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 B2B585

Entry ID Method Resolution Chain Position Source
AF-B2B585-F1 Predicted AlphaFoldDB

No variants for B2B585

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B2B585

No associated diseases with B2B585

1 regional properties for B2B585

Type Name Position InterPro Accession
domain Peptidase M28 165 - 343 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
MINPISFRPG PVTFWTTLVY LALLIPIVII NETVPPAPAA ADDGKIEGVN LTEAWLDLTR
70 80 90 100 110 120
ITRGYHPYNS RFNEEVRGYL LGRVGEILEG SGVGGKKGNV TVFDDLRSNV TGLMAGSVVP
130 140 150 160 170 180
TPGSAQVAAY FEGTNILVYV RGKGDDEGDW WRRSAEGGEM EGVRKNERGL VLVNAHYDSV
190 200 210 220 230 240
STGYGATDDG MGVVTCLQVI KYFAHPDHQP ERGIVVMLNN GEEDYLYGAR ALGQHPLNPY
250 260 270 280 290 300
IHTFLNLEGA GAGGRANLFR TTDREVTAAY AGTSDPFGTV IASDAFGLGF IRSGTDYSVL
310 320 330 340 350 360
YDVYGQRGLD LAFFKPRSRY HTNRDDATHT SKASLWHMLS AAIHTASKLS GDTGDTFVGA
370 380 390 400 410 420
RPDGARNKVR NGSPSNGVWF DLFGKGFVNF GLRGMFAWSL TVLVATPLIL VLATYILHKL
430 440 450 460 470 480
DKYYFFTSSV RTYDQPDFEP VLVGGWKGAF RFPFAFIVSG ALSLAVAFLM RKVNPFIIYS
490 500 510 520 530 540
HRYSVIAMIF SLFYFTFWSI MRGANFARPS ALHRGYVNIW LFILGWATLV AVTVTEDRFK
550 560 570 580 590 600
LGAGYPIVFL QTAVCLTTFL TLCELFALPK KTAWGQQVRE DHEVHDYYQP QSGNNNTRTE
610 620 630 640 650 660
SPPPLPQIPH QPSLVPPATR DSNASTLRQG DGNDTDDEDA AVPTERTPLV GGGNATSEHF
670 680 690 700 710 720
RTTFATTYRR SITALVNGAR KYGQDGDEPF EHEQAWSGRL PSWLWFFQFL ILGPFTIILA
730 740 750 760 770 780
AQTGLMLVDA VHQTGADGSN LLLPYLIVFA FTVLVLLPIT PVIHRISHHI PVFLLVVFVG
790 800 810 820 830 840
TLIYNLVAFP FSEESRYKVY FVQQIDLDTA DNRVCYNGVD EYVHKIIAEL PSASGRNVTC
850 860 870 880 890 900
GESKRAELVS CCYDGVDVAP RLGSETPEED TPIEEIYKSL ATVTATRGEG NKAQLEIEAD
910 920 930 940 950 960
NTKACFLEFK QPISGFNVQG GSEWDDRFGQ FPEGGIKQLK LWHRQRGERW VVDVEWKDAE
970 980 990 1000 1010
KLEGQVVCAW SDANEAGTIP ALDEGLRYSP VWAAITKFAE GLVEGRKGFS V