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CAZyme Information: PSURA_85409T0-p1

You are here: Home > Sequence: PSURA_85409T0-p1

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 Phytophthora ramorum
Lineage Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora ramorum
CAZyme ID PSURA_85409T0-p1
CAZy Family GT71
CAZyme Description N-arginine dibasic convertase NRD1 and related Zn2+-dependent endopeptidases, insulinase superfamily
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1361 PramPr-102_SC0180|CGC1 154094.54 5.9385
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PramorumPr-102 15743 N/A 251 15492
Gene Location Start: 34968; End:39277  Strand: +

Full Sequence      Download help

MMKAAIALML  GASSLSVATA  DPRVMIESTY  TDTRGLNDLA  QAAQGKYMGT  ATDIKQLSDQ60
YYTQELNNTK  DFSMITPANA  MKWDATEAKQ  GVFTFDDADK  IVAFANATGA  RVRCHALVWH120
QQVPAWVESL  EKAELLEAMS  NHITKVMTHF  GDSCYSWDVV  NEAMDEDGSY  RQSFWFEKTG180
KEYISAAYKT  ANAVKKKLGL  KVKLYYNDYN  INIANKKSDA  VLEMVGALRN  VSNWVDGVGF240
QSHYSNNDTA  STVGSDIFWN  LRRFTLSRVD  VALTELDVKT  SSANPTVTEQ  QQQVGIYTNA300
VSACKKTKRC  VGVTVWDFVD  TYSWVEASAP  LLYYQPEGAN  TPLVRKATYD  AVTAGWIFRV360
VKLVKFDGME  RVVQCDGIDV  SSLDERDFKY  VTLPNGLHAL  VVSDATTETA  SAAMDVRVGF420
HSDPDAVPGL  AHFCEHMLFL  GTRKFPDENS  YSAFLAANGG  SSNAFTAGRD  TNFYFDVGAA480
HLHEALDRFA  QFFIAPLFTP  SATEREVNAV  DSESTNYLQD  DSWRINQLER  GLGNVKHPYH540
KFGVGNKETL  SVTPAEQGID  VREQLLTFYH  EFYSASIMKL  VIYGKEDVET  LSQWACELFT600
EIPNSMRRSP  AFDQEQPYTA  DQLARRLEVV  PVMDWKVVQV  SWVLPPLRGK  GYSQQHASVL660
SHLIGHEGQG  SLLSYLKKKK  WANSVYAGIV  EDYDEFSLFV  VSFDVTEDGV  ERADDVLKAM720
FQYMHLMRAS  PWDKWVFDEL  EIMSKTHFMF  QSKSPPADFT  SVVAANMHTF  PKRDIVSEGV780
LYFPHEWEQA  LELLRLMTPE  QMRVLIACQT  LEERAVSEEK  WYGTKYREMP  LPIKFLEEMA840
NPGANCALRL  PHPNDFVVTD  LNLVDERTVD  TQHNHPHTIR  NDDFCRVWYK  PDVTFKKPRT900
FAVATFHSPE  VNPTPYSYAL  SALFVSCLKD  ELNEYSYDAL  LAGMNYKLRL  NGSNIYLSAG960
GYSSKLPILV  QRILEVMGSF  ETHIGDEAFK  RVKHAKCRSF  ENMRLEEAHR  HAVQQESNLL1020
HERSWDIDEI  VSAIRSCSFR  DVIAHSKRLF  RQVYCDILLY  GNLKRSEAMD  LADLIVDQVR1080
APRALSMPST  SKYWIGRQVQ  LSCGVHYIYK  CVHPNPDNAN  CAVNCIYQIG  VENYIDRAKL1140
ALFSQMVDEP  LFDQLRTKEQ  LGYTVYSTPS  RANDVQSFKV  VVQSNVAPPE  LIEQRIEAFW1200
VEFRKTVADT  SADQLQKHIQ  SVVKGYIEKP  KSQEEEVQAL  LVEVANHQYE  FGRKTKLAKL1260
VRTLQLSDVL  QFFDDYIRPE  GPMRKKLSVH  IYGNETRLEK  LGDCSESGWS  AFDNQSQTGL1320
MAAMALASAG  PASRDVKTEY  IKDSQDFKRR  TLVYEAPVAA  L1361

Enzyme Prediction      help

EC 3.2.1.8:31

CAZyme Signature Domains help

Created with Snap68136204272340408476544612680748816884952102010881156122412923289GH10
Family Start End Evalue family coverage
GH10 37 335 2.7e-83 0.9438943894389439

