SitesBLAST
Comparing WP_013260052.1 NCBI__GCF_000143965.1:WP_013260052.1 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)
8qhpA Cysteine tRNA ligase homodimer (see paper)
39% identity, 53% coverage: 309:719/775 of query aligns to 3:404/410 of 8qhpA
Q06752 Cysteine--tRNA ligase; Cysteinyl-tRNA synthetase; CysRS; EC 6.1.1.16 from Bacillus subtilis (strain 168) (see paper)
34% identity, 60% coverage: 309:775/775 of query aligns to 3:465/466 of Q06752
- S270 (≠ V581) modified: Phosphoserine
1u0bB Crystal structure of cysteinyl-tRNA synthetase binary complex with trnacys (see paper)
36% identity, 60% coverage: 309:774/775 of query aligns to 2:460/461 of 1u0bB
- active site: H37 (≠ D344), H40 (≠ L347)
- binding zinc ion: C28 (= C335), C209 (= C520), H234 (= H545), E238 (= E549)
- binding : R10 (= R317), G39 (= G346), H40 (≠ L347), T43 (≠ R350), Q158 (≠ V464), G166 (= G472), A167 (≠ K473), R168 (≠ T474), W205 (= W516), G227 (≠ S538), L230 (= L541), F232 (= F543), M259 (≠ V570), V260 (= V571), M261 (≠ V572), M267 (≠ A578), G296 (≠ Q608), H297 (= H609), Q301 (≠ A613), Q311 (≠ L623), A315 (≠ T627), R318 (= R630), T321 (≠ D633), N351 (≠ G673), P353 (≠ A675), E354 (≠ K676), S357 (≠ G679), F360 (= F682), R364 (≠ K686), N367 (= N689), R427 (= R741), W432 (≠ F746), D436 (= D750), R439 (= R753), L449 (≠ V763), E450 (≠ A764), D451 (= D765), R459 (≠ H773)
P21888 Cysteine--tRNA ligase; Cysteinyl-tRNA synthetase; CysRS; EC 6.1.1.16 from Escherichia coli (strain K12) (see 4 papers)
36% identity, 60% coverage: 309:774/775 of query aligns to 2:460/461 of P21888
- C28 (= C335) binding Zn(2+); mutation C->D,S: No effect on cysteine persulfide synthase activity. Loss of cysteine--tRNA ligase activity; when associated with S-209.
- G29 (= G336) binding L-cysteine
- T68 (≠ A375) binding L-cysteine
- K73 (≠ R380) mutation to A: Strongly decreases cysteine persulfide synthase activity.
- KIIK 73:76 (≠ RTVN 380:383) mutation to AIIA: Strongly decreases cysteine persulfide synthase activity.
- K76 (≠ N383) mutation to A: Strongly decreases cysteine persulfide synthase activity.
- W205 (= W516) mutation to Y: Reduces cysteine binding. Strongly reduces cysteine--tRNA ligase activity.
- C209 (= C520) binding Zn(2+); mutation to D: No effect on cysteine persulfide synthase; when associated with C-28.; mutation to S: Loss of cysteine--tRNA ligase activity; when associated with S-28.
- H234 (= H545) binding L-cysteine; binding Zn(2+)
- E238 (= E549) binding Zn(2+)
- K266 (= K577) mutation to A: Strongly decreases cysteine persulfide synthase activity.
- KMSK 266:269 (≠ KANR 577:580) mutation to AMSA: Strongly decreases cysteine persulfide synthase activity.
- K269 (≠ R580) mutation to A: Strongly decreases cysteine persulfide synthase activity.
