SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing RR42_RS14485 FitnessBrowser__Cup4G11:RR42_RS14485 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 2 hits to proteins with known functional sites (download)

A6NK06 Cis-aconitate decarboxylase; CAD; Aconitate decarboxylase; Aconitate decarboxylase 1; Cis-aconitic acid decarboxylase; Immune-responsive gene 1 protein; EC 4.1.1.6 from Homo sapiens (Human) (see paper)
25% identity, 81% coverage: 82:470/483 of query aligns to 75:449/481 of A6NK06

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D93 (= D100) mutation to A: Abolished cis-aconitate decarboxylase activity.
T97 (= T104) to M: strongly reduced cis-aconitate decarboxylase activity; dbSNP:rs767323284; mutation to A: Strongly reduced cis-aconitate decarboxylase activity.
H103 (= H112) mutation to A: Abolished cis-aconitate decarboxylase activity.
N152 (= N162) to S: increased cis-aconitate decarboxylase activity
H159 (≠ L169) to Q: strongly reduced cis-aconitate decarboxylase activity; reduced protein stability; to R: strongly reduced cis-aconitate decarboxylase activity; reduced protein stability; dbSNP:rs1471882722; mutation to A: Abolished cis-aconitate decarboxylase activity.
K207 (= K221) mutation to A: Abolished cis-aconitate decarboxylase activity.
K272 (= K284) to Q: strongly reduced cis-aconitate decarboxylase activity; reduced protein stability; dbSNP:rs1018207074; mutation to A: Abolished cis-aconitate decarboxylase activity.
R273 (≠ A286) to H: does not affect cis-aconitate decarboxylase activity
H277 (≠ E290) to Y: strongly reduced cis-aconitate decarboxylase activity; reduced protein stability; dbSNP:rs1289708092; mutation to A: Abolished cis-aconitate decarboxylase activity.
Y318 (≠ I331) mutation to A: Abolished cis-aconitate decarboxylase activity.
R331 (= R344) to H: strongly reduced cis-aconitate decarboxylase activity; reduced protein stability; dbSNP:rs755737247

6r6uA Crystal structure of human cis-aconitate decarboxylase (see paper)
25% identity, 81% coverage: 82:470/483 of query aligns to 72:446/458 of 6r6uA

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binding (r,r)-2,3-butanediol: A148 (vs. gap), F155 (≠ G168), F242 (≠ Y258), Y243 (≠ D259)

Query Sequence

>RR42_RS14485 FitnessBrowser__Cup4G11:RR42_RS14485
MSAPISNVRPEPDPVMADIVDYVTRYQVKSALAYDTARNCLIDTLGCGLEALSYPACTKL
LGPIVPGTVVPNGAKVPGTQFQLDPIQAAFNIGAMIRWLDFNDTWLAAEWGHPSDNLGGI
LATADWLSRNNVAAGRKPLTMKDVLTGMIKAHEIQGCIALENAFNKVGLDHVVLVKVAST
AVVAQMLGLAVDEILNAVSLAWVDGQALRTYRHAPNTGSRKSWAAGDATSRAVRLALIAR
TGEMGYPSVLSAKGWGFYDVLFKGQPFRFQRPYGTYVMENVLFKIAFPAEFHAQTAVEAA
MTLHGQLCAAGKTAAQIRQVTIRTHEACIRIIDKKGPLANPADRDHCIQYMVAVPLLFGR
LSAEDYEDKIAADPRIDALRDKIVCVEDPRFTADYHDPDKRSIANALTVTLDDGTVLPEV
VVDYPLGHKRRRDEGIPLLVEKFKTNLARRFPARQQQAILAVSLDQARLEAMPVNEYVDL
YVI

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