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CAZyme Information: EPrPRT00000013138-p1

You are here: Home > Sequence: EPrPRT00000013138-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 Pythium arrhenomanes
Lineage Oomycota; NA; ; Pythiaceae; Pythium; Pythium arrhenomanes
CAZyme ID EPrPRT00000013138-p1
CAZy Family AA17
CAZyme Description Phosphatidylinositol kinase (PIK-L3).
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
4568 502795.02 8.1101
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_ParrhenomanesATCC12531 13857 1223556 52 13805
Gene Location Start: 67841; End:84340  Strand: -

Full Sequence      Download help

MDVSNGPAND  AESALPLVKE  PVAVDNADEQ  RRRKLVVIAL  SLLALVGLLA  LSEISTGGYA60
FGSSRDTRSF  RDDKKIVVLL  SSGRDSQSCA  RALVAAKDLA  FRSSRVHFRV  YEEIAVHHDD120
SCLQVFCELS  PRDCKALLRT  KRLQVTRRDV  SGSLGASVGL  HVLEGMVDRK  SFENDFYLAV180
DANIEFTKHW  DLELLKQWYS  IGNDRAILSV  SPPAIEIKGM  NHGMLFLQCS  ARIHSKDPDP240
VVEFNPPEPK  PLVKGDSLGA  ALLATVPVLQ  AQYSERFHFG  LVSSLLSVRS  DPHLAHLVVG300
HEYMRATRFW  TKGFDFYAPA  RDILYYRYEL  PLAPHEKGET  DAAIGMSSRR  IRRLLKLPLS360
SPLFEFELLP  DVHILNRLPS  NDALRPYVPQ  LLHLLLEVLY  RDNEDNALLA  LKTVFDLHRN420
YRPGLRSEVQ  AFLDLVQQMY  KNVHVTVRKQ  FAEAVVTPPS  SQAAASPTVS  TVATTPTTTA480
AASAASTVET  SGTTPPSVDG  AVSTLSTAST  TETTSDPAAT  TTTAEPVMPV  KTESASAPLS540
IAAVSSESPA  AAVDTKADGS  APPQPPSAAP  GVAAATPSTP  VSSIASSTVA  VDEPLWSSME600
SFKAISELPL  IIMLLFQCYP  TFIESHVPVL  VPLMMNLLSL  RAPDSAPRQH  PQRYVDFLDC660
QVKTLSFVTY  LLRGCATLMR  PFQDAICEST  VKLLTVCPKD  AFVLRKDIFV  AARHIISTEF720
RRGFYAQLEL  LMDDDVLIGK  GRCSFHQIRP  LAYSTLADMI  HHVRDMLTLS  QVSHIVDFYG780
KRIHDATLPI  SIQTTSIRLL  LNLVDISAKN  DDADGWKGRT  ILSRILLIIA  SKFGSTLASL840
PVAIGLSLRS  AADRGGAGAA  PTADLLDAGA  MDKIRQSTLL  PKAVVEKAPH  EKKLDALLAP900
YLNAVPRSAS  GSVDSFLADE  EPCIRDVKSL  LRTMILGVRA  VIWCTANYRN  PHAKDLTSMD960
ANASHVSGSD  ISAALQGTAT  ESSGGIASRP  SSAGSTNADA  TSAAHAYPLT  DDERKLISRV1020
LQNGLRCSIL  YTLSENTLAE  EKQMLDHFAG  AFTVLDAPDF  RDLFLANMEL  LYECILQDHA1080
ILTVPQHFLA  NSNVSCWFAE  ILLKFLITQM  KDLSVAAEGD  VPDMKREHKV  LEMDSLRFER1140
MRVVKQEHRA  SIVLRLFKIV  FGSVTLFKSN  ESALFPHLRT  IIESCLKEAT  FTKHPDNYLL1200
