CAZyme Information: MGYG000002458_03234

Basic Information

• Species: Yersinia aleksiciae
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Yersinia; Yersinia aleksiciae
• CAZyme ID: MGYG000002458_03234
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1822		195165.93	5.5073

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002458	4525402	Isolate	Finland	Europe

• Gene Location: Start: 6912; End: 12380 Strand: +

Full Sequence      

MLEKKSNLGKLQLNTADLKCAREILESHKESKNPGPMYDFLITKGDRYAILANGVVNGNS
IAGEIAISYLKSVAGGHNQPITEVQLINIRYDMALGYLDMLQSRLDSRTGTIYGDINHKQ
AEKFHYIVLNKYGLPPEAWTLNPVLKVMPENFREGYWQDTLNAAGKPAKEIWLSYYTTKY
MFDKLSTSEAVDQPEIRIWLKTVSDIDNLGAVASALGNQLFTSDEAPPVSTQQCNIDISI
TPSPLATQRITDEDQARRDVANGYLVNKPTHSLSFTDGTLDKTDFASVQMGSMASGGIRP
GEIQLDPNTQPSRYLSEYYLERPYYLLPETGLFDAATLNGLSAQTTMNTYVDPLLLDLSG
RGVKISGLRDGVLFDSDNSGTLKRTGWAGPDTGMLVIDNGSGKIENISQMYSEYYAGATG
VEGQPGERRYQDGFAALASEDSDGNGVIDKGDPVWHKLRVWYDSSGNGIVDRGELRTLHH
WRISQINVDASAIDNDIRNGNRVMARSIFMMNGKPREVLAVNFISSPVSNTITKRDNNGA
FIRSVIGDVTTTAYVQLSNKKAKLFADVLAVNNIYGGNKDDILTASAAGSWLVGRGGSNT
YKGKSGNDVFVISASDDPNNIQGNGGTDTVLITGDKAVALNMAHSGITIAQGGDGDDIIL
SGGDSGVFIKGGKGNSTLVGGGGNDVLSGGGGKNRIVGGSGKAVIYAGSQGDIIYASEQG
SIIHAGGGTDRIYGNKSDDVIVAGKGDALIDGGGGINVVALHGSYADYTMTRTKGGYQVK
DKVADRDGTLTLKNIQKLNFADISAVALGENRIIPLNDILIYGDGSPISRFLDTNIPAQA
VLGNDFRFNNETKLVIANVSDAIGGTVQLKDDGDVLFMPDSTFTGVMSFKYEVKSTTGDP
ALFVMNLPSGESTTMRATVVMRSADIPNDPLLIKQTYLNDINVIPVWQDYTGKGVRIGQF
EPGGQFATVPEIFDIQHPDLVANVDPHWLATQQNTGVLPEAISNHASMVAGVMVAAKNQV
GGVGVAYDATLGGHYLSNNGADLTTLGKMSSYDVVNHSWGFKHEFAISNVSSGMINLANI
LNTTLHYAAANGRGGLGTIIVTSGGNQREQGGSTQGSLMSNSRFGIQVGAMNAKADLSTL
RAHSEPFSNTGASLLISAPGSHILSSSHQITTERGAVFGAQYSHEQGTSFAAPIVSGIAA
LMLQANPNLGFRDVQTILALSARRVDDTATQWRINRAKNWNGGGMHVSHDYGFGVVDARA
AVRLAESWTVQKTNANQQVLEARHRFGARGPLSAGMARETSIVLSDNLDFDIEQVEVDFS
ANVGRLGDLTLTLISPNGTKSILLDRAGKKTTDSDDHGDVDVDTGSQISGDFNHTFMSTH
HRGEQSGGQWRLMVRNSQNGLPVELKKWSLRLFGSQISHDDTYFYTDEFTALVAQLPARA
ILDDVIDGVAGGRNTLNAAAMSGDVKVNLLTGKASLGGTPLTIRSPEHIHNLMGGDGNDT
LTAGKQHSVLDGGRGINLLEGGVGKEIFVVRQRANGSDWIVNFDADKGELIQLVGFADQR
FDTVQLIQAEKDVKVQLADNQHIIIKDRQVTALKAHHFHFEDTFAPPAGYFDSRMRIEGP
KAAPIVLDTSAAAKPSGIMLNGGGGGVSLSFVDNKMVAALSGKVYQRDNAKPSIYVVMSQ
QGKLEYGNAVRGFRAGIDKIDLSAVGIRNFSELTLTKRRSMVINGLALIQGVDIKSAAQG
PEGHSIELAYLDGLDVEHLDAKDFIFAEADAMLSDSPFTHDDMGQLINITADFDRSIRDY
ESVFVPAKTAQLVAPTLTAGPC

