CAZyme Information: Afu1g03380-T-p1

Basic Information

• Species: Aspergillus fumigatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fumigatus
• CAZyme ID: Afu1g03380-T-p1
• CAZy Family: GT90
• CAZyme Description: Ortholog of A. nidulans FGSC A4 : AN0265, A. niger CBS 513.88 : An01g04760, A. oryzae RIB40 : AO090005000763, Aspergillus wentii : Aspwe1_0049645 and Aspergillus sydowii : Aspsy1_0027812

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1660		182803.69	8.0515

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AfumigatusAf293	10130	330879	290	9840

• Gene Location: location=Chr1_A_fumigatus_Af293:978458-983547(-)

Full Sequence      

MLPSVASFPSVQPHHHLHPYYTADTATPPYDSNSTSFAPSLPGSDINKDHSQSFSRTRLQ
YPHPVQRFGLHDTASPQPSPKHAAEHALRRKTPNGTLAAGYDGTPGDTTIQPPATKHILV
SPLDSGHLVPPQTGFVSDNWQQASLDQSSAAKHVVFPPVFKNDASRGNIAPGDMVTDVNG
TGWVRSLNYIPGADSMLNQSLPMQSAQQRFYVQNGAYVPTVLPATLQPCLGPTASAGSGP
YGPYWPDGVYIPYRPAAFRDTRFNHLNQTGLPFFDAAQQSFNNANTALPGSHGEAGGWST
APPGILSHGTAVKGNFPPRHSEQKSLDSSLNHRVLPLHIRTNPSTGFSTNQGGESFSVLP
ASNGPGLPGAFPSAHSRAANVEFKEKILSWAHGVYVDLLASIHQARRNSISQAGSDGQPL
RLKPSIYPKPPRQPGLDFSQSNSPEFHRHNSYPSSHYDGRHQKTNILGYSRPVDTTATFQ
HSRRPSMGQFQQYATSDSQMLDRLRHTGRVTVPGPAPRLSFSATGENSTTANAMSALEML
SHLCMESGWEWIDGMLLGGCLAYGLGDYPKAMRWYSRIIARDATHVEAISNLAATLLALD
RREEAMQHWLRAVKLRPSFFEAVEHLIGLLCSSQRGKEAVNIIDYVQNSLRFPKNGDCFA
TDEHASETESDADSGASSVGSYEKASFDYDDDFGRSLTGNQKPSEASAVGFGSSGYAIPG
CDNGRMLALVHAKGNMLYALGDNAGAAAAFEDAVLIAAGRRRHGIQSLIKQIYTAFSQGS
HQAYSPLNSHESQEIILLYPDKALQTSKLVFAPCGTPPGIKFVAEGLARKAALSTTSNSL
LSLAKIYQDGMSNISGSGIPKKSPGVRDILALYYLSLSLQPSPSTANNVGILLAGIQNNA
AGKSLPRSSGEAQHPEVPGVVPGSGISLALAYYNYGLHLDSRHAHLYTNLGSLLKDIGQL
QAAIRMYEQAVQCDGNFDIALANLANAVKDAGRVNDAITYYKRAVKVNPEFAEAVCGLAN
ALNSVCNWVGRGGIANGYGFRDRWHVTEQGMLRDASTSETGSGWIQRVVDIVNRQLKEGE
SWGLGLLSPNTIEQLCVQIAPALESRRSACGSLATILQSWAGQRWEGSRIVKLIERANRS
ITWQWYQDRYIYGKEYPLTKYQRPQLPSGLTVPNAPTVLPFHTFTCPLSAKQIRQISQRN
GLRISCSTLRSPWLPATVYPPPPPPNPYLKVGYVSSDFNNHPLAHLMQSVFGLHNPSRVK
AYCYATTASDKSVHRQQIEKEAPVFHDASCWPIERLVKQIVDDGIHILVNLNGYTRGARN
EVFAARPAPIHMSFMGFAGTLGAEWCDYILADEISIPVDTLGPGRRNARIEDRLLEQDHG
EELEDWVYGEKIVYTRDTFFCCDHRQSAPDAKDARITWEQEQERRWRMRKELFPNLSDDT
IILGNFNQLYKIEPTTFRTWLRILARIPNAVLWLLRFPDLGEQNLRETAIAWAGRETASR
IIFTDVAPKNAHISRAKILDLFLDTPECNAHTTATDVLWSGTPLLTYPRYKYKMCSRMAS
SILSSALPDSDAGRKARDELTAVSDEDYEDKAIRLCLSLRYNPGCGGRASGRLFDLRRML
FEERMGSRLFDTKRWVRDLENAYDQVWKRWVNGEEGDIWL

Enzyme Prediction     

No EC number prediction in Afu1g03380-T-p1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
404688	Glyco_transf_41	9.02e-102	1176	1639	28	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.
226428	Spy	1.81e-57	1229	1649	260	617	Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones].
276809	TPR	3.54e-14	929	1006	20	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	4.18e-14	944	1022	1	79	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	2.02e-10	559	641	8	90	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRD87816.1|GT41	0.0	1	1660	1	1668
QMW26123.1|GT41	0.0	1	1660	1	1668
QMW38206.1|GT41	0.0	1	1660	1	1668
UCK58648.1|GT41	0.0	1	1660	1	1668
BCS08203.1|GT41	0.0	1	1660	1	1670

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A01_A	3.75e-75	1229	1657	235	705	O-GlcNAc transferase from Drososphila melanogaster [Drosophila melanogaster],5A01_B O-GlcNAc transferase from Drososphila melanogaster [Drosophila melanogaster],5A01_C O-GlcNAc transferase from Drososphila melanogaster [Drosophila melanogaster]
5NPR_A	1.17e-73	1176	1657	179	710	The human O-GlcNAc transferase in complex with a thiol-linked bisubstrate inhibitor [Homo sapiens]
5NPS_A	1.19e-73	1176	1657	180	711	The human O-GlcNAc transferase in complex with a bisubstrate inhibitor [Homo sapiens]
3PE3_A	1.32e-73	1176	1657	185	716	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	1.43e-73	1176	1657	184	715	Chain AAA, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9M8Y0|SEC_ARATH	6.62e-85	1176	1655	535	960	Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SEC OS=Arabidopsis thaliana OX=3702 GN=SEC PE=1 SV=1
sp|Q8CGY8|OGT1_MOUSE	2.73e-71	1176	1657	503	1034	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Mus musculus OX=10090 GN=Ogt PE=1 SV=2
sp|P81436|OGT1_RABIT	6.48e-71	1176	1657	503	1034	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Oryctolagus cuniculus OX=9986 GN=OGT PE=1 SV=2
sp|O15294|OGT1_HUMAN	8.64e-71	1176	1657	503	1034	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Homo sapiens OX=9606 GN=OGT PE=1 SV=3
sp|Q27HV0|OGT1_PIG	2.05e-70	1176	1657	503	1034	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit OS=Sus scrofa OX=9823 GN=OGT PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000042	0.000010

TMHMM  Annotations     

There is no transmembrane helices in Afu1g03380-T-p1.