LLRALFRSIS  GGKYENFYKE  VFPLLPGILS  ALMRLQQHIQ  KPSMHEVLLE  LCLTIPARLS1260
SLLQYLPSLM  KSVIGGRNRQ  YQMDPLELAF  ESEPQRRALV  MEFAWRGLDV  NKKPVALGLH1320
MDVLLRRAAA  ILHRYHRKAP  HEWEHVVRKD  ARLSDSDEYD  DHANTAGATA  GGAVVEASLA1380
ASAGGGSASS  SLLLEKDDKT  LELERQAAAN  VKQTILQYKR  YAFDVVASAT  TIAMQLSEAE1440
EPDEDEDEEN  DEEEEEDDAM  NGAETSMRPS  VVWESELPTR  QLLLKTLFET  MDDIDFGEAA1500
TRLLMRTATQ  MTKKVSDVCD  RHEPNFAALS  TLQPSSLLPG  NRGLSPGRHL  ATAKRIEVLR1560
QASYGTPFVV  VPHSRAAAFF  QAFASAILGG  LSSPNSQVVD  GAKKVLERVV  ETALHHYEAD1620
IDAASAAYKG  GALFLTLTDV  FAHACFDKSS  WRVKLGGVTG  LRLLVDLLAA  PFCHENELVI1680
VKALFFVLSD  HPSEVSATVS  VETGEALLAV  VDKARDVRGL  DIEAFSSGAI  KRGDFMSCTA1740
FQETEIFQMF  VVEFLSPKAA  ARRCARQCIA  RVAAFTGTTE  SAMLFPYQQL  ISKQITGCPL1800
RSLSSATRIG  YIDAMAHALS  IQPTIFPLTK  ELMTFLQDVW  RLISDDATPS  ATEAATTAAP1860
GIAGGATSTS  SNVPVSAQEY  PFGLSQASEL  RIAAVKLFRA  AFLAAPDDMN  QHHEARNRFV1920
GVFFRYLTRQ  PLELVTCAQQ  ALSDVIQLNK  QHKEITLPKE  LLQQCLRPVL  LNLADYRKLN1980
LPLLDGLSRL  LTLLSSCFNV  TLGEKLLEHL  KQWRDPDRIM  KAGIWKRGDE  PAVAAAIVDL2040
FHLLPPNESF  LESLVDCVVE  LEAVLPQYGS  YGKMSSPYRL  PLTRFLNRYA  STSIAFFLKR2100
DKLIEPKYSS  LFQELLKLPE  ALPLRNILLS  ETGAESLMAA  TFVAASKTED  IKMQAQIQLN2160
AHKAAAQAVA  NAQAQGLSPS  AAEARGMQAR  AAYVAKATAQ  VNAQQALKVQ  SQVQIQANAQ2220
KLHAQTLAAA  QAQGLSLVQA  QAKAQFASKD  YIAKAQSQVA  ASTALPSPIS  SSAVTPSLAN2280
TASPHHVTQL  QAQQLHAQIQ  VNAQKVHAQA  LAAAHAQGLK  PIQAQEKAKQ  AQATYVHRAK2340
AQAQAKIARA  AQTSSLSSAL  PTTPSALSTV  APFTSKAQQE  ALELLYQGLR  LIRFHYESKL2400
LVKILVTYCR  AKPDDVQVLL  DLLSAFVHRS  SSFDNSVLQL  FYQQHVAHAY  SPYNKRQIVH2460
AMQVLIMPVL  TTSFDDPTVN  NTDMLDADTV  QWMLREILAS  KDTPTGSPPS  DAVLTLRIEL2520
LKLGTLLIQH  MSKYVTEHRK  EVIKFAWNHL  KAHDLTSKLW  AYVNVCRFIS  VYDTPPKIVL2580
QVYVALLRTH  EMDARFLVRK  AFDILLPALP  SRLPPNEFIK  AIKWTKKIAY  EEGHQLGQLV2640
HIWFLIVRHP  ALFYPFRGQF  VPLMVNSLNR  LAIPPSSTPD  NRRLAVNIVD  LIIAWEHTRR2700
ERVASRPVTP  AAAGDGAALK  RRALQAAAGE  EETKSESESP  SQKRRKVMSG  TSEDASAVAV2760
AANGSVAASS  PTAKTAAAAY  SEDDFELNAP  MIDLVLNFAF  RFALASADKQ  ETSRLSKTCG2820
ELFDKALRLW  PSASVRFSYF  DKLIAVTAEA  ILRQQPLPTP  TPPTQSMPTF  FAVPKGAPLS2880
