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CAZyme Information: MGYG000001183_00039

You are here: Home > Sequence: MGYG000001183_00039

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 UMGS1441 sp900551755
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; CAG-274; UMGS1441; UMGS1441 sp900551755
CAZyme ID MGYG000001183_00039
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1157 MGYG000001183_1|CGC1 122128.86 4.3385
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001183 2128086 MAG Austria Europe
Gene Location Start: 46850;  End: 50323  Strand: +

Full Sequence      Download help

MNNVLKRFLS  VVLSAAMVFS  SVAFVNISAV  MADGSSYISE  EGGWLESAYV  EWTSVPNATG60
FAAYVKKAND  ADSSYVKLDN  ELIRKYPTYF  RADAVGLAAG  QYVMKVVPYI  NGALDESAAF120
VSGTLDVKAN  DRSGSAFSSK  SPYYGKGVGA  YNNDGTLKSD  AQVVYVTKDT  AKTVKADIIT180
GKNGSSETIT  GFQSIIDAKQ  KGLDTRPLDF  RIIGTIEKND  LDRISSSAEG  LQIKGKNAGA240
ELNITIEGIG  EDAVIRGFGI  LCRNVGNVEL  RNFAVMLCMD  DSISVDTDNN  TLWIHNLDLF300
YGSTGGDADQ  AKGDGTVDVK  GKSNFVTVSY  NHFWDSGKSS  LCGMGSEVTS  SHITYHHNWF360
DHSDSRHPRI  RVQSVHIYNN  YFDGNAKYGV  GVTLGSSAFV  ESNYFRNCKH  PMMSSKQGSD420
IMENDKTGVP  DFSAKGTFSS  ENGGAIKAYN  NHIEGSDADK  FNGGVEPVYY  DATATGTNGK480
ATQYDAYLAT  TRDEKVPSTV  KALAGGSSYN  NFDTDTSNFD  LGVDEANITP  VEDVPSVVTK540
YAGRVNGGDF  KNDSKYTVLN  DDKSYAVDTV  LKAALSSYTS  SLVSVGGLNA  GGEVDTTVST600
ETTTEVTTEK  TSEVTTEKVS  ETTTEKATET  TTSNSTPVEI  GEAQTGFVSD  NTSDTGAGVS660
VTFNSATNKW  TLSDSSTTAA  AEIKIPFATQ  SKGKVIISGS  VEPSTTASKW  AFVQILGTKA720
DGTQGEVFGF  GGGANKTDLS  ARVNAGAYTK  FGTFTAKNYD  YTAIIDLDNK  TVELTVDGVK780
STYTGLDAES  IEGVYSTTSK  KGERNVSLSV  PYVGVIGDAV  ETTTVAESST  ETTTVEKTTV840
NETSSETTTE  NVTPDPDFVY  GDVDGSGERN  IKDVNLLIEQ  IRNGAVNVIK  GINDVNNDGV900
VDTADVATLL  QKVLNSNFKM  PCEPNVTEPT  TVTTIVATTE  ATTETTTVAP  TEATTEDTTA960
TTTTETTTVT  TTVETTTEAT  TVEPTTVTTT  ETTTVTTTVE  TTTEATTAET  TTEATTEGTT1020
SASASSWTAG  DTVPSWLSVS  GTVSGTAEKN  SNGNVAFSTA  NGSAFANTIK  LAENGTFTIT1080
PEKAGIVKVY  VAANNNNANK  GTLTATIDDK  TVGTYNLPGR  KDSSANAFEV  TVDAANAGKA1140
ITFTTSYKAL  LFKVECN1157

Enzyme Prediction      help

No EC number prediction in MGYG000001183_00039.

