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CAZyme Information: MGYG000000967_00062

You are here: Home > Sequence: MGYG000000967_00062

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 sp900543365
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; CAG-274; UMGS1441; UMGS1441 sp900543365
CAZyme ID MGYG000000967_00062
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1635 171204.11 4.4013
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000967 1698990 MAG Spain Europe
Gene Location Start: 19386;  End: 24293  Strand: +

Full Sequence      Download help

MKKCLKKTLS  GILAATMLFS  SVTVSNVFAA  PSFSQVGGWF  ESIYAEIPSI  KDADVTGVSY60
SGATSGTLSG  DDLTYLVRDM  SGGVRIDVPG  LKAGTYTLTV  TTSSGTVTKD  NIIVQEYDRS120
GYAHYNYTEG  VGAYNDDGTV  KANAKILYVT  NENKDTVSVT  SKDGTTVTGI  GNILNSAGKD180
AGTGTTSKGG  KPNTNAGIIG  KLADDGTPLV  VRIVGDVKAP  AGVTAYDSVD  YGGTVGDNGY240
MARMQGGKDV  TIEGIGADSS  INGWGIHFIC  DTVGYSKGNG  KSFEVRNIKF  QNVPEDCVGM300
EGQQEGSTIT  AGVERCWVHN  CSFYAPSISN  PAESDKSGGD  GACDFKRGQY  FTNSYCYYKG360
YHKTNLVGSS  DSSLQFNLTY  HHNYWQNCEA  RGPLGRQANI  HMYNNYYEGQ  TDYAMNTRAN420
CYIFSEYNLF  YMCKNPQRVD  AGAIKSYNDS  LSGCIEAMEA  KVVTDKSTKV  SSGCKYENFD480
TDSSLSYIPS  NNYKLDTSIV  SAKKNIMAYA  GTMKENPVTA  ESVNTSIVLS  DRQPTASVQL540
PYDKDLNSSY  VTNKSGAIDN  IVFNVGKTAV  DSISTATDTN  GQNIVFYVNE  PVNISITDGG600
ATYPVILLND  SGEAIITGTG  TANNVPAGTY  FIQSSGFQPG  KSGSPAKFKE  AKITHLSIVS660
AGSELPTIAE  PTTSEPTTSD  SSNPTEGTTS  NQEPDTEETT  SKPYDGEGLV  WNYTSGENTL720
GVNFNGNDYT  GSSVTYNGST  FTKAAKMESS  TSIGFTAPGS  GKLTIVSKSS  KNPATIKVNG780
ETVTISQDGA  TTIDVPAGAV  NITKGTTSTY  LYLLEFKGDS  VETTTNVTTV  TEATTEATTK840
AEATTEATTE  ATTVPEGVVV  SVGSTTAKTG  DKITVPVKLT  GLNTLENYAV  TVNYDSNVLT900
LSDVVSFVDS  NNFVVNKNNA  GVIKVAYAND  NAGSDDSFNG  DVLFSMTFTV  KSENDTTSSI960
NATVNQLNDG  VTATVVNGTV  TVDNAVTPVS  IPGDVNKDGV  VNSVDAAIVL  KIASGIITDT1020
TPYDMVAADC  DGKFGIDGRD  VIWILNHQTT  DDNTSTTEAT  TEETTSKTED  TTKAEATTES1080
TTTSPVVTDG  LPAGSYDLTA  SVTDKIDTTN  ARDVSTAGIK  LRSENYIEFV  AGVSGKLTLT1140
VSGKAAKLVS  VANGAETEVA  LNSNSANVTA  GTTYRVYGTE  SGSNTTITNL  VLASDGTVVE1200
PTTQATTNSE  VTTSKTETTT  KTSGGDATTE  TTTTDLSGAI  NISAGDSASL  ATALKNATAG1260
TTINLAPGTY  KMSAATSMSK  SGTASKPITV  TCANGMATLD  YDGTSGRAIT  AKADYINFSN1320
LTVKNGGDNG  MYITGGHINV  ENCIFQANGD  TGLQISGGGN  NVLVKNCTSF  DNLQTENADG1380
FAAKLGAGEN  VVFDGCIAYC  NSDDGWDLFS  KSGDQQNKYP  ITLRNCIAFK  NGQLTDGTVE1440
KSGDRNGFKL  GGGGYGAAHI  VENCIAFDNG  ACGFTDNNNP  SLAVLKNCTG  YSNATADVKK1500
HNFSIYRATE  GIEVTNCLSY  VLNADPNGDG  KDRFDGSSSG  TTYNANATVA  NSVFGCANKY1560
YKIAGATKIT  ATTQLATNGT  EVTVSDSDFQ  TLELPYTDIL  KVHEQMRNAD  GSIKLNGFLQ1620
PKAGTDIEGM  GAQFN1635

