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CAZyme Information: MGYG000000403_00006

You are here: Home > Sequence: MGYG000000403_00006

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
Lineage Bacteria; Firmicutes_A; Clostridia; Monoglobales_A; UBA1381; UBA4716;
CAZyme ID MGYG000000403_00006
CAZy Family PL21
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1216 MGYG000000403_1|CGC1 136119.67 4.6227
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000403 2138464 MAG Sweden Europe
Gene Location Start: 7679;  End: 11329  Strand: +

Full Sequence      Download help

MTKKYITRRF  IAAVLSAAML  CGVAFSAFAD  GINYGDKVEN  PSIPLLLDEK  NTVKNGNLVF60
EAEDMKLASD  MVIGQNENAS  GGKYITGATG  TTKGSNSGNK  NPSYSMNIKV  EKSGPYSIWI120
RARITHNGAD  SINLAVNSKH  YEYFALPIEP  DWQWINLKST  SLPAGMVAIN  FRYAEPPAWI180
DKVLITADTE  FVPKEMNDMP  NAVEMGDVIY  PEPEIKPISG  HPRLFLTKDY  IPELVKKREA240
PELAKAWKVI  DDWADLYIDA  KLPERDSGNF  SENILMRIQA  KALKYVMDDS  DKELADEVIR300
LAKDYLKTVS  FSNGGDVTRN  RGDVMVMAAI  VYDWCYDRMT  DEDKQYFIKR  FKELALEKEV360
GYPPTNLSSV  TSHTGEGEIM  RDLLSAGIAC  YDEDTEIYNL  AGGRFFSEMT  EPRKMYYDAG420
RHPEGSSYGP  YRFQWEAFAA  VIFDRMGIHN  VFGENMKNVN  YHWLYDMRPD  GFRMKEGDEP480
TFSAANYFYY  MGTERRSAMI  VGSLFKDPYI  RGRYLKESAS  GGYVNDYFWT  VLFDDPEVGA540
KEPYDLPLTE  FNGWPLSGMV  ARTSWQDGLD  SPAVVASVTM  KAINTGDHMH  RDAGAFSIYY600
KGALAIDSGE  YQGQSGGYGY  PHDMNYNKKS  IAHNVVTVYD  PDEKDNQVLS  STNDGGQRYP660
RTSGMAKTLE  ELTADDAILA  EEKAHSAGPN  DKTPEYSYLK  GDLTKAYTDK  ITDYKRSFVF720
LNLDDEDYPA  AAVVFDKVDS  KKKEFKKKWL  LHSIEEPDVE  GDTTTIARTE  YGFDGKLVNK780
TLLPETKNLS  IEKIGGSGKE  FWVENQNFAN  APKANGTEQG  AWRIEVSPKN  EAESDTFLNA840
MYVTDNSSEL  PQLEAEKIET  DDYVGALIKD  RAVLFAKDSE  PKNNEIKISC  GKETAFLITD900
VAEGTWQISG  NGLNIFANSE  KDGNCLYFRV  PAGEYTVTPT  EAHEETAENV  PEMQVKTSGD960
FTVWDEKARQ  FLYAESKLID  GVPYVQAKRI  FEKYDSAVKW  DGGTGEITIS  SGGKTIRIKS1020
GSTAAVMNKE  EIQLQYAPVI  IDGVTYVYPC  DFTELTGKEF  SFDETAKMLL  VRDKKSEPVP1080
IKGIDEENVI  KPVTVACSDS  DTNIADNASD  LDLTTRWSAN  GDGQWLMYDM  GEVVPISRVA1140
LAFYLGSQRQ  TYFDIQLSND  AKTFTTVYSG  ASSGKTENPE  FYPINYSARY  IRFMGHGTAA1200
NRTGWNSVTE  MTVLKK1216

Enzyme Prediction      help

No EC number prediction in MGYG000000403_00006.

