SitesBLAST
Comparing WP_002720845.1 NCBI__GCF_000015985.1:WP_002720845.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
P0AAI3 ATP-dependent zinc metalloprotease FtsH; Cell division protease FtsH; EC 3.4.24.- from Escherichia coli (strain K12) (see 4 papers)
56% identity, 93% coverage: 4:593/633 of query aligns to 2:594/644 of P0AAI3
- L201 (= L203) mutation to N: No in vivo protease activity, no in vitro ATPase activity.
- F225 (= F227) mutation F->A,D,E,G,N,Q,R,S,T: Does not complement ftsH1 at 42 degrees Celsius, no protease activity in vivo.; mutation F->C,H: Partially complements ftsH1 at 42 degrees Celsius, some protease activity in vivo.; mutation F->I,L,M,V,W,Y: Complements ftsH1 at 42 degrees Celsius, restores protease activity in vivo.
- G227 (= G229) mutation to A: Does not complement ftsH1 at 42 degrees Celsius, no protease activity in vivo.
- T297 (= T299) mutation to A: Low protease activity in vivo, low ATPase activity in vitro, complements ftsH1 at 42 degrees Celsius.
- N298 (= N300) mutation to A: No in vivo protease activity.
- D304 (= D306) mutation D->A,N: No in vivo protease activity, no in vitro ATPase activity; probably still binds ATP.; mutation to E: Low protease activity in vivo, low ATPase activity in vitro, complements ftsH1 at 42 degrees Celsius.
- L307 (= L309) mutation to A: Low protease activity in vivo.
- R309 (= R311) mutation R->A,L,K: No in vivo protease activity, no ATPase activity in vitro; probably still binds ATP.
- R312 (= R314) mutation R->A,L,K: No in vivo protease activity, no ATPase activity in vitro; probably still binds ATP.
- H414 (= H416) mutation to Y: Loss of protease function.
- E415 (= E417) mutation to Q: Loss of protease activity in vivo.
- H418 (= H420) mutation to Y: In tolZ21; loss of protease function in vivo, retains about 25% ATPase activity, temperature sensitive.
- E463 (≠ K465) mutation to K: In ftsH1; a temperature-sensitive mutant which increases the frequency of lysogenization of phage lambda; when associated with A-587.
- E476 (= E478) mutation E->D,K,V: Severe loss of protease function that is restored by excess Zn.; mutation to Q: Little effect on protease function.
- H536 (vs. gap) mutation to R: In hflB29; increases the frequency of lysogenization of phage lambda.
- E582 (= E581) mutation E->D,K,Q: No effect on protease function.; mutation to V: Decreased protease function.
P37476 ATP-dependent zinc metalloprotease FtsH; Cell division protease FtsH; EC 3.4.24.- from Bacillus subtilis (strain 168) (see paper)
51% identity, 93% coverage: 5:592/633 of query aligns to 6:601/637 of P37476
- K207 (= K200) mutation to N: Does not complement an ftsH deletion, loss of ATPase activity.
- E424 (= E417) mutation to Q: Does not complement an ftsH deletion, loss of protease activity against casein.
Q9WZ49 ATP-dependent zinc metalloprotease FtsH; EC 3.4.24.- from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see 2 papers)
49% identity, 94% coverage: 3:595/633 of query aligns to 2:604/610 of Q9WZ49
- G164 (≠ A157) binding
- GTGKT 204:208 (= GTGKT 197:201) binding
- L209 (= L202) binding
- H343 (= H336) binding
- E371 (≠ M364) binding
- G404 (= G397) mutation to L: Complete loss of protease activity and of oligomerization.
- H423 (= H416) binding
- E424 (= E417) active site
- H427 (= H420) binding
- D500 (= D494) binding ; mutation to A: Complete loss of protease activity.
Q5SI82 ATP-dependent zinc metalloprotease FtsH; EC 3.4.24.- from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
51% identity, 92% coverage: 13:597/633 of query aligns to 8:596/624 of Q5SI82
- G399 (= G397) mutation to L: No effect on protease activity against alpha-casein.
