SitesBLAST
Comparing WP_275452883.1 NCBI__GCF_001431535.1:WP_275452883.1 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)
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, 67% coverage: 124:381/386 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, 67% coverage: 123:381/386 of query aligns to 9:268/271 of Q72J02
- C192 (= C305) 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 (= C381) 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, 67% coverage: 123:382/386 of query aligns to 11:266/270 of D4GSF3
- C188 (= C305) 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, 70% coverage: 112:383/386 of query aligns to 50:318/460 of O95396
- 158:238 (vs. 220:304, 48% identical) Interaction with NFS1
- C239 (= C305) mutation to A: Impairs sulfurtransferase activity.
- C316 (= C381) 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, 63% coverage: 124:365/386 of query aligns to 11:247/249 of P12282
- R14 (= R127) mutation R->A,K: No effect.; mutation to A: No activity; when associated with A-73.
- C44 (≠ S157) mutation to A: No effect.
- R73 (= R186) mutation to A: No effect. No activity; when associated with A-14.; mutation to K: Substantially reduced activity.
- C128 (≠ G241) mutation to A: No effect.; mutation to Y: No activity.
- D130 (= D243) mutation to A: No activity.; mutation to E: Substantially reduced activity.
- C142 (= C255) mutation to A: No effect.
- C172 (= C288) mutation to A: No zinc bound and no enzyme activity.
- C175 (= C291) mutation to A: No zinc bound and no enzyme activity.
- C187 (= C305) mutation to A: No effect.
- C231 (≠ M349) mutation to A: No effect.
- C244 (= C362) mutation to A: No zinc bound and almost no enzyme activity.
- C247 (= C365) 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, 67% coverage: 122:381/386 of query aligns to 66:340/482 of O59954
- G82 (= G138) mutation to D: In cnxF21ts and cnxF24ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.
- G100 (= G156) mutation to S: In cnxF1285; impairs molybdopterin biosynthesis.
- R130 (= R186) mutation to Q: In cnxF200; impairs molybdopterin biosynthesis.
- C185 (≠ G241) mutation to Y: In cnxF472; impairs molybdopterin biosynthesis.
- E215 (≠ D271) mutation to K: In cnxF119; impairs molybdopterin biosynthesis.
- G264 (= G316) 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, 63% coverage: 124:365/386 of query aligns to 10:239/240 of 1jwbB
- active site: R13 (= R127), D129 (= D243)
- binding adenosine monophosphate: G37 (= G151), G39 (= G153), G40 (= G154), D61 (= D175), F62 (≠ D176), K85 (= K199), L108 (≠ R222), C127 (≠ G241), T128 (≠ S242), D129 (= D243), N130 (= N244), V133 (≠ L247)
- binding zinc ion: C171 (= C288), C236 (= C362), C239 (= C365)
1jw9B Structure of the native moeb-moad protein complex (see paper)
45% identity, 63% coverage: 124:365/386 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, 73% coverage: 101:381/386 of query aligns to 15:311/440 of P38820
- C225 (= C305) 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, 65% coverage: 117:365/386 of query aligns to 2:243/244 of 1zfnA
- active site: R11 (= R127), D127 (= D243)
- binding adenosine-5'-triphosphate: I34 (≠ L150), G35 (= G151), G37 (= G153), G38 (= G154), D59 (= D175), R70 (= R186), Q71 (= Q187), K83 (= K199), T126 (≠ S242), D127 (= D243), T131 (≠ L247)
- binding zinc ion: C169 (= C288), C172 (= C291), C240 (= C362), C243 (= C365)
P30138 Sulfur carrier protein ThiS adenylyltransferase; EC 2.7.7.73 from Escherichia coli (strain K12) (see 3 papers)
45% identity, 65% coverage: 117:365/386 of query aligns to 2:243/251 of P30138
- C169 (= C288) binding
- C172 (= C291) binding
- W174 (≠ F293) mutation to A: No adenylation of ThiS.
- C184 (= C305) mutation to S: No cross-link formed with ThiS. No effect on ThiS thiocarboxylate formation in vitro. Does not support growth.
