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 C5DDZ2

Entry ID Method Resolution Chain Position Source
AF-C5DDZ2-F1 Predicted AlphaFoldDB

No variants for C5DDZ2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for C5DDZ2

No associated diseases with C5DDZ2

1 regional properties for C5DDZ2

Type Name Position InterPro Accession
domain Peptidase M28 133 - 320 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
MLAQFLRSLF RFRKTTVSVL LVATYVVVFL LNVWDRIRYQ YSLPEDNKHH KQLLDASWID
70 80 90 100 110 120
LQSITRKPHP YTSRENDAVH DFLLHRVTEL VEGAPHAEVS DDYKEGNHLV FKQPDVFNSS
130 140 150 160 170 180
STESRIVSFE SSNIVVKITG SQPELPGLLI SAHFDSVPTA LGATDDGVGI VTLLALITRY
190 200 210 220 230 240
AKKQPRRTLV FNLNNNEEFG LLGASAFLNH RWRPLVDYVL NLEGTGAGGK AVLFRTSDTN
250 260 270 280 290 300
TASIYKNAVK TQPFGNSIYQ QAFYDRYISS ETDYKVYEQA GLRGWDIAFY KPRALYHTIK
310 320 330 340 350 360
DSTQFTSQAS LWNMMHASLQ LADFIAFESF EDEPKDRSPA VYFDIIGTFF VTASTKDLFT
370 380 390 400 410 420
LNCVVLSVIP VIILVLEFVI QRRKTRERNP LLVWLRLPFS MFISYLVTAT FRSSLFRVNP
430 440 450 460 470 480
LIFSRDYVSP TIGFSFTFLI LNYLVLSLLE YLAPSRDLKT VSFVELFFGM WIALLWATIR
490 500 510 520 530 540
LCTSKYTATG VYPITVLYLL MSFGAIVGLV CSAFKRKHSV VKAKDSEETA APNTYSSIEE
550 560 570 580 590 600
SPQQATNTEA PNENSPEEHD ERAPLLRASN SSQVSSVTNV SEAPSSALKA FVVSALNYDW
610 620 630 640 650 660
SVQFLAVVPL ASFFVIMCLS LILDGIYQTC QEGFQATWNV SKISMLGGML LAIPVLPFCY
670 680 690 700 710 720
KLNYFVSMVL LFAAASAGIF SFERAPFTES SPLKLRFSQE LNLHDELGFS TVNVFGRQGA
730 740 750 760 770 780
GIEQILRNIP STQNAHSNVE CTSNGQGSET CRYAGPRPHL VSSSSIPELS DILSIKVLSN
790 800 810 820 830 840
NRKSSGRSSY EPINAELVIN VKENRLCTIG FNSSQFAEHD YGQSPVKQVT IFGNAHHDNR
850 860 870 880 890 900
TRSQLSTLDG LSRDDEENRI FKWNRGINSL QLHKLDFERN YYHVGIQWMP TILSQDADEE
910 920 930 940 950 960
SSDALGLKIR CFWGEYDSVS IINGEVKRKV PALDELLAYS PKEVSFSNRE AGLVIVNDYI
EL