Comparing Pf1N1B4_3813 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_3813 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 7 hits to proteins with known functional sites (download)
Q9I2Y2 Phosphoserine phosphatase ThrH; PSP; PSPase; EC 3.1.3.3 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see paper)
89% identity, 100% coverage: 1:205/205 of query aligns to 1:205/205 of Q9I2Y2
1rkvA Structure of phosphate complex of thrh from pseudomonas aeruginosa (see paper)
89% identity, 100% coverage: 1:205/205 of query aligns to 2:206/206 of 1rkvA
1rkuA Crystal structure of thrh gene product of pseudomonas aeruginosa (see paper)
89% identity, 100% coverage: 1:205/205 of query aligns to 2:206/206 of 1rkuA
4ap9A Crystal structure of phosphoserine phosphatase from t.Onnurineus in complex with ndsb-201 (see paper)
32% identity, 87% coverage: 2:180/205 of query aligns to 10:180/200 of 4ap9A
1l7oA Crystal structure of phosphoserine phosphatase in apo form (see paper)
24% identity, 68% coverage: 33:172/205 of query aligns to 32:176/200 of 1l7oA
Sites not aligning to the query:
O53289 Phosphoserine phosphatase SerB2; PSP; PSPase; O-phosphoserine phosphohydrolase; Protein-serine/threonine phosphatase; EC 3.1.3.3; EC 3.1.3.16 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
30% identity, 60% coverage: 48:171/205 of query aligns to 230:360/409 of O53289
Sites not aligning to the query:
7qplA Crystal structure of phosphoserine phosphatase (serb) from brucella melitensis in complex with phosphate and magnesium
28% identity, 75% coverage: 39:192/205 of query aligns to 124:273/295 of 7qplA
Sites not aligning to the query:
>Pf1N1B4_3813 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_3813
VEIACLDLEGVLVPEIWIAFAEKTGIDSLRATTRDIPDYDVLMKQRLRILDEHGLKLSDI
QEVIATLKPLEGASEFVDWLRERFQVVILSDTFYEFSQPLMRQLGFPTLLCHRLITDDAG
RVTGYQLRQKDPKRQSVLAFKSLYYRVIAAGDSYNDTTMLGEADAGILFHAPDNVIREFP
QFPAVHSFAELKQEFIKASNRALSL
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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