1li7A Crystal structure of cysteinyl-tRNA synthetase with cysteine substrate bound (see paper)
35% identity, 53% coverage: 309:719/775 of query aligns to 2:378/386 of 1li7A
- active site: H37 (≠ D344), H40 (≠ L347)
- binding cysteine: C28 (= C335), G29 (= G336), I30 (≠ P337), T31 (≠ S338), T68 (≠ A375), W189 (= W516), L214 (= L541), H218 (= H545)
- binding zinc ion: C28 (= C335), C193 (= C520), H218 (= H545)
2q3dA 2.2 a resolution crystal structure of o-acetylserine sulfhydrylase (oass) from mycobacterium tuberculosis in complex with the reaction intermediate alpha-aminoacrylate (see paper)
47% identity, 38% coverage: 3:300/775 of query aligns to 1:305/306 of 2q3dA
- active site: K44 (= K46), S266 (= S263), P293 (= P288)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K46), T71 (= T73), S72 (= S74), N74 (= N76), T75 (= T77), Q144 (= Q147), V177 (≠ L181), G178 (= G182), T179 (= T183), G180 (≠ S184), T182 (= T186), G222 (≠ N219), I223 (≠ M220), S266 (= S263), P293 (= P288), D294 (= D289)
P9WP55 O-acetylserine sulfhydrylase; OAS sulfhydrylase; OASS; Cysteine synthase A; CSase A; O-acetylserine (thiol)-lyase A; OAS-TL A; O-acetylserine-specific cysteine synthase; Sulfide-dependent cysteine synthase; EC 2.5.1.47 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
47% identity, 38% coverage: 3:300/775 of query aligns to 1:305/310 of P9WP55
- K44 (= K46) modified: N6-(pyridoxal phosphate)lysine
- N74 (= N76) binding pyridoxal 5'-phosphate
- GTGGT 178:182 (≠ GTSGT 182:186) binding pyridoxal 5'-phosphate
- S266 (= S263) binding pyridoxal 5'-phosphate
3tqoA Structure of the cysteinyl-tRNA synthetase (cyss) from coxiella burnetii. (see paper)
34% identity, 53% coverage: 309:721/775 of query aligns to 5:381/387 of 3tqoA
3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
46% identity, 38% coverage: 3:295/775 of query aligns to 1:300/300 of 3zeiA
- active site: K44 (= K46), S266 (= S263), P293 (= P288)
- binding 3-[(Z)-[(5Z)-5-[[2-(2-hydroxy-2-oxoethyloxy)phenyl]methylidene]-3-methyl-4-oxidanylidene-1,3-thiazolidin-2-ylidene]amino]benzoic acid: T71 (= T73), S72 (= S74), I126 (= I128), Q144 (= Q147), F145 (= F148), K215 (vs. gap), G222 (≠ N219), A225 (≠ E222), F227 (≠ L224)
- binding pyridoxal-5'-phosphate: K44 (= K46), N74 (= N76), V177 (≠ L181), G178 (= G182), T179 (= T183), G180 (≠ S184), T182 (= T186), G222 (≠ N219), S266 (= S263), P293 (= P288), D294 (= D289)
2q3cA 2.1 a resolution crystal structure of o-acetylserine sulfhydrylase (oass) holoenzyme from mycobacterium tuberculosis in complex with the inhibitory peptide dfsi (see paper)
46% identity, 38% coverage: 3:295/775 of query aligns to 1:300/300 of 2q3cA
- active site: K44 (= K46), S266 (= S263), P293 (= P288)
- binding : T71 (= T73), S72 (= S74), G73 (= G75), T75 (= T77), M122 (≠ T124), Q144 (= Q147), K215 (vs. gap), G222 (≠ N219), A225 (≠ E222)
1li7B Crystal structure of cysteinyl-tRNA synthetase with cysteine substrate bound (see paper)
35% identity, 53% coverage: 309:719/775 of query aligns to 2:367/375 of 1li7B
P16703 Cysteine synthase B; CSase B; O-acetylserine (thiol)-lyase B; OAS-TL B; O-acetylserine sulfhydrylase B; EC 2.5.1.47 from Escherichia coli (strain K12) (see paper)
42% identity, 38% coverage: 11:303/775 of query aligns to 6:295/303 of P16703
- N71 (= N76) binding pyridoxal 5'-phosphate
- S255 (= S263) binding pyridoxal 5'-phosphate
2bhtA Crystal structure of o-acetylserine sulfhydrylase b (see paper)
