SitesBLAST
Comparing WP_057506797.1 NCBI__GCF_001431535.1:WP_057506797.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
Q9VLJ8 Adenylyltransferase and sulfurtransferase MOCS3; Molybdenum cofactor synthesis protein 3; Ubiquitin activating enzyme 4; EC 2.7.7.80; EC 2.8.1.11 from Drosophila melanogaster (Fruit fly) (see paper)
48% identity, 68% coverage: 118:375/380 of query aligns to 71:325/453 of Q9VLJ8
Sites not aligning to the query:
- 62 modified: Phosphothreonine
Q72J02 Sulfur carrier protein adenylyltransferase; E1-like protein TtuC; Sulfur carrier protein MoaD adenylyltransferase; Sulfur carrier protein ThiS adenylyltransferase; Sulfur carrier protein TtuB adenylyltransferase; tRNA two-thiouridine-synthesizing protein C; EC 2.7.7.80; EC 2.7.7.73; EC 2.7.7.- from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
52% identity, 68% coverage: 117:375/380 of query aligns to 9:268/271 of Q72J02
- C192 (= C299) modified: Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in TtuB); mutation to S: Not able to form a thioester complex with TtuB.
- C268 (= C375) mutation to S: Still able to form a thioester complex with TtuB.
D4GSF3 SAMP-activating enzyme E1; Ubiquitin-like activating enzyme of archaea; Ubl-activating enzyme; EC 2.7.7.- from Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) (see paper)
51% identity, 68% coverage: 117:376/380 of query aligns to 11:266/270 of D4GSF3
- C188 (= C299) mutation to S: Loss of activity since this mutant is not able to complement a ubaA deletion in trans to restore sampylation and tRNA thiolation.
O95396 Adenylyltransferase and sulfurtransferase MOCS3; Molybdenum cofactor synthesis protein 3; Molybdopterin synthase sulfurylase; MPT synthase sulfurylase; EC 2.7.7.80; EC 2.8.1.11 from Homo sapiens (Human) (see 5 papers)
47% identity, 72% coverage: 106:377/380 of query aligns to 50:318/460 of O95396
- 158:238 (vs. 214:298, 48% identical) Interaction with NFS1
- C239 (= C299) mutation to A: Impairs sulfurtransferase activity.
- C316 (= C375) modified: Disulfide link with 324; mutation to A: Does not affect sulfurtransferase activity.
Sites not aligning to the query:
- 324 modified: Disulfide link with 316; C→A: Does not affect sulfurtransferase activity.
- 365 C→A: Does not affect sulfurtransferase activity.
- 412 active site, Cysteine persulfide intermediate; for sulfurtransferase activity; modified: Cysteine persulfide; C→A: Abolishes sulfurtransferase activity.
- 413 K→R: Does not affect sulfurtransferase specificity and activity.
- 414 L→K: Does not affect sulfurtransferase specificity and activity.
- 415 G→A: Does not affect sulfurtransferase specificity and activity.
- 416 N→V: Does not affect sulfurtransferase specificity and activity.
- 417 D→R: Results in 470-fold increased activity.; D→T: Results in 90-fold increased activity.
- 458 P→G: Does not affect sulfurtransferase specificity and activity.
- 460 Y→A: Does not affect sulfurtransferase specificity and activity.
P12282 Molybdopterin-synthase adenylyltransferase; MoaD protein adenylase; Molybdopterin-converting factor subunit 1 adenylase; Sulfur carrier protein MoaD adenylyltransferase; EC 2.7.7.80 from Escherichia coli (strain K12) (see 2 papers)
46% identity, 64% coverage: 118:359/380 of query aligns to 11:247/249 of P12282
- R14 (= R121) mutation R->A,K: No effect.; mutation to A: No activity; when associated with A-73.
- C44 (≠ S151) mutation to A: No effect.
- R73 (= R180) mutation to A: No effect. No activity; when associated with A-14.; mutation to K: Substantially reduced activity.
- C128 (≠ G235) mutation to A: No effect.; mutation to Y: No activity.
- D130 (= D237) mutation to A: No activity.; mutation to E: Substantially reduced activity.
- C142 (= C249) mutation to A: No effect.
- C172 (= C282) mutation to A: No zinc bound and no enzyme activity.
- C175 (= C285) mutation to A: No zinc bound and no enzyme activity.
- C187 (= C299) mutation to A: No effect.
- C231 (≠ M343) mutation to A: No effect.
- C244 (= C356) mutation to A: No zinc bound and almost no enzyme activity.
