CAZyme Information: MGYG000001806_00637

Basic Information

• Species: Prevotella sp900553965
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900553965
• CAZyme ID: MGYG000001806_00637
• CAZy Family: PL11
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1496	MGYG000001806_13|CGC2	160009.58	5.1666

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001806	3097082	MAG	Denmark	Europe

• Gene Location: Start: 22410; End: 26900 Strand: +

Full Sequence      

MKRILFICVFFCLMGLTTRAQRHVDKLDRSLVAVKVNGGVYCSWRILGEEYYDVTYNIYR
DGTKLNDKPLTVSNYTDAGGTASSVYTVEPVVRGMAKAKSKGAKPMSNGYLEIRPDHGNL
SGTFVPNDATAADLDGDGELELIVKFDHANTGDDTYTVIEAYKLDGTKLWWINCGRNMGD
FQNNEINIAAYDWDLDGRAECIMRAADGTVIHMADGTTQTIGDPSKNYRPTEDGQWFVHD
GAEYLLYLDGLTAKPYQVMPYPLKRLEPGESSLTTAWGDGYGHRSSKYFFGAPYFDGKKP
SIFLARGIYTRHKMIAYDVNPADHSLTTRWTWNCNTPGSIWYGQGYHNYIVADVDWDGRD
EIVFGSMTIDDNGRGLASTGLGHGDAQHVSDFDPYRHGQEFFGCNEDRPGNNLCDATTRK
ILYRYSCGNDDGRGIMGNFSNDYPGCQGVSARDPGLISSVTYKTLDGGSKSDIAQNMNIY
WDGDLCEESFNGSGSHDTEGVILKYGTGRIANLAGSLTNNYTKATPCLMADLFGDWREEV
VMRTADNNIRIYTSTIATKWRNYTLWHDHQYRNAIVWQMNGYNQPPHVSYFLGELEGITV
APPPLTTTGRTVIANGSSIGSDCNDKHVMLDETGDMTVNVTDGASPYILTDNAPTWVQGR
DNAANIVTTSYTHTLTGGALTGAMRLVKQGDGTLVMPAASHTYTGFTDIWAGTLRLDGSL
ENSRLWLNRHTTLISNGGKFMKGIQADYNSTIVPGGQGTIGSLTADSLILNFGSAVAIDL
NAADRTADRINVATLSIEKKNWANGPAYSTPVFHVNLLMNSDNVADGEGKYLIGEVGKLD
GSLDDILIEGVTSYKSALSLEDGKLYLTLTAFHAGTVSWIGAEDAVWSTDGSANFESADG
SGMRGFVPDDEVIFDDNAVSTDVTISGKVKPSSIVFNNAKKTFTINGDSIVGNPTLTVNG
TGTVIINNENRIGATSINKGKLSVRTLANNAGTDFGALGGVTSAINISGGATLSVQESNT
TSQTINVGEGGANLDVVSGTTLTMSTGIKQSVSGQTLTKLGEGALTLGSGNSVSKLVIRT
GSVNTIESNGLIQLPSIVAFEGGTLYDSNSEGSYTTNSTNFVVENGQTGAIYCDPRCEYT
GNFSGAGRLTFYAAGVRNYINGDWNNFTGTLIPALSKRGTYDPVFYFTSTKGLVNATLVL
NTGMTINNDGKNIPLGTVTGTGTLAGSGSYYVGDKDNDFTFGAYSTSKIVKRGTGTMKII
SLGRITAPVEVQAGTLSFNNSSLATLVNGSNAMTVSGTGVVLGQGLIHSLTVNSGGSLYP
RASYDMNNPGIIKANGALTVANGATVGLVIGSSKCSQLQAKFITINGTLKVSLADNFVPK
VGTEYTLWTASSSFGGTPTLELQDLPAGFAWDTTGLLSATGVIKIAEGSGISSVSSAEEV
ACEVYSLTGQKLGTFTAQRSEIRSRLASYNINMNARTFIIKMRTAGGTEVKKMSVK

Enzyme Prediction     

No EC number prediction in MGYG000001806_00637.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
PL11	21	607	5.3e-164	0.9603960396039604

