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CAZyme Information: PADG_03299-t30_1-p1

You are here: Home > Sequence: PADG_03299-t30_1-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 Paracoccidioides brasiliensis
Lineage Ascomycota; Eurotiomycetes; ; NA; Paracoccidioides; Paracoccidioides brasiliensis
CAZyme ID PADG_03299-t30_1-p1
CAZy Family GH16
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1450 159783.32 5.2139
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PbrasiliensisPb18 8522 502780 132 8390
Gene Location Start: 3038048; End:3043395  Strand: -

Full Sequence      Download help

MATRSHGLLQ  ALLIWTLLSL  QILASVMSPV  LINPLRNAHE  NKMHDLVPRN  QLGTNVVLPP60
SVAKATQLDI  DEARRIVDDA  IKEASALNKA  RLEHPLRNHY  QLKPGTGTSR  RGEPNGDAPP120
PPLFQISKEI  AAAAALIAEV  EAVAETRDSS  KSKADYSYID  VMYNRTVVRR  ADAFWMEDIE180
RKGAWPFGND  RSFKVFRNVK  DYGAVGNGVN  DDTEAIKRAI  ADTGTCGEKC  NGATTKNSIV240
YFPSGTYLVS  STIETHFGSQ  VIGNANDRPV  IKAASSFIGL  GVLSTNHYVE  NGGNGTDGNA300
KEWYVNTANF  YRQIRNFRID  ITATNQGAYI  AALHYQVAQA  TSLSNIDFIV  SSNPGTTQQA360
IFSENGSGGI  LSDLTFTGGN  FGIYGGNQQF  TAQRLQFTNC  KTAVQLIWDW  GWIWKNIQIT420
GSTTGFKLMS  EDNVPRSGSI  MVLDSIFRNT  DTALLTFPAK  QERAKGTTGI  TLDNVAFDKV480
RNAVADNQGK  VYLAGSVGSI  NTWALGPVYF  DSSQRDFTLG  MSFDTSREST  LLADRLSALP540
KAPFFERPRP  QYEGVPVSDF  VHMKDYAKGD  GVTDDTEAFQ  RVLREHSTDR  IIFVDAGSYI600
LTDTIIIPVG  ARIVGEGWSQ  LVASGPNFQD  ERAPRSLVLV  GQPGDTGEVE  IQDLLFTTKG660
PTAGAVLVEW  NIKASSPGSA  GMWDSHVRIG  GASGTKLTST  ECPAIRNGVN  SDDCKSGSLM720
MHITESSSAY  MENVWLWVAD  HDIDDPHLQD  DNNTMVQTSV  YSARGLLVES  AEATWLYGTS780
SEHAIYYQYN  FYKAKNVFAG  MIQTESPYYQ  PTPKPPAPFE  GAIGVLPGDP  DFGGCRDGTP840
GCDASWGLRI  INSSQTYIAG  AGLYSWFTTY  TQECVDKRNC  QNALIELKGN  GPRVRIHNLI900
TIGATNMLTS  DGSEVPSQDN  LAVDYHPYWS  QVTVIDPFQN  RGARGLTTPT  SPDKSGRQCP960
NIPPEVNVPG  GKYPPDIPVM  GRPGKSDHGY  FTLVNGSPYN  WMLTYNHSYQ  LDQWKWHNVP1020
AGESIQGEWK  FARASNRYDD  KGEAYYKIDG  TDKSFQIWAR  FYEDDPENAF  HLRVLYDGLE1080
TKDVKRGTSL  DYRTRGGYGG  MRAINWVLTG  SEEEGYWSSH  SPPVAWMSSI  LNIIGDRKVK1140
HVCMPGSHDA  GMSKLDGHTQ  FADEGNTLTQ  YLSVYDQLRR  GSRYFDVRPA  IGNGGKYLTG1200
HYSYVDVLGI  GWQGGNGESI  QEIVDGINRF  TAENPELIII  NLDLTLDTDN  GYKPFNDEQW1260
SKTFDLFEGV  KYLQGNLEGD  LTERTMNDYI  GAGGAAVIVI  ASGGPTRPEK  GIYSNRQFPR1320
YDSYSNSDDP  AAMADDQLAK  LKGNRNIVSD  TTERKDTFHI  FSWTLTLSRV  FERTIADQSI1380
ELGYDPLFWR  GYHAFTPFSY  PNVVYMDFIG  SADQSETTLE  KTHGEVTALA  MAVNMELASR1440
NCYVGGGTMV  1450

Enzyme Prediction      help

No EC number prediction in PADG_03299-t30_1-p1.

CAZyme Signature Domains help

Created with Snap721452172903624355075806527257978709421015108711601232130513778727GH55
Family Start End Evalue family coverage
GH55 168 920 2e-254 0.9716216216216216