- C247 (= C359) mutation to A: No zinc bound and almost no enzyme activity.
O59954 Adenylyltransferase and sulfurtransferase uba4; Common component for nitrate reductase and xanthine dehydrogenase protein F; Ubiquitin-like protein activator 4; EC 2.7.7.80; EC 2.8.1.11 from Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) (see paper)
42% identity, 68% coverage: 116:375/380 of query aligns to 66:340/482 of O59954
- G82 (= G132) mutation to D: In cnxF21ts and cnxF24ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.
- G100 (= G150) mutation to S: In cnxF1285; impairs molybdopterin biosynthesis.
- R130 (= R180) mutation to Q: In cnxF200; impairs molybdopterin biosynthesis.
- C185 (≠ G235) mutation to Y: In cnxF472; impairs molybdopterin biosynthesis.
- E215 (≠ D265) mutation to K: In cnxF119; impairs molybdopterin biosynthesis.
- G264 (= G310) mutation to S: In cnxF142ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.
1jwbB Structure of the covalent acyl-adenylate form of the moeb-moad protein complex (see paper)
45% identity, 64% coverage: 118:359/380 of query aligns to 10:239/240 of 1jwbB
- active site: R13 (= R121), D129 (= D237)
- binding adenosine monophosphate: G37 (= G145), G39 (= G147), G40 (= G148), D61 (= D169), F62 (≠ D170), K85 (= K193), L108 (≠ R216), C127 (≠ G235), T128 (≠ S236), D129 (= D237), N130 (= N238), V133 (≠ L241)
- binding zinc ion: C171 (= C282), C236 (= C356), C239 (= C359)
1jw9B Structure of the native moeb-moad protein complex (see paper)
45% identity, 64% coverage: 118:359/380 of query aligns to 10:239/240 of 1jw9B
P38820 Adenylyltransferase and sulfurtransferase UBA4; Needs CLA4 to survive protein 3; Ubiquitin-like protein activator 4; EC 2.7.7.-; EC 2.8.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 4 papers)
37% identity, 74% coverage: 95:375/380 of query aligns to 15:311/440 of P38820
- C225 (= C299) mutation C->A,S: Abolishes adenylyltransferase activity but not sulfurtransferase activity.
Sites not aligning to the query:
- 397 mutation C->A,S: Abolishes sulfurtransferase activity but not adenylyltransferase activity.
1zfnA Structural analysis of escherichia coli thif (see paper)
45% identity, 66% coverage: 111:359/380 of query aligns to 2:243/244 of 1zfnA
- active site: R11 (= R121), D127 (= D237)
- binding adenosine-5'-triphosphate: I34 (≠ L144), G35 (= G145), G37 (= G147), G38 (= G148), D59 (= D169), R70 (= R180), Q71 (= Q181), K83 (= K193), T126 (≠ S236), D127 (= D237), T131 (≠ L241)
- binding zinc ion: C169 (= C282), C172 (= C285), C240 (= C356), C243 (= C359)
P30138 Sulfur carrier protein ThiS adenylyltransferase; EC 2.7.7.73 from Escherichia coli (strain K12) (see 3 papers)
45% identity, 66% coverage: 111:359/380 of query aligns to 2:243/251 of P30138
- C169 (= C282) binding
- C172 (= C285) binding
- W174 (≠ F287) mutation to A: No adenylation of ThiS.
- C184 (= C299) mutation to S: No cross-link formed with ThiS. No effect on ThiS thiocarboxylate formation in vitro. Does not support growth.
