Q750Z6

PR
Gene name
AGL209W
Protein name
Vacuolar membrane protease
Names
FXNA-related family protease 1
Species
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
KEGG Pathway
ago:AGOS_AGL209W
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

518-604 (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 Q750Z6

Entry ID Method Resolution Chain Position Source
AF-Q750Z6-F1 Predicted AlphaFoldDB

No variants for Q750Z6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q750Z6

No associated diseases with Q750Z6

2 regional properties for Q750Z6

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 42 - 52 IPR001412
domain RNA-binding S4 domain 336 - 398 IPR002942

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
fungal-type vacuole membrane The lipid bilayer surrounding a vacuole, the shape of which correlates with cell cycle phase. The membrane separates its contents from the cytoplasm of the cell. An example of this structure is found in Saccharomyces cerevisiae.
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.

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
MKLTKAVFRF RRTNLSTLLV ITYLVITTLY VWDHFRYHFT LPSDYNYAQM LADAWLDLEI
70 80 90 100 110 120
ITQYPHPYAS HANDKVHDYL LDRVKEITRD SMFAEISDDY GMGLRTLFRQ EDAISGTKES
130 140 150 160 170 180
TVVYYESSNV LARVQGRNSA LDGLLLSAHY DSVPSGYGAT DDGMGVVSML AILTHYVKNQ
190 200 210 220 230 240
PERTLVFNFN NNQEFGLAGA SAFFEHPWSK EISYVINLEG TGAGGKAVLF RTSDVSTAQV
250 260 270 280 290 300
YAEAVRQQPF GNSMYQQGFY NGHIGTETDF QVYEDQGLRG WDIAFYRPRN LYHTAKDTVL
310 320 330 340 350 360
YTSKQALWHM LHTALQLTDY MAINKPDMED TSNAVYFDLF GKWFVVWSAR SLFYWNCIIL
370 380 390 400 410 420
ALFPSILAIL FLVAYDMQLL KFNFWDAMLR LPVSVCLAYF CVKLFQVLVG QLNPYVFSRD
430 440 450 460 470 480
YVSPILAEAS MFIFMNYVIL SSWERLRPLR DFKTVALVEV SMVLWIYLIS VTRWLRDSDY
490 500 510 520 530 540
TATGLYPFTI GYTFVSIGAI IGVFCATFKA KLNPEDDSYV GDSKVDIEQQ QMLMQHQYQQ
550 560 570 580 590 600
HSQKHSNQHS PHHSTHHSAQ HSVHHSPRQS IHQVPSSEQR QRDASETPHV IISVDHTAGH
610 620 630 640 650 660
QEDSEVTPLL NTGTVAPFPK PVPERVSRKS FLRNVVTSIL NYDWSIQFMV VTPWVTYFTW
670 680 690 700 710 720
ICLDLIMGAM NQTIQESAKG TTFVTHMALI GSLLLSLPML PFTYKLHSFA GMLFLLLAVT
730 740 750 760 770 780
TAVWTIVAPP FTESSPLKLR FLQTIDLDKN NSSSVYLYGR ERTFMEPILD DIPSVTKYRC
790 800 810 820 830 840
VEYAGDGVDI CEYNGMPPRM FNNHHEAESD WTKIMTLEIL KDDRNSTSRT PYQPITAELK
850 860 870 880 890 900
INVEENRVCT LNFNSTAFKN WKQGVSPLRE VVILHENPSS NVTPSFYNTA MKNGYYQDEF
910 920 930 940 950 960
GNDHYRWNNG ITELQLHKLD FKRGYYKIGL EWIPQLLYRG YDPATSSSEE DDALGVSVTC
970 980 990 1000 1010
YWGEYDTDSI TDGFATTNVP AYDELRKYSP KNIIYSSKEK GMVSVTKYVE L