SitesBLAST

E35 (≠ Q44) binding
E76 (≠ V83) binding
Y135 (= Y144) mutation to A: 300-fold decrease in activity with spermine as substrate. Retains the ability to inhibit PrprA activity.; mutation Y->C,F: 100-fold decrease in activity with spermine as substrate.; mutation to S: Loss of activity with spermine as substrate.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

3wr7A Crystal structure of spermidine acetyltransferase from escherichia coli (see paper)
24% identity, 88% coverage: 16:171/178 of query aligns to 3:158/170 of 3wr7A

query
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3wr7A

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binding coenzyme a: Y28 (≠ N41), Q83 (≠ G96), I84 (≠ M97), Q91 (= Q104), G92 (= G105), K93 (≠ I106), G94 (= G107), L95 (≠ V108), A96 (≠ G109), I119 (≠ E132), K126 (≠ A139), Y131 (= Y144)
binding spermidine: E31 (≠ Q44), Y34 (≠ F47), E39 (≠ K52)

4r9mA Crystal structure of spermidine n-acetyltransferase from escherichia coli (see paper)
30% identity, 59% coverage: 67:171/178 of query aligns to 57:159/169 of 4r9mA

query
sites
4r9mA

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binding magnesium ion: E73 (≠ V83)

Sites not aligning to the query:

binding magnesium ion: 32

6vfnA Crystal structure of speg allosteric polyamine acetyltransferase from bacillus thuringiensis in complex with spermine (see paper)
24% identity, 88% coverage: 16:171/178 of query aligns to 2:157/167 of 6vfnA

query
sites
6vfnA

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binding spermine: N19 (≠ Y33), E30 (≠ Q44), Y33 (≠ F47), E34 (≠ P48), E38 (≠ K52), I47 (≠ L57), D49 (= D59), Q50 (≠ L60), R53 (≠ N63)

A0R3F9 Acetyltransferase Pat; GCN5-related N-acetyltransferase; GNAT; Protein acetyltransferase; Pat; EC 2.3.1.- from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
38% identity, 37% coverage: 92:157/178 of query aligns to 232:296/333 of A0R3F9

query
sites
A0R3F9

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E234 (≠ N94) mutation to A: Shows a lower rate of acetylation of USP in the absence of cAMP than the wild-type protein, but in the presence of cAMP, an increase in the rate of acetyltransferase activity is observed.

Sites not aligning to the query:

95 R→K: No increase in the rate of acetylation in the presence of cAMP, presumably because of its inability to bind cAMP.

4ollA Camp-binding acyltransferase from mycobacterium smegmatis (see paper)
37% identity, 37% coverage: 92:156/178 of query aligns to 218:281/316 of 4ollA

query
sites
4ollA

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Sites not aligning to the query:

binding calcium ion: 171, 172

4r3lA Crystal structure of ard1 n-terminal acetyltransferase from sulfolobus solfataricus bound to substrate peptide fragment and coa (see paper)
34% identity, 60% coverage: 67:172/178 of query aligns to 44:154/157 of 4r3lA

query
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4r3lA

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binding coenzyme a: I82 (≠ M97), A83 (= A98), V84 (= V99), R89 (≠ Q104), R90 (≠ G105), G92 (= G107), I93 (≠ V108), A94 (≠ G109), T95 (≠ S110), N122 (= N137), Y123 (≠ H138), P124 (≠ A139), L128 (= L143), Y129 (= Y144), K131 (≠ R146)
binding : H78 (= H91), V80 (≠ L95), E117 (= E132), Y143 (= Y158), Y144 (≠ F160)

Sites not aligning to the query:

binding coenzyme a: 23
binding : 25, 27

4r3kA Crystal structure of ard1 n-terminal acetyltransferase from sulfolobus solfataricus bound to coa (see paper)
34% identity, 60% coverage: 67:172/178 of query aligns to 44:154/157 of 4r3kA

query
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4r3kA

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binding calcium ion: V118 (= V133), R119 (≠ Y134), N122 (= N137)
binding coenzyme a: I82 (≠ M97), A83 (= A98), V84 (= V99), R89 (≠ Q104), R90 (≠ G105), G92 (= G107), A94 (≠ G109), T95 (≠ S110), Y123 (≠ H138), P124 (≠ A139), L128 (= L143), Y129 (= Y144)

