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CAZyme Information: KAG6572510.1

You are here: Home > Sequence: KAG6572510.1

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 Phytophthora cinnamomi
Lineage Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora cinnamomi
CAZyme ID KAG6572510.1
CAZy Family AA1
CAZyme Description putative UDP-N-acetylglucosamine-peptide N-acetylglucosaminyltransferase 110 kDa subunit
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1370 155674.20 5.9001
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PcinnamomiGKB4 19981 N/A 0 19981
Gene Location Start: 203085; End:207269  Strand: +

Full Sequence      Download help

MAPPLACLAL  FLSLRCLIDP  SEAATVLVVT  PENEASLTLA  AQLYRKAQDA  SELPDKERLF60
RESIDAYPEL  APAYNNLAML  VLERHGRDEA  VQLLERGLQA  AEATNDRENV  ANIHNNLGFV120
TREYGKWSVA  HSLAALRHFD  AALEIDPEFT  GALYNKASVF  LALRRDMECK  ELLLKVLELE180
PDNRQAHLDL  GRIYFEHGDL  EKALQHEDRV  IEMAMTTKQK  LEGMHNKGVF  LREYGFLARA240
LDVYSQMLAI  ASVESYVLVD  IMNAKRLFCD  WRDMEALENQ  VVAAAQRQLD  FEMPEEPVQF300
LPYDSTLLKL  PDNFRKTLAM  RASKQYEQPS  TLELLPLPWR  ENEPTWDRPL  TPQRLKVGYL360
SFDFRDHPMG  HLTLGLIEQH  AALARGVDTI  CYSYGPNSEA  SAPWRRQFEE  KCGMFRDLLG420
MSDLEAAQAI  GLDGIDVLVD  LMAHTKGARL  GIPSLRPSRI  TVNYLGYPGT  MGSTFTDFAM480
VDKSVVPPEV  ATKTMSEQVV  YLPHTYQANR  YEVSIASCGA  DTECQRMNRS  QHSLPTDAMV540
FCNFNTINKM  ETESFSVWMS  ILRQVPKSVL  WLLAPSGEDA  VRVMELLNEQ  AMAHGVLPSR600
IIFAPRVDKL  SHLARVTVAD  LFLDSFIYNA  HSTAADALWA  NVPIVTFWGD  TFPSRVAASL660
IQKAIPFPEL  ISHSVKDYER  IAVHLAKTPS  VLRHIRSLLA  SHSLTSPLFN  TKQTTESIET720
AYEVMHDVVN  RLHPFTKEDS  SSRFQLIIHP  EHTAKAFDNA  EIAYARVDNA  LRQGISLQES780
GDYIGARHAY  SRVLRATPGN  PDVIHLLGTI  FYQTGELERA  VEYITRAVTA  NPHVSWYHSN840
LGVAYAALEK  LDLAEAEFQL  ALQLDPANRI  AISKLGELYT  AQKAFDRVVE  LYATYGEAAY900
FFTGKTSASQ  EDIEKAYLDY  FEALTKTGRS  LDAIKLLEDA  VQQHPTLFQL  SYNLGVMYNE960
AERYDEGNQR  QFATVLAQGR  YLYETKGKHF  KKIPRPEHKV  VIAFYCHEYG  QEWWEHWGPS1020
SLDTGLGGSE  EALVFLSREL  QMLGYWVEIY  GDPSPQDVST  LDQADQDVVR  WYPHYTYDVD1080
DRGVDMFVAW  RYHISLAMGK  TAWKKFLWMH  DLPQEDAKRS  TELLNNVDRI  FCLSDFHASM1140
FPERLQSKIT  VHTNAVDPSF  FVDGPNHADR  LVYGSSPSRG  LYAVLQAWPR  IREAIPTAEL1200
SVFYGFRPAF  IKWGHSHMAN  FTVWMAEMDR  LLTETPGVRY  VGLVNHAQLA  KEYSYAGFYL1260
YPTTFSETSC  ISLMKAMVNG  AIPITSRFPA  SALPETVDEF  DLGPRALQQN  SIVADSEWME1320
LWIQSIVDAV  RDEQQAFTIR  HRMKRFARKK  YRWEHIALQW  HQVISKPRFP  1370

Enzyme Prediction      help

EC - -

CAZyme Signature Domains help

Created with Snap6813720527434241147954861668575382289095910271096116412331301109518GT41
Family Start End Evalue family coverage
GT41 131 727 8e-109 0.5801418439716312