2dhrA Whole cytosolic region of atp-dependent metalloprotease ftsh (g399l) (see paper)
58% identity, 73% coverage: 140:599/633 of query aligns to 1:456/458 of 2dhrA
3kdsE Apo-ftsh crystal structure (see paper)
54% identity, 70% coverage: 150:593/633 of query aligns to 2:426/427 of 3kdsE
7wi4B Cryo-em structure of e.Coli ftsh protease cytosolic domains (see paper)
54% identity, 71% coverage: 143:593/633 of query aligns to 1:400/410 of 7wi4B
- binding phosphoaminophosphonic acid-adenylate ester: V14 (= V156), A15 (= A157), P54 (= P196), G55 (= G197), G57 (= G199), K58 (= K200), T59 (= T201), L60 (= L202)
- binding magnesium ion: A79 (= A232), S80 (= S233)
- binding zinc ion: H236 (= H416), H240 (= H420), D314 (= D494)
7wi4A Cryo-em structure of e.Coli ftsh protease cytosolic domains (see paper)
54% identity, 71% coverage: 143:593/633 of query aligns to 1:400/410 of 7wi4A
- binding phosphoaminophosphonic acid-adenylate ester: A15 (= A157), P54 (= P196), G55 (= G197), T56 (= T198), G57 (= G199), K58 (= K200), T59 (= T201), L60 (= L202), H156 (= H336)
- binding zinc ion: H236 (= H416), H240 (= H420), D314 (= D494)
Q9FGM0 ATP-dependent zinc metalloprotease FTSH 11, chloroplastic/mitochondrial; AtFTSH11; EC 3.4.24.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
51% identity, 72% coverage: 138:592/633 of query aligns to 346:784/806 of Q9FGM0
- G564 (= G360) mutation to A: In atts244; loss of thermotolerance.
P32795 Mitochondrial inner membrane i-AAA protease supercomplex subunit YME1; Protein OSD1; Tat-binding homolog 11; Yeast mitochondrial escape protein 1; EC 3.4.24.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
48% identity, 79% coverage: 102:598/633 of query aligns to 227:713/747 of P32795
- K327 (= K200) mutation K->I,R,T: Does not complement a YME1 deletion mutant, for K327R no longer binds or degrades COX2. Probably has no ATPase activity.
- Y354 (≠ F227) mutation Y->A,C,I,L,V: Partially complements a YME1 deletion mutant.; mutation Y->F,W: Complements a YME1 deletion mutant.; mutation Y->K,N,R,T: Does not complement a YME1 deletion mutant.; mutation to S: Does not complement a YME1 deletion mutant, retains 20% protease activity in vitro, binds an unfolded hybrid substrate protein.
- E381 (= E254) mutation to Q: Does not complement a YME1 deletion mutant, no longer binds or degrades COX2. Probably has no ATPase activity.
- E541 (= E417) mutation E->A,G,V: Does not complement a YME1 deletion mutant, for E541A stabilizes otherwise unstable COX2.
2ceaC Cell division protein ftsh (see paper)
53% identity, 70% coverage: 150:595/633 of query aligns to 8:419/421 of 2ceaC
- binding adenosine-5'-diphosphate: G15 (≠ A157), P54 (= P196), G55 (= G197), T56 (= T198), G57 (= G199), K58 (= K200), T59 (= T201), L60 (= L202), I177 (= I332), H181 (= H336), G205 (= G360), A206 (= A361), E209 (≠ M364)
- binding magnesium ion: P54 (= P196), K58 (= K200)
- binding zinc ion: H253 (= H416), H257 (= H420), D330 (= D494)
2ce7C Edta treated (see paper)
53% identity, 70% coverage: 150:595/633 of query aligns to 8:419/421 of 2ce7C
- binding adenosine-5'-diphosphate: G15 (≠ A157), P54 (= P196), G55 (= G197), T56 (= T198), G57 (= G199), K58 (= K200), T59 (= T201), L60 (= L202), I177 (= I332), H181 (= H336), G205 (= G360), A206 (= A361), E209 (≠ M364)
- binding zinc ion: H253 (= H416), H257 (= H420), D330 (= D494)
6az0E Mitochondrial atpase protease yme1 (see paper)
51% identity, 70% coverage: 153:597/633 of query aligns to 2:434/439 of 6az0E
- binding adenosine-5'-diphosphate: V5 (= V156), C6 (≠ A157), G46 (= G197), T47 (= T198), G48 (= G199), K49 (= K200), T50 (= T201), L51 (= L202), H182 (= H336), G206 (= G360), A207 (= A361)
- binding zinc ion: H262 (= H416), H266 (= H420), D340 (= D494)
6az0C Mitochondrial atpase protease yme1 (see paper)
51% identity, 70% coverage: 153:597/633 of query aligns to 2:434/439 of 6az0C
- binding adenosine-5'-triphosphate: C6 (≠ A157), P45 (= P196), G46 (= G197), G48 (= G199), K49 (= K200), T50 (= T201), L51 (= L202), H182 (= H336)
- binding zinc ion: H262 (= H416), H266 (= H420), D340 (= D494)
- binding : V75 (≠ M226), Y76 (≠ F227), V77 (= V228)
6az0B Mitochondrial atpase protease yme1 (see paper)
51% identity, 70% coverage: 153:597/633 of query aligns to 2:434/439 of 6az0B
- binding adenosine-5'-triphosphate: C6 (≠ A157), P45 (= P196), G46 (= G197), T47 (= T198), G48 (= G199), K49 (= K200), T50 (= T201), L51 (= L202), H182 (= H336), G206 (= G360), A207 (= A361)
- binding magnesium ion: T50 (= T201), D102 (= D253)
- binding zinc ion: H262 (= H416), H266 (= H420), D340 (= D494)
P39925 Mitochondrial respiratory chain complexes assembly protein AFG3; ATPase family gene 3 protein; Tat-binding homolog 10; EC 3.4.24.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
40% identity, 94% coverage: 6:603/633 of query aligns to 118:740/761 of P39925
- E559 (= E417) mutation to Q: Abolishes proteolytic activity; impairs synthesis of respiratory chain proteins COB and COX1. No effect on m-AAA protease assembly.
