CAZyme Information: MGYG000002461_00717

Basic Information

• Species: Yersinia kristensenii
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Yersinia; Yersinia kristensenii
• CAZyme ID: MGYG000002461_00717
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1813		193692.99	5.6078

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002461	4771112	Isolate	Finland	Europe

• Gene Location: Start: 774153; End: 779594 Strand: -

Full Sequence      

MLQQNSNAGKLQLNAADLACARQLLEAHNESKDPGPMYDFLASKGDRYAILANGVVRGDS
IAGAMAIHYLESVAASHNQPITDIGLNDIRYDMALGYLDTQQSRLDKSPTGIIYGDIGHE
QATQFHNRVFNDHGLPSKAWTLDQVFKAIDERSQPIYWQWVLNAAGKPKEELWLSVDTYQ
KMALSAKVAPDGIRESSREWFDRVDSLSGYWALAKSSTSQLFSSDQTTAVAGQECNIDIN
ITPTPQAVQRIADEDQARRDVTNGYLVNKPTHSFSFTDSSLDKTDFTSVQMGGMASGGIR
PGEVQLDPNVQPSRYLSDYYLERPSYILPETGLFDAATLNSLSAQTTVNTYVDPLLLDLT
GKGVALTGIEDGVLFDTDNSRTLKRTGWAGPNTGMLVLDDGSGKIDNISQMYSEYYGGMA
GVNGQPGEKRYQNGFAALASEDADSNGAIDRHDPIWRKLRIWQDASHNGRVDPGELKTLD
EWQITQINLNASPVEDDTRGGNRVMARGVFSIRGRQHEVLAVNFASSPVSNSIFKRDANG
AFMRSVSNGVTTSAYAQLTDSSGIFSADELKVNNIYGGNGDDWLRASAAGSWLVGRGGSN
WYIGNTGDDVFVISASDDTENIRGNGGRDTVLIAGKKGVALNMARSGITLAQGGDGDDII
VSGGNRSVFIKGGNGNATLVGGGGNDVLAGGSGKNRIVGGSGKAVIYAGPQGDTIYASEQ
GSIIYAGGGADRIYGNKGNDVIEAGQGDALIDGGSGINVVALHGTHADYIITRTDSGYLI
RDKVAGRDGTLALKNIQKLNFSDISAIDLHGNTIIPIDDVLSFSQPGRAIHRHWEQRIPA
ASLLANDLQFNGGEPIYLASVGDAVGGTVKLNTQKDVIFTPDRTFTGMMSFKYEVGGIPA
ASVVDLSSGESAVMRATVMLLTPDIPQDPFIAKQTYLNDINVIPIWQNYTGKGIRIGQFE
PGGEFATGPEIFDIQHPDLVANVDPTWLATQKKTGVLPAEISNHATMVAGVMVAARNSSG
GIGVAYGATLGGHYLSNDGHDLTTLGKMSSYDVVNHSWSSKPDFALSHTEGGALNLPNTL
KTVARYAAANGRGGLGTIIVTAGGNQREQGGSAQGSLMNHTRFGIQVGAINAPADLSTLQ
THSAPFSNPGASLLVSAPGSRVLSSSHQIKAARGAVFGAEYSTEQGTSFAAPIVSGIAAL
MLEANPNLGYRDVQQILALSASRVKDPSSHWRINSAKNWNGGGMHVSHDYGFGAVDARAA
VRLAESWTSKNTDDNQQDLEQNHYYSLWRRLYAGGLDSSSVTMTNGLNVEQVEVDFSANI
GRLGDLTLKLISPSGSESILLNRAGKKTVVNDADTGSGLAGHFNYTFMSTHHRGEDSTGQ
WRLEVSTAKNALPVKLNSWSLRLFGRKPTADDIYFYTDEFAAQIVEQPARAILNDTVNGV
AGGRNTLNTAAMSGDVAVNLATGKANLAGSLLTIRSPETMHNVVSGDGNDILTAGRNNSL
LDGGRGRNTLVGGAGKEIFVVRKRAGGHDDIINFDANKGEVINLVGFAEKKFSALLLKQQ
RNDVHVQLADNQMIIIKNRQITALQAQHFNFQNRFTPPASYVDSRVSMDTPTPAVTKQHG
IRLNGGGGGITLRTNAQGKMVAALSGTVYQRENAEPSTFVVVPQEEQSDYGNAVRGFRHG
IDKIDLSAVGIRNFSELSVIKRNAMVINGLALIQGVNITSAATGLEGKSINLAYLDGVDV
EQLDAKDFIFADTETIFSTAETMQADAPFVPNDIAQLVNFIPDFVGAAREYQGICPQSKL
PQFLSHLLTASNY

Enzyme Prediction     

No EC number prediction in MGYG000002461_00717.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04059	Peptidases_S8_Protein_convertases_Kexins_Furin-like	6.79e-62	926	1221	1	296	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.
cd04848	Peptidases_S8_Autotransporter_serine_protease_like	2.19e-26	950	1217	1	262	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	3.22e-24	972	1253	13	287	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.
cd07498	Peptidases_S8_15	1.03e-23	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.
173787	cd00306	5.41e-23	1002	1220	44	241	Peptidases_S8_S53 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
SDU86200.1	3.75e-211	239	1591	280	1679
SBW81129.1	2.42e-210	239	1591	276	1675
AEE95448.1	1.43e-12	926	1320	149	485
AOH85652.1	3.01e-12	353	496	44	191
AIY26234.1	5.43e-10	940	1266	146	468

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1OT5_A	1.09e-32	928	1405	13	470	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]
1R64_A	1.16e-32	928	1405	15	472	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	1.58e-32	928	1405	22	479	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]
1P8J_A	1.05e-31	926	1408	6	468	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]
7LCU_A	1.86e-31	926	1418	6	476	ChainA, Furin [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O17798	7.54e-32	923	1405	172	642	Furin-like protease kpc-1 OS=Caenorhabditis elegans OX=6239 GN=kpc-1 PE=1 SV=3
P29145	6.06e-31	925	1390	155	609	PC3-like endoprotease variant B OS=Hydra vulgaris OX=6087 PE=2 SV=1
P29146	8.93e-31	925	1390	155	609	PC3-like endoprotease variant A OS=Hydra vulgaris OX=6087 PE=2 SV=1
P13134	9.63e-31	928	1405	135	592	Kexin OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=KEX2 PE=1 SV=1
P09958	3.59e-30	926	1408	113	575	Furin OS=Homo sapiens OX=9606 GN=FURIN PE=1 SV=2

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
1.000044	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002461_00717.