SitesBLAST
Comparing AZOBR_RS07945 FitnessBrowser__azobra:AZOBR_RS07945 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 15 hits to proteins with known functional sites (download)
Q51330 Oxalate:formate antiporter; OFA; Oxalate:formate antiport protein; Oxalate:formate exchange protein from Oxalobacter formigenes (see 4 papers)
36% identity, 98% coverage: 3:424/432 of query aligns to 5:416/418 of Q51330
- C28 (≠ S27) mutation to G: Slight decrease in activity; when associated with A-271.
- Q56 (= Q55) mutation to C: Residual activity.
- F59 (= F58) mutation to C: Loss of activity.
- Q66 (≠ E65) mutation to C: Residual activity.
- S69 (≠ L68) mutation to C: Residual activity.
- C271 (≠ T283) mutation to A: Slight decrease in activity; when associated with G-28.
- G349 (= G360) mutation to C: Loss of activity.
- K355 (= K366) mutation K->C,G,Q,T: Loss of activity.; mutation to R: Residual activity.
- G362 (≠ I373) mutation to C: Residual activity.
- G363 (≠ P374) mutation to C: Residual activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
8hpkA Crystal structure of the bacterial oxalate transporter oxlt in an oxalate-bound occluded form (see paper)
36% identity, 93% coverage: 12:412/432 of query aligns to 3:390/390 of 8hpkA
6zguA Crystal structure of a mfs transporter with bound 3-(2-methylphenyl) propanoic acid at 2.41 angstroem resolution
31% identity, 94% coverage: 15:418/432 of query aligns to 4:398/404 of 6zguA
6zgtA Crystal structure of a mfs transporter with bound 2-naphthoic acid at 2.39 angstroem resolution
31% identity, 94% coverage: 15:418/432 of query aligns to 4:398/404 of 6zgtA
6zgsA Crystal structure of a mfs transporter with bound 3-phenylpropanoic acid at 2.39 angstroem resolution
31% identity, 94% coverage: 15:418/432 of query aligns to 4:398/404 of 6zgsA
A0LNN5 L-lactate transporter; SfMCT from Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB) (see paper)
30% identity, 95% coverage: 7:416/432 of query aligns to 5:412/412 of A0LNN5
- L28 (≠ Q33) mutation to A: Loss of transport activity.
- Y119 (= Y123) binding ; mutation Y->A,F: Loss of transport activity.
- L145 (≠ F149) mutation to A: Strong decrease in transport activity.
- H250 (≠ Q244) mutation to A: Strong decrease in transport activity.; mutation to F: Loss of transport activity.
- R256 (≠ Q250) mutation to A: No change in transport activity.; mutation to D: Increases transport activity.
- D257 (= D251) mutation to A: Loss of transport activity.
- N276 (= N280) mutation to A: Loss of transport activity.
- R280 (= R284) binding ; mutation to A: Abolishes L-lactate binding and L-lactate transport.
- Y331 (≠ W335) mutation to A: Loss of transport activity.; mutation to F: No change in transport activity.
- F335 (≠ Y339) mutation to A: Increases transport activity.
- F359 (≠ Y363) mutation to A: Loss of transport activity.
- C362 (≠ K366) mutation to A: Decrease in transport activity.
- K377 (≠ A380) mutation K->A,D: No change in transport activity.
- D378 (= D381) mutation to A: Loss of transport activity.
- Y383 (≠ W386) mutation to A: Loss of transport activity.; mutation to F: Strong decrease in transport activity.
6zgrA Crystal structure of a mfs transporter with bound 1- hydroxynaphthalene-2-carboxylic acid at 2.67 angstroem resolution
31% identity, 94% coverage: 15:418/432 of query aligns to 4:393/399 of 6zgrA
6g9xA Crystal structure of a mfs transporter at 2.54 angstroem resolution (see paper)
31% identity, 94% coverage: 15:418/432 of query aligns to 4:390/396 of 6g9xA
6zguB Crystal structure of a mfs transporter with bound 3-(2-methylphenyl) propanoic acid at 2.41 angstroem resolution
31% identity, 88% coverage: 32:410/432 of query aligns to 15:364/364 of 6zguB
6zgtB Crystal structure of a mfs transporter with bound 2-naphthoic acid at 2.39 angstroem resolution
31% identity, 88% coverage: 32:410/432 of query aligns to 15:364/364 of 6zgtB
6zgsB Crystal structure of a mfs transporter with bound 3-phenylpropanoic acid at 2.39 angstroem resolution
31% identity, 88% coverage: 32:410/432 of query aligns to 15:364/364 of 6zgsB
6g9xB Crystal structure of a mfs transporter at 2.54 angstroem resolution (see paper)
30% identity, 89% coverage: 32:414/432 of query aligns to 17:368/368 of 6g9xB
6zgrB Crystal structure of a mfs transporter with bound 1- hydroxynaphthalene-2-carboxylic acid at 2.67 angstroem resolution
30% identity, 88% coverage: 32:410/432 of query aligns to 17:363/364 of 6zgrB
O60669 Monocarboxylate transporter 2; MCT 2; Solute carrier family 16 member 7 from Homo sapiens (Human) (see paper)
23% identity, 83% coverage: 70:429/432 of query aligns to 74:445/478 of O60669
- R143 (= R138) mutation to A: Reduces pyruvate transmembrane transporter activity. Reduces pyruvate transmembrane transporter activity. No effect on protein abundance. Does not affect cell surface localization. Dominant negative mutant.
