Q6CKC6

PR
Gene name
KLLA0F11748g
Protein name
Vacuolar membrane protease
Names
FXNA-related family protease 1
Species
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
KEGG Pathway
kla:KLLA0_F11748g
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

495-606 (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 Q6CKC6

Entry ID Method Resolution Chain Position Source
AF-Q6CKC6-F1 Predicted AlphaFoldDB

No variants for Q6CKC6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6CKC6

No associated diseases with Q6CKC6

1 regional properties for Q6CKC6

Type Name Position InterPro Accession
domain Peptidase M28 132 - 319 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
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
MMANYFRSTF KFRKTTVSTL FVLTVLVISI LTWFDANKYK SNLPDDKSSN SLLDAAWHDL
70 80 90 100 110 120
QVITEKPHPY TSHFNDNVHD YLLQRVEQIS KKSKFIEVSD DSANGVSKLF QHLDVFNDSS
130 140 150 160 170 180
TETRLVYYES SNILVKVEGK SPQLPGLLLS AHFDSVPTGY GATDDGKGVV SLLALLQYYS
190 200 210 220 230 240
ENQPERTIVF NFNNNEEFGL LGATIFTYSE WFKLVSYVIN LEGAGAGSKA ALFRTSDTAT
250 260 270 280 290 300
ALLYEKSVKD QPFGNSIYQQ GFYSRFVSSE TDYKIYELNG LRGWDIAFYK PRDMYHTGKD
310 320 330 340 350 360
TVQHTSKAAL WHMLNIAWQL SKYVVADQTT ASQEILDDES NSSPAIYFDI ISKWFFVVSA
370 380 390 400 410 420
RQLYVWNIVL LCVLPITLIL LRIVCNKLGT WRMPTSALFT RIPFALFVSS FTIYFTKELL
430 440 450 460 470 480
LQLNPTIWSR NFILPFLFCI SEFLLINTLV LALFEYLWPI QDFKTLSLLE LSAIAWLFLL
490 500 510 520 530 540
KCTWDLSSSG FKATGVYPVT VFYLFISLAS MFGLCSMCFG KRPNATNDYD NSEFMRPDTN
550 560 570 580 590 600
DTHSIECPRQ PEDSETTETS PLINTPSSSV QSSPIASSKS LPGAVQYLQR TLNYDWSAQY
610 620 630 640 650 660
LLAVPINAFL IWESLFNLFD ALSMTVQESN KATEAVFKFA IYGAIFLCSP LLPFTTKLNR
670 680 690 700 710 720
FVVIILGVVT ILAASFSLFA APYTELAPLK LRFVQRIDIS RETKQNVEIY GRAGANIQEV
730 740 750 760 770 780
LSSLPSRPNV SCKDSGSGTE LCVYEGMWPN FGIPMKVDVV KNTHNDKEHF EYEPYFADLR
790 800 810 820 830 840
INVADNRLCL MKFNTTGKKH LKQVEFKVGN ETTTHSYRTD EGIDSLLLHK LSWNVPYYDV
850 860 870 880 890 900
QLKWIPQYTA EGSSDTLGVS IDCYWGEFDE TIVNGQVVQK IPAYNELLQF LPETFIVSNR
910
ESGMVTIHKY LEL