Q8LQJ8

PR
Gene name
FTSH5 (Os01g0574500, LOC_Os01g39260, B1151A10.26-1, OsJ_002241)
Protein name
ATP-dependent zinc metalloprotease FTSH 5, mitochondrial
Names
OsFTSH5
Species
Oryza sativa subsp japonica (Rice)
KEGG Pathway
osa:4326311
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

633-715 (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 Q8LQJ8

Entry ID Method Resolution Chain Position Source
AF-Q8LQJ8-F1 Predicted AlphaFoldDB

No variants for Q8LQJ8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8LQJ8

No associated diseases with Q8LQJ8

5 regional properties for Q8LQJ8

Type Name Position InterPro Accession
domain Peptidase M41 477 - 657 IPR000642
domain AAA+ ATPase domain 262 - 398 IPR003593
domain ATPase, AAA-type, core 266 - 395 IPR003959
conserved_site ATPase, AAA-type, conserved site 366 - 384 IPR003960
domain AAA ATPase, AAA+ lid domain 418 - 461 IPR041569

Functions

Description
EC Number
Subcellular Localization
  • Mitochondrion
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
chloroplast thylakoid Sac-like membranous structures (cisternae) in a chloroplast combined into stacks (grana) and present singly in the stroma (stroma thylakoids or frets) as interconnections between grana. An example of this component is found in Arabidopsis thaliana.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
ATP-dependent peptidase activity Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis.
metal ion binding Binding to a metal ion.
metalloendopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in 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.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
O88967 Yme1l1 ATP-dependent zinc metalloprotease YME1L1 Mus musculus (Mouse) PR
A2ZVG7 FTSH9 ATP-dependent zinc metalloprotease FTSH 9, chloroplastic/mitochondrial Oryza sativa subsp japonica (Rice) PR
Q9FGM0 FTSH11 ATP-dependent zinc metalloprotease FTSH 11, chloroplastic/mitochondrial Arabidopsis thaliana (Mouse-ear cress) PR
O80983 FTSH4 ATP-dependent zinc metalloprotease FTSH 4, mitochondrial Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MAWRRVLSQV ARNRSAYAIC NEIIYANPSR ILRGDTIAGG TLRNLHERYQ SSYVGSFARR
70 80 90 100 110 120
MRQMDSPSEA SLLKEIYRSD PERVIQIFES QPSLHSNPSA LAEYVKALVR VDRLEDSTLL
130 140 150 160 170 180
KTLQRGIAAS AREEENLGSV SENLGSVSAF RSAGQVTKDG ILGTANAPIH MVTAETGQFK
190 200 210 220 230 240
EQLWRTFRSI ALTFLLISGI GALIEDRGIS KGLGLNEEVQ PSMESNTKFS DVKGVDEAKA
250 260 270 280 290 300
ELEEIVHYLR DPKRFTRLGG KLPKGVLLVG PPGTGKTMLA RAIAGEAGVP FFSCSGSEFE
310 320 330 340 350 360
EMFVGVGARR VRDLFAAAKK RSPCIIFMDE IDAIGGSRNP KDQQYMKMTL NQLLVELDGF
370 380 390 400 410 420
KQNEGIIVIA ATNFPESLDK ALVRPGRFDR HIVVPNPDVE GRRQILESHM SKVLKSDDVD
430 440 450 460 470 480
LMIIARGTPG FSGADLANLV NVAALKAAMD GAKAVTMNDL EYAKDRIMMG SERKSAVISD
490 500 510 520 530 540
ESRKLTAYHE GGHALVAIHT EGAHPVHKAT IVPRGMALGM VAQLPDKDET SVSRKQMLAR
550 560 570 580 590 600
LDVCMGGRVA EELIFGDSEV TSGASSDFQQ ATAVARAMVT KYGMSKQLGF VSYNYEDDGK
610 620 630 640 650 660
SMSTETRLLI EKEVKCFVEN AYNNAKNILI KHNKELHALA NALLEHETLT GAQIKNILAQ
670 680 690 700 710
VNNKQQQEHA IEAPQKTPAV PSSPAASAAA AAAAAAAAAQ QAAAKAKGEI AGIGS