CDD Domains      download full data without filtering help

Created with Snap68136204272340408476544612680748816884952102010881156122412923771317Ptr3781281PRK1510136352Glyco_hydro_107481033Peptidase_M16_M81352Glyco_10
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
223956 Ptr 0.0 377 1317 13 928
Secreted/periplasmic Zn-dependent peptidases, insulinase-like [Posttranslational modification, protein turnover, chaperones].
185056 PRK15101 3.16e-98 378 1281 34 918
protease3; Provisional
395262 Glyco_hydro_10 1.04e-96 36 352 1 308
Glycosyl hydrolase family 10.
406571 Peptidase_M16_M 1.93e-88 748 1033 1 283
Middle or third domain of peptidase_M16. Peptidase_M16_M is the third domain of peptidase_M16 in eukaryotes of the insulin-degrading-enzyme type. Insulin-degrading enzymes - insulysin - are zinc metallopeptidases that metabolize several bioactive peptides, including insulin and the amyloid-beta-peptide. The tertiary structure of insulin-degrading enzymes resembles a clamshell composed of four structurally similar domains arranged to enclose a large central chamber. Substrates must enter the chamber, and it is likely that a hinge-like conformational change allows substrate binding and product release. Triphosphates are found to dock between the inner surfaces of the non-catalytic domains three and four.
214750 Glyco_10 6.51e-80 81 352 1 263
Glycosyl hydrolase family 10.

CAZyme Hits      help

Created with Snap68136204272340408476544612680748816884952102010881156122412922358AOV63057.1|GH106357AOV63056.1|GH101357UIZ28775.1|GH101357UIZ24493.1|GH1015356AOV63055.1|GH10
Hit ID E-Value Query Start Query End Hit Start Hit End
AOV63057.1|GH10 4.02e-200 2 358 1 355
AOV63056.1|GH10 9.80e-184 6 357 5 358
UIZ28775.1|GH10 4.87e-160 1 357 1 355
UIZ24493.1|GH10 4.29e-156 1 357 1 353
AOV63055.1|GH10 1.54e-127 15 356 12 350

