CAZyme Information: MGYG000001306_03278

Basic Information

• Species: Phocaeicola coprocola
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola coprocola
• CAZyme ID: MGYG000001306_03278
• CAZy Family: CBM67
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1267	MGYG000001306_67|CGC2	143939.6	7.2917

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001306	4295617	Isolate	not provided	not provided

• Gene Location: Start: 41859; End: 45662 Strand: -

Full Sequence      

MKTTYFIKTLLLTCCLIPAIMLAENVSVTQLKTEQLSNPMGIDTASPRLGWQLESDKQNV
MQTAYHILVASSPELLAQDKGDIWDSGKVQSSSSQWIQYAGKPLKSNDLCYWKVKSYTTV
GESEWSQPATWSIGLLGEVKWKGRWIGLDKVFPWEKETAHSRLSARYLRKEFSISKPIKR
ATVFICGLGLYELFINGQHIGNQVLTPAPTDYRKTVLYNTFDVTSLLTTNNAIGVTLGNG
RYYTMQQKYKSYKIVNFGYPKLRLNLLIEYTDDSKETIATDTSWRITANGPIRSNNEYDG
EIYDARYELGDWTKPGYDDSQWLEAERVGMPGGTLRSQMTSPMTIVQTIKPIKISPLGDK
YILDLGQNIAGWIRMKIKGNTGDTIRLRFSETLSANGELYRDNFRHAESTDFYICNGKEN
GATWAPRFVYHGFRFVEISGYKNAKLSDFTGEVVSDNLEPIGTFECSDTTLNRIHQNAWW
GILDNYKGMPVDCPQRDERQPWLGDRTMGCWGESFLFDNSTLYSKWTRDICEAQREDGCI
PDVAPAFWMYYSDNVTWPAALPFACDMLYTQFGNREPIERCYPYIRKWMLHLHKEYLKDG
LITKDRYGDWCVPPESLELIHSKDSARITDGTLISTAYYIKLLDMMSRFASLQNLEEDRN
QWQAWAKEMKDAFNKKYLHIERGTSQKPGNPLYPDSIRYSNNTVTANLLPLAFDIVPEDC
QKDVTGQIIANTILRNGGHIGCGVIGVQWLLRELSRRGFSDVAFLLASNKTYPSWGYMAQ
QGATTIWELWNGNTANPAMNSGNHVMLLGDLLPWCYENAAGIRSDREKTGFKHIILKPDF
SIQNLFWVNASYRSLYGKIESRWKKTLTHVEWDITIPCNTTAEVHFPDGSIQQIGSGKYH
YAVEIPAIHPAVIQNEFLYEKAPFPECHASTIVELDNGDLVTAFFGGTKERNPDVCIWVC
RKSHDSNTWTAPIKAADGVFDLDDPDATIAGVTADIKDHRKACWNPVLFQVPGGDLLLFF
KIGLNVPDWTGWLVRSKDGGKTWSKREPLPKGFLGPIKNKPEFINGRIICPSSTEGNAGW
RIHMEYSDDMGKTWKTTGPIDAEQEFLSQHQGIGADDSLKRPIQVIQPSILKHKDGTLQV
ICRTRNSHLATSWSKDNGTTWSKVTLIDELPNNNSGTDAVTLKDGRHVLVYNNSKPQLRA
KKAVRTPLNLALSEDGIHWKPVLTLEDSPIREYSYPAIIQGKDGKLHITFTWRRELIKYM
KIDLDKL

Enzyme Prediction     

No EC number prediction in MGYG000001306_03278.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH78	359	885	1.1e-157	0.9841269841269841
GH33	919	1250	5.3e-38	0.9122807017543859
CBM67	154	333	2.3e-37	0.9545454545454546

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam17389	Bac_rhamnosid6H	4.25e-131	462	818	4	339	Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.
pfam13088	BNR_2	1.90e-98	938	1248	1	280	BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
pfam08531	Bac_rhamnosid_N	6.78e-72	176	347	1	172	Alpha-L-rhamnosidase N-terminal domain. This family consists of bacterial rhamnosidase A and B enzymes. This domain is probably involved in substrate recognition.
cd15482	Sialidase_non-viral	6.06e-54	917	1263	4	339	Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
pfam05592	Bac_rhamnosid	6.86e-35	352	455	1	102	Bacterial alpha-L-rhamnosidase concanavalin-like domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADY36775.1	0.0	6	1267	9	1270
QIU95828.1	0.0	22	1263	20	1284
CBK65853.1	0.0	26	1266	22	1285
QUR43127.1	0.0	26	1266	22	1285
QUT29077.1	0.0	26	1266	22	1285

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6I60_A	2.60e-188	19	887	22	899	Structureof alpha-L-rhamnosidase from Dictyoglumus thermophilum [Dictyoglomus thermophilum H-6-12],6I60_B Structure of alpha-L-rhamnosidase from Dictyoglumus thermophilum [Dictyoglomus thermophilum H-6-12]
3W5M_A	2.37e-122	28	907	6	1034	CrystalStructure of Streptomyces avermitilis alpha-L-rhamnosidase [Streptomyces avermitilis MA-4680 = NBRC 14893],3W5N_A Crystal Structure of Streptomyces avermitilis alpha-L-rhamnosidase complexed with L-rhamnose [Streptomyces avermitilis MA-4680 = NBRC 14893]
6GSZ_A	5.01e-105	27	903	3	865	Crystalstructure of native alfa-L-rhamnosidase from Aspergillus terreus [Aspergillus terreus]
4X6K_A	2.08e-08	1036	1267	240	482	Crystalstructure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with Siastatin B [[Ruminococcus] gnavus CC55_001C]
4X47_A	2.09e-08	1036	1267	243	485	Crystalstructure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with Neu5Ac2en [[Ruminococcus] gnavus ATCC 29149],4X49_A Crystal structure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with oseltamivir carboxylate [[Ruminococcus] gnavus ATCC 29149],4X4A_A Crystal structure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with 2,7-Anhydro-Neu5Ac [[Ruminococcus] gnavus ATCC 29149]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
T2KNB2	2.49e-137	19	894	22	886	Alpha-L-rhamnosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22090 PE=1 SV=2
P9WF03	3.16e-132	24	883	27	875	Alpha-L-rhamnosidase OS=Alteromonas sp. (strain LOR) OX=1537994 GN=LOR_34 PE=1 SV=1
T2KPL4	1.86e-130	37	894	41	914	Alpha-L-rhamnosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22170 PE=2 SV=1
Q82PP4	6.92e-121	28	903	6	1030	Alpha-L-rhamnosidase OS=Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680) OX=227882 GN=SAVERM_828 PE=1 SV=1
T2KM26	5.89e-18	274	912	513	1158	Bifunctional sulfatase/alpha-L-rhamnosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22250 PE=1 SV=2

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
0.000458	0.996733	0.002150	0.000251	0.000226	0.000186

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001306_03278.