CDD Domains      download full data without filtering help

Created with Snap681372052743424114795486166857538228909591027109611641233130177725Spy269718Glyco_transf_4110021364GT4_PimA-like771863TPR801892TPR
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
226428 Spy 3.39e-89 77 725 18 614
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones].
404688 Glyco_transf_41 5.47e-72 269 718 2 543
Glycosyl transferase family 41. This family of glycosyltransferases includes O-linked beta-N-acetylglucosamine (O-GlcNAc) transferase, an enzyme which catalyzes the addition of O-GlcNAc to serine and threonine residues. In addition to its function as an O-GlcNAc transferase, human OGT also appears to proteolytically cleave the epigenetic cell-cycle regulator HCF-1.
340831 GT4_PimA-like 2.72e-16 1002 1364 2 365
phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.
276809 TPR 2.73e-15 771 863 5 97
Tetratricopeptide repeat. The Tetratricopeptide repeat (TPR) typically contains 34 amino acids and is found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans. It is present in a variety of proteins including those involved in chaperone, cell-cycle, transcription, and protein transport complexes. The number of TPR motifs varies among proteins. Those containing 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein. It has been proposed that TPR proteins preferentially interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes.
276809 TPR 5.61e-15 801 892 1 92
Tetratricopeptide repeat. The Tetratricopeptide repeat (TPR) typically contains 34 amino acids and is found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans. It is present in a variety of proteins including those involved in chaperone, cell-cycle, transcription, and protein transport complexes. The number of TPR motifs varies among proteins. Those containing 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein. It has been proposed that TPR proteins preferentially interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes.

CAZyme Hits      help

Created with Snap681372052743424114795486166857538228909591027109611641233130117564AIG56498.1|GT41354728ALF56465.1|GT41354725ALF56607.1|GT41261728BAG05864.1|GT41237728QLE54208.1|GT41
Hit ID E-Value Query Start Query End Hit Start Hit End
AIG56498.1|GT41 3.71e-95 17 564 17 559
ALF56465.1|GT41 5.53e-89 354 728 23 380
ALF56607.1|GT41 9.30e-88 354 725 16 370
BAG05864.1|GT41 4.75e-87 261 728 176 617
QLE54208.1|GT41 1.77e-85 237 728 556 1021

