CAZyme Information: FOIG_11302-t36_1-p1

Basic Information

• Species: Fusarium odoratissimum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium odoratissimum
• CAZyme ID: FOIG_11302-t36_1-p1
• CAZy Family: PL1
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1926		216060.30	6.9034

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FodoratissimumNRRL54006	16975	1089451	341	16634

• Gene Location: location=JH658291.1:350274-357040(-)

Full Sequence      

MTRKNVLHGVFLRPSRRVRVFAFLFFFVAATWTFTIKSRSTCSVEEDIARDYPLIYRHVH
SFNGTGGAWHIPPYWADMHSKQPHNILDAARIASKAALSKRERQMPFSNIPLLVHQTWKK
TAADSWNPRILPWVELWLEDSIYIDRGPSMAYLFWDDTGMRALVEEFENDFLERYDTLLT
PVERSDVFRILVCKHFGGIYGDLDTELIQHPATWISGSDMATWTDPKTGKAHGYYNTSVT
PDYETPVVSLLWGLEADNDPESDAYWRQSYTYPQQLSQWAFAAAPQHPVFERYMDNLRNY
TKDNEPTAQNSDPLKRTGPAAVTLATKSWLEDHVGFRWASLTGLKDGGKSKLVHDILILP
ITGFHPSHGSRNGVMGRKPITDPAARLCHHGTGLWKHFNFVGEYGKRQPKLQLNREYNGR
SKMAEALGIASGAAGLLSLAIEVTKLSYTYIASVRGAPKSLTSYIGELATLTSVLLQLDD
LIQARRVNSQNSQILSKALNDCKQEVEHLKAKLERKVSYGRIKAKVAALAWPLSESELQD
KVNMLHRYNGIFSSALQADSLTVAIATNKELQDFRHSTEAKEIIAWYKSDVAIEVSTSHL
EDYCPSTWQTFLSGSFYQSWRSGSTPVVWGYGKPGAGKTVLAALVLRDVKSGNLPGTAIA
SHFFSSSRTKESVSNVLRSLIAQTLRGCPVIPQEALALYEKGSQNLMITDLINVLGAIAK
SMTTCIILDALDECPFLPKLFNILLTLQELGVRIFATARDLPKIRKHFEKKPRVKISATR
QDLDFYVNHRLEHGEVDVESIGTELKSDLVSAIVKMAAGSFLLARLIMDHITSLLTIKDI
RKALISLPANYDEAYLSTFDRIIKQTPGLKDLALKSLNFISYVKEPLRIVELQHALATEE
GMLEIDPEDLQTSKAIISSCLGLLVVSGPEMTVEFVHSTARQFLQRRPEGMDKHPHLTIV
RSCISYMSTNEMRQGRCTSHEDITQRCLKQPFLHYAANFYGYHAQEVEEECFDQLSEFLQ
DDVVRESSWQLLNFKAHLDTSVSESVFDSSPRNVLALHVAAFWGFKTYIDKSLSYTRRGT
PSTQKQNLNKTDSHGWTPLHWAVSMGHKSMVEILLRSGASPDLPDLAGWTPTFWAAFKGH
ADIIEMLWRYDTAPFRCDIKGLTPLHWAVSAGQTEIIKRLLKLKTRFGQYQKSPVLSLPS
LDDLTVARARALANKANESPFKFYSEGTDIEMFSAIFNALKHSFRDKENKPRERCEGYYT
FDPFLYGPFGQSLKADHGRRARPDRDYKWGKPDVGFFEFVDQLLIHATRSQDLPIIKLVL
DLKLIKASGIDNIALLHEAAASGWAEGMSALIALGADVNNGDTRYGQTPLHRACQNQREE
AIKLLLAIDKIEINAQAKNGRTPIMDLMTASYKEKGVDLYKLMIARGASISIKDTEGNSL
MHFAMRTCNTTIVQMLCTAGLSIESPNKSGQLPLHWMAHWNYFEFRKSVTADEAESIREQ
RHECMKLVFELSSPSSLDSVCDWENGATPSKETPLSLALSRNNWDLAAKLLRHIKQPGNT
SFFGDAKTHTIHELCTVCERLASVSMPSSHNPTILYYELQPLPLDDWTHLLQLFLDAGAD
INEVNWKGDTPLQLCVQRAASIPVIDTLLKLGGNPYQANRDGLDCFQLALLHYDEAGSSE
IMRCIRTYANTHPEPAHYFCQGGFLIAPDTPIDNEETRYLQVLRQTNAINCETRSGRTLI
YEAASRGSTHLVQGLLDHDAYPHYIDDFGSSALHAAAMQQAPTTVAVLLQVGADVHQVSL
ARGTPLHACLEAFNNSTISSEAVEVVRILLSYGTDPNHAVVRDDRTETSLSLPLKALCQS
IYFPHLDRATPEDSDRLVLEVLKLLVDAGARVADSADDIIVGVVAKMEGYELLWEEMRSQ
LMTSRS

Enzyme Prediction     

No EC number prediction in FOIG_11302-t36_1-p1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
293786	ANK	1.44e-25	1094	1182	1	89	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.
293786	ANK	2.72e-19	1087	1147	27	87	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	8.20e-18	1099	1182	1	82	Ankyrin repeats (3 copies).
293786	ANK	9.87e-18	1336	1434	6	98	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.
226297	OCH1	6.53e-16	110	365	82	304	Mannosyltransferase OCH1 or related enzyme [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGI99627.1|GT32	0.0	160	1400	1	1207
QGI68738.1|GT32	0.0	160	1400	1	1069
QGI85929.1|GT32	0.0	160	1400	1	1069
CCT73207.1|GT32	1.39e-250	1	408	1	406
QPC63324.1|GT32	9.79e-213	1	406	1	406