CAZyme Signature Domains help

Created with Snap5711517323128934740446252057863669475280986792598310411099241407PL1
Family Start End Evalue family coverage
PL1 241 407 4.1e-42 0.8118811881188119

CDD Domains      download full data without filtering help

Created with Snap571151732312893474044625205786366947528098679259831041109996411PelB243409Amb_all239405Pec_lyase_C860914Dockerin_I861914Dockerin_1
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 6.96e-50 96 411 2 279
Pectate lyase [Carbohydrate transport and metabolism].
smart00656 Amb_all 3.84e-30 243 409 17 190
Amb_all domain.
pfam00544 Pec_lyase_C 1.39e-18 239 405 31 211
Pectate lyase. This enzyme forms a right handed beta helix structure. Pectate lyase is an enzyme involved in the maceration and soft rotting of plant tissue.
cd14256 Dockerin_I 2.69e-06 860 914 1 57
Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex.
pfam00404 Dockerin_1 0.005 861 914 1 56
Dockerin type I repeat. The dockerin repeat is the binding partner of the cohesin domain pfam00963. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome. The dockerin repeats, each bearing homology to the EF-hand calcium-binding loop bind calcium.

CAZyme Hits      help

Created with Snap571151732312893474044625205786366947528098679259831041109923587BCJ94010.1|CBM77|PL11600ACX62589.1|CBM77|PL11593AYB46946.1|CBM77|PL11593QOT09127.1|CBM77|PL112590ACR72247.1|PL1|PL9_1
Hit ID E-Value Query Start Query End Hit Start Hit End
BCJ94010.1 3.45e-191 23 587 32 566
ACX62589.1 8.15e-189 1 600 1 573
AYB46946.1 1.90e-187 1 593 1 566
QOT09127.1 2.09e-186 1 593 1 566
ACR72247.1 2.11e-182 12 590 16 576

PDB Hits      download full data without filtering help

Created with Snap57115173231289347404462520578636694752809867925983104110991814073VMV_A2434051VBL_A2124331AIR_A2124332EWE_A2453903ZSC_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
3VMV_A 1.86e-24 181 407 20 248
Crystalstructure of pectate lyase Bsp165PelA from Bacillus sp. N165 [Bacillus sp. N16-5],3VMW_A Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165 in complex with trigalacturonate [Bacillus sp. N16-5]
1VBL_A 4.84e-20 243 405 133 330
Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
1AIR_A 4.29e-19 212 433 63 290
ChainA, PECTATE LYASE C [Dickeya chrysanthemi],1O88_A Chain A, Pectate Lyase C [Dickeya chrysanthemi],1O8D_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8E_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8F_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8G_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8H_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8I_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8J_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8K_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8L_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8M_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1PLU_A Chain A, Protein (pectate Lyase C) [Dickeya chrysanthemi],2PEC_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi]
2EWE_A 1.04e-18 212 433 63 290
ChainA, Pectate lyase C [Dickeya chrysanthemi]
3ZSC_A 2.56e-14 245 390 71 221
Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]

Swiss-Prot Hits      download full data without filtering help

Created with Snap5711517323128934740446252057863669475280986792598310411099181414sp|Q8GCB2|PTLY_BACLI181414sp|Q65DC2|PTLY_BACLD181414sp|B1B6T1|PTLY_BACSP243428sp|Q5AVN4|PLYA_EMENI212432sp|P0C1C1|PLY2_PECCA
Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8GCB2 2.44e-26 181 414 57 281
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
Q65DC2 2.44e-26 181 414 57 281
Pectate trisaccharide-lyase OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=BLi04129 PE=3 SV=1
B1B6T1 2.44e-26 181 414 57 281
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
Q5AVN4 1.86e-20 243 428 99 287
Pectate lyase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=plyA PE=1 SV=1
P0C1C1 1.21e-19 212 432 84 310
Pectate lyase 2 OS=Pectobacterium carotovorum OX=554 GN=pel2 PE=3 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
0.000329 0.999001 0.000158 0.000207 0.000159 0.000142

TMHMM  Annotations      download full data without filtering help

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