Sites not aligning to the query:

binding coenzyme a: 23

4lx9A Archaeal amino-terminal acetyltransferase (nat) bound to acetyl coenzyme a (see paper)
34% identity, 60% coverage: 67:172/178 of query aligns to 44:154/157 of 4lx9A

query
sites
4lx9A

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binding acetyl coenzyme *a: I82 (≠ M97), V84 (= V99), R89 (≠ Q104), R90 (≠ G105), G92 (= G107), A94 (≠ G109), T95 (≠ S110), E117 (= E132), P124 (≠ A139), L128 (= L143), Y129 (= Y144), K131 (≠ R146)
binding zinc ion: H78 (= H91), E117 (= E132)

Sites not aligning to the query:

binding acetyl coenzyme *a: 23

5c88A Crystal structure of ard1 n-terminal acetyltransferase from sulfolobus solfataricus in monoclinic form (see paper)
34% identity, 60% coverage: 67:172/178 of query aligns to 44:154/158 of 5c88A

query
sites
5c88A

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binding coenzyme a: I82 (≠ M97), V84 (= V99), R89 (≠ Q104), R90 (≠ G105), G92 (= G107), A94 (≠ G109), T95 (≠ S110), N122 (= N137), P124 (≠ A139), A125 (= A140), A127 (≠ K142), L128 (= L143)

Q980R9 N-alpha-acetyltransferase; NAT; Amino-terminal acetyltransferase; N-terminal acetyltransferase; EC 2.3.1.255; EC 2.3.1.258 from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus) (see 4 papers)
34% identity, 60% coverage: 67:172/178 of query aligns to 54:164/167 of Q980R9

query
sites
Q980R9

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S75 (≠ A85) Plays an important role in modulating multiple conformations of loop regions and contributes to protein thermostability; mutation to A: Has a melting temperature about 3 degrees Celsius lower than that of the wild-type.
S82 (vs. gap) Plays an important role in modulating multiple conformations of loop regions and contributes to protein thermostability; mutation to A: Has a melting temperature about 3 degrees Celsius lower than that of the wild-type.
H88 (= H91) binding ; mutation to A: 2.5- and 1.5-fold decrease of the catalytic efficiency and affinity for Ser-N-terminal peptide compared to the wild-type, respectively. Loss of acetyltransferase activity for Met-N-terminal peptide.; mutation to F: 2.5-fold decrease of the catalytic efficiency for Ser-N-terminal peptide, but almost same affinity compared to the wild-type. Loss of acetyltransferase activity for Met-N-terminal peptide.; mutation to Q: 2.5-fold decrease of the catalytic efficiency for Ser-N-terminal peptide, but 1.5-fold increase of the affinity compared to the wild-type. Loss of acetyltransferase activity for Met-N-terminal peptide.
IAV 92:94 (≠ MAV 97:99) binding
R100 (≠ G105) mutation to A: 7-fold decrease of the affinity, with no significant difference in the catalytic efficiency. Same fold compared to the wild-type.
RKGIAT 100:105 (≠ GIGVGS 105:110) binding
T105 (≠ S110) mutation to A: 3-fold decrease of the affinity, with no significant difference in the catalytic efficiency. Same fold compared to the wild-type.
Y125 (≠ E130) mutation to A: Same catalytic efficiency and 1.7-fold decrease of the affinity for Ser-N-terminal peptide compared to the wild-type. 1.5- and 2.5-fold decrease of the catalytic efficiency and affinity for Met-N-terminal peptide compared to the wild-type, respectively.
E127 (= E132) binding ; mutation to A: Same catalytic efficiency and slight decrease of the affinity for Ser-N-terminal peptide compared to the wild-type. Loss of acetyltransferase activity for Met-N-terminal peptide.; mutation to H: 1.3-fold decrease of the catalytic efficiency for Ser-N-terminal peptide, but almost same affinity compared to the wild-type. 1.7-fold decrease of the catalytic efficiency and 1.3-fold increase of the affinity for Met-N-terminal peptide compared to the wild-type.; mutation to Q: 2.3-fold decrease of the catalytic efficiency and 1.3-fold increase of the affinity for Ser-N-terminal peptide compared to the wild-type. 5-fold decrease of the catalytic efficiency and slight decrease of the affinity for Met-N-terminal peptide compared to the wild-type. Loss of acetyltransferase activity for Ser and Met-N-terminal peptide; when associated with Gln-35.
R129 (≠ Y134) mutation to A: Slight decrease of the catalytic efficiency and of the affinity for Ser-N-terminal peptide compared to teh wild-type. 2.5-fold increase of the catalytic efficiency and almost the same affinity for Met-N-terminal peptide compared to the wild-type.
N132 (= N137) binding ; mutation to A: 4.5-fold decrease of the affinity, with no significant difference in the catalytic efficiency. Same fold compared to the wild-type.
YEK 139:141 (≠ YKR 144:146) binding
Y154 (≠ F160) binding ; mutation to A: 1.3-fold decrease of the catalytic efficiency for Ser-N-terminal peptide, but same affinity compared to the wild-type. 6.5-fold decrease of the catalytic efficiency for Met-N-terminal peptide, but same affinity compared to the wild-type.; mutation to F: Almost same catalytic efficiency for Ser-N-terminal peptide and slight decrease of the affinity compared to the wild-type. 5-fold decrease of the catalytic efficiency for Met-N-terminal peptide and 1.5-fold decrease of the affinity compared to the wild-type.