PDB Hits      download full data without filtering help

Created with Snap681362042723404084765446126807488168849521020108811561224129237813496B70_A37813492G47_A37813492JG4_A37813493E4Z_A37812953QZ2_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
6B70_A 1.60e-204 378 1349 9 955
Cryo-EM structure of human insulin degrading enzyme in complex with FAB H11-E heavy chain, FAB H11-E light chain and insulin [Homo sapiens],6B70_B Cryo-EM structure of human insulin degrading enzyme in complex with FAB H11-E heavy chain, FAB H11-E light chain and insulin [Homo sapiens],6B7Y_A Cryo-EM structure of human insulin degrading enzyme [Homo sapiens],6B7Y_B Cryo-EM structure of human insulin degrading enzyme [Homo sapiens],6B7Z_A Cryo-EM structure of human insulin degrading enzyme in complex with FAB H11 heavy chain and FAB H11 light chain [Homo sapiens],6B7Z_B Cryo-EM structure of human insulin degrading enzyme in complex with FAB H11 heavy chain and FAB H11 light chain [Homo sapiens],6BF6_A Cryo-EM structure of human insulin degrading enzyme [Homo sapiens],6BF6_B Cryo-EM structure of human insulin degrading enzyme [Homo sapiens],6BF7_A Cryo-EM structure of human insulin degrading enzyme in complex with FAB H11-E heavy chain, FAB H11-E light chain [Homo sapiens],6BF7_B Cryo-EM structure of human insulin degrading enzyme in complex with FAB H11-E heavy chain, FAB H11-E light chain [Homo sapiens],6BF8_A Cryo-EM structure of human insulin degrading enzyme in complex with insulin [Homo sapiens],6BF8_B Cryo-EM structure of human insulin degrading enzyme in complex with insulin [Homo sapiens],6BF9_A Cryo-EM structure of human insulin degrading enzyme in complex with FAB H11-E heavy chain, FAB H11-E light chain [Homo sapiens],6BF9_B Cryo-EM structure of human insulin degrading enzyme in complex with FAB H11-E heavy chain, FAB H11-E light chain [Homo sapiens],6BFC_A Cryo-EM structure of human insulin degrading enzyme in complex with insulin [Homo sapiens],6BFC_B Cryo-EM structure of human insulin degrading enzyme in complex with insulin [Homo sapiens]
2G47_A 1.66e-204 378 1349 25 971
Chain A, Insulin-degrading enzyme [Homo sapiens],2G47_B Chain B, Insulin-degrading enzyme [Homo sapiens],2G48_A Chain A, Insulin-degrading enzyme [Homo sapiens],2G48_B Chain B, Insulin-degrading enzyme [Homo sapiens],2G49_A Chain A, Insulin-degrading enzyme [Homo sapiens],2G49_B Chain B, Insulin-degrading enzyme [Homo sapiens],2G54_A Chain A, Insulin-degrading enzyme [Homo sapiens],2G54_B Chain B, Insulin-degrading enzyme [Homo sapiens],2G56_A Chain A, Insulin-degrading enzyme [Homo sapiens],2G56_B Chain B, Insulin-degrading enzyme [Homo sapiens],2JBU_A Crystal structure of human insulin degrading enzyme complexed with co- purified peptides. [Homo sapiens],2JBU_B Crystal structure of human insulin degrading enzyme complexed with co- purified peptides. [Homo sapiens],3E50_A Chain A, Insulin-degrading enzyme [Homo sapiens],3E50_B Chain B, Insulin-degrading enzyme [Homo sapiens]
2JG4_A 2.33e-204 378 1349 25 971
Substrate-free IDE structure in its closed conformation [Homo sapiens],2JG4_B Substrate-free IDE structure in its closed conformation [Homo sapiens]
3E4Z_A 6.46e-204 378 1349 25 971
Chain A, Insulin-degrading enzyme [Homo sapiens],3E4Z_B Chain B, Insulin-degrading enzyme [Homo sapiens]
3QZ2_A 1.27e-203 378 1295 25 933
The structure of cysteine-free human insulin degrading enzyme [Homo sapiens],3QZ2_B The structure of cysteine-free human insulin degrading enzyme [Homo sapiens],4DTT_A Crystal structure of human insulin degrading enzyme (ide) in complex with compund 41367 [Homo sapiens],4DTT_B Crystal structure of human insulin degrading enzyme (ide) in complex with compund 41367 [Homo sapiens],4IFH_A Crystal structure of human insulin degrading enzyme (IDE) in complex with compound BDM44619 [Homo sapiens],4IFH_B Crystal structure of human insulin degrading enzyme (IDE) in complex with compound BDM44619 [Homo sapiens],4IOF_A Crystal structure analysis of Fab-bound human Insulin Degrading Enzyme (IDE) [Homo sapiens],4IOF_B Crystal structure analysis of Fab-bound human Insulin Degrading Enzyme (IDE) [Homo sapiens],4RE9_A Crystal structure of human insulin degrading enzyme (IDE) in complex with compound 71290 [Homo sapiens],4RE9_B Crystal structure of human insulin degrading enzyme (IDE) in complex with compound 71290 [Homo sapiens],5UOE_A Crystal Structure Analysis of Elbow-Engineered-Fab-Bound Human Insulin Degrading Enzyme (IDE) [Homo sapiens],5UOE_B Crystal Structure Analysis of Elbow-Engineered-Fab-Bound Human Insulin Degrading Enzyme (IDE) [Homo sapiens],5UOE_C Crystal Structure Analysis of Elbow-Engineered-Fab-Bound Human Insulin Degrading Enzyme (IDE) [Homo sapiens],5UOE_D Crystal Structure Analysis of Elbow-Engineered-Fab-Bound Human Insulin Degrading Enzyme (IDE) [Homo sapiens],5UOE_E Crystal Structure Analysis of Elbow-Engineered-Fab-Bound Human Insulin Degrading Enzyme (IDE) [Homo sapiens],6B3Q_A Cryo-EM structure of human insulin degrading enzyme in complex with insulin [Homo sapiens],6B3Q_B Cryo-EM structure of human insulin degrading enzyme in complex with insulin [Homo sapiens],7K1D_A Chain A, Insulin-degrading enzyme [Homo sapiens],7K1D_B Chain B, Insulin-degrading enzyme [Homo sapiens],7K1E_A Chain A, Insulin-degrading enzyme [Homo sapiens],7K1E_B Chain B, Insulin-degrading enzyme [Homo sapiens],7K1F_A Chain A, Insulin-degrading enzyme [Homo sapiens],7K1F_B Chain B, Insulin-degrading enzyme [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Created with Snap68136204272340408476544612680748816884952102010881156122412923841349sp|Q24K02|IDE_BOVIN3781349sp|P14735|IDE_HUMAN3761349sp|P35559|IDE_RAT3761349sp|Q9JHR7|IDE_MOUSE3831291sp|Q06010|STE23_YEAST
Hit ID E-Value Query Start Query End Hit Start Hit End Description
sp|Q24K02|IDE_BOVIN 5.16e-204 384 1349 60 1000
Insulin-degrading enzyme OS=Bos taurus OX=9913 GN=IDE PE=2 SV=1
sp|P14735|IDE_HUMAN 7.25e-204 378 1349 54 1000
Insulin-degrading enzyme OS=Homo sapiens OX=9606 GN=IDE PE=1 SV=4
sp|P35559|IDE_RAT 3.03e-202 376 1349 52 1000
Insulin-degrading enzyme OS=Rattus norvegicus OX=10116 GN=Ide PE=1 SV=1
sp|Q9JHR7|IDE_MOUSE 6.90e-200 376 1349 52 1000
Insulin-degrading enzyme OS=Mus musculus OX=10090 GN=Ide PE=1 SV=1
sp|Q06010|STE23_YEAST 3.56e-182 383 1291 69 965
A-factor-processing enzyme OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=STE23 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000253 0.999714 CS pos: 20-21. Pr: 0.9592

TMHMM  Annotations      help

There is no transmembrane helices in PSURA_85409T0-p1.