Comparing 5209718 FitnessBrowser__PV4:5209718 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 20 (the maximum) hits to proteins with known functional sites (download)
P37595 Isoaspartyl peptidase; Beta-aspartyl-peptidase; EcAIII; Isoaspartyl dipeptidase; EC 3.4.19.5 from Escherichia coli (strain K12) (see 2 papers)
51% identity, 91% coverage: 31:347/348 of query aligns to 6:313/321 of P37595
Q7L266 Isoaspartyl peptidase/L-asparaginase; Asparaginase-like protein 1; Beta-aspartyl-peptidase; Isoaspartyl dipeptidase; L-asparagine amidohydrolase; EC 3.4.19.5; EC 3.5.1.1 from Homo sapiens (Human) (see 4 papers)
40% identity, 90% coverage: 27:338/348 of query aligns to 2:292/308 of Q7L266
4pvrA Crystal structure of partially-cleaved human l-asparaginase protein in complex with l-aspartate (see paper)
39% identity, 90% coverage: 27:338/348 of query aligns to 3:282/298 of 4pvrA
4osxA Structure of uncleaved glycine-bound human l-asparaginase protein (see paper)
39% identity, 90% coverage: 27:338/348 of query aligns to 3:284/300 of 4osxA
4o0hA Crystal structure of human l-asparaginase protein with covalently linked substrate l-asparagine (see paper)
38% identity, 90% coverage: 27:338/348 of query aligns to 3:279/295 of 4o0hA
4o48A Crystal structure of cleaved guinea pig l-asparaginase type iii in complex with l-aspartate (see paper)
39% identity, 90% coverage: 27:338/348 of query aligns to 3:282/298 of 4o48A
8c0iAAA Isoaspartyl peptidase subunit alpha (see paper)
52% identity, 44% coverage: 31:182/348 of query aligns to 5:156/156 of 8c0iAAA
1jn9A Structure of putative asparaginase encoded by escherichia coli ybik gene (see paper)
52% identity, 44% coverage: 31:182/348 of query aligns to 5:156/158 of 1jn9A
Q47898 N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase; Aspartylglucosaminidase; AGA; Glycosylasparaginase; N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase; EC 3.5.1.26 from Elizabethkingia miricola (Chryseobacterium miricola) (see 5 papers)
40% identity, 77% coverage: 65:332/348 of query aligns to 67:313/340 of Q47898
Sites not aligning to the query:
1p4vA Crystal structure of the glycosylasparaginase precursor d151n mutant with glycine (see paper)
39% identity, 77% coverage: 65:332/348 of query aligns to 22:268/295 of 1p4vA
4r4yA Structural basis of a point mutation that causes the genetic disease aspartylglucosaminuria (see paper)
39% identity, 77% coverage: 65:332/348 of query aligns to 20:266/293 of 4r4yA
2zalB Crystal structure of e. Coli isoaspartyl aminopeptidase/l-asparaginase in complex with l-aspartate (see paper)
56% identity, 39% coverage: 213:347/348 of query aligns to 1:135/135 of 2zalB
8c23DDD Isoaspartyl peptidase subunit beta (see paper)
55% identity, 39% coverage: 213:347/348 of query aligns to 1:135/135 of 8c23DDD
2gezB Crystal structure of potassium-independent plant asparaginase (see paper)
53% identity, 38% coverage: 213:345/348 of query aligns to 1:130/133 of 2gezB
Q9H6P5 Threonine aspartase 1; Taspase-1; EC 3.4.25.- from Homo sapiens (Human) (see 2 papers)
32% identity, 85% coverage: 31:327/348 of query aligns to 44:359/420 of Q9H6P5
2a8jB Crystal structure of human taspase1 (acivated form) (see paper)
31% identity, 82% coverage: 31:314/348 of query aligns to 4:253/313 of 2a8jB
4pv2C Crystal structure of potassium-dependent plant-type l-asparaginase from phaseolus vulgaris in complex with k+ and na+ cations (see paper)
41% identity, 44% coverage: 29:182/348 of query aligns to 3:154/158 of 4pv2C
2gezC Crystal structure of potassium-independent plant asparaginase (see paper)
40% identity, 43% coverage: 29:178/348 of query aligns to 3:151/166 of 2gezC
4pu6B Crystal structure of potassium-dependent plant-type l-asparaginase from phaseolus vulgaris in complex with k+ cations (see paper)
47% identity, 38% coverage: 213:345/348 of query aligns to 1:130/131 of 4pu6B
P20933 N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase; Aspartylglucosaminidase; Glycosylasparaginase; N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase; EC 3.5.1.26 from Homo sapiens (Human) (see 11 papers)
32% identity, 62% coverage: 57:273/348 of query aligns to 36:266/346 of P20933
Sites not aligning to the query:
>5209718 FitnessBrowser__PV4:5209718
MRSTITPSLLAGLMGLLISTSTVAETQPFSIAIHGGAGTISKANLTEAQQQAYRDKLKEA
VDAGYKVLEKGGDSLTAVTTAINILEDSPLFNAGKGAVYTYDGTHEMDASIMDGRNLNAG
AVAGVKHIKNPINLARAVMDKSPHVMLSGQGAEEFALSQDFSLVPVTYFDTESRYQQLID
AKAKLKAAESKEAGKPDYQASVNYLDLDYKFGTVGAVALDKQGNLAAGTSTGGMTVKRFG
RIGDSPVIGAGTYAENQVCAVSATGHGEYFIRYHVAGDICAKVKYQQKSILQAADEVINQ
RLITAGGTGGVIAIDQRGNIATPFNTEGMYRATRKGGEPAKVMIWQDN
Or try a new SitesBLAST search
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