SitesBLAST
Comparing WP_004313514.1 NCBI__GCF_000310185.1:WP_004313514.1 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)
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)
47% identity, 95% coverage: 1:247/260 of query aligns to 4:248/249 of P12282
- R14 (= R11) mutation R->A,K: No effect.; mutation to A: No activity; when associated with A-73.
- C44 (≠ S41) mutation to A: No effect.
- R73 (= R70) mutation to A: No effect. No activity; when associated with A-14.; mutation to K: Substantially reduced activity.
- C128 (= C125) mutation to A: No effect.; mutation to Y: No activity.
- D130 (= D127) mutation to A: No activity.; mutation to E: Substantially reduced activity.
- C142 (= C139) mutation to A: No effect.
- C172 (= C170) mutation to A: No zinc bound and no enzyme activity.
- C175 (= C173) mutation to A: No zinc bound and no enzyme activity.
- C187 (= C186) mutation to A: No effect.
- C231 (≠ M230) mutation to A: No effect.
- C244 (= C243) mutation to A: No zinc bound and almost no enzyme activity.
- C247 (= C246) mutation to A: No zinc bound and almost no enzyme activity.
1zfnA Structural analysis of escherichia coli thif (see paper)
53% identity, 95% coverage: 1:247/260 of query aligns to 1:244/244 of 1zfnA
- active site: R11 (= R11), D127 (= D127)
- binding adenosine-5'-triphosphate: I34 (≠ V34), G35 (= G35), G37 (= G37), G38 (= G38), D59 (= D59), R70 (= R70), Q71 (= Q71), K83 (= K83), T126 (= T126), D127 (= D127), T131 (= T131)
- binding zinc ion: C169 (= C170), C172 (= C173), C240 (= C243), C243 (= C246)
1jwbB Structure of the covalent acyl-adenylate form of the moeb-moad protein complex (see paper)
46% identity, 95% coverage: 1:247/260 of query aligns to 3:240/240 of 1jwbB
- active site: R13 (= R11), D129 (= D127)
- binding adenosine monophosphate: G37 (= G35), G39 (= G37), G40 (= G38), D61 (= D59), F62 (≠ H60), K85 (= K83), L108 (≠ R106), C127 (= C125), T128 (= T126), D129 (= D127), N130 (= N128), V133 (≠ T131)
- binding zinc ion: C171 (= C170), C236 (= C243), C239 (= C246)
1jw9B Structure of the native moeb-moad protein complex (see paper)
46% identity, 95% coverage: 1:247/260 of query aligns to 3:240/240 of 1jw9B
P30138 Sulfur carrier protein ThiS adenylyltransferase; EC 2.7.7.73 from Escherichia coli (strain K12) (see 3 papers)
53% identity, 95% coverage: 1:247/260 of query aligns to 1:244/251 of P30138
- C169 (= C170) binding Zn(2+)
- C172 (= C173) binding Zn(2+)
- W174 (≠ F175) mutation to A: No adenylation of ThiS.
- C184 (= C186) mutation to S: No cross-link formed with ThiS. No effect on ThiS thiocarboxylate formation in vitro. Does not support growth.
- C240 (= C243) binding Zn(2+)
- C243 (= C246) binding Zn(2+)
1zud3 Structure of this-thif protein complex (see paper)
52% identity, 95% coverage: 1:247/260 of query aligns to 1:239/240 of 1zud3
1jwaB Structure of the atp-bound moeb-moad protein complex (see paper)
44% identity, 92% coverage: 1:239/260 of query aligns to 3:217/217 of 1jwaB
- active site: R13 (= R11), D129 (= D127)
- binding adenosine-5'-triphosphate: G39 (= G37), G40 (= G38), D61 (= D59), F62 (≠ H60), R72 (= R70), K85 (= K83), L108 (≠ R106), D129 (= D127), N130 (= N128), V133 (≠ T131)
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)
43% identity, 95% coverage: 1:247/260 of query aligns to 64:310/453 of Q9VLJ8
Sites not aligning to the query:
- 62 modified: Phosphothreonine
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)
48% identity, 93% coverage: 5:247/260 of query aligns to 9:249/270 of D4GSF3
- C188 (= C186) 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.
