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CAZyme Information: MGYG000000069_01888

You are here: Home > Sequence: MGYG000000069_01888

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Clostridium_A leptum
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Clostridium_A; Clostridium_A leptum
CAZyme ID MGYG000000069_01888
CAZy Family GH141
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1776 MGYG000000069_5|CGC1 193293.02 4.0966
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000069 3099132 Isolate United Kingdom Europe
Gene Location Start: 1195;  End: 6525  Strand: +

Full Sequence      Download help

MEDRNVAHTV  YVSTTGNDDT  GDGSQGKPFA  TIEKAKEHVR  TLDKDSGDIV  VKIAGGLYEL60
EDTIVFDEND  SGNENCTIYY  EAVDGEEPII  SGGKLLEGDW  EEATEVDWLD  DGIKAYKTDL120
VRNDKLRAIY  VNGERASMTR  RSARPLRSVG  NYSVTKGEAD  WAWISKSGIK  EGNVFAADFG180
LPADTRNPQN  IELESGSTWV  KAIVCADTLE  ETPEGDTQVN  FQMPYAAIAQ  QPSWNCNYNP240
TGNNDVVNVF  EWLSEPGEFY  FDQAGSTLYY  IPKEGEDMAD  AEVIIPELVT  LVDIKGSTPK300
QDYAAHITFR  GLTFAYSDWN  LAEVDGSHGN  ATVQGCTYMN  KFSTGNWHDD  MYRSYDVAPA360
AVHATSAHDI  AILDGKIEMT  GYLGFHAEND  VYNIEVTGNY  IGHTGGGGVT  IGHPQHVYEN420
DTEEHWVGGS  GSNNAGPDKE  KFQNGTEAVP  KNIYIRNNYF  LENCYFFPGC  SPIATYFTQN480
MWIEHNFIYK  CSYSAMSIGW  GWCNFDGEVG  SDSQLPGLPT  TTSRNNHVNY  NRIEDYASIL540
QDCGGIYTLG  QQGDGTPGGT  DYSQYSEFNG  NYINVYRETP  DWVNEGRWIN  GFHPDEGSAY600
ILFDSNVITN  TLRNVYEMNN  WRRKHDLVVT  NGFSNSSKSE  TTAPNCSLDQ  YVSAESIWPK660
AGNNVVLNSG  LEDEYTYLID  ETVMPDSYYE  LASNVRLSAG  DTLNRRGLLE  ADDEVWLAPA720
GTKDFAEGPT  MTKAAGNEKT  ITVPMELGEY  KLYIKYANGQ  VSDASEFTVY  VGESKDLANV780
AEGQNYSVSE  LKPLVLELDT  DNYTFTLNGE  KIKNGHSIST  EASWELKATP  IGESEATKTI840
TFTTSVSLAN  KLLPKNLTVS  PEGLVEFAEA  LNDAGYSIWL  AESGLSAFDE  NDPRQSYAAG900
DSASMKAPKT  PGTYVLSVTK  ADDKTQIDSQ  SDAKVRVLNM  VTAGNGLATY  GTPTIGEGET960
DPIWNSAPAL  VIEKHLTMKD  NGTASGVAKA  MWDEENLYVM  VEVQDPVLNS  DSSQVHEQDS1020
IEIFVDETNC  KASSYQAGMG  QYRINYKNEQ  TFNGSGIEEG  FESYARIVDG  GYVIEAKIPF1080
KTVDPAANDK  IGFDVQINDA  NADGTRQDIV  MWYDETGNSW  QSGANWGEVT  LEEKSPIPTN1140
GLNIWLNADR  GVTLGGDDGD  SVLSWENQGS  MDATFTAEAE  TAPTLGVNEN  GVPSLVFSGG1200
KDDQGTLGGD  GDFMTFDGVD  FNNKSEMTMI  VVSHYTGKSV  GNPSGDWTSG  DKYCAIFAEE1260
AGGWGSLFMS  PYHDWTSARF  GTGKDFCNIK  YYDRDEIDRT  AVTIATKDGA  KEKLYVDGVL1320
GAEKNDAVAV  TKNIGSKMHI  GASYSDYKWT  YFKGTISEIL  IYDRALSDAE  IEQVNTYLTQ1380
KYVTSLESIT  VSGPTKTQYE  IGDELDLTGL  VVTAHYSDGS  EAAVEDYEVS  GFDSSTAGEK1440
TITVTYQDKT  TTFTVNVKEA  APVVTLESIT  VSGPTKTEYE  IGDELDLTGL  VVTAHYSDGN1500
EKVLSAGDYE  VSGFDSSTAG  EKTITVTYQD  KTTAFTVNVK  EAAPVVTLES  ITVSGPTKTE1560
YKIGEELDLT  GLVVTAHYST  GDEATVTGYE  VSGFDSSTAG  EKTITVTYQG  KTAAFKVTVK1620
ETEKPVVTLE  SITVSGPNKT  EYKIGEELDL  TGLVVIAHYS  DGSYQEVTDY  EVSGFDSAAA1680
GEKTVTVTYQ  GETVSFKITV  KEDIASSEQP  GESGKPDDNQ  SSSQPDDTQS  GSGSQDDQNI1740
QTGDSMAPYV  GVAIVLILLS  GLGVAIALII  RRRRLG1776

Enzyme Prediction      help

No EC number prediction in MGYG000000069_01888.