SLAILDAVLG  ILNALITPEV  VSHSARPVPY  VVQYAPRVMK  LLEPCFDRAN  GDIQTGLTTF2940
LRRMVELYPP  GRAVSQELSA  CKFYPWLQEI  VADRLQSAVA  LQQEFLTSLP  SHAASSAVAS3000
GSSGGGATQK  TKNKQGGGST  AAAATASGVS  SPASVKSEPK  AGQASPGTAA  AAGSPAKRQK3060
TAGSDPAVAL  KVKAALAAAQ  SARSSGIPPS  KKEPGDKHKK  KSSHGEKESA  GFAAGTKAGS3120
TASSSGVKKK  GVAAQHATSG  LLSHKMAVEL  LIVTLRLLSK  CSLPSADHRR  VYTNLLIHCL3180
ESSTNDKMTL  LTKMSSFERL  HEVAARPLYD  EYYRLVLKLC  DPSSDVKHSY  FHITPSLPQS3240
HSLTTHFVAG  LLAPDAEIRE  QFLKYLYEAA  ASGSPDAAED  SLPTGRLLLV  LRQDWQACGS3300
RYWIAVAVET  MLSAATNSTP  TGSPRANSKR  RLSGQLSPTS  PSPSSQLDLL  RALRYLAHVD3360
VEIAEELWIQ  LFRETWQQLS  TPQQAHVSSQ  LVKTFSSKFN  KRDFSAMRLC  EFQVENASLR3420
VESRLRWIEA  LSSIYKTLSD  DDLRVGLSLE  HIAQPETRAA  LVLESLGCVH  EAQEEYFKAL3480
SKAQSGRVSM  DDVNLFELRL  WEERWVACAK  QLCQWQLMHD  FAKATQNQDL  LLDCVWKRGD3540
WHGAKQLLNF  VEVKESIQMM  YDIKHASQLH  TLPNLKPSIN  TWRERLPNKW  EPILMWDDIL3600
TWRSHMFQVV  KNTFSWSDAQ  MLACMHDSPW  SVIRLAHTAR  KQHLPDVCLG  ALSKLYTIPA3660
MDVQDAFSKL  REQVSICYES  ASEYTGGLAI  LNNTNLDYFS  LRQKAEMFRL  KALFLEAMGN3720
STDANQTFSH  CLQICDSYGK  GWLSFASQTI  ACYLQAIHHR  CNAARLMIAR  VLWLLSMDDP3780
HRGVLIQAFE  AHGKQLPIWI  WIVWIPQLLM  ALGRPEAPQI  RGLLRGLSAK  FPQALYYTMR3840
AFFLENRDSS  MAAQQQQMSG  QGQVSGSAPT  TPQSSGSTGA  ATTVTASTGG  PGTPTFSGTP3900
VYYRTKTGQV  VAVPSTMPLN  HVQQIPGLVA  PARPTPSAFG  VALSQVMTVD  AWRERLLLGS3960
GGADGASSQA  TSSSSSSSSA  ASSSMPTKPE  LGPVQYTEDL  LNFLRRTHDS  LTFEMECVLE4020
EMITKFRPEP  EEELLTAVHS  LLLKCYQLPR  LSQREPVPRM  LRAALEKVCR  KLFAVTAAST4080
TTGSAVGAPP  PPQQHKNEKY  VEFVAEFKAA  FEADFAPDAS  LLSAPIQEER  VTLFEMMDRL4140
KKWRNLLQAR  VQHQSCGYST  GRASTLRLEH  CSRFLMELSS  SNMEVPGQYI  ADREPIKDLH4200
ARIQHFDNDV  DVLLRSGYTQ  RRLTMGGSDG  ATYSFLVQYA  MTHTTRTDER  MAQMYLLLNR4260
LLARHKETRK  RNAVFHVPRV  VPLTPRSCRA  SDTDPDLPME  LYRQRISEAY  AAMAMAAQHD4320
ASETISPQQE  DEQLALAKAR  AFDEVCASHV  PETLLAKYIF  ERSAHADAYF  EFRSEFTKHL4380
ALSSLLAYVL  FVGDRAPHRI  LFSRRTARVV  SAELRPGYAS  SGLLEASTSM  PFRLTRNLHN4440
FVTRPGVHGP  FSALMGEEEL  LGNQLGLFFR  DDLLSWHASK  TRLAATASSA  GMADSASQQQ4500
QQQRQRRLES  QVQQRVDANV  SLVLERIRGV  SLKKETDSQR  GKSVRELLEI  ATSPERQREM4560
YPTWCPWL4568