- C240 (= C356) binding
- C243 (= C359) binding
1jwaB Structure of the atp-bound moeb-moad protein complex (see paper)
41% identity, 61% coverage: 118:350/380 of query aligns to 10:215/217 of 1jwaB
- active site: R13 (= R121), D129 (= D237)
- binding adenosine-5'-triphosphate: G39 (= G147), G40 (= G148), D61 (= D169), F62 (≠ D170), R72 (= R180), K85 (= K193), L108 (≠ R216), D129 (= D237), N130 (= N238), V133 (≠ L241)
1zud3 Structure of this-thif protein complex (see paper)
44% identity, 66% coverage: 111:359/380 of query aligns to 2:238/240 of 1zud3
6yubA Crystal structure of uba4 from chaetomium thermophilum (see paper)
40% identity, 55% coverage: 117:325/380 of query aligns to 12:214/423 of 6yubA
Sites not aligning to the query:
6yubB Crystal structure of uba4 from chaetomium thermophilum (see paper)
40% identity, 55% coverage: 117:325/380 of query aligns to 13:213/289 of 6yubB
Sites not aligning to the query:
3h9jA Crystal structure of e. Coli mccb + ampcpp + semet mcca (see paper)
25% identity, 66% coverage: 108:359/380 of query aligns to 81:337/339 of 3h9jA
- active site: R157 (= R180)
- binding diphosphomethylphosphonic acid adenosyl ester: G124 (= G147), G125 (= G148), D146 (= D169), D148 (= D171), R157 (= R180), K170 (= K193), N193 (= N221), I194 (= I222), A213 (≠ S236), D214 (= D237), H215 (≠ N238)
- binding zinc ion: C257 (= C282), C334 (= C356), C337 (= C359)
- binding : R313 (≠ L335), G315 (≠ R337)
3h5nA Crystal structure of e. Coli mccb + atp (see paper)
25% identity, 66% coverage: 108:359/380 of query aligns to 81:337/338 of 3h5nA
- active site: R157 (= R180)
- binding adenosine-5'-triphosphate: G124 (= G147), D146 (= D169), N154 (= N177), R157 (= R180), Q158 (= Q181), K170 (= K193), N193 (= N221), I194 (= I222), A213 (≠ S236), D214 (= D237), H215 (≠ N238)
- binding zinc ion: C257 (= C282), C260 (= C285), C334 (= C356), C337 (= C359)
3h5rA Crystal structure of e. Coli mccb + succinimide (see paper)
25% identity, 66% coverage: 108:359/380 of query aligns to 81:338/340 of 3h5rA
- active site: R157 (= R180)
- binding zinc ion: C257 (= C282), C260 (= C285), C335 (= C356), C338 (= C359)
- binding : I126 (≠ L149), S212 (≠ G235), A213 (≠ S236), A237 (= A259), G238 (≠ A260), Y239 (≠ F264), V245 (= V270), P280 (= P292), R314 (≠ L335), G316 (≠ R337)
Sites not aligning to the query:
3h5aC Crystal structure of e. Coli mccb (see paper)
24% identity, 66% coverage: 108:359/380 of query aligns to 81:346/358 of 3h5aC
6om4B The structure of microcin c7 biosynthetic enzyme mccb in complex with n-formylated mcca (see paper)
24% identity, 60% coverage: 133:359/380 of query aligns to 107:343/344 of 6om4B
- binding magnesium ion: D145 (= D171), E148 (= E174)
- binding 5'-O-[(S)-amino(hydroxy)phosphoryl]adenosine: G121 (= G147), D143 (= D169), N144 (≠ D170), K167 (= K193), I191 (= I222), S209 (≠ G235), A210 (≠ S236), D211 (= D237), H212 (≠ N238)
- binding pyrophosphate 2-: N151 (= N177), R154 (= R180), Q155 (= Q181), K167 (= K193)
- binding zinc ion: C254 (= C282), C257 (= C285), C340 (= C356), C343 (= C359)
- binding : I123 (≠ L149), S209 (≠ G235), A210 (≠ S236), D211 (= D237), N233 (≠ Y258), A234 (= A259), G235 (≠ A260), Y236 (≠ F264), V237 (≠ D265), V242 (= V270), V261 (vs. gap), A262 (vs. gap), Y265 (vs. gap), R319 (≠ L335), G321 (≠ R337), W323 (≠ D339), Q332 (≠ T348)
Sites not aligning to the query:
Query Sequence
>WP_057506797.1 NCBI__GCF_001431535.1:WP_057506797.1
MRIPEITPELALQRLSEGAVLIDVREPHERAGGMAEGARGIALADLQAAPATHLPRLEQD
ILLICQTGKRSADAARFLHAAGYTQVASVAGGTVAWRLQQLPLVQPAGSAEDRDFHDRYS
RHLLLPQVGVDGQRLLQRSRVLVLGAGGLGSPAGFYLAAAGVGQLRFVDDDRVERSNLHR
QIVHTDASVGQYKVDSARERLLALNPSIAIEAIAERATSANIDALMDGVDVVLDGSDNFP
LRYLLNDACIKHATPLVYAAIERFDGQVSVFDAGRQRGVAPCYRCLFPQPPPPEFAPNCA
EAGVLGALPGLAGVLQATEVLKLLLGIGEPLTGRLLRFDALSMRFRETRLSPDPHCAVCA
PGQDFPGYIDYAAFCSNPQR
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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