PDB Hits      download full data without filtering help

Created with Snap68137205274342411479548616685753822890959102710961164123313012667226Q4M_A2667225NPR_A2667225NPS_A2667223PE3_A2667226TKA_AAA
Hit ID E-Value Query Start Query End Hit Start Hit End Description
6Q4M_A 8.79e-54 266 722 156 702
Crystal structure of the O-GlcNAc transferase Asn648Tyr mutation [Homo sapiens]
5NPR_A 1.45e-53 266 722 150 696
The human O-GlcNAc transferase in complex with a thiol-linked bisubstrate inhibitor [Homo sapiens]
5NPS_A 1.48e-53 266 722 151 697
The human O-GlcNAc transferase in complex with a bisubstrate inhibitor [Homo sapiens]
3PE3_A 1.58e-53 266 722 156 702
Chain A, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit [Homo sapiens],3PE3_B Chain B, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit [Homo sapiens],3PE3_C Chain C, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit [Homo sapiens],3PE3_D Chain D, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit [Homo sapiens],3PE4_A Structure of human O-GlcNAc transferase and its complex with a peptide substrate [Homo sapiens],3PE4_C Structure of human O-GlcNAc transferase and its complex with a peptide substrate [Homo sapiens],3TAX_A A Neutral Diphosphate Mimic Crosslinks the Active Site of Human O-GlcNAc Transferase [Homo sapiens],3TAX_C A Neutral Diphosphate Mimic Crosslinks the Active Site of Human O-GlcNAc Transferase [Homo sapiens],4AY5_A Human O-GlcNAc transferase (OGT) in complex with UDP and glycopeptide [Homo sapiens],4AY5_B Human O-GlcNAc transferase (OGT) in complex with UDP and glycopeptide [Homo sapiens],4AY5_C Human O-GlcNAc transferase (OGT) in complex with UDP and glycopeptide [Homo sapiens],4AY5_D Human O-GlcNAc transferase (OGT) in complex with UDP and glycopeptide [Homo sapiens],4AY6_A Human O-GlcNAc transferase (OGT) in complex with UDP-5SGlcNAc and substrate peptide [Homo sapiens],4AY6_B Human O-GlcNAc transferase (OGT) in complex with UDP-5SGlcNAc and substrate peptide [Homo sapiens],4AY6_C Human O-GlcNAc transferase (OGT) in complex with UDP-5SGlcNAc and substrate peptide [Homo sapiens],4AY6_D Human O-GlcNAc transferase (OGT) in complex with UDP-5SGlcNAc and substrate peptide [Homo sapiens],4CDR_A Human O-GlcNAc transferase in complex with a bisubstrate inhibitor, Goblin1 [Homo sapiens],4CDR_B Human O-GlcNAc transferase in complex with a bisubstrate inhibitor, Goblin1 [Homo sapiens],4CDR_C Human O-GlcNAc transferase in complex with a bisubstrate inhibitor, Goblin1 [Homo sapiens],4CDR_D Human O-GlcNAc transferase in complex with a bisubstrate inhibitor, Goblin1 [Homo sapiens],4GYW_A Crystal structure of human O-GlcNAc Transferase in complex with UDP and a glycopeptide [Homo sapiens],4GYW_C Crystal structure of human O-GlcNAc Transferase in complex with UDP and a glycopeptide [Homo sapiens],4GYY_A Crystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc and a peptide substrate [Homo sapiens],4GYY_C Crystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc and a peptide substrate [Homo sapiens],4GZ3_A Crystal structure of human O-GlcNAc Transferase with UDP and a thioglycopeptide [Homo sapiens],4GZ3_C Crystal structure of human O-GlcNAc Transferase with UDP and a thioglycopeptide [Homo sapiens],4GZ5_A Crystal structure of human O-GlcNAc Transferase with UDP-GlcNAc [Homo sapiens],4GZ5_B Crystal structure of human O-GlcNAc Transferase with UDP-GlcNAc [Homo sapiens],4GZ5_C Crystal structure of human O-GlcNAc Transferase with UDP-GlcNAc [Homo sapiens],4GZ5_D Crystal structure of human O-GlcNAc Transferase with UDP-GlcNAc [Homo sapiens],4GZ6_A Crystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc [Homo sapiens],4GZ6_B Crystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc [Homo sapiens],4GZ6_C Crystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc [Homo sapiens],4GZ6_D Crystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc [Homo sapiens],4N39_A Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (11-26) [Homo sapiens],4N3A_A Crystal Structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (1-26)E10A [Homo sapiens],4N3B_A Crystal Structure of human O-GlcNAc Transferase bound to a peptide from HCF-1 pro-repeat2(1-26)E10Q and UDP-5SGlcNAc [Homo sapiens],4N3C_A Crystal Structure of human O-GlcNAc Transferase bound to a peptide from HCF-1 pro-repeat2(1-26) and UDP-GlcNAc [Homo sapiens],4XI9_A Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (RBL2) [Homo sapiens],4XI9_B Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (RBL2) [Homo sapiens],4XI9_C Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (RBL2) [Homo sapiens],4XI9_D Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (RBL2) [Homo sapiens],4XIF_A Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (keratin-7) [Homo sapiens],4XIF_B Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (keratin-7) [Homo sapiens],4XIF_C Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (keratin-7) [Homo sapiens],4XIF_D Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (keratin-7) [Homo sapiens],5BNW_A The active site of O-GlcNAc transferase imposes constraints on substrate sequence [Homo sapiens],5C1D_A Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (RB2L) [Homo sapiens],5VIE_A Chain A, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit [Homo sapiens],5VIE_C Chain C, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit [Homo sapiens],5VIF_A Electrophilic probes for deciphering substrate recognition by O-GlcNAc transferase [Homo sapiens],6E37_A O-GlcNAc Transferase in complex with covalent inhibitor [Homo sapiens],6MA1_A Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (11-26) and inhibitor 4a [Homo sapiens],6MA2_A Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (11-26) and inhibitor ent-1a [Homo sapiens],6MA3_A Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (11-26) and inhibitor 2a [Homo sapiens],6MA4_A Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (11-26) and inhibitor 3a [Homo sapiens],6MA5_A Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (11-26) and inhibitor 1a [Homo sapiens]
6TKA_AAA 1.67e-53 266 722 155 701
Chain AAA, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Created with Snap6813720527434241147954861668575382289095910271096116412331301353722sp|Q9M8Y0|SEC_ARATH266722sp|Q8CGY8|OGT1_MOUSE266722sp|P81436|OGT1_RABIT266722sp|O15294|OGT1_HUMAN266722sp|Q27HV0|OGT1_PIG
Hit ID E-Value Query Start Query End Hit Start Hit End Description
sp|Q9M8Y0|SEC_ARATH 1.97e-57 353 722 590 948
Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SEC OS=Arabidopsis thaliana OX=3702 GN=SEC PE=1 SV=1
sp|Q8CGY8|OGT1_MOUSE 2.46e-52 266 722 474 1020
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Mus musculus OX=10090 GN=Ogt PE=1 SV=2
sp|P81436|OGT1_RABIT 9.99e-52 266 722 474 1020
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Oryctolagus cuniculus OX=9986 GN=OGT PE=1 SV=2
sp|O15294|OGT1_HUMAN 1.32e-51 266 722 474 1020
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Homo sapiens OX=9606 GN=OGT PE=1 SV=3
sp|Q27HV0|OGT1_PIG 3.06e-51 266 722 474 1020
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Sus scrofa OX=9823 GN=OGT PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000255 0.999705 CS pos: 23-24. Pr: 0.9591

TMHMM  Annotations      help

There is no transmembrane helices in KAG6572510.1.