Enzyme Prediction      help

EC 2.4.1.-:1

CAZyme Signature Domains help

Created with Snap2284566859131142137015981827205522842512274029693197342636543882411143392290GT60
Family Start End Evalue family coverage
GT60 76 357 1.2e-31 0.8727272727272727

CDD Domains      download full data without filtering help

Created with Snap22845668591311421370159818272055228425122740296931973426365438824111433942034478PIKK_TRRAP33794568TEL135563773FAT42034455PIKKc42034476PIKKc_TOR
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
270707 PIKK_TRRAP 7.83e-85 4203 4478 1 252
Pseudokinase domain of TRansformation/tRanscription domain-Associated Protein. TRRAP belongs to the the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. It contains a FATC (FRAP, ATM and TRRAP, C-terminal) domain and has a large molecular weight. Unlike most PIKK proteins, however, it contains an inactive PI3K-like pseudokinase domain, which lacks the conserved residues necessary for ATP binding and catalytic activity. TRRAP also contains many motifs that may be critical for protein-protein interactions. TRRAP is a common component of many histone acetyltransferase (HAT) complexes, and is responsible for the recruitment of these complexes to chromatin during transcription, replication, and DNA repair. TRRAP also exists in non-HAT complexes such as the p400 and MRN complexes, which are implicated in ATP-dependent remodeling and DNA repair, respectively. The TRRAP pseudokinase domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.
227365 TEL1 1.57e-38 3379 4568 1073 2105
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms].
396714 FAT 1.47e-27 3556 3773 80 342
FAT domain. The FAT domain is named after FRAP, ATM and TRRAP.
270708 PIKKc 3.83e-25 4203 4455 1 198
Catalytic domain of Phosphoinositide 3-kinase-related protein kinases. PIKK subfamily members include ATM (Ataxia telangiectasia mutated), ATR (Ataxia telangiectasia and Rad3-related), TOR (Target of rapamycin), SMG-1 (Suppressor of morphogenetic effect on genitalia-1), and DNA-PK (DNA-dependent protein kinase). PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). They show strong preference for phosphorylating serine/threonine residues followed by a glutamine and are also referred to as (S/T)-Q-directed kinases. They all contain a FATC (FRAP, ATM and TRRAP, C-terminal) domain. PIKKs have diverse functions including cell-cycle checkpoints, genome surveillance, mRNA surveillance, and translation control. The PIKK catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.
270713 PIKKc_TOR 9.43e-22 4203 4476 1 277
Catalytic domain of Target of Rapamycin. TOR contains a rapamycin binding domain, a catalytic domain, and a FATC (FRAP, ATM and TRRAP, C-terminal) domain at the C-terminus. It is also called FRAP (FK506 binding protein 12-rapamycin associated protein). TOR is a central component of the eukaryotic growth regulatory network. It controls the expression of many genes transcribed by all three RNA polymerases. It associates with other proteins to form two distinct complexes, TORC1 and TORC2. TORC1 is involved in diverse growth-related functions including protein synthesis, nutrient use and transport, autophagy and stress responses. TORC2 is involved in organizing cytoskeletal structures. TOR is a member of the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). The TOR catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.