Enzyme Prediction     

No EC number prediction in MGYG000002458_03234.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04059	Peptidases_S8_Protein_convertases_Kexins_Furin-like	1.63e-63	927	1223	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	8.94e-27	973	1218	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.
cd04848	Peptidases_S8_Autotransporter_serine_protease_like	1.75e-25	951	1223	1	267	Peptidase S8 family domain in Autotransporter serine proteases. Autotransporter serine proteases belong to Peptidase S8 or Subtilase family. Subtilases, or subtilisin-like serine proteases, have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Autotransporters are a superfamily of outer membrane/secreted proteins of gram-negative bacteria. The presence of these subtilisin-like domains in these autotransporters are may enable them to be auto-catalytic and may also serve to allow them to act as a maturation protease cleaving other outer membrane proteins at the cell surface.
pfam00082	Peptidase_S8	5.30e-25	973	1229	13	279	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	1.17e-22	973	1221	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SBW81129.1	9.57e-226	227	1603	268	1678
SDU86200.1	1.94e-225	193	1603	230	1682
AIY26234.1	1.14e-08	919	1277	120	478
QLI81262.1	2.17e-07	996	1266	222	474
CAG23448.1	5.38e-07	919	1224	121	443

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1R64_A	5.08e-32	928	1422	14	480	The2.2 A crystal structure of Kex2 protease in complex with Ac-Arg-Glu-Lys-boroArg peptidyl boronic acid inhibitor [Saccharomyces cerevisiae],1R64_B The 2.2 A crystal structure of Kex2 protease in complex with Ac-Arg-Glu-Lys-boroArg peptidyl boronic acid inhibitor [Saccharomyces cerevisiae]
2ID4_A	6.92e-32	928	1422	21	487	The1.9 A structure of Kex2 in complex with an Ac-R-E-R-K-chloromethyl ketone inhibitor. [Saccharomyces cerevisiae],2ID4_B The 1.9 A structure of Kex2 in complex with an Ac-R-E-R-K-chloromethyl ketone inhibitor. [Saccharomyces cerevisiae]
1OT5_A	1.16e-31	928	1417	12	473	The2.4 Angstrom Crystal Structure of Kex2 in complex with a peptidyl-boronic acid inhibitor [Saccharomyces cerevisiae],1OT5_B The 2.4 Angstrom Crystal Structure of Kex2 in complex with a peptidyl-boronic acid inhibitor [Saccharomyces cerevisiae]
1P8J_A	1.43e-31	927	1415	6	466	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	5.28e-31	927	1415	6	466	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O17798	2.35e-31	868	1415	118	643	Furin-like protease kpc-1 OS=Caenorhabditis elegans OX=6239 GN=kpc-1 PE=1 SV=3
P13134	3.87e-30	928	1422	134	600	Kexin OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=KEX2 PE=1 SV=1
Q63415	5.25e-30	928	1415	142	613	Proprotein convertase subtilisin/kexin type 6 OS=Rattus norvegicus OX=10116 GN=Pcsk6 PE=1 SV=1
P23377	6.28e-30	927	1415	113	573	Furin OS=Rattus norvegicus OX=10116 GN=Furin PE=1 SV=1
P29122	9.60e-30	928	1415	161	632	Proprotein convertase subtilisin/kexin type 6 OS=Homo sapiens OX=9606 GN=PCSK6 PE=1 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
1.000063	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002458_03234.