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CAZyme Information: ATY64919.1

You are here: Home > Sequence: ATY64919.1

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 Cordyceps militaris
Lineage Ascomycota; Sordariomycetes; ; Cordycipitaceae; Cordyceps; Cordyceps militaris
CAZyme ID ATY64919.1
CAZy Family GH81
CAZyme Description Glycoside family 35
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1019 CP023325|CGC27 112037.77 6.4388
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_CmilitarisATCC34164 9362 N/A 75 9287
Gene Location Start: 5115132; End:5118608  Strand: +

Full Sequence      Download help

MKFLWGALVA  LSALSATLAA  ETTHAPGSFS  YNRTDFLLNG  QPFQIIGGQM  DPQRIPPEYW60
THRLKMARAM  GLNTIFSYLY  WNLHESRPGA  WDFSGRNDVA  RFFRLAQQEG  LQVVLRPGPY120
ICGERDWGGF  PAWLSQVPGM  AVRQNNRPFL  DAAKSYLDRL  GKELGQLQIT  QGGPILMTQL180
ENEYGSFGTD  KTYLAALAAM  LRDNFDVFLY  TNDGGGQSYL  EGGQLHGVLA  VIDGDSQSGF240
AARDKYVTDP  TSLGPQLNGE  YYISWIDQWG  SDYPHQQIAG  SQADVAKAVA  DLDWTLAGGY300
SFSIYMFHGG  TNFGFENGGI  RDDGPLAAMT  TSYDYGAPLD  ESGRPTDVYF  RLRDMIQKYV360
PKGSIPSVPA  MPARAAVPEF  QLRPAAALFD  LQGRPTRQAS  DPVSMDALGQ  AYGYVLYQHT420
VATDVAGNVA  IGDGARDRAI  IYVNGVRSGV  VDTIYKTPST  VSVTLRKGDK  LQILVENLGR480
VDVRQRLREQ  VKGIVGHVSV  GGTVLTNWCM  HSIPLDTLPA  GLDGKKTHVV  RQKDGPVFYT540
GSFDMPAGAA  ADPSGDTFLA  VPKGIKGVLW  VNGVNMGRYW  TVGPQQSLTH  NTVDTSSTLT600
LAMSRPQTPP  HEPRYNVHVA  PTTISQLIRT  AFPNIELVSS  SELTSHRGYN  NRLYLLTVRR660
RGGPSCVFRD  TDAAERELVL  KANGRFFLAD  KVQNEVGCLQ  VLGQYCPAIP  TPTVFAWSEE720
GHDVCLASPA  GPEIKNVTLA  IPDGEKRHGG  WILMSRLPGA  PLSVCDLDEV  SRLDIMRQLA780
GVTASWRTNI  PAQRYIGNIQ  FHQSVHASEP  DFAIVKNSGP  RPQDLVVRGM  LVDELRITTP840
ITSVTEQYTR  KLEQKLTLLE  TSDTYRPNRH  LAPEIRRFVA  ETLPRLTKQQ  PSHFVFTHYD900
LSPRNILVGG  SPPQISGIVD  FEFAGFFPPV  EEFLNDAVGN  EGDWPDHLYA  AYLAELEARG960
VATPAAGIGA  AEWETARCLE  RVADNVAPWW  LPGKYTGSAL  EEQFAKSAAE  LRENMRKLS1019

Enzyme Prediction      help

EC 3.2.1.23:2

CAZyme Signature Domains help

Created with Snap501011522032543053564074585095606116627137648158669179681306GH35
Family Start End Evalue family coverage
GH35 36 357 1.1e-97 0.993485342019544

CDD Domains      download full data without filtering help

Created with Snap5010115220325430535640745850956061166271376481586691796835356Glyco_hydro_358580PLN0305929594GanA667960APH875929APH_ChoK_like
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
396048 Glyco_hydro_35 6.50e-113 35 356 1 315
Glycosyl hydrolases family 35.
166698 PLN03059 2.75e-55 8 580 9 659
beta-galactosidase; Provisional
224786 GanA 2.28e-32 29 594 1 579
Beta-galactosidase GanA [Carbohydrate transport and metabolism].
396281 APH 8.40e-08 667 960 14 232
Phosphotransferase enzyme family. This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.
270690 APH_ChoK_like 1.28e-07 875 929 94 145
Aminoglycoside 3'-phosphotransferase and Choline Kinase family. This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).

CAZyme Hits      help

Created with Snap5010115220325430535640745850956061166271376481586691796811019ATY64919.1|GH358588UNI19525.1|GH353588QLI69147.1|GH358588QKX60376.1|GH3525588QRD02051.1|GH35
Hit ID E-Value Query Start Query End Hit Start Hit End
ATY64919.1|GH35 0.0 1 1019 1 1019
UNI19525.1|GH35 5.14e-274 8 588 10 588
QLI69147.1|GH35 3.81e-265 3 588 11 595
QKX60376.1|GH35 2.04e-253 8 588 14 602
QRD02051.1|GH35 1.83e-180 25 588 33 589

