CAZyme Information: MGYG000001027_00582

Basic Information

• Species: CAG-56 sp900752065
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-56; CAG-56 sp900752065
• CAZyme ID: MGYG000001027_00582
• CAZy Family: GH123
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1870		204054.26	4.9692

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001027	2760146	MAG	Sweden	Europe

• Gene Location: Start: 359; End: 5971 Strand: +

Full Sequence      

MKKAGKKILCVLLTLVLALPLNLLPMQAAAGEADEVLTLKPNVEDTAQENYFTYTAYTGK
TWDRKESEAFIDLGTEDSKAEQCYYEIHFKGNGIKLYANKSTLHGMVKYTVDGKDEQTVD
LYATSRTGAQLVYEKSGLTEGDHVLKAVTLNQKNSASSAKIVNQVAYAEITHQPYTGGDP
DMGGTIADVNTQHTQNLYGTVKTQNTASAALKAWKNDKAISELVLFSKNCALENVTVTAS
ALTNGTATIPAGNVTATFIKSTKAYNGSYLGYGSKDRAVPAATASNRSESSDILYQKGGS
VDIPYNSLQPVWVEFAIPKGTAAGTYTGTLTANADGIAAPLTFTYTVEVQDAELPDVSEL
AKVFDVELWQYPYSSAEYYNVTPFSEEHLAIMRSSMEKYKEVGGHAITTTIVEEAWNGQT
YSKNDVHYPSMVKWTKNSDGSFAYDYTDFDKWVTFCKSLGLGDKIVLYSIAPWHNSFTYW
EGDTLKYEAFTPGNDRYNTVWTDFLTKLIAHLEEKGWFEESYIGIDERGFNAKAFDLIDS
VKNSQGVSLKTAGAMDGFVDKKDLAMQVDDLNVGDSAAQTHAEDFAQLLADREEAGLRTT
LYSCTEHRPGNFSLSAPMESYWSIVNAGKAGTAGFLRWAYDAWVEDPLNDTTHNAFEPGD
CFLIYPAEKNAEDKTCKSSVRLERMAEGFRDVNKLLLIEKEVPALADEIDALYAGISTTA
SLGRTYLTATEKTQLEEETNAFKAGVADITSKYIAAKSGGLTNDITSLAIEEGASASMAS
GSTMQLHTAFTPENVLNTRVNWSSSNPAAVTVSSTGKLTAVQAGTSVITAVSAQDSTKSA
AITITVTGAAVEDAAKVSYYSFDSMDGNVIKDEWGSRNGTSQGATLSDGKSGKALTITEA
GKSAVLNGTANVGDAWTVAYWVNGTASGGRSSVLMDSTKNYSFDTSISGAKGGVHVGTGS
GDILTFNYTYPVNTWVHMTWTQDKTNGLSLYINGELIQTNNWTATNAFTCPIDVIGGTGF
TGKIDELKIYNRVLTPAEISSIMQMEGLNIQETRKEMNIGDTWQIAVNLISSQADKTVTF
TSADPSIASVDKNGMVTAKKRGTTEITVENKAGGYKATVQIIVTKVLKLYNTLKDYELPE
QYLSDIEKHDLTHARHYLGQPDMIMLDDEKTLITVYPVGHGRGAIVMQVSTDAGETWTEK
TDAPQSWQTSYETPTIYKLNMTDGTTKLIVISGRPANFGAPTGGWDTSISTDNGQTWSEF
ETYCEYLGDGSRNETVVAMASLIQLKNEDGEYIDKWMGVYHDGGTFVNYKTYLTFDENGN
QQWSTPEPYLSEYRSIEQGHQICEVGLFRSPDGKRIVGLARSQSHNNPSTMFYSDDEGET
WSEPVDLPGSLAGERHKAVYDPTDPTGQRMIITFREICYDLNKNDQMDGNSDWLAGDWIG
WVGTYDQLMNLDDGQFRVLLCRDWAANAKSGDTGYTGIVVQSDGTFIMDTYGHWDKEVSE
SLIPYNVYNDLCYIKQAKFKLSDLDSMVLPDVKASIQNAINSAPTDASGYTRESWDALQE
ALKNAQAAVDGSSSTQLQCYAALEALKTAKLSLEEGTYEPAPEDPTEAKEQLEGVIAQAA
EKKDASKYTEDSWKDFQIALANAQKVQQNASSTKTEIEAAMAELNNAMGALKLADSAKPD
PSTGKPNIENPGQTVPLPTPDVTIEEGKIYDSGNYYYKVTSTDKKTAEVTGIKNKKITKI
TVYSSVKLGNDNYKITSIAASAFKNNKKVKSAVIRSNVESIGNNAFAGCTGLKTVSINST
KLKKIGNKAFFNCKKLKSIRIKSKVLTKAGKNAFKGISKKAVIKVPKAKYKKYVKVLAKK
GQSKTVKIKK

Enzyme Prediction     

No EC number prediction in MGYG000001027_00582.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH123	184	743	6.5e-165	0.9776951672862454

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam13320	DUF4091	7.04e-22	631	699	1	66	Domain of unknown function (DUF4091). This presumed domain is functionally uncharacterized. This domain family is found in bacteria, archaea and eukaryotes, and is approximately 70 amino acids in length. There is a single completely conserved residue G that may be functionally important.
sd00036	LRR_3	3.55e-21	1744	1846	14	114	leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions.
pfam13385	Laminin_G_3	1.96e-20	906	1040	9	151	Concanavalin A-like lectin/glucanases superfamily. This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.
sd00036	LRR_3	2.09e-20	1744	1836	37	127	leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions.
sd00036	LRR_3	4.57e-20	1754	1846	1	91	leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBA55846.1	0.0	26	1654	20	1714
VEG17315.1	0.0	26	1653	41	1734
BAQ98792.1	0.0	26	1653	20	1713
ADP36622.1	0.0	26	1653	20	1713
ALE12069.1	0.0	26	1653	13	1706

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5FQE_A	3.93e-102	171	755	19	604	Thedetails of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FQE_B The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FQF_A The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FQF_B The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FR0_A The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens]
5FQG_A	4.59e-101	171	755	19	604	Thedetails of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FQH_A The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens]
5L7V_A	3.61e-83	156	701	9	519	ChainA, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7V_B Chain B, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482]
5L7R_A	5.34e-83	156	701	24	534	ChainA, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7R_B Chain B, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7U_A Chain A, Glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7U_B Chain B, Glycoside hydrolase [Phocaeicola vulgatus ATCC 8482]
5HO0_A	1.59e-06	793	1044	580	845	Crystalstructure of AbnA (closed conformation), a GH43 extracellular arabinanase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5HO2_A Crystal structure of AbnA (open conformation), a GH43 extracellular arabinanase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5HOF_A Crystal structure of AbnA, a GH43 extracellular arabinanase from Geobacillus stearothermophilus, in complex with arabinopentaose [Geobacillus stearothermophilus],5HP6_A Structure of AbnA, a GH43 extracellular arabinanase from Geobacillus stearothermophilus (a new conformational state) [Geobacillus stearothermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
E8MGH9	1.62e-08	1533	1696	1738	1904	Beta-L-arabinobiosidase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=hypBA2 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
0.000279	0.999024	0.000205	0.000170	0.000149	0.000140

TMHMM  Annotations     

start	end
9	31