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6V9V_A	2.89e-09	1336	1789	67	534	Structure of TRPA1 modified by Bodipy-iodoacetamide with bound calcium, LMNG [Homo sapiens],6V9V_B Structure of TRPA1 modified by Bodipy-iodoacetamide with bound calcium, LMNG [Homo sapiens],6V9V_C Structure of TRPA1 modified by Bodipy-iodoacetamide with bound calcium, LMNG [Homo sapiens],6V9V_D Structure of TRPA1 modified by Bodipy-iodoacetamide with bound calcium, LMNG [Homo sapiens],6V9W_A Structure of TRPA1 (ligand-free) with bound calcium, LMNG [Homo sapiens],6V9W_B Structure of TRPA1 (ligand-free) with bound calcium, LMNG [Homo sapiens],6V9W_C Structure of TRPA1 (ligand-free) with bound calcium, LMNG [Homo sapiens],6V9W_D Structure of TRPA1 (ligand-free) with bound calcium, LMNG [Homo sapiens],6V9Y_A Structure of TRPA1 bound with A-967079, PMAL-C8 [Homo sapiens],6V9Y_B Structure of TRPA1 bound with A-967079, PMAL-C8 [Homo sapiens],6V9Y_C Structure of TRPA1 bound with A-967079, PMAL-C8 [Homo sapiens],6V9Y_D Structure of TRPA1 bound with A-967079, PMAL-C8 [Homo sapiens]
6V9X_A	2.89e-09	1336	1789	67	534	Structure of TRPA1 modified by iodoacetamide, PMAL-C8 [Homo sapiens],6V9X_B Structure of TRPA1 modified by iodoacetamide, PMAL-C8 [Homo sapiens],6V9X_C Structure of TRPA1 modified by iodoacetamide, PMAL-C8 [Homo sapiens],6V9X_D Structure of TRPA1 modified by iodoacetamide, PMAL-C8 [Homo sapiens]
6PQO_A	2.92e-09	1336	1789	68	535	Cryo-EM structure of the human TRPA1 ion channel in complex with the covalent agonist JT010 [Homo sapiens],6PQO_B Cryo-EM structure of the human TRPA1 ion channel in complex with the covalent agonist JT010 [Homo sapiens],6PQO_C Cryo-EM structure of the human TRPA1 ion channel in complex with the covalent agonist JT010 [Homo sapiens],6PQO_D Cryo-EM structure of the human TRPA1 ion channel in complex with the covalent agonist JT010 [Homo sapiens],6PQP_A Cryo-EM structure of the human TRPA1 ion channel in complex with the covalent agonist BITC [Homo sapiens],6PQP_B Cryo-EM structure of the human TRPA1 ion channel in complex with the covalent agonist BITC [Homo sapiens],6PQP_C Cryo-EM structure of the human TRPA1 ion channel in complex with the covalent agonist BITC [Homo sapiens],6PQP_D Cryo-EM structure of the human TRPA1 ion channel in complex with the covalent agonist BITC [Homo sapiens]
6PQQ_A	2.92e-09	1336	1789	68	535	Cryo-EM structure of human TRPA1 C621S mutant in the apo state [Homo sapiens],6PQQ_B Cryo-EM structure of human TRPA1 C621S mutant in the apo state [Homo sapiens],6PQQ_C Cryo-EM structure of human TRPA1 C621S mutant in the apo state [Homo sapiens],6PQQ_D Cryo-EM structure of human TRPA1 C621S mutant in the apo state [Homo sapiens]
3J9P_A	3.13e-09	1336	1789	476	943	Structure of the TRPA1 ion channel determined by electron cryo-microscopy [unidentified],3J9P_B Structure of the TRPA1 ion channel determined by electron cryo-microscopy [unidentified],3J9P_C Structure of the TRPA1 ion channel determined by electron cryo-microscopy [unidentified],3J9P_D Structure of the TRPA1 ion channel determined by electron cryo-microscopy [unidentified]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q10323|IMT3_SCHPO	9.39e-09	110	234	57	178	Inositol phosphoceramide mannosyltransferase 3 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPAC17G8.11c PE=1 SV=1
sp|O75762|TRPA1_HUMAN	1.49e-08	1336	1789	67	534	Transient receptor potential cation channel subfamily A member 1 OS=Homo sapiens OX=9606 GN=TRPA1 PE=1 SV=3
sp|Q9Z148|EHMT2_MOUSE	5.15e-07	1386	1482	824	916	Histone-lysine N-methyltransferase EHMT2 OS=Mus musculus OX=10090 GN=Ehmt2 PE=1 SV=2
sp|Q96KQ7|EHMT2_HUMAN	1.50e-06	1386	1482	771	863	Histone-lysine N-methyltransferase EHMT2 OS=Homo sapiens OX=9606 GN=EHMT2 PE=1 SV=3
sp|P38287|CSH1_YEAST	2.21e-06	104	204	56	147	Mannosyl phosphorylinositol ceramide synthase CSH1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=CSH1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.979536	0.020501

TMHMM  Annotations     

Start	End
20	36