CAZyme Information: MGYG000002292_02136

Basic Information

• Species: TF01-11 sp003529475
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; TF01-11; TF01-11 sp003529475
• CAZyme ID: MGYG000002292_02136
• CAZy Family: GH5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1608		174355.59	6.7602

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002292	3137432	Isolate	China	Asia

• Gene Location: Start: 73875; End: 78701 Strand: +

Full Sequence      

MKRNKRIMAIIMTIAMVLTSANLPQISIKAKAAVTPPAENMKDTSILTVKGDDLSSNLGN
HVSGEAYNGYLQSMTKASANADYYKITFKVAEGTAEDTKIVTFQPYDTSYQGWQDNIIKL
SDAQYDEENAQYVAYISGDKIRDSYTTGGKFNGINVSFCQAEPAITLTGLYTSKVVDPNA
TPSPEEVRWEEEQKVVVWGDDSKTTYGHEIMQDVSVQDIVAGLGDAGSKFAFSKVKGQKV
TVYIKVTKCSRYSRIKISGGNLAANSVTSNKELIGVDNTTNMKENGGSGYKNSAHFLHAG
WGTTGGYGSGMGQKESAIYKFADSSVKTGTEESAGVRLRRMTTDVEAYICGIKFGSVGSV
TVSQPDADGKVTFKEGFDASNVESWNKDDTDVEPKPEPELRADEAKAIQTIIDIFKGYKQ
SEILDETVWNTIKSDIKDAEALVADETSLSKDIKALRKQMESYTATVTEEIDRTATRNGL
KESIDYCKSLKEGDYSNKDTFAKLADAITTAEKAYTNVSDTRLNYKAARDTLEKVRVALA
KNVSTESSNPKTFRILDKKTVTKEMGAGINLGNTMDGGLYDSSETGWQAYKTTKDYIKAL
HDAGYNTVRIPVTWGSHINDDYTIDEAWINRVQEIVDYCVDQDMYAIVNIHHDGAANHDD
RGNNTPACWLDTYSQNIEKVYQKYEGVWNTIANRFKDYDEHVIFESMNEVTDAHGTATNE
DDAVLNALNQLFINTVRATGSNNTKRWLAITGRFATTAAIITMPEDTLADSGDLGTTRLM
FAVHIYKSNNNVRWSYDDLKQWQSSMSSSYKNVGNLDVNMPIYVGEYGVRTKAQNGSATG
YNNAERALNYEMCAAIADFYNAVPVVWDQGTGNYLGVETEQGLFTDWNRPELKPVYDDVV
HGTIRGTLEAGKSTDLSERMSAIYTSYGHATTSDNSVSKDPEIEKATDIALSDTKVEIKA
GERKTITATPDSSRDIVLWSTADDTVATVYDGVIHAKAGGVTTVYAKSQSGSVEKAIQVI
VQSTGEETATAIKTEKAYYEMTEGDTLTLNASLTPADSKDAITYTSSNTSIATVSSSGKV
TAENAGKTYIIVKAASGVSTIVAIKVNKKSSSGTVNVTLNALFANGLTEKSEPVTMNGDG
QYTLTFDLGKDLSDDGVKAGITKLEDLTAIYIRDTNTLKPVVSAASIRYDKITVNDKELT
LKKLDSMDADGFKNLLKDNGQLDSNDPINGWDGCAVEEVSINSSKHSVSFTGVDNPTKIS
VTFTIKGMKFFPGKEKEKEATKIESVTANKIVMPEIGSSTEIELNMTPVTTDSEVTFYST
DSAVAVVDNAAHTVDADGKIKVNVTAVGKGTTTIVGITENGLKVFYTVGVGDMSADDLAE
PQDPTPSGLDGSEPEPTPTVEPTATPTVEPTATPTNKPAEPTSPANGAKDQKITAPAKLT
KAISSKAFAIKAKTDGNGKLTYKSSNTKVAAINAKGVIKVKAYGTTNIVINAAATNNYKA
AQKVCKLTVTPKAVKVTKVTRAKSGKKISLKWKKDKTVKGYQVTYSTDKKFKKGVKKVTV
KKAKTVKKTISKGIKAKKKCYVKVRSYVKAGGKTIYGPYSKVRKVSAK