- N147 (≠ A142) mutation to A: Reduces pyruvate transmembrane transporter activity. Reduces pyruvate transmembrane transporter activity. No effect on protein abundance. Does not affect cell surface localization.
- F262 (≠ H256) mutation to A: No effect on protein abundance. Does not affect cell surface localization.
- D293 (≠ N280) May be protonated during monocarboxylate transport; mutation to N: Reduced proton-dependent active symport, but not pyruvate transport.
- R297 (= R284) mutation R->L,D: Reduces pyruvate transmembrane transporter activity. No effect on protein abundance. Does not affect cell surface localization.
- N305 (vs. gap) mutation to A: Reduces pyruvate transmembrane transporter activity. No effect on protein abundance. Does not affect cell surface localization.
- F351 (≠ W335) mutation to A: Reduces pyruvate transmembrane transporter activity. No effect on protein abundance. Does not affect cell surface localization.
- S355 (≠ Y339) mutation S->G,A: Reduces pyruvate transmembrane transporter activity. No effect on protein abundance. Does not affect cell surface localization.
- E360 (≠ A344) mutation to A: Reduces pyruvate transmembrane transporter activity. No effect on protein abundance. Does not affect cell surface localization.
- T445 (= T429) to S: in dbSNP:rs3763980
Sites not aligning to the query:
- 18 W→A: Reduces pyruvate transmembrane transporter activity. No effect on protein abundance. Does not affect cell surface localization. Dominant negative mutant.
- 20 W→A: Reduces pyruvate transmembrane transporter activity. No effect on protein abundance. Does not affect cell surface localization. Dominant negative mutant.
- 34 Y→F: Reduces pyruvate transmembrane transporter activity. No effect on protein abundance. Does not affect cell surface localization.
- 38 K→D: Reduces pyruvate transmembrane transporter activity. No effect on protein abundance. Does not affect cell surface localization.
- 70 Y→A: No effect on protein abundance. Does not affect cell surface localization.
Q6ZSM3 Monocarboxylate transporter 12; MCT 12; Creatine transporter 2; CRT2; Solute carrier family 16 member 12 from Homo sapiens (Human) (see 3 papers)
21% identity, 78% coverage: 77:413/432 of query aligns to 110:468/516 of Q6ZSM3
- D329 (≠ N280) mutation to A: Decreases creatine efflux activity. Loss of localization to the plasma membrane.
- D360 (≠ V309) mutation to A: Does not affect creatine efflux activity. Does not affect plasma membrane localization.
- D387 (≠ W335) mutation to A: Does not affect creatine efflux activity.
- G437 (= G384) to S: found in a patient with age-related cataract; uncertain significance; decreases creatine transport; dbSNP:rs759863805
Sites not aligning to the query:
- 67 R→A: Abolishes creatine efflux activity. Does not affect plasma membrane localization.
- 95 D→A: Decreases in the creatine efflux activity. Does not affect plasma membrane localization.
- 245:516 natural variant: Missing (in CTRCT47; loss of localization to the plasma membrane; retained in the endoplasmic reticulum where it undergoes degradation by the proteasome; has no dominant effect on wild-type protein expression and localization)
Query Sequence
>AZOBR_RS07945 FitnessBrowser__azobra:AZOBR_RS07945
MRQTGAQSALPVGGRWMQLLAGVICMSMIANLQYGWTLFVEPIDDKHGWGRAAIQVAFTI
FIVTETWLVPVEGWFVDRFGPRIVVLFGSVLCAASWALNAVADSLLVLYVAAAIGGIGAG
AVYGTCVGNALKWFPDRRGLAAGITAAGFGAGSALTVVPIATMIETSGYEATFMAFGLGQ
GLVVFALAWLLVAPPSAPLARGGFATPPAQRQYTPSQMVRTPVFWVMYAMFVMVAGGGLM
ATAQLGPIAQDFGLAHAPVSILGLTLPALTFALSIDRVLNGLTRPFFGWVSDHIGRENTM
FIAFAIEAVGIVALSLYGRDPVAFVLLTGLVFFAWGEIYSLFPACCADTFGSKFAASNAG
LLYTAKGTAALLIPFANIIADATGSWHAVFLLAAAVNALAAVLALFVLRPMRNRMAAESL
DARSGRSVTATP
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