A4R254

PR
Gene name
MGG_06752
Protein name
Vacuolar membrane protease
Names
FXNA-related family protease 1
Species
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae)
KEGG Pathway
mgr:MGG_06752
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

549-653 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for A4R254

Entry ID Method Resolution Chain Position Source
AF-A4R254-F1 Predicted AlphaFoldDB

No variants for A4R254

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A4R254

No associated diseases with A4R254

2 regional properties for A4R254

Type Name Position InterPro Accession
domain Glycosyl transferase, family 28, C-terminal 372 - 437 IPR007235
domain Diacylglycerol glucosyltransferase, N-terminal 144 - 312 IPR009695

Functions

Description
EC Number
Subcellular Localization
  • Vacuole membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
vacuolar membrane The lipid bilayer surrounding the vacuole and separating its contents from the cytoplasm of the cell.

2 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
metalloexopeptidase activity Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.

1 GO annotations of biological process

Name Definition
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSNPFAFRSA QVTFWTTVVY LALLVPLVVI NEGVPPVQPD GSLFLDRGLN LTEAWLDLGH
70 80 90 100 110 120
ITERFHHQNS RENDVVRDYL RLRIEQIIAA NDAEARTTVF NDLTSNVTYL AWGSAVPTHY
130 140 150 160 170 180
QGNNLYVYIR GKDDDQGEWW HNARAGKLIG KGGVLVNAHF DSVSTAYGAT DDGMGTVTVL
190 200 210 220 230 240
QMIRYFTKPG NQPQRGIVAL LNNAEEPGLL GAAAFGKSPL LPFIHTFLNL EGAGAGSRCV
250 260 270 280 290 300
LFRSTDREVT SAFSNVQSPF GSVVGSDGFK MGLVRSGTDY SVWHDIYGQR GLDLAFYRPR
310 320 330 340 350 360
ALYHTNQDDT KHTSRESLWQ MMAASTTTLI NLSADTGSDY IGDRPDGDRS KAPNGSPSDG
370 380 390 400 410 420
VWFDLFGSTF VLFGLRGMFA WSLTVLIVGP LTLFGMMYLV HKQGKGYAFH TKLRATSDSS
430 440 450 460 470 480
SEDGDDEDGE VIRLGGWKGF FRFPFALIVA GALVTGAALL LRKMNPFIIY SSEYAVWAMM
490 500 510 520 530 540
ISLFYFGFWL IMRGSSYTRP SALHRLYVHI WLFILGWVAL VFATVLEDRM RIASGYIFVF
550 560 570 580 590 600
WESQVFLATL VAVCELFSLP RKIDFARGAA EEAEVRDHLE AVPHSDAVIA PSLEEATSPQ
610 620 630 640 650 660
RAGQSSNSPQ EDDEDDVPDE ETPLFRKAGR GNKLDTSFLR RGYRRSVSAI MDSNNEAEDG
670 680 690 700 710 720
PKRKQPFEGE QAWSGPMVTS TWILQFLLLG PFMVILGGQV GLLLTSAVNQ TGVDGSSLLA
730 740 750 760 770 780
PYLMIAALSA ILLMPLSPFI HRVTKHVPLF LLAVAFATLI YSLVAFPFSP RAPYKTFFRQ
790 800 810 820 830 840
TVDLDTGDTQ VHLAGVEQYL RKIIADVPSA LGQEIACDAS SSRRDLVDCT YDAAQVPPIP
850 860 870 880 890 900
TYGSGKKSFD LPPGVSPGPA YYGKLLTVTV VNTTAKIATQ GSKTARLKID AVDTRVVELR
910 920 930 940 950 960
FSKEGPPIRS FRVVGADSWD DRFGAFPDDG ARVLRLWRRD WESSFVVDIT WKVDGGNTRG
970 980 990 1000 1010
LEGRAVALWS DANDAVNTMP AFREVVRYAP AWATVSKAAP GLVEGSKAFK V