SitesBLAST
Comparing HSERO_RS05840 FitnessBrowser__HerbieS:HSERO_RS05840 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)
5i39A High resolution structure of l-amino acid deaminase from proteus vulgaris with the deletion of the specific insertion sequence (see paper)
25% identity, 88% coverage: 22:404/433 of query aligns to 18:379/383 of 5i39A
- active site: F66 (≠ N74), Q69 (= Q77), A70 (≠ V78), Q248 (vs. gap), P267 (= P282)
- binding flavin-adenine dinucleotide: V30 (= V38), G31 (= G39), G33 (= G41), I34 (≠ Y42), L35 (≠ T43), V53 (≠ L61), E54 (≠ D62), K55 (≠ A63), Q62 (≠ A70), S63 (= S71), F66 (≠ N74), Y67 (≠ G75), Q69 (= Q77), A196 (≠ R211), A197 (≠ V212), G226 (≠ T244), G227 (≠ N245), W229 (≠ Y247), Q248 (vs. gap), Q250 (vs. gap), G321 (= G347), M323 (≠ V349), T348 (≠ N373), G349 (= G374), W350 (≠ R375), G351 (= G376), M352 (≠ I377), T353 (≠ A378)
3pvcA Crystal structure of apo mnmc from yersinia pestis (see paper)
28% identity, 59% coverage: 34:287/433 of query aligns to 236:479/635 of 3pvcA
- binding flavin-adenine dinucleotide: I240 (≠ V38), G241 (= G39), G242 (≠ A40), G243 (= G41), I244 (≠ Y42), V245 (≠ T43), A265 (= A63), D266 (≠ H64), A273 (= A70), S274 (= S71), N276 (≠ R73), A280 (≠ Q77), E404 (≠ R211), L405 (≠ V212), T434 (= T244), R437 (≠ T248), G454 (≠ A262), V456 (≠ S264), Y477 (≠ E285)
Sites not aligning to the query:
3sglA The crystal structure of mnmc from yersinia pestis bound with fad and sam (see paper)
28% identity, 59% coverage: 34:287/433 of query aligns to 233:475/630 of 3sglA
- binding flavin-adenine dinucleotide: I237 (≠ V38), G238 (= G39), G239 (≠ A40), G240 (= G41), I241 (≠ Y42), V242 (≠ T43), A262 (= A63), D263 (≠ H64), A270 (= A70), S271 (= S71), N273 (≠ R73), A277 (≠ Q77), E401 (≠ R211), L402 (≠ V212), T430 (= T244), G450 (≠ A262), Y473 (≠ E285)
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 534, 583, 584, 585, 586, 587, 588
- binding s-adenosylmethionine: 33, 34, 35, 36, 37, 38, 39, 68, 69, 123, 124, 145, 146, 147
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)
24% identity, 50% coverage: 30:247/433 of query aligns to 262:463/668 of P77182
- G271 (= G39) 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, 50% coverage: 30:247/433 of query aligns to 267:468/668 of 3ps9A
- binding flavin-adenine dinucleotide: I275 (≠ V38), G276 (= G39), G277 (≠ A40), G278 (= G41), I279 (≠ Y42), A280 (≠ T43), C299 (≠ D62), A300 (= A63), D301 (vs. gap), A308 (= A70), S309 (= S71), N311 (≠ R73), A315 (≠ Q77), Q436 (≠ R211), L437 (≠ V212), N466 (= N245), G467 (= G246)
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 469, 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
>HSERO_RS05840 FitnessBrowser__HerbieS:HSERO_RS05840
MTKHSNPAFPPSLWAATAGEFSGAPPLQASARYDVAIVGAGYTGLSTALHLAQAGVSVCV
LDAHAPGWGASGRNGGQVIPGLKYDPDQLRVMFGSAVADPLIAAIGSAADTVFDLIARHG
IECEAQRAGWIQPTHSPKMMRALEARARQWMAEGAPAQLMDGAEVTRRIGTGAYVGGWKD
ERAGSLHPLKYCRGLAQAAQRLGVVIHGDTRVTRLERRQGGWRLHGPSGEQGPHIDAERV
VLATNGYTDDLWPHLRQSVIAANSFIVATRPLPPALGASILPGGEVTSDSRRLLLYYRRD
AQGRLLMGGRGPFGEPQGPADFAHLERSVALLFPQLAGVEYEYRWSGRVAITRDFLPHVH
EPAPGLSIALGYNGRGIAMATMMGQRLAQRLIGPAGTAFPFPVSTIAPIPLHGLQRFYIA
AGVAWYSVLDRFS
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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