CDD Domains      download full data without filtering help

Created with Snap7214521729036243550758065272579787094210151087116012321305137711311434PI-PLCXDc_like_2196427Pectate_lyase_311321434PI-PLCXDc_like11321413PI-PLCc_bacteria_like11441335PI-PLCXDc_like_1
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
176558 PI-PLCXDc_like_2 1.69e-115 1131 1434 1 300
Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins. This subfamily corresponds to the catalytic domain present in a group of uncharacterized hypothetical proteins found in bacteria and fungi, which are similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs.
403800 Pectate_lyase_3 2.01e-81 196 427 1 213
Pectate lyase superfamily protein. This family of proteins possesses a beta helical structure like Pectate lyase. This family is most closely related to glycosyl hydrolase family 28.
176529 PI-PLCXDc_like 2.43e-53 1132 1434 2 288
Catalytic domain of phosphatidylinositol-specific phospholipase C X domain containing and similar proteins. This family corresponds to the catalytic domain present in phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD) which are bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) sequence homologs mainly found in eukaryota. The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs and their bacterial homologs contain a single TIM-barrel type catalytic domain, X domain, which is more closely related to that of bacterial PI-PLCs. Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may be distinct from that of typical eukaryotic PI-PLCs.
176500 PI-PLCc_bacteria_like 7.08e-32 1132 1413 2 262
Catalytic domain of bacterial phosphatidylinositol-specific phospholipase C and similar proteins. This subfamily corresponds to the catalytic domain present in bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13) and their sequence homologs found in eukaryota. Bacterial PI-PLCs participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although their precise physiological function remains unclear, bacterial PI-PLCs may function as virulence factors in some pathogenic bacteria. Bacterial PI-PLCs contain a single TIM-barrel type catalytic domain. Its catalytic mechanism is based on general base and acid catalysis utilizing two well conserved histidines, and consists of two steps, a phosphotransfer and a phosphodiesterase reaction. Eukaryotic homologs in this family are named as phosphatidylinositol-specific phospholipase C X domain containing proteins (PI-PLCXD). They are distinct from the typical eukaryotic phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11), which have a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, which is closely related to that of bacterial PI-PLCs. Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may be distinct from that of typical eukaryotic PI-PLCs. This family also includes a distinctly different type of eukaryotic PLC, glycosylphosphatidylinositol-specific phospholipase C (GPI-PLC), an integral membrane protein characterized in the protozoan parasite Trypanosoma brucei. T. brucei GPI-PLC hydrolyzes the GPI-anchor on the variant specific glycoprotein (VSG), releasing dimyristyl glycerol (DMG), which may facilitate the evasion of the protozoan to the host's immune system. It does not require Ca2+ for its activity and is more closely related to bacterial PI-PLCs, but not mammalian PI-PLCs.
176557 PI-PLCXDc_like_1 6.20e-11 1144 1335 14 185
Catalytic domain of uncharacterized hypothetical proteins similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins. This subfamily corresponds to the catalytic domain present in a group of uncharacterized hypothetical proteins found in bacteria and fungi, which are similar to eukaryotic phosphatidylinositol-specific phospholipase C, X domain containing proteins (PI-PLCXD). The typical eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) has a multidomain organization that consists of a PLC catalytic core domain, and various regulatory domains. The catalytic core domain is assembled from two highly conserved X- and Y-regions split by a divergent linker sequence. In contrast, eukaryotic PI-PLCXDs contain a single TIM-barrel type catalytic domain, X domain, and are more closely related to bacterial PI-PLCs, which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). Although the biological function of eukaryotic PI-PLCXDs still remains unclear, it may distinct from that of typical eukaryotic PI-PLCs.

CAZyme Hits      help

Created with Snap7214521729036243550758065272579787094210151087116012321305137711450QSS51941.1|GH553451450QSS69923.1|GH55411447QBZ61798.1|GH5562938UKZ47543.1|GH5562938UKZ74106.1|GH55
Hit ID E-Value Query Start Query End Hit Start Hit End
QSS51941.1|GH55 0.0 1 1450 1 1446
QSS69923.1|GH55 0.0 345 1450 2 1107
QBZ61798.1|GH55 0.0 41 1447 41 1428
UKZ47543.1|GH55 0.0 62 938 64 932
UKZ74106.1|GH55 0.0 62 938 64 932

PDB Hits      download full data without filtering help

Created with Snap721452172903624355075806527257978709421015108711601232130513771749155M5Z_A1729203EQN_A1412737CHU_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
5M5Z_A 7.90e-182 174 915 6 736
Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila],5M60_A Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila]
3EQN_A 3.06e-169 172 920 24 743
Chain A, Glucan 1,3-beta-glucosidase [Phanerodontia chrysosporium],3EQN_B Chain B, Glucan 1,3-beta-glucosidase [Phanerodontia chrysosporium],3EQO_A Chain A, Glucan 1,3-beta-glucosidase [Phanerodontia chrysosporium],3EQO_B Chain B, Glucan 1,3-beta-glucosidase [Phanerodontia chrysosporium]
7CHU_A 2.25e-06 141 273 27 149
Chain A, Putative pectin lyase [Geobacillus virus E2],7CHU_B Chain B, Putative pectin lyase [Geobacillus virus E2],7CHU_C Chain C, Putative pectin lyase [Geobacillus virus E2]

Swiss-Prot Hits      download full data without filtering help

Created with Snap72145217290362435507580652725797870942101510871160123213051377170920sp|D4B0V1|E13B_ARTBC172923sp|P49426|EXG1_COCCA167927sp|P53626|E13B_TRIHA
Hit ID E-Value Query Start Query End Hit Start Hit End Description
sp|D4B0V1|E13B_ARTBC 1.90e-169 170 920 39 862
Probable glucan endo-1,3-beta-glucosidase ARB_02077 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02077 PE=1 SV=1
sp|P49426|EXG1_COCCA 8.04e-144 172 923 46 776
Glucan 1,3-beta-glucosidase OS=Cochliobolus carbonum OX=5017 GN=EXG1 PE=1 SV=1
sp|P53626|E13B_TRIHA 3.68e-51 167 927 30 752
Glucan endo-1,3-beta-glucosidase BGN13.1 OS=Trichoderma harzianum OX=5544 GN=bgn13.1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.058814 0.941165 CS pos: 28-29. Pr: 0.3242

TMHMM  Annotations      download full data without filtering help

Start End
7 29