SitesBLAST
Comparing AZOBR_RS25655 FitnessBrowser__azobra:AZOBR_RS25655 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 5 hits to proteins with known functional sites (download)
Q63342 Dimethylglycine dehydrogenase, mitochondrial; ME2GLYDH; EC 1.5.8.4 from Rattus norvegicus (Rat) (see 2 papers)
27% identity, 88% coverage: 16:388/426 of query aligns to 33:413/857 of Q63342
- CV 52:53 (≠ FT 37:38) binding
- EK 73:74 (≠ EA 57:58) binding
- 80:88 (vs. 64:74, 18% identical) binding
- H84 (≠ R68) modified: Tele-8alpha-FAD histidine
- V212 (= V208) binding
- W244 (≠ Y239) binding
- F-GYGII 390:395 (≠ CNGRGVA 364:370) binding
Sites not aligning to the query:
- 573:575 binding
- 669 binding
- 676:678 binding
- 737 binding
Q9UI17 Dimethylglycine dehydrogenase, mitochondrial; ME2GLYDH; EC 1.5.8.4 from Homo sapiens (Human) (see 4 papers)
26% identity, 88% coverage: 14:388/426 of query aligns to 38:420/866 of Q9UI17
- CV 59:60 (≠ FT 37:38) binding
- EK 80:81 (≠ EA 57:58) binding
- 87:95 (vs. 64:74, 18% identical) binding
- H91 (≠ R68) modified: Tele-8alpha-FAD histidine
- H109 (≠ I101) to R: in DMGDHD; shows 10 fold lower catalytic efficiency due to lower cofactor saturation and reduced thermal stability; dbSNP:rs121908331
- V219 (= V208) binding
- S279 (≠ D265) to P: in dbSNP:rs532964
- F-GYGII 397:402 (≠ CNGRGVA 364:370) binding
Sites not aligning to the query:
- 530 A → G: in dbSNP:rs1805073
- 646 S → P: in dbSNP:rs1805074
4pabB Crystal structure of the precursor form of rat dmgdh complexed with tetrahydrofolate (see paper)
26% identity, 85% coverage: 28:388/426 of query aligns to 6:376/824 of 4pabB
- active site: T53 (= T76), E102 (vs. gap), H226 (≠ S256), Y255 (≠ A278)
- binding flavin-adenine dinucleotide: I11 (= I33), G12 (= G34), G14 (= G36), C15 (≠ F37), V16 (≠ T38), L35 (vs. gap), E36 (= E57), K37 (≠ A58), G43 (= G64), S44 (≠ A65), T45 (≠ S66), H47 (≠ R68), A48 (≠ N69), A49 (≠ N70), G50 (= G71), L51 (≠ I74), V175 (= V208), A204 (≠ T236), G205 (≠ N237), W207 (≠ Y239), H226 (≠ S256), Y228 (≠ Q258), G326 (= G339), I328 (= I341), F353 (≠ C364), Y355 (≠ R367), G356 (= G368), I357 (≠ V369), I358 (≠ A370)
Sites not aligning to the query:
- active site: 536
- binding (6s)-5,6,7,8-tetrahydrofolate: 523, 536, 538, 550, 612, 613, 632, 639, 680, 700
P77182 tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC; tRNA mnm(5)s(2)U biosynthesis bifunctional protein; EC 2.1.1.61; EC 1.5.-.- from Escherichia coli (strain K12) (see paper)
23% identity, 58% coverage: 10:256/426 of query aligns to 245:478/668 of P77182
- G271 (= G34) mutation to Q: 4-fold decrease in activity, but no change in FAD binding.
Sites not aligning to the query:
- 64 E→A: Loss of methyltransferase activity.
- 178 D→A: Strong decrease in methyltransferase activity.
- 180 F→A: Strong decrease in methyltransferase activity.
- 567 R→A: Loss of activity, but no change in FAD binding.
- 618 R→A: Loss of activity, but no change in FAD binding.
3ps9A Crystal structure of mnmc from e. Coli (see paper)
23% identity, 58% coverage: 10:256/426 of query aligns to 250:483/668 of 3ps9A
- binding flavin-adenine dinucleotide: I275 (= I33), G276 (= G34), G277 (= G35), G278 (= G36), I279 (≠ F37), A280 (≠ T38), C299 (≠ E57), A300 (= A58), D301 (≠ S59), A308 (= A65), S309 (= S66), N311 (≠ R68), A315 (≠ Q72), Q436 (≠ P207), L437 (≠ V208), N466 (= N237), G467 (= G238), Q469 (≠ A240)
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 486, 488, 509, 570, 572, 620, 621, 622, 624, 625
- binding s-adenosylmethionine: 33, 71, 72, 73, 74, 106, 107, 108, 161, 162, 183, 184, 185
Query Sequence
>AZOBR_RS25655 FitnessBrowser__azobra:AZOBR_RS25655
IWQRPDSLWEATAPPPPALPVLKDSVEADLLVIGGGFTGLSAALHAAESGKRAVVLEASE
IGRGASGRNNGQVIPTLTRPDPEDLIAKFGQERGERFVALIRDSAETLFALIRRLNIDCA
AEQTGWVQPVHSPGRIAIAERRAKQWGSRGAPVELLDRAGISALLGTDAYYGGWMNRSGG
HINPLALARGLAGKAVEAGASVFINSPVLSVERRGDRWVARTPDGTVTTHALVLGTNGYA
AAVFPEIRTEVVPVLSWQMATQPLDEAQRRSILPGRQAMSDTHGDLRFMRYTADHRLVSG
GALLVPVDGADRLRRIVGLRLASMFPTLRGLRFDYVWNGRIAMTTDYTPRVHQLGPNAFT
WAGCNGRGVALSVSLGRELAYAALGRDPAELALPLTEPRPLPFNDLLQRIGPFKLLQYRW
NDIREI
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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