Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q6BMD6

Entry ID Method Resolution Chain Position Source
AF-Q6BMD6-F1 Predicted AlphaFoldDB

No variants for Q6BMD6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6BMD6

No associated diseases with Q6BMD6

1 regional properties for Q6BMD6

Type Name Position InterPro Accession
domain Peptidase M28 171 - 361 IPR007484

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
MAETESGTGN SPSHRLSETS NASGNRSHQQ SKQIASYKSS KPNVFIRFIR AIFGYRKTSV
70 80 90 100 110 120
TLFVFITIIA TLILVELSNS LDFSVKLPTN NLERTILDNS WLDLQKIGKE EHPYTSKGND
130 140 150 160 170 180
YVHDYLEAKI TELIGKSLFI ECDNDVNYTN NIIFKTENDL YNQVTYYESN NLLVRINGSD
190 200 210 220 230 240
SSLPALLVSA HFDSVPSSFG VTDDGMGIAS LLGILNYYSS DGIDQPMRTI ILNFNNNEEF
250 260 270 280 290 300
GLMGATSFLH HPWFKQVRYF LNLEGTGAGG KAVLFRGTDY GIVKYFKHVR YPFGTSLFQQ
310 320 330 340 350 360
GFNNHLIHSE TDYKIYKENG GIRGIDLAFY KPRDIYHTAS DSIKNIDIKS LWHMLSNSLD
370 380 390 400 410 420
FVEIVSSQRI DLDDEDTSPE SDEKSREFAI FSSFFNWFFV IPASQLVLIN VTCLAVIPLI
430 440 450 460 470 480
SLPLLVIIFN YKKNWHIGFI NAIKFPVSLV LSICILNIIT HNVIASINEF LPNSSYDSIV
490 500 510 520 530 540
STLYSLFLLL NYLFLNGINF IFKGYKGLYH DEKLILIIQT SFIYWVLLIV STNKLSKNKI
550 560 570 580 590 600
GNDHTGEFPL IMLFLLQSIG ALFGLFSWSF KKTTPDELRN NDDEACQALL SREEHNNYGS
610 620 630 640 650 660
NEAELESGEP ISSNSSVSLN SSSSQVTNNL VKNLRKSFSY DWSIQYVVIV PLSSLIVYNT
670 680 690 700 710 720
GSLLLSGLNK SIQESLNAEK LIFDLIQLVA VTLAIPFLPF IFKINRLLVT ALVLVFCSGF
730 740 750 760 770 780
ISIFLKSPFD QLNPLKLRFV QSINLDESSD ISVVNVFGRY GSPMNNVLLD LPSLKETNES
790 800 810 820 830 840
LECNNLQDGM QLCSYKTLLS PNLSPDVTDF NDYLDVQVLK NSSSDYPYGL LSGEIKINVP
850 860 870 880 890 900
ENRVCRLSFN NSNFENSKQS LVRTILVYED NNYENSSNKL FPFEVSEFQL ANLPEGFSRD
910 920 930 940 950 960
KKGTYIYKNL NGIDKLELNK LSWDKPYHVG FQWMPKFVDS VSAENENTNV PYTTDFNNLG
970 980 990 1000 1010
IQVECFWGNL GYANNENKSE DERIPAYGEV LHYSPNYVSW ANKESGLVSV SKYVEI