Sites not aligning to the query:

33 L→A: 20- and 2-fold decrease of the catalytic efficiency and affinity for Ser-N-terminal peptide. 11-fold decrease of the catalytic efficiency for Met-N-terminal peptide, but almost same affinity compared to the wild-type.
34 P→A: 20-fold decrease of the catalytic efficiency for Ser-N-terminal peptide, but almost same affinity compared to the wild-type. 18-fold decrease of the catalytic efficiency for Met-N-terminal peptide, but almost same affinity compared to the wild-type.
35 Plays an important role in substrate specificity; E→A: Slight increase of the catalytic efficiency for Ser-N-terminal peptide, but 4-fold decrease of the affinity compared to the wild-type. 6-fold increase of the catalytic efficiency for Met-N-terminal peptide and slight decrease of the affinity compared to the wild-type.; E→F: Strong decrease of the acetyltransferase activity with Ser-N-terminal peptide such as Alba. 2-fold increase of acetyltransferase activity for Ala-N-terminal peptide such as Hjc compared to the wild-type.; E→Q: Loss of acetyltransferase activity for Ser and Met-N-terminal peptide; when associated with Gln-127.; E→V: Alters the N-terminal substrate specificity and allows large N-terminal end residue of the substrate to be accommodated in a substrate-binding pocket. 4-fold increase of the acetyltransferase activity with Met-N-terminal peptide such as SSB compared to the wild-type. 2-fold increase of acetyltransferase activity with Ala-N-terminal peptide such as Hjc.; E→W: Low acetyltransferase activity with Ala-, Met- and Ser-N-terminal peptide.
37 binding ; Y→A: 34-fold decrease of the catalytic efficiency for Ser-N-terminal peptide and slight decrease of the affinity compared to the wild-type. Loss of acetyltransferase activity for Met-N-terminal peptide.; Y→F: Same catalytic efficiency and slight decrease of the affinity for Ser-N-terminal peptide compared to the wild-type. 3-fold decrease of the catalytic efficiency and 1.3-fold increase of the affinity for Met-N-terminal peptide compared to the wild-type.

4jwpA Crystal structure of ribosomal-protein-alanine n-acetyltransferase from brucella melitensis in complex with acetyl coa
28% identity, 87% coverage: 18:171/178 of query aligns to 6:161/165 of 4jwpA

query
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binding acetyl coenzyme *a: A30 (≠ Q44), V88 (≠ M97), Y89 (≠ A98), V90 (= V99), R95 (≠ Q104), G96 (= G105), G98 (= G107), G100 (= G109), R101 (≠ S110), G122 (≠ E132), A129 (= A139), S130 (≠ A140), A132 (≠ K142)
binding calcium ion: E110 (≠ L119), E113 (≠ N122)

2vzyC Crystal structure of rv0802c from mycobacterium tuberculosis in an unliganded form. (see paper)
28% identity, 76% coverage: 41:176/178 of query aligns to 39:166/189 of 2vzyC

query
sites
2vzyC

N

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binding acetate ion: S87 (≠ N94), G88 (= G96), S89 (≠ M97), R105 (≠ L113), S123 (≠ L131)

Query Sequence

>6938689 FitnessBrowser__SB2B:6938689
MSAQSPSIYRTTDGRIQVRHSDANDIGAIRAIYSQPSCFANTLQHPFPSLEKWQRRLGDL
PDNCYSLVAEIDGEIVGQAGMEVFANPRRKHVANLGMAVSEDYQGIGVGSALLAAMMELA
HNWLAVRRIELEVYTDNHAAIKLYKRHGFVIEGEAIGYAFRGGEYVDAFLMASCRDFG

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