD_E X-ray structure of human furin in complex with the competitive inhibitor Phac-RVR-Amba [Homo sapiens],4OMD_F X-ray structure of human furin in complex with the competitive inhibitor Phac-RVR-Amba [Homo sapiens],4RYD_A X-ray structure of human furin in complex with the competitive inhibitor para-guanidinomethyl-Phac-R-Tle-R-Amba [Homo sapiens],4RYD_B X-ray structure of human furin in complex with the competitive inhibitor para-guanidinomethyl-Phac-R-Tle-R-Amba [Homo sapiens],4RYD_C X-ray structure of human furin in complex with the competitive inhibitor para-guanidinomethyl-Phac-R-Tle-R-Amba [Homo sapiens],4RYD_D X-ray structure of human furin in complex with the competitive inhibitor para-guanidinomethyl-Phac-R-Tle-R-Amba [Homo sapiens],4RYD_E X-ray structure of human furin in complex with the competitive inhibitor para-guanidinomethyl-Phac-R-Tle-R-Amba [Homo sapiens],4RYD_F X-ray structure of human furin in complex with the competitive inhibitor para-guanidinomethyl-Phac-R-Tle-R-Amba [Homo sapiens],5JMO_A X-ray structure of furin in complex with the inhibitory antibody Nb14 [Homo sapiens],5JMO_B X-ray structure of furin in complex with the inhibitory antibody Nb14 [Homo sapiens],5JXG_A Structure of the unliganded form of the proprotein convertase furin. [Homo sapiens],5JXH_A Structure the proprotein convertase furin in complex with meta-guanidinomethyl-Phac-RVR-Amba at 2.0 Angstrom resolution. [Homo sapiens],5JXI_A Structure of the unliganded form of the proprotein convertase furin in presence of EDTA. [Homo sapiens],5JXJ_A Structure of the proprotein convertase furin complexed to meta-guanidinomethyl-Phac-RVR-Amba in presence of EDTA [Homo sapiens],5MIM_A Xray structure of human furin bound with the 2,5-dideoxystreptamine derived small molecule inhibitor 1n [Homo sapiens],6EQV_A X-ray structure of the proprotein convertase furin bound with the competitive inhibitor Phac-Cit-Val-Arg-Amba [Homo sapiens],6EQW_A X-ray structure of the proprotein convertase furin bound with the competitive inhibitor 4-aminomethyl-phenylacetyl-Arg-Val-Arg-Amba [Homo sapiens],6EQX_A X-ray structure of the proprotein convertase furin bound with the competitive inhibitor Arg-Arg-Arg-Val-Arg-Amba [Homo sapiens],6HLB_A X-ray structure of furin in complex with the cyclic peptide c[succinyl-Phe-2-Nal-(Arg)4-Lys]-Arg-4-Amba [Homo sapiens],6HLD_A X-ray structure of furin in complex with the cyclic peptide c[succinyl-Phe-2-Nal-(Arg)3-Lys]-Lys-4-Amba [Homo sapiens],6HLE_A X-ray structure of furin in complex with the P6-P2-cyclized peptide H-Lys-Arg-Arg-Tle-Lys-4-Amba [Homo sapiens],6HZA_A X-ray structure of furin in complex with the cyclic peptide c[glutaryl-Arg-Arg-Lys]-Arg-4-Amba [Homo sapiens],6HZB_A X-ray structure of furin in complex with the cyclic inhibitor c[glutaryl-Arg-Arg-Lys]-Lys-4-Amba [Homo sapiens],6HZC_A X-ray structure of furin in complex with the cyclic inhibitor c[glutaryl-BVK-Lys-Arg-Arg-Tle-Lys]-4-Amba [Homo sapiens],6HZD_A X-ray structure of furin in complex with the cyclic inhibitor c[glutaryl-Arg-Arg-Arg-Lys]-Arg-4-Amba [Homo sapiens],6YD2_A Chain A, Furin [Homo sapiens]
4Z2A_A	2.34e-31	926	1409	4	465	Crystalstructure of unglycosylated apo human furin @1.89A [Homo sapiens]
7LCU_A	3.35e-31	926	1409	6	467	ChainA, Furin [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P23377	8.94e-31	926	1409	113	574	Furin OS=Rattus norvegicus OX=10116 GN=Furin PE=1 SV=1
Q28193	1.58e-30	926	1409	113	574	Furin OS=Bos taurus OX=9913 GN=FURIN PE=1 SV=1
P23188	3.58e-30	926	1409	113	574	Furin OS=Mus musculus OX=10090 GN=Furin PE=1 SV=2
P09958	3.60e-30	926	1409	113	574	Furin OS=Homo sapiens OX=9606 GN=FURIN PE=1 SV=2
P29119	2.41e-29	926	1392	111	554	Furin-1 OS=Xenopus laevis OX=8355 GN=furin PE=2 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
1.000065	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002524_00617.