Comparing 3606580 FitnessBrowser__Dino:3606580 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 16 hits to proteins with known functional sites (download)
4pqaA Crystal structure of succinyl-diaminopimelate desuccinylase from neisseria meningitidis mc58 in complex with the inhibitor captopril (see paper)
39% identity, 98% coverage: 2:374/379 of query aligns to 3:371/375 of 4pqaA
4o23A Crystal structure of mono-zinc form of succinyl diaminopimelate desuccinylase from neisseria meningitidis mc58 (see paper)
38% identity, 100% coverage: 2:379/379 of query aligns to 3:376/376 of 4o23A
P44514 Succinyl-diaminopimelate desuccinylase; SDAP desuccinylase; N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase; EC 3.5.1.18 from Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) (see 3 papers)
37% identity, 98% coverage: 5:374/379 of query aligns to 6:371/377 of P44514
5vo3A Crystal structure of dape in complex with the products (succinic acid and diaminopimelic acid) (see paper)
37% identity, 98% coverage: 5:374/379 of query aligns to 10:375/380 of 5vo3A
7lgpB Dape enzyme from shigella flexneri
38% identity, 100% coverage: 1:379/379 of query aligns to 3:377/377 of 7lgpB
7t1qA Crystal structure of the succinyl-diaminopimelate desuccinylase (dape) from acinetobacter baumannii in complex with succinic acid
37% identity, 96% coverage: 15:379/379 of query aligns to 16:376/377 of 7t1qA
4h2kA Crystal structure of the catalytic domain of succinyl-diaminopimelate desuccinylase from haemophilus influenzae (see paper)
40% identity, 46% coverage: 5:180/379 of query aligns to 8:182/258 of 4h2kA
Sites not aligning to the query:
4op4B Crystal structure of the catalytic domain of dape protein from v.Cholerea in the zn bound form (see paper)
39% identity, 46% coverage: 5:180/379 of query aligns to 6:180/265 of 4op4B
Sites not aligning to the query:
7uoiA Crystallographic structure of dape from enterococcus faecium
26% identity, 99% coverage: 3:379/379 of query aligns to 9:383/383 of 7uoiA
3pfoA Crystal structure of a putative acetylornithine deacetylase (rpa2325) from rhodopseudomonas palustris cga009 at 1.90 a resolution
24% identity, 85% coverage: 42:363/379 of query aligns to 78:406/426 of 3pfoA
Q8C165 N-fatty-acyl-amino acid synthase/hydrolase PM20D1; Peptidase M20 domain-containing protein 1; PM20D1; EC 3.5.1.114; EC 3.5.1.14 from Mus musculus (Mouse) (see paper)
21% identity, 61% coverage: 48:278/379 of query aligns to 105:384/503 of Q8C165
Sites not aligning to the query:
7rsfA Acetylornithine deacetylase from escherichia coli
23% identity, 97% coverage: 11:377/379 of query aligns to 12:377/380 of 7rsfA
P37111 Aminoacylase-1; ACY-1; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14 from Sus scrofa (Pig) (see paper)
34% identity, 28% coverage: 5:112/379 of query aligns to 13:124/407 of P37111
Sites not aligning to the query:
4mmoA The crystal structure of a m20 family metallo-carboxypeptidase sso-cp2 from sulfolobus solfataricus
26% identity, 42% coverage: 61:218/379 of query aligns to 64:221/437 of 4mmoA
Q03154 Aminoacylase-1; ACY-1; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14 from Homo sapiens (Human) (see 6 papers)
33% identity, 27% coverage: 12:112/379 of query aligns to 22:124/408 of Q03154
Sites not aligning to the query:
1q7lA Zn-binding domain of the t347g mutant of human aminoacylase-i (see paper)
33% identity, 27% coverage: 12:112/379 of query aligns to 16:118/192 of 1q7lA
Sites not aligning to the query:
>3606580 FitnessBrowser__Dino:3606580
MTDPVALTADLIRCPSVTPEEGGALSLLEARLSAAGFACTRVDRNGIANLFARWGEKGHA
RSFGFNGHTDVVPVGARADWRFDPFGAQVEGDWMYGRGAVDMKSAVAAFAAAAMDFVADT
PPDGAVILAITGDEEGDAKDGTVALLDWMAAQGEAMDVCLVGEPTCPDEMGEMMKIGRRG
SMTFFFEALGVQGHSAYPHRAKNPLPALAKLVDRLAGLELDTGTDHFDPSTLAVTTFDTG
NPANNVIPAACRATVNIRFNDAHSSESLTAMVRGIAAEVAAETGIEITDRVSVSGESFIT
PPGRLSDLVAAAVETETGRVPVLSTSGGTSDARFVQHHCPVVEFGLVGKSMHQVDERVAI
AQIPQLKAIYTRILRDYFA
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SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.
Lawrence Berkeley National Laboratory