CAZyme Signature Domains help

Created with Snap88177266355444532621710799888976106511541243133214201509159816879610GH1419581131CBM9
Family Start End Evalue family coverage
GH141 9 610 5.4e-115 0.9924098671726755
CBM9 958 1131 7.5e-51 0.9835164835164835

CDD Domains      download full data without filtering help

Created with Snap88177266355444532621710799888976106511541243133214201509159816879481132CBM9_like_19581132CBM9_19641127CBM9_like_415551619Big_314731539Big_3
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00005 CBM9_like_1 4.71e-88 948 1132 4 185
DOMON-like type 9 carbohydrate binding module of xylanases. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. The CBM9 domain frequently occurs in tandem repeats; members found in this subfamily typically co-occur with glycosyl hydrolase family 10 domains and are annotated as endo-1,4-beta-xylanases. CBM9 from Thermotoga maritima xylanase 10A is reported to have specificity for polysaccharide reducing ends.
pfam06452 CBM9_1 7.51e-59 958 1132 3 182
Carbohydrate family 9 binding domain-like. CBM9_1 is a C-terminal domain on bacterial xylanase proteins, and it is tandemly repeated in a number of family-members. The CBM9 module binds to amorphous and crystalline cellulose and a range of soluble di- and monosaccharides as well as to cello- and xylo- oligomers of different degrees of polymerization. Comparison of the glucose and cellobiose complexes during crystallisation reveals surprising differences in binding of these two substrates by CBM9-2. Cellobiose was found to bind in a distinct orientation from glucose, while still maintaining optimal stacking and electrostatic interactions with the reducing end sugar.
cd09619 CBM9_like_4 3.67e-19 964 1127 12 187
DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily are often located at the C-terminus of longer proteins and may co-occur with various other domains.
pfam07523 Big_3 3.40e-14 1555 1619 1 67
Bacterial Ig-like domain (group 3). This family consists of bacterial domains with an Ig-like fold. Members of this family are found in a variety of bacterial surface proteins.
pfam07523 Big_3 1.17e-13 1473 1539 1 67
Bacterial Ig-like domain (group 3). This family consists of bacterial domains with an Ig-like fold. Members of this family are found in a variety of bacterial surface proteins.

CAZyme Hits      help

Created with Snap881772663554445326217107998889761065115412431332142015091598168710937AWI67019.1|GH14161249ACL75355.1|CBM9|GH14111760AUX40294.1|GH1416771QNU65850.1|CBM6|GH1419803ALX09871.1|CBM6|GH141
Hit ID E-Value Query Start Query End Hit Start Hit End
AWI67019.1 0.0 10 937 148 1078
ACL75355.1 1.90e-299 6 1249 44 1686
AUX40294.1 1.00e-141 11 760 19 720
QNU65850.1 2.96e-140 6 771 40 755
ALX09871.1 7.59e-138 9 803 44 779

PDB Hits      download full data without filtering help

Created with Snap881772663554445326217107998889761065115412431332142015091598168794811311I82_A94911407NWN_AAA76065MQP_A162817002L7Y_A147415394FDW_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
1I82_A 3.35e-45 948 1131 5 187
Family9 Carbohydrate-Binding Module From Thermotoga Maritima Xylanase 10a With Cellobiose [Thermotoga maritima],1I8A_A Family 9 Carbohydrate-Binding Module From Thermotoga Maritima Xylanase 10a With Glucose [Thermotoga maritima],1I8U_A Family 9 Carbohydrate-Binding Module From Thermotoga Maritima Xylanase 10a [Thermotoga maritima]
7NWN_AAA 1.03e-29 949 1140 26 214
ChainAAA, Beta-xylanase [Caldicellulosiruptor kristjanssonii I77R1B],7NWO_AAA Chain AAA, Beta-xylanase [Caldicellulosiruptor kristjanssonii I77R1B],7NWP_AAA Chain AAA, Beta-xylanase [Caldicellulosiruptor kristjanssonii I77R1B],7NWQ_AAA Chain AAA, Beta-xylanase [Caldicellulosiruptor kristjanssonii I77R1B]
5MQP_A 1.33e-29 7 606 24 580
Glycosidehydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_B Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_C Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_D Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_E Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_F Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_G Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_H Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron]
2L7Y_A 3.28e-06 1628 1700 5 81
Solutionstructure of a putative surface protein [Streptococcus pneumoniae]
4FDW_A 4.89e-06 1474 1539 32 98
Crystalstructure of a putative cell surface protein (BACOVA_01565) from Bacteroides ovatus ATCC 8483 at 2.05 A resolution [Bacteroides ovatus ATCC 8483]

Swiss-Prot Hits      download full data without filtering help

Created with Snap88177266355444532621710799888976106511541243133214201509159816879141131sp|Q60042|XYNA_THENE8941131sp|Q60037|XYNA_THEMA9431154sp|C6CRV0|XYNA1_PAESJ9481134sp|P38535|XYNX_ACETH9481134sp|P36917|XYNA_THESA
Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q60042 3.64e-40 914 1131 842 1053
Endo-1,4-beta-xylanase A OS=Thermotoga neapolitana OX=2337 GN=xynA PE=1 SV=1
Q60037 6.37e-40 894 1131 829 1057
Endo-1,4-beta-xylanase A OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=xynA PE=1 SV=1
C6CRV0 1.40e-39 943 1154 865 1080
Endo-1,4-beta-xylanase A OS=Paenibacillus sp. (strain JDR-2) OX=324057 GN=xynA1 PE=1 SV=1
P38535 1.81e-38 948 1134 714 897
Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX PE=3 SV=1
P36917 7.09e-37 948 1134 862 1045
Endo-1,4-beta-xylanase A OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000049 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

start end
1748 1770