PDB Hits      download full data without filtering help

Created with Snap50101152203254305356407458509560611662713764815866917968215887KDV_A315883THC_A175883WEZ_A175883WF3_A275886EON_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
7KDV_A 1.02e-104 21 588 10 586
Chain A, Beta-galactosidase [Mus musculus],7KDV_C Chain C, Beta-galactosidase [Mus musculus],7KDV_E Chain E, Beta-galactosidase [Mus musculus],7KDV_G Chain G, Beta-galactosidase [Mus musculus],7KDV_I Chain I, Beta-galactosidase [Mus musculus],7KDV_K Chain K, Beta-galactosidase [Mus musculus]
3THC_A 1.97e-103 31 588 13 578
Crystal structure of human beta-galactosidase in complex with galactose [Homo sapiens],3THC_B Crystal structure of human beta-galactosidase in complex with galactose [Homo sapiens],3THC_C Crystal structure of human beta-galactosidase in complex with galactose [Homo sapiens],3THC_D Crystal structure of human beta-galactosidase in complex with galactose [Homo sapiens],3THD_A Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin [Homo sapiens],3THD_B Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin [Homo sapiens],3THD_C Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin [Homo sapiens],3THD_D Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin [Homo sapiens]
3WEZ_A 2.64e-103 17 588 23 602
Crystal structure of human beta-galactosidase in complex with NOEV [Homo sapiens],3WEZ_B Crystal structure of human beta-galactosidase in complex with NOEV [Homo sapiens],3WEZ_C Crystal structure of human beta-galactosidase in complex with NOEV [Homo sapiens],3WEZ_D Crystal structure of human beta-galactosidase in complex with NOEV [Homo sapiens],3WF0_A Crystal structure of human beta-galactosidase in complex with 6S-NBI-DGJ [Homo sapiens],3WF0_B Crystal structure of human beta-galactosidase in complex with 6S-NBI-DGJ [Homo sapiens],3WF0_C Crystal structure of human beta-galactosidase in complex with 6S-NBI-DGJ [Homo sapiens],3WF0_D Crystal structure of human beta-galactosidase in complex with 6S-NBI-DGJ [Homo sapiens],3WF1_A Crystal structure of human beta-galactosidase in complex with 6S-NBI-GJ [Homo sapiens],3WF1_B Crystal structure of human beta-galactosidase in complex with 6S-NBI-GJ [Homo sapiens],3WF1_C Crystal structure of human beta-galactosidase in complex with 6S-NBI-GJ [Homo sapiens],3WF1_D Crystal structure of human beta-galactosidase in complex with 6S-NBI-GJ [Homo sapiens],3WF2_A Crystal structure of human beta-galactosidase in complex with NBT-DGJ [Homo sapiens],3WF2_B Crystal structure of human beta-galactosidase in complex with NBT-DGJ [Homo sapiens],3WF2_C Crystal structure of human beta-galactosidase in complex with NBT-DGJ [Homo sapiens],3WF2_D Crystal structure of human beta-galactosidase in complex with NBT-DGJ [Homo sapiens]
3WF3_A 1.38e-102 17 588 23 602
Crystal structure of human beta-galactosidase mutant I51T in complex with Galactose [Homo sapiens],3WF3_B Crystal structure of human beta-galactosidase mutant I51T in complex with Galactose [Homo sapiens],3WF3_C Crystal structure of human beta-galactosidase mutant I51T in complex with Galactose [Homo sapiens],3WF3_D Crystal structure of human beta-galactosidase mutant I51T in complex with Galactose [Homo sapiens],3WF4_A Crystal structure of human beta-galactosidase mutant I51T in complex with 6S-NBI-DGJ [Homo sapiens],3WF4_B Crystal structure of human beta-galactosidase mutant I51T in complex with 6S-NBI-DGJ [Homo sapiens],3WF4_C Crystal structure of human beta-galactosidase mutant I51T in complex with 6S-NBI-DGJ [Homo sapiens],3WF4_D Crystal structure of human beta-galactosidase mutant I51T in complex with 6S-NBI-DGJ [Homo sapiens]
6EON_A 8.38e-101 27 588 26 574
Galactanase BT0290 [Bacteroides thetaiotaomicron VPI-5482]

Swiss-Prot Hits      download full data without filtering help

Created with Snap501011522032543053564074585095606116627137648158669179688588sp|P48982|BGAL_XANMN1588sp|Q9TRY9|BGAL_CANLF31588sp|O19015|BGAL_FELCA21588sp|P23780|BGAL_MOUSE30588sp|Q60HF6|BGAL_MACFA
Hit ID E-Value Query Start Query End Hit Start Hit End Description
sp|P48982|BGAL_XANMN 4.97e-110 8 588 9 571
Beta-galactosidase OS=Xanthomonas manihotis OX=43353 GN=bga PE=1 SV=1
sp|Q9TRY9|BGAL_CANLF 1.98e-104 1 588 7 602
Beta-galactosidase OS=Canis lupus familiaris OX=9615 GN=GLB1 PE=1 SV=3
sp|O19015|BGAL_FELCA 2.82e-104 31 588 37 603
Beta-galactosidase OS=Felis catus OX=9685 GN=GLB1 PE=2 SV=1
sp|P23780|BGAL_MOUSE 2.24e-103 21 588 27 603
Beta-galactosidase OS=Mus musculus OX=10090 GN=Glb1 PE=1 SV=1
sp|Q60HF6|BGAL_MACFA 1.51e-102 30 588 35 601
Beta-galactosidase OS=Macaca fascicularis OX=9541 GN=GLB1 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000296 0.999674 CS pos: 19-20. Pr: 0.9802

TMHMM  Annotations      help

There is no transmembrane helices in ATY64919.1.