P40341 Mitochondrial respiratory chain complexes assembly protein YTA12; Tat-binding homolog 12; EC 3.4.24.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
47% identity, 78% coverage: 109:603/633 of query aligns to 299:794/825 of P40341
- E614 (= E417) mutation to Q: Abolishes proteolytic activity; impairs synthesis of respiratory chain proteins COB and COX1. No effect on m-AAA protease assembly.
Q96TA2 ATP-dependent zinc metalloprotease YME1L1; ATP-dependent metalloprotease FtsH1; Meg-4; Presenilin-associated metalloprotease; PAMP; YME1-like protein 1; EC 3.4.24.- from Homo sapiens (Human) (see 3 papers)
50% identity, 71% coverage: 151:598/633 of query aligns to 336:771/773 of Q96TA2
- E439 (= E254) mutation to Q: Loss of ATPase and protease activity. Loss of PRELID1 degradation. Cannot restore OMA1 degradation in YME1L-depleted cells.
- E600 (= E417) mutation to Q: Loss of protease activity. Cannot restore OMA1 degradation in YME1L-depleted cells.
Sites not aligning to the query:
- 206 R → W: in OPA11; does not affect localization to mitochondria; abolishes processing to mature form by MPP; results in decreased mitochondrial protein catabolism; has very low protease activity; results in mitochondrial fragmentation; dbSNP:rs1057519312
2ce7D Edta treated (see paper)
52% identity, 70% coverage: 150:595/633 of query aligns to 8:411/413 of 2ce7D
- binding adenosine-5'-diphosphate: V14 (= V156), G15 (≠ A157), G55 (= G197), T56 (= T198), G57 (= G199), K58 (= K200), T59 (= T201), L60 (= L202), H182 (= H336), G206 (= G360), A207 (= A361), E210 (≠ M364)
- binding zinc ion: H258 (= H416), H262 (= H420), D321 (= D494)
Q8JZQ2 AFG3-like protein 2; EC 3.4.24.- from Mus musculus (Mouse) (see 2 papers)
42% identity, 94% coverage: 5:597/633 of query aligns to 143:749/802 of Q8JZQ2
- R389 (= R236) to G: in par
- E574 (= E417) mutation to Q: Absence of proteolytic activity. Loss of its processing into the mature form.
Sites not aligning to the query:
- 1:38 modified: transit peptide, Mitochondrion
Query Sequence
>WP_002720845.1 NCBI__GCF_000015985.1:WP_002720845.1
MGNARNIAFWVVLFLLILALFNLFSGGQTTSSSRTISYSDFIARVDNGEVSSVTLDGERV
MVRGKDGTQYVAIKPQGEEVTDRLINHGVEVRAEAQEQSGFFSLISLWLPFLVLIGIWIF
FMNRMQGGGRGGAMGFGKSRAKLLTEKQGRVTFDDVAGIDEAKEELEEIVEFLRNPQKFS
RLGGKIPKGALLVGPPGTGKTLLARAIAGEAGVPFFTISGSDFVEMFVGVGASRVRDMFE
QAKKNAPCIVFIDEIDAVGRARGVGIGGGNDEREQTLNQLLVEMDGFEANEGVIIVAATN
RKDVLDPALLRPGRFDRTIHVPNPDIKGREKILSVHARKVPLGPNVDLRLIARGTPGFSG
ADLMNLVNEAALLAARVGRRFVTMDDFENAKDKVMMGAERRSMVLTADQKEKTAYHEAGH
AIVGLNLPKCDPVYKATIIPRGGALGMVVSLPEMDRLNMHKDEGKQKIAMTMAGKAAEII
KYGEEAVSSGPAGDIQQASALARAMVMRWGMSDVVGNIDYAEAHEGYQGNTAGFSVSAET
KKMIEAEVKRLIDEGYQTAYRILTEKSEEFERLAKGLLEYETLTGDQIRRVIAGEPIDSD
DDADRPVGGGSVAAIPKTRPKVIKADGGLEPSV
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory