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CAZyme Information: FVEG_13550-t26_1-p1

You are here: Home > Sequence: FVEG_13550-t26_1-p1

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 Fusarium verticillioides
Lineage Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium verticillioides
CAZyme ID FVEG_13550-t26_1-p1
CAZy Family GT20
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1031 115081.04 5.9812
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Fverticillioides7600 16240 334819 371 15869
Gene Location Start: 2753799; End:2757209  Strand: +

Full Sequence      Download help

MIDMMDSGTS  RRSVSMSGAV  INGSIRHVTG  LSLGASTPVP  VVAIIGDKGS  GKTSLFEALS60
GLSLHGSRLS  STKFPIHAYF  THSNRTGTTL  RARIRPGKVD  GQNEELSDHL  QSFEVNYEGD120
LAAVNLPQIV  NQATNHMQIA  TAFSDEKEQE  EQQVSDNVLV  IEISGPDFFN  MEIVDTPGLS180
SSPAVDDTQE  VTRSLIMDLV  RQPNTLILSV  VDATSDMSTQ  EGPRLARAAD  VTGNRIVAAV240
TKCDLVPPEE  RRFVLRAMRN  KERHLGHPWF  AIRSLSSNER  DQDCTLETRN  SVEDAFFSEM300
EWSVLKRRRR  VGAPSLKDYL  KTRVNVLLRG  SIELLTTILN  TPSHSVAPSH  APSITEKVQQ360
TNIYAVSQET  VVADVDLEFA  SDAPRPTPLL  NAVGVGLTVA  ICLCLIGLGC  SSMAVEIASE420
GHWYRLFLLV  TAPPQVILSL  FFCQAIVVTI  FQMIGPVSQL  KVNSKFYSAK  RTKRLDGTKV480
LLPHVTIQCP  VYKEGLEGVI  RPTVQSLSAA  IRNYESFGGT  ASIFINDDGM  QLVSEEEAEE540
RRMFYKENNI  GWVARPGHNV  NGEGIKRFIR  RGKFKKASNM  NYALGISLKV  EDKLVQIDRH600
EKWTQVDEDA  AYQKCLDEVL  SEELGRAWVG  GNIRVGDYLL  LVDSDTRVPK  DCLIDAVSEL660
EASPQVAILQ  FTSGVMNVTT  SYFESGITFF  TNLIYTAITY  AVANGDVSPF  VGHNAFIRWS720
ALQEVGSQDG  GIINGEQDPN  ATTPYEKFWS  ESHVSEDFDI  SLRLQTLGYH  IRLGAYCGDG780
FKEGVSLTVY  DELARWEKYA  YGCSELLFWP  IKDWWRHGIF  TPLFKRFVMS  NMPLGSKITI840
MSYIGTYYAI  GYSWIGSLLN  YFLIGWLNGE  LDHYYMSSWR  VWVALVVVFS  IAGNITLALI900
RYRSQQVSLL  KELWTCFKWV  ALMFIFLGGI  SMHVCKAIMC  HMLSIDISWG  ATSKEVEDTN960
FFQEISIIIG  GFKYVFIFCL  AVTALMICGV  YAFPYLWRID  ELVAIFPLGT  VIFCHFFLPI1020
ALNPNLMKFT  W1031

Enzyme Prediction      help

No EC number prediction in FVEG_13550-t26_1-p1.

CAZyme Signature Domains help

Created with Snap511031542062573093604124635155676186707217738248769279791192GT2
Family Start End Evalue family coverage
GT2 638 863 1.8e-47 0.9695431472081218

CDD Domains      download full data without filtering help

Created with Snap5110315420625730936041246351556761867072177382487692797938320DLP_1638855Glyco_trans_2_342242Dynamin_N426957BcsA32246DYNc
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
206738 DLP_1 4.36e-47 38 320 2 265
Dynamin_like protein family includes dynamins and Mx proteins. The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes interferon-induced Mx proteins that inhibit a wide range of viruses by blocking an early stage of the replication cycle. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.
404513 Glyco_trans_2_3 2.51e-43 638 855 1 193
Glycosyl transferase family group 2. Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.
395279 Dynamin_N 4.26e-17 42 242 1 167
Dynamin family.
224136 BcsA 3.77e-16 426 957 1 427
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility].
197491 DYNc 4.11e-12 32 246 17 205
Dynamin, GTPase. Large GTPases that mediate vesicle trafficking. Dynamin participates in the endocytic uptake of receptors, associated ligands, and plasma membrane following an exocytic event.

CAZyme Hits      help

Created with Snap51103154206257309360412463515567618670721773824876927979161031CCT73007.1|GT0161031QGI99503.1|GT0161031QGI68613.1|GT01371031QKD62182.1|GT03701031QGI85813.1|GT0
Hit ID E-Value Query Start Query End Hit Start Hit End
CCT73007.1|GT0 0.0 16 1031 1 1016
QGI99503.1|GT0 0.0 16 1031 1 1034
QGI68613.1|GT0 0.0 16 1031 1 1034
QKD62182.1|GT0 0.0 137 1031 1 912
QGI85813.1|GT0 0.0 370 1031 5 642

PDB Hits      download full data without filtering help

Created with Snap51103154206257309360412463515567618670721773824876927979393354P4S_A393634P4T_A393634P4U_A393354P4S_B393355UOT_0
Hit ID E-Value Query Start Query End Hit Start Hit End Description
4P4S_A 1.21e-13 39 335 13 285
GMPPCP-bound stalkless-MxA [Homo sapiens]
4P4T_A 1.63e-13 39 363 34 326
GDP-bound stalkless-MxA [Homo sapiens]
4P4U_A 1.68e-13 39 363 34 326
Nucleotide-free stalkless-MxA [Homo sapiens]
4P4S_B 1.93e-13 39 335 28 300
GMPPCP-bound stalkless-MxA [Homo sapiens]
5UOT_0 1.05e-12 39 335 26 297
CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_1 CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_2 CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_3 CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_4 CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_5 CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_6 CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_7 CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_8 CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_9 CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_A CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_B CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_C CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_D CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_E CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_F CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_G CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_H CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_I CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_J CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_K CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_L CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_M CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_N CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_O CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_P CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_Q CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_R CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_S CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_T CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_U CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_V CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_W CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_X CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_Y CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_Z CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_a CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_b CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_c CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_d CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_e CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_f CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_g CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_h CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_i CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_j CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_k CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_l CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_m CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_n CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_o CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_p CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_q CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_r CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_s CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_t CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_u CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_v CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_w CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_x CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_y CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_z CryoEM structure of the helical assembly of full length MxB [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Created with Snap5110315420625730936041246351556761867072177382487692797939347sp|P18588|MX1_RAT39347sp|P09922|MX1B_MOUSE39335sp|A7VK00|MX2_PIG39320sp|Q6PW23|MX_EPICO39320sp|Q4U4N4|MX2_ICTPU
Hit ID E-Value Query Start Query End Hit Start Hit End Description
sp|P18588|MX1_RAT 5.80e-15 39 347 61 344
Interferon-induced GTP-binding protein Mx1 OS=Rattus norvegicus OX=10116 GN=Mx1 PE=1 SV=1
sp|P09922|MX1B_MOUSE 2.22e-14 39 347 36 320
Interferon-induced GTP-binding protein Mx1 OS=Mus musculus OX=10090 GN=Mx1 PE=1 SV=1
sp|A7VK00|MX2_PIG 2.51e-14 39 335 115 385
Interferon-induced GTP-binding protein Mx2 OS=Sus scrofa OX=9823 GN=MX2 PE=2 SV=1
sp|Q6PW23|MX_EPICO 1.15e-13 39 320 33 290
Interferon-induced GTP-binding protein Mx OS=Epinephelus coioides OX=94232 GN=mx PE=2 SV=1
sp|Q4U4N4|MX2_ICTPU 1.51e-13 39 320 32 289
Interferon-induced GTP-binding protein Mx2 OS=Ictalurus punctatus OX=7998 GN=mx2 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000046 0.000000

TMHMM  Annotations      download full data without filtering help

Start End
392 414
426 448
843 865
878 900
913 935
975 997
1002 1024