42% identity, 37% coverage: 11:300/775 of query aligns to 6:292/294 of 2bhtA
- active site: K41 (= K46), S69 (= S74), Q199 (≠ E207), G203 (= G211), S255 (= S263), C280 (≠ P288)
- binding pyridoxal-5'-phosphate: K41 (= K46), N71 (= N76), M173 (≠ L181), G174 (= G182), T175 (= T183), T176 (≠ S184), T178 (= T186), G208 (= G216), S255 (= S263), C280 (≠ P288)
5xemA Crystal structure of a hydrogen sulfide-producing enzyme (fn1220) from fusobacterium nucleatum in complex with l-lanthionine-plp schiff base
41% identity, 38% coverage: 5:297/775 of query aligns to 2:302/302 of 5xemA
- binding (2R)-2-azanyl-3-[(2R)-2-azanyl-3-oxidanyl-3-oxidanylidene-propyl]sulfanyl-propanoic acid: K42 (= K46), T69 (= T73), S70 (= S74), N72 (= N76), T73 (= T77), M120 (≠ T124), Q142 (= Q147), G176 (= G182), T177 (= T183), G220 (= G216), M221 (≠ L217), G222 (≠ N219), S224 (≠ K221)
- binding calcium ion: L300 (= L295), S301 (= S296), N302 (≠ T297)
- binding pyridoxal-5'-phosphate: K42 (= K46), N72 (= N76), T175 (≠ L181), G176 (= G182), T177 (= T183), G178 (≠ S184), S180 (≠ T186), G220 (= G216), S266 (= S263), T293 (vs. gap), D294 (= D289)
5xenA Crystal structure of a hydrogen sulfide-producing enzyme (fn1220) from fusobacterium nucleatum in complex with l-serine-plp schiff base
41% identity, 38% coverage: 5:295/775 of query aligns to 2:300/300 of 5xenA
- binding pyridoxal-5'-phosphate: K42 (= K46), K42 (= K46), N72 (= N76), N72 (= N76), T175 (≠ L181), T175 (≠ L181), G176 (= G182), G176 (= G182), T177 (= T183), T177 (= T183), G178 (≠ S184), G178 (≠ S184), S180 (≠ T186), S180 (≠ T186), G220 (= G216), G220 (= G216), S266 (= S263), S266 (= S263), T293 (vs. gap), T293 (vs. gap), D294 (= D289), D294 (= D289)
- binding serine: K42 (= K46), T69 (= T73), S70 (= S74), N72 (= N76), T73 (= T77), Q142 (= Q147)
2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
45% identity, 37% coverage: 13:300/775 of query aligns to 7:301/302 of 2efyA
- active site: K40 (= K46), S70 (= S74), E200 (= E207), S204 (≠ G211), S263 (= S263)
- binding 5-oxohexanoic acid: T69 (= T73), G71 (= G75), T73 (= T77), Q141 (= Q147), G175 (= G182), G219 (≠ N219), M220 (= M220), P222 (≠ E222)
- binding pyridoxal-5'-phosphate: K40 (= K46), N72 (= N76), Y172 (≠ A179), G175 (= G182), T176 (= T183), G177 (≠ S184), T179 (= T186), G219 (≠ N219), S263 (= S263), P289 (= P288), D290 (= D289)
2ecqA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 3-hydroxylactate
45% identity, 37% coverage: 13:300/775 of query aligns to 7:301/302 of 2ecqA
- active site: K40 (= K46), S70 (= S74), E200 (= E207), S204 (≠ G211), S263 (= S263)
- binding (3s)-3-hydroxybutanoic acid: K40 (= K46), G71 (= G75), T73 (= T77), Q141 (= Q147), G219 (≠ N219)
- binding pyridoxal-5'-phosphate: K40 (= K46), N72 (= N76), Y172 (≠ A179), G173 (≠ T180), G175 (= G182), T176 (= T183), T179 (= T186), G219 (≠ N219), S263 (= S263), P289 (= P288)
2ecoA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-methylvalerate
45% identity, 37% coverage: 13:300/775 of query aligns to 7:301/302 of 2ecoA
- active site: K40 (= K46), S70 (= S74), E200 (= E207), S204 (≠ G211), S263 (= S263)
- binding 4-methyl valeric acid: K40 (= K46), T69 (= T73), G71 (= G75), T73 (= T77), Q141 (= Q147), G175 (= G182), T176 (= T183), G219 (≠ N219)
- binding pyridoxal-5'-phosphate: K40 (= K46), N72 (= N76), Y172 (≠ A179), G175 (= G182), T176 (= T183), T179 (= T186), G219 (≠ N219), S263 (= S263), P289 (= P288), D290 (= D289)
6ujdA Crystal structure of cysteine-tRNA ligase from elizabethkingia sp.