Enzyme Prediction      help

EC 4.2.2.2

CAZyme Signature Domains help

Created with Snap81163245327408490572654735817899981106211441226130813891471155312471628PL9242431PL1722808CBM77
Family Start End Evalue family coverage
PL9 1247 1628 5.5e-93 0.9064171122994652
PL1 242 431 9.2e-44 0.8316831683168316
CBM77 722 808 1.3e-17 0.8252427184466019

CDD Domains      download full data without filtering help

Created with Snap811632453274084905726547358178999811062114412261308138914711553246436PelB247430Amb_all208430Pec_lyase_C733813CBM77858995Type_I_cohesin_like
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 1.49e-26 246 436 99 279
Pectate lyase [Carbohydrate transport and metabolism].
smart00656 Amb_all 1.73e-26 247 430 15 186
Amb_all domain.
pfam00544 Pec_lyase_C 5.04e-16 208 430 1 211
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.
pfam18283 CBM77 6.76e-16 733 813 29 108
Carbohydrate binding module 77. This domain is the non-catalytic carbohydrate binding module 77 (CBM77) present in Ruminococcus flavefaciens. CBMs fulfil a critical targeting function in plant cell wall depolymerisation. In CBM77, a cluster of conserved basic residues (Lys1092, Lys1107 and Lys1162) confer calcium-independent recognition of homogalacturonan.
cd08548 Type_I_cohesin_like 9.36e-12 858 995 1 135
Type I cohesin domain, interaction partner of dockerin. 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 cohesins; their interactions with dockerin mediate assembly of a range of dockerin-borne enzymes to the complex.

CAZyme Hits      help

Created with Snap81163245327408490572654735817899981106211441226130813891471155335525ADU23076.1|CBM37|CBM77|PL132820ACR71161.1|CBM77|PL13671BBF42492.1|PL135635CDR31241.1|PL11529ADZ82421.1|PL1
Hit ID E-Value Query Start Query End Hit Start Hit End
ADU23076.1 4.30e-219 35 525 760 1249
ACR71161.1 7.19e-206 32 820 41 896
BBF42492.1 2.42e-141 3 671 2 668
CDR31241.1 9.24e-117 35 635 332 894
ADZ82421.1 1.49e-68 1 529 1 487

PDB Hits      download full data without filtering help

Created with Snap8116324532740849057265473581789998110621144122613081389147115532484303VMV_A126014931RU4_A2434362QX3_A2495165AMV_A2495161BN8_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
3VMV_A 1.82e-19 248 430 79 246
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]
1RU4_A 1.59e-16 1260 1493 48 292
ChainA, Pectate lyase [Dickeya chrysanthemi]
2QX3_A 6.44e-13 243 436 67 252
Structureof pectate lyase II from Xanthomonas campestris pv. campestris str. ATCC 33913 [Xanthomonas campestris pv. campestris],2QX3_B Structure of pectate lyase II from Xanthomonas campestris pv. campestris str. ATCC 33913 [Xanthomonas campestris pv. campestris]
5AMV_A 1.51e-12 249 516 128 399
Structuralinsights into the loss of catalytic competence in pectate lyase at low pH [Bacillus subtilis],5X2I_A Polygalacturonate Lyase by Fusing with a Self-assembling Amphipathic Peptide [Bacillus subtilis subsp. subtilis str. 168]
1BN8_A 1.71e-12 249 516 149 420
BacillusSubtilis Pectate Lyase [Bacillus subtilis]

Swiss-Prot Hits      download full data without filtering help

Created with Snap81163245327408490572654735817899981106211441226130813891471155312491493sp|P0C1A6|PLYL_DICCH12601493sp|P0C1A7|PLYL_DICD3248517sp|Q65DC2|PTLY_BACLD248517sp|B1B6T1|PTLY_BACSP248517sp|Q8GCB2|PTLY_BACLI
Hit ID E-Value Query Start Query End Hit Start Hit End Description
P0C1A6 6.10e-18 1249 1493 62 317
Pectate lyase L OS=Dickeya chrysanthemi OX=556 GN=pelL PE=3 SV=1
P0C1A7 1.08e-15 1260 1493 73 317
Pectate lyase L OS=Dickeya dadantii (strain 3937) OX=198628 GN=pelL PE=1 SV=1
Q65DC2 1.99e-15 248 517 108 341
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 1.99e-15 248 517 108 341
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
Q8GCB2 1.99e-15 248 517 108 341
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA 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
0.000216 0.999130 0.000165 0.000174 0.000153 0.000140

TMHMM  Annotations      download full data without filtering help

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