- C240 (= C362) binding
- C243 (= C365) binding
1jwaB Structure of the atp-bound moeb-moad protein complex (see paper)
41% identity, 60% coverage: 124:356/386 of query aligns to 10:215/217 of 1jwaB
- active site: R13 (= R127), D129 (= D243)
- binding adenosine-5'-triphosphate: G39 (= G153), G40 (= G154), D61 (= D175), F62 (≠ D176), R72 (= R186), K85 (= K199), L108 (≠ R222), D129 (= D243), N130 (= N244), V133 (≠ L247)
1zud3 Structure of this-thif protein complex (see paper)
44% identity, 65% coverage: 117:365/386 of query aligns to 2:238/240 of 1zud3
6yubA Crystal structure of uba4 from chaetomium thermophilum (see paper)
40% identity, 54% coverage: 123:331/386 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, 54% coverage: 123:331/386 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, 65% coverage: 114:365/386 of query aligns to 81:337/339 of 3h9jA
- active site: R157 (= R186)
- binding diphosphomethylphosphonic acid adenosyl ester: G124 (= G153), G125 (= G154), D146 (= D175), D148 (= D177), R157 (= R186), K170 (= K199), N193 (= N227), I194 (= I228), A213 (≠ S242), D214 (= D243), H215 (≠ N244)
- binding zinc ion: C257 (= C288), C334 (= C362), C337 (= C365)
- binding : R313 (≠ L341), G315 (≠ R343)
3h5nA Crystal structure of e. Coli mccb + atp (see paper)
25% identity, 65% coverage: 114:365/386 of query aligns to 81:337/338 of 3h5nA
- active site: R157 (= R186)
- binding adenosine-5'-triphosphate: G124 (= G153), D146 (= D175), N154 (= N183), R157 (= R186), Q158 (= Q187), K170 (= K199), N193 (= N227), I194 (= I228), A213 (≠ S242), D214 (= D243), H215 (≠ N244)
- binding zinc ion: C257 (= C288), C260 (= C291), C334 (= C362), C337 (= C365)
3h5rA Crystal structure of e. Coli mccb + succinimide (see paper)
25% identity, 65% coverage: 114:365/386 of query aligns to 81:338/340 of 3h5rA
- active site: R157 (= R186)
- binding zinc ion: C257 (= C288), C260 (= C291), C335 (= C362), C338 (= C365)
- binding : I126 (≠ L155), S212 (≠ G241), A213 (≠ S242), A237 (= A265), G238 (≠ A266), Y239 (≠ F270), V245 (= V276), P280 (= P298), R314 (≠ L341), G316 (≠ R343)
Sites not aligning to the query:
3h5aC Crystal structure of e. Coli mccb (see paper)
24% identity, 65% coverage: 114:365/386 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, 59% coverage: 139:365/386 of query aligns to 107:343/344 of 6om4B
- binding magnesium ion: D145 (= D177), E148 (= E180)
- binding 5'-O-[(S)-amino(hydroxy)phosphoryl]adenosine: G121 (= G153), D143 (= D175), N144 (≠ D176), K167 (= K199), I191 (= I228), S209 (≠ G241), A210 (≠ S242), D211 (= D243), H212 (≠ N244)
- binding pyrophosphate 2-: N151 (= N183), R154 (= R186), Q155 (= Q187), K167 (= K199)
- binding zinc ion: C254 (= C288), C257 (= C291), C340 (= C362), C343 (= C365)
- binding : I123 (≠ L155), S209 (≠ G241), A210 (≠ S242), D211 (= D243), N233 (≠ Y264), A234 (= A265), G235 (≠ A266), Y236 (≠ F270), V237 (≠ D271), V242 (= V276), V261 (vs. gap), A262 (vs. gap), Y265 (vs. gap), R319 (≠ L341), G321 (≠ R343), W323 (≠ D345), Q332 (≠ T354)
Sites not aligning to the query:
Query Sequence
>WP_275452883.1 NCBI__GCF_001431535.1:WP_275452883.1
MADNVAMRIPEITPELALQRLSEGAVLIDVREPHERAGGMAEGARGIALADLQAAPATHL
PRLEQDILLICQTGKRSADAARFLHAAGYTQVASVAGGTVAWRLQQLPLVQPAGSAEDRD
FHDRYSRHLLLPQVGVDGQRLLQRSRVLVLGAGGLGSPAGFYLAAAGVGQLRFVDDDRVE
RSNLHRQIVHTDASVGQYKVDSARERLLALNPSIAIEAIAERATSANIDALMDGVDVVLD
GSDNFPLRYLLNDACIKHATPLVYAAIERFDGQVSVFDAGRQRGVAPCYRCLFPQPPPPE
FAPNCAEAGVLGALPGLAGVLQATEVLKLLLGIGEPLTGRLLRFDALSMRFRETRLSPDP
HCAVCAPGQDFPGYIDYAAFCSNPQR
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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