33% identity, 50% coverage: 309:695/775 of query aligns to 3:377/406 of 6ujdA
4lmbA Crystal structure analysis of o-acetylserine sulfhydrylase cysk2 complexed with cystine from microcystis aeruginosa 7806 (see paper)
44% identity, 38% coverage: 8:300/775 of query aligns to 6:308/310 of 4lmbA
- active site: K46 (= K46), S269 (= S263)
- binding cysteine: K46 (= K46), T74 (= T73), S75 (= S74), N77 (= N76), T78 (= T77), M101 (≠ A100), M125 (≠ T124), M125 (≠ T124), Q147 (= Q147), F148 (= F148), Q224 (= Q215), G225 (= G216), G225 (= G216), I226 (≠ L217), A228 (≠ E222)
- binding pyridoxal-5'-phosphate: K46 (= K46), N77 (= N76), V180 (≠ L181), G181 (= G182), T182 (= T183), G183 (≠ S184), T185 (= T186), G225 (= G216), S269 (= S263), P296 (= P288)
Query Sequence
>WP_013260052.1 NCBI__GCF_000143965.1:WP_013260052.1
MTLRMVDNVLELIGETPLVRLGRVTPLGGAPIYAKLEYLNPGGSVKDRAALRMLEAAEVS
GELTRDKIVLEATSGNTGIGLAMVCAVKGYRMLFTMSESASEERRKILRAYGADILLTPA
HLATDGAIEEAYRLAREEPERYFLVDQFNNYNNVMAHYQHGTADEIHRATQGRARVVVAT
LGTSGTAMGLAKRLHELDPAIKLVAVEPYQGHKIQGLKNMKESLRPGIFDPHLPDQIVNV
DDDAAYAMARRLAREEGIFVGMSAGAAVVAAVEQARGLSEGMVVAILPDGGERYLSTPLF
VSEKVPEPLKFFNTLTRRIDELRPVRPGRVGIYACGPSLDGPPDLGLCRRMIFADLLRRY
LELRGFEVKLVVNIADIDDRTVNQCLAEGAELKEFTARWEKAFHEDMAALNVLPASDYPK
ASEHIPEMIEETRKLLAKDLAYEKLRSVYFNISRYPNYGQLSHVDLNAIQKGKTVDFDYY
EKENPSDFTLFKRASLQELKAGVYWPTPWGNCRPGWHVECACMSAGHLGQPFDIHLASSD
LIFPHGDNEIAIAESLYGKPLANLWLHSEVVVVDGKKANRVQGNDVSLRELLEQGHSPQA
VRYWMLSQHYRRALRFAPEQLDLAERTVRRLNDFVARLRFLTPAPDDAQAEDVDQLIYET
RYRFQEAMDNDLGVAKAQGHIFAFIKAINRLAAGEGLTMAQIQKVLEFMQRLDSVLGVMN
FDGSSWDPAIEELVQKREQARADGDFALADRLREQLAEMGVQVADTPSGARWHRA
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