CAZyme Signature Domains help

Created with Snap60121182243304364425486547608668729790851912972103310941155573642PL2110981211CBM32
Family Start End Evalue family coverage
PL21 573 642 1.6e-25 0.9583333333333334
CBM32 1098 1211 4.9e-19 0.8951612903225806

CDD Domains      download full data without filtering help

Created with Snap6012118224330436442548654760866872979085191297210331094115510981211F5_F8_type_C9791071Cu_amine_oxidN1858938HepII_C10931211FA58C59165CBM35_mannanase-like
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00754 F5_F8_type_C 7.11e-14 1098 1211 7 127
F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
pfam07833 Cu_amine_oxidN1 1.88e-13 979 1071 1 93
Copper amine oxidase N-terminal domain. Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.
pfam18675 HepII_C 6.76e-09 858 938 2 87
Heparinase II C-terminal domain. Heparinase II (HepII) is an 85-kDa dimeric enzyme that depolymerizes both heparin and heparan sulfate glycosaminoglycans. The protein is composed of three domains: an N-terminal alpha-helical domain, a central two-layered beta-sheet domain, and a C-terminal domain forming a two-layered beta-sheet. The C-terminal domain contains nine beta-strands packed together in a manner resembling a beta-barrel.
cd00057 FA58C 3.98e-07 1093 1211 14 137
Substituted updates: Jan 31, 2002
cd04086 CBM35_mannanase-like 1.39e-04 59 165 2 98
Carbohydrate Binding Module 35 (CBM35); appended to several carbohydrate binding enzymes, including several glycoside hydrolase (GH) family 26 mannanase domains. This family includes carbohydrate binding module 35 (CBM35) domains that are appended to several carbohydrate binding enzymes, including periplasmic component of ABC-type sugar transport system involved in carbohydrate transport and metabolism, and several glycoside hydrolase (GH) domains, including GH26. These CBM6s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. Examples of proteins having CMB35s belonging to this family are mannanase A from Clostridium thermocellum (GH26), Man26B from Paenibacillus sp. BME-14 (GH26), and the multifunctional Cel44C-Man26A from Paenibacillus polymyxa GS01 (which has two GH domains, GH44 and GH26). GH26 mainly includes mannan endo-1,4-beta-mannosidase which hydrolyzes 1,4-beta-D-linkages in mannans, galacto-mannans, glucomannans, and galactoglucomannans, but displays little activity towards other plant cell wall polysaccharides. A few proteins belonging to this family have additional CBM3 domains; these CBM3s are not found in the CBM6-CBM35-CBM36_like superfamily.

CAZyme Hits      help

Created with Snap601211822433043644254865476086687297908519129721033109411552101209BBH20141.1|PL21217938QHW00380.1|PL21217935ACU04612.1|PL21_1|4.2.2.7|4.2.2.8217935ABJ17170.1|PL21_1|4.2.2.7|4.2.2.8217935AAB18277.1|PL21_1|4.2.2.7|4.2.2.8
Hit ID E-Value Query Start Query End Hit Start Hit End
BBH20141.1 1.59e-202 210 1209 228 1219
QHW00380.1 6.24e-169 217 938 67 799
ACU04612.1 4.20e-167 217 935 44 768
ABJ17170.1 1.16e-166 217 935 44 768
AAB18277.1 1.16e-166 217 935 44 768

PDB Hits      download full data without filtering help

Created with Snap601211822433043644254865476086687297908519129721033109411552179352FUQ_A2179353E80_A2179353E7J_A2179352FUT_A108712145ZU6_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2FUQ_A 7.16e-169 217 935 19 743
ChainA, heparinase II protein [Pedobacter heparinus],2FUQ_B Chain B, heparinase II protein [Pedobacter heparinus]
3E80_A 7.61e-169 217 935 21 745
Structureof Heparinase II complexed with heparan sulfate degradation disaccharide product [Pedobacter heparinus],3E80_B Structure of Heparinase II complexed with heparan sulfate degradation disaccharide product [Pedobacter heparinus],3E80_C Structure of Heparinase II complexed with heparan sulfate degradation disaccharide product [Pedobacter heparinus]
3E7J_A 4.78e-166 217 935 21 745
ChainA, Heparinase II protein [Pedobacter heparinus],3E7J_B Chain B, Heparinase II protein [Pedobacter heparinus]
2FUT_A 2.89e-163 217 935 20 744
ChainA, heparinase II protein [Pedobacter heparinus],2FUT_B Chain B, heparinase II protein [Pedobacter heparinus]
5ZU6_A 1.58e-24 1087 1214 29 157
ACBM32 derived from alginate lyase B (AlyB-OU02) [Vibrio]

Swiss-Prot Hits      download full data without filtering help

Created with Snap60121182243304364425486547608668729790851912972103310941155217935sp|C6XZB6|HEPB_PEDHD
Hit ID E-Value Query Start Query End Hit Start Hit End Description
C6XZB6 8.41e-168 217 935 44 768
Heparin and heparin-sulfate lyase OS=Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3) OX=485917 GN=hepB PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000475 0.997311 0.001368 0.000412 0.000226 0.000171

TMHMM  Annotations      download full data without filtering help

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