CAZyme Information: GAQ10567.1

Basic Information

• Species: Aspergillus lentulus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus lentulus
• CAZyme ID: GAQ10567.1
• CAZy Family: GH89
• CAZyme Description: ANK_REP_REGION domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A0S7E7I2]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1464		165231.55	5.7234

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AlentulusIFM54703	9916	N/A	259	9657

• Gene Location: location=BCLY01000016:1270528-1277001(+)

Full Sequence      

MHQTVRKFAHGDYTVGWICALPETEFVAAGAMLDEEHPVLPALHSQDSNSYLLETTGKVS
AATVAKDMLRSFPAVRFGLMVGIGGGAPYYGTQGYDNTEFGELEEEDSEDDLEDIRDIRL
GDVVVSLHSKSAEAVVQYDFGKSLQEKEFVHTGGKLNKPPAIVLSAVSVLQQQHRRKGYT
TSELLVDTLSKNPGMAEEFRYPGSAKDRLFKPDIVHLEGRKSCKACCGPNNVNLVRRTDR
HGTAPKIHYGTIGSADQVMEDAILRDKWAQKEKIICFEMEAAGLMDAFPCLVIRGICDYA
DSHKNKNWQPYAAATAASYAKELLLVIPGQGVMDLCPIKQSLGKIEANVDKMRSKLAREE
DHDLLNWITPDDYGPLQSDYFRRRQARTGEWLLNSMEFQMWLKRSRETLFCPGIPGAGKT
ILTSVVINYLTGRTSEDRSLGVAYVYCNFQRKDEHTADRLLSSLLKQLSERLPTIPGEYS
RVFILVDALDECRESENYRRRFLSEIFSLQARCGINIFATSRMNGEIEMLFANAIPLEIR
ATDHDVEIYLDERMRLQQLDILDDDTKNEIKRTVVDATGGMFLLAKLHIKSLLSLPTKGH
IKDALRNLAKGEQALDKIYNRTMERIEDQVRERRDLAKRILFWIFYARRPLSTEEIRHAL
AVKMQSAKLDKDYLPSTNLVRSLCLGLVTIDGESGMIRLVHYTTQEYFRRTQSRWFHDAE
LEIVKTCITYLSFNTLQTGFCSDDAEFETRLQSNVLYNYAARNWGHHAREASIRARQSNS
GLLNGAAKVSSLDQDMPTQRASVDLEAYSVLTEMVLEFLNSESNTSGSSQAMLVDEDYIG
FFNYSQNVPQRMTSMHLAAYFGLSDIVQMLIQNQHYPDTEDSYERTPLSWAAENGYEAAV
KILLNRGVAVDSRDLFYQTPLLWAARNGHEAVVKMLLDRDAARGVLLYYYYRTVGLSSRH
FESSHDLHDLLLHLNVDGMLALRRTILPYFCILFLLNIIYLYFYLHRERFSSPPQDQHSP
SRLWQQLHPLLEEYKPNCSQPVLRGSAGTQRFDAVKETGRPNYVSNVDEILLPMQAAHDG
FLHAIHSLKLDRAYTPGTTGIVSSAGGTYLPTFLVSLLLLRRTGSTLPVELFMKDRSEYE
ASICETVLPPLGVKCLVLSDILAGQDNLQSMEKIEGFQIKSFAMLFSSFESFLWLDADCV
PLYDPAVILDSEPFESTGLVTWPDFWANSAAPVYFNISRQPEPLSTTRQATEAGILAVSK
KTHFPTLLLAAYYNYYGPDYYYILLDQGAPGAGDKDTFLHAATALNETFYSVSEKPVDVG
NVAPWNAKVAINAGYIQADPIQDYNLTSQQKWRVKDPSVAKPPRAFFVHAGDPEFNPGND
LLGQKLVDSDGNPTRLWTHPPEAMERLGYDAERAFWEATVSVACDIRPAFESWKSKSGLC
EQVKEHWEAVFENPDVKVPVFAGS

Enzyme Prediction     

No EC number prediction in GAQ10567.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT71	1099	1324	2.5e-60	0.9356060606060606

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
402574	Mannosyl_trans3	1.30e-44	1100	1338	3	266	Mannosyltransferase putative. This family is conserved in fungi. Several members are annotated as being alpha-1,3-mannosyltransferase but this could not be confirmed.
293786	ANK	1.63e-22	853	941	4	92	ankyrin repeats. Ankyrin repeats are one of the most abundant repeat motifs, and generally function as scaffolds for protein-protein interactions in processes including cell cycle, transcriptional regulation, signal transduction, vesicular trafficking, and inflammatory response. Although predominantly found in eukaryotic proteins, they are also found in some bacterial and viral proteins. Less is known of their physiological roles in prokaryotes. Some bacterial ANK proteins play key roles in microbial pathogenesis by mimicking or manipulating host function(s). The pathogen Providencia alcalifaciens N-formyltransferase ankyrin repeats function in small molecule binding and allosteric control. Ankyrin-repeat proteins have been associated with a number of human diseases.
403870	Ank_2	2.87e-18	855	941	1	85	Ankyrin repeats (3 copies).
293786	ANK	4.67e-13	883	941	1	59	ankyrin repeats. Ankyrin repeats are one of the most abundant repeat motifs, and generally function as scaffolds for protein-protein interactions in processes including cell cycle, transcriptional regulation, signal transduction, vesicular trafficking, and inflammatory response. Although predominantly found in eukaryotic proteins, they are also found in some bacterial and viral proteins. Less is known of their physiological roles in prokaryotes. Some bacterial ANK proteins play key roles in microbial pathogenesis by mimicking or manipulating host function(s). The pathogen Providencia alcalifaciens N-formyltransferase ankyrin repeats function in small molecule binding and allosteric control. Ankyrin-repeat proteins have been associated with a number of human diseases.
223738	ANKYR	1.62e-12	831	939	86	202	Ankyrin repeat [Signal transduction mechanisms].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS22049.1|GT71	1.63e-249	979	1462	1	482
BCR89914.1|GT71	5.37e-172	1021	1461	46	492
QRD87247.1|GT71	3.71e-158	1023	1461	49	488
QMW26613.1|GT71	3.71e-158	1023	1461	49	488
QMW38692.1|GT71	3.71e-158	1023	1461	49	488

PDB Hits     

GAQ10567.1 has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q59KJ7|MNN21_CANAL	9.52e-56	1068	1446	217	648	Alpha-1,2-mannosyltransferase MNN21 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=MNN21 PE=3 SV=1
sp|Q5AD72|MNN24_CANAL	2.99e-46	1100	1448	294	704	Alpha-1,2-mannosyltransferase MNN24 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=MNN24 PE=3 SV=1
sp|Q5AP90|MNN23_CANAL	1.10e-37	1069	1312	144	424	Alpha-1,2-mannosyltransferase MNN23 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=MNN23 PE=3 SV=2
sp|Q5A687|MNN22_CANAL	1.64e-36	1078	1390	142	499	Alpha-1,2-mannosyltransferase MNN22 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=MNN22 PE=2 SV=1
sp|Q59WF4|MNN2_CANAL	3.24e-36	1097	1410	185	518	Alpha-1,2-mannosyltransferase MNN2 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=MNN2 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000068	0.000002

TMHMM  Annotations     

Start	End
986	1005
1098	1120