CAZyme Hits      help

Created with Snap22845668591311421370159818272055228425122740296931973426365438824111433967360UIZ27043.1|GT6073354CCA22278.1|GT6067365UIZ22347.1|GT6074365CCA18910.1|GT6072367UIZ25379.1|GT60
Hit ID E-Value Query Start Query End Hit Start Hit End
UIZ27043.1|GT60 2.35e-88 67 360 108 404
CCA22278.1|GT60 3.54e-53 73 354 34 306
UIZ22347.1|GT60 9.43e-30 67 365 51 336
CCA18910.1|GT60 4.57e-27 74 365 85 364
UIZ25379.1|GT60 4.25e-18 72 367 68 362

PDB Hits      download full data without filtering help

Created with Snap22845668591311421370159818272055228425122740296931973426365438824111433937245685OEJ_B37445676IG9_T37445675OJS_T37221287KTS_A342945675Y81_B
Hit ID E-Value Query Start Query End Hit Start Hit End Description
5OEJ_B 6.00e-205 372 4568 79 3825
Chain B, Tra1 subunit within the chromatin modifying complex SAGA [Komagataella pastoris],6TB4_L Chain L, Transcription-associated protein [Komagataella phaffii GS115],6TBM_L Chain L, Transcription-associated protein [Komagataella phaffii GS115]
6IG9_T 1.32e-170 374 4567 82 3743
Tra1 subunit from Saccharomyces cerevisiae SAGA complex [Saccharomyces cerevisiae],6T9I_T cryo-EM structure of transcription coactivator SAGA [Saccharomyces cerevisiae S288C],6T9J_T SAGA Tra1 module [Saccharomyces cerevisiae S288C]
5OJS_T 1.34e-170 374 4567 105 3766
Cryo-EM structure of the SAGA and NuA4 coactivator subunit Tra1 [Saccharomyces cerevisiae S288C]
7KTS_A 4.85e-106 372 2128 94 1585
Chain A, Transformation/transcription domain-associated protein,Transformation/transcription domain-associated protein,Transformation/transcription domain-associated protein,Transformation/transcription domain-associated protein,Transformation/transcription domain-associated protein [Homo sapiens]
5Y81_B 1.37e-96 3429 4567 31 1114
NuA4 TEEAA sub-complex [Saccharomyces cerevisiae S288C]

Swiss-Prot Hits      download full data without filtering help

Created with Snap2284566859131142137015981827205522842512274029693197342636543882411143393724568sp|Q9Y4A5|TRRAP_HUMAN3724568sp|A0A0R4ITC5|TRRAP_DANRE3744567sp|P38811|TRA1_YEAST3724568sp|Q8I8U7|TRA1_DROME5654568sp|Q9HFE8|TRA1_SCHPO
Hit ID E-Value Query Start Query End Hit Start Hit End Description
sp|Q9Y4A5|TRRAP_HUMAN 7.81e-198 372 4568 94 3859
Transformation/transcription domain-associated protein OS=Homo sapiens OX=9606 GN=TRRAP PE=1 SV=3
sp|A0A0R4ITC5|TRRAP_DANRE 1.51e-196 372 4568 94 3841
Transformation/transcription domain-associated protein OS=Danio rerio OX=7955 GN=trrap PE=3 SV=1
sp|P38811|TRA1_YEAST 6.77e-170 374 4567 82 3743
Transcription-associated protein 1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=TRA1 PE=1 SV=1
sp|Q8I8U7|TRA1_DROME 1.37e-168 372 4568 85 3790
Transcription-associated protein 1 OS=Drosophila melanogaster OX=7227 GN=Nipped-A PE=1 SV=4
sp|Q9HFE8|TRA1_SCHPO 2.66e-158 565 4568 198 3699
Transcription-associated protein 1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=tra1 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000020 0.000020

TMHMM  Annotations      download full data without filtering help

Start End
35 57