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10318	RGL11	3.92e-177	24	590	1	564	Rhamnogalacturonan lyase of the polysaccharide lyase family 11. The rhamnogalacturonan lyase of the polysaccharide lyase family 11 (RGL11) cleaves glycoside bonds in polygalacturonan as well as RG (rhamnogalacturonan) type-I through a beta-elimination reaction. Functionally characterized members of this family, YesW and YesX from Bacillus subtilis, cleave glycoside bonds between rhamnose and galacturonic acid residues in the RG-I region of plant cell wall pectin. YesW and YesX work synergistically, with YesW cleaving the glycoside bond of the RG chain endolytically, and YesX converting the resultant oligosaccharides through an exotype reaction. This domain is sometimes found in architectures with non-catalytic carbohydrate-binding modules (CBMs). There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain through a beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11.
pfam18370	RGI_lyase	4.87e-36	22	105	1	85	Rhamnogalacturonan I lyases beta-sheet domain. This is the beta-sheet domain found in rhamnogalacturonan (RG) lyases, which are responsible for an initial cleavage of the RG type I (RG-I) region of plant cell wall pectin. Polysaccharide lyase family 11 carrying this domain, such as YesW (EC:4.2.2.23) and YesX (EC:4.2.2.24), cleave glycoside bonds between rhamnose and galacturonic acid residues in RG-I through a beta-elimination reaction. Other family members carrying this domain are hemagglutinin A, lysine gingipain (Kgp) and Chitinase C (EC:3.2.1.14).
pfam12951	PATR	5.86e-04	686	714	1	28	Passenger-associated-transport-repeat. This Autotransporter-associated beta strand repeat model represents a core 32-residue region of a class of bacterial protein repeat found in one to 30 copies per protein. Most proteins with a copy of this repeat have domains associated with membrane autotransporters (pfam03797). The repeats occur with a periodicity of 60 to 100 residues. A pattern of sequence conservation is that every second residue is well-conserved across most of the domain. These repeats as likely to have a beta-helical structure. This repeat plays a role in the efficient transport of autotransporter virulence factors to the bacterial surface during growth and infection. The repeat is always associated with the passenger domain of the autotransporter. For these reasons it has been coined the Passenger-associated Transport Repeat (PATR). The mechanism by which the PATR motif promotes transport is uncertain but it is likely that the conserved glycines (see HMM Logo) are required for flexibility of folding and that this folding drives secretion. Autotransporters that contain PATR(s) associate with distinct virulence traits such as subtilisin (S8) type protease domains and polymorphic outer-membrane protein repeats, whilst SPATE (S6) type protease and lipase-like autotransporters do not tend to contain PATR motifs.
TIGR02601	autotrns_rpt	0.001	686	717	2	32	autotransporter-associated beta strand repeat. This model represent a core 32-residue region of a class of bacterial protein repeat found in one to 30 copies per protein. Most proteins with a copy of this repeat have domains associated with membrane autotransporters (pfam03797, TIGR01414). The repeats occur with a periodicity of 60 to 100 residues. A pattern of sequence conservation is that every second residue is well-conserved across most of the domain. pfam05594 is based on a longer, much more poorly conserved multiple sequence alignment and hits some of the same proteins as this model with some overlap between the hit regions of the two models. It describes these repeats as likely to have a beta-helical structure. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
NF033176	auto_AIDA-I	0.001	882	1317	4	469	autotransporter adhesin AIDA-I.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIM09959.1	0.0	15	1471	5	1519
AGB29439.1	0.0	2	1471	3	1500
BCS86257.1	7.57e-305	25	869	3	866
QJC87652.1	1.90e-133	20	604	32	609
QYX44216.1	2.28e-133	20	604	38	615

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2Z8R_A	4.68e-132	20	604	1	578	Crystalstructure of rhamnogalacturonan lyase YesW at 1.40 A resolution [Bacillus subtilis],2Z8R_B Crystal structure of rhamnogalacturonan lyase YesW at 1.40 A resolution [Bacillus subtilis],2Z8S_A Crystal structure of rhamnogalacturonan lyase YesW complexed with digalacturonic acid [Bacillus subtilis],2Z8S_B Crystal structure of rhamnogalacturonan lyase YesW complexed with digalacturonic acid [Bacillus subtilis],2ZUX_A Crystal structure of rhamnogalacturonan lyase YesW complexed with rhamnose [Bacillus subtilis],2ZUX_B Crystal structure of rhamnogalacturonan lyase YesW complexed with rhamnose [Bacillus subtilis]
4CAG_A	5.04e-126	15	594	2	577	Bacilluslicheniformis Rhamnogalacturonan Lyase PL11 [Bacillus licheniformis]
2ZUY_A	1.90e-123	21	604	5	599	Crystalstructure of exotype rhamnogalacturonan lyase YesX [Bacillus subtilis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O31526	6.22e-131	20	604	38	615	Rhamnogalacturonan endolyase YesW OS=Bacillus subtilis (strain 168) OX=224308 GN=yesW PE=1 SV=1
O31527	8.18e-123	21	604	5	599	Rhamnogalacturonan exolyase YesX OS=Bacillus subtilis (strain 168) OX=224308 GN=yesX 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
0.000223	0.999155	0.000180	0.000147	0.000146	0.000137

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001806_00637.