Enzyme Prediction     

No EC number prediction in MGYG000002292_02136.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	583	870	6.4e-71	0.9927536231884058

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00150	Cellulase	1.41e-46	582	868	14	267	Cellulase (glycosyl hydrolase family 5).
COG2730	BglC	1.05e-17	547	744	33	232	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
pfam04886	PT	2.25e-06	1395	1423	1	32	PT repeat. This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a variety of proteins, however it is not clear if these repeats are homologous to each other. The alignment represents nine copies of this repeat.
pfam04886	PT	2.82e-06	1392	1422	4	35	PT repeat. This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a variety of proteins, however it is not clear if these repeats are homologous to each other. The alignment represents nine copies of this repeat.
NF033186	internalin_K	9.90e-06	1307	1446	432	572	class 1 internalin InlK. Internalins, as found in the intracellular human pathogen Listeria monocytogenes, are paralogous surface-anchored proteins with an N-terminal signal peptide, leucine-rich repeats, and a C-terminal LPXTG processing and cell surface anchoring site. Members of this family are internalin K (InlK), a virulence factor. See articles PMID:17764999. for a general discussion of internalins, and PMID:21829365, PMID:22082958, and PMID:23958637 for more information about internalin K.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AUO18792.1	2.13e-188	463	1374	162	1050
AUO19859.1	1.16e-114	462	1106	19	642
BCN29385.1	1.32e-52	545	1006	339	786
QNU65955.1	1.50e-50	542	897	28	409
BAE44526.1	1.04e-49	542	906	27	403

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2JEP_A	2.74e-47	557	906	34	393	Nativefamily 5 xyloglucanase from Paenibacillus pabuli [Paenibacillus pabuli],2JEP_B Native family 5 xyloglucanase from Paenibacillus pabuli [Paenibacillus pabuli],2JEQ_A Family 5 xyloglucanase from Paenibacillus pabuli in complex with ligand [Paenibacillus pabuli]
4IM4_A	3.27e-46	561	906	10	334	ChainA, Endoglucanase E [Acetivibrio thermocellus],4IM4_B Chain B, Endoglucanase E [Acetivibrio thermocellus],4IM4_C Chain C, Endoglucanase E [Acetivibrio thermocellus],4IM4_D Chain D, Endoglucanase E [Acetivibrio thermocellus],4IM4_E Chain E, Endoglucanase E [Acetivibrio thermocellus],4IM4_F Chain F, Endoglucanase E [Acetivibrio thermocellus]
6MQ4_A	1.27e-45	561	907	15	349	ChainA, cellulase [Acetivibrio cellulolyticus]
6WQP_A	1.30e-45	550	892	8	348	GH5-4broad specificity endoglucanase from Ruminococcus champanellensis [Ruminococcus champanellensis],6WQP_B GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis [Ruminococcus champanellensis],6WQV_A GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis with bound cellotriose [Ruminococcus champanellensis],6WQV_B GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis with bound cellotriose [Ruminococcus champanellensis],6WQV_C GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis with bound cellotriose [Ruminococcus champanellensis],6WQV_D GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis with bound cellotriose [Ruminococcus champanellensis]
3NDY_A	5.32e-42	554	903	8	344	Thestructure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_B The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_C The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_D The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDZ_A The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_B The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_C The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_D The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O08342	1.25e-46	553	906	35	398	Endoglucanase A OS=Paenibacillus barcinonensis OX=198119 GN=celA PE=1 SV=1
P23660	1.93e-43	564	875	33	339	Endoglucanase A OS=Ruminococcus albus OX=1264 GN=celA PE=1 SV=1
P28621	2.41e-43	543	917	26	384	Endoglucanase B OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engB PE=3 SV=1
P10477	2.91e-42	561	906	60	384	Cellulase/esterase CelE OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celE PE=1 SV=2
P16216	4.86e-41	552	892	63	390	Endoglucanase 1 OS=Ruminococcus albus OX=1264 GN=Eg I PE=1 SV=1

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
0.000222	0.999059	0.000210	0.000186	0.000151	0.000134

TMHMM  Annotations     

start	end
7	26