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)
41% identity, 95% coverage: 1:246/260 of query aligns to 61:318/482 of O59954
- G82 (= G22) mutation to D: In cnxF21ts and cnxF24ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.
- G100 (= G40) mutation to S: In cnxF1285; impairs molybdopterin biosynthesis.
- R130 (= R70) mutation to Q: In cnxF200; impairs molybdopterin biosynthesis.
- C185 (= C125) mutation to Y: In cnxF472; impairs molybdopterin biosynthesis.
- E215 (≠ D155) mutation to K: In cnxF119; impairs molybdopterin biosynthesis.
- G264 (= G197) mutation to S: In cnxF142ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.
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)
45% identity, 95% coverage: 1:247/260 of query aligns to 55:301/460 of O95396
- 158:238 (vs. 104:185, 45% identical) Interaction with NFS1
- C239 (= C186) mutation to A: Impairs sulfurtransferase activity.
Sites not aligning to the query:
- 316 modified: Disulfide link with 324; C→A: Does not affect sulfurtransferase activity.
- 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.
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)
44% identity, 95% coverage: 2:247/260 of query aligns to 4:253/271 of Q72J02
- C192 (= C186) modified: Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in TtuB); mutation to S: Not able to form a thioester complex with TtuB.
Sites not aligning to the query:
- 268 C→S: Still able to form a thioester complex with TtuB.
6yubB Crystal structure of uba4 from chaetomium thermophilum (see paper)
39% identity, 82% coverage: 1:212/260 of query aligns to 7:213/289 of 6yubB
Sites not aligning to the query:
6yubA Crystal structure of uba4 from chaetomium thermophilum (see paper)
39% identity, 82% coverage: 1:212/260 of query aligns to 6:214/423 of 6yubA
Sites not aligning to the query:
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)
34% identity, 95% coverage: 4:250/260 of query aligns to 42:293/440 of P38820
- C225 (= C186) 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.
3h9jA Crystal structure of e. Coli mccb + ampcpp + semet mcca (see paper)
27% identity, 95% coverage: 2:248/260 of query aligns to 85:339/339 of 3h9jA
- active site: R157 (= R70)
- binding diphosphomethylphosphonic acid adenosyl ester: G124 (= G37), G125 (= G38), D146 (= D59), D148 (= D61), R157 (= R70), K170 (= K83), N193 (≠ R106), I194 (≠ L107), A213 (≠ T126), D214 (= D127), H215 (≠ N128)
- binding zinc ion: C257 (= C170), C334 (= C243), C337 (= C246)
- binding : R313 (= R221), G315 (≠ L223)
3h5nA Crystal structure of e. Coli mccb + atp (see paper)
27% identity, 95% coverage: 2:247/260 of query aligns to 85:338/338 of 3h5nA
- active site: R157 (= R70)
- binding adenosine-5'-triphosphate: G124 (= G37), D146 (= D59), N154 (= N67), R157 (= R70), Q158 (= Q71), K170 (= K83), N193 (≠ R106), I194 (≠ L107), A213 (≠ T126), D214 (= D127), H215 (≠ N128)
- binding zinc ion: C257 (= C170), C260 (= C173), C334 (= C243), C337 (= C246)
3h5aC Crystal structure of e. Coli mccb (see paper)
26% identity, 95% coverage: 2:248/260 of query aligns to 85:348/358 of 3h5aC
3h5rA Crystal structure of e. Coli mccb + succinimide (see paper)
26% identity, 95% coverage: 2:248/260 of query aligns to 85:340/340 of 3h5rA
- active site: R157 (= R70)
- binding zinc ion: C257 (= C170), C260 (= C173), C335 (= C243), C338 (= C246)
- binding : I126 (≠ L39), S212 (≠ C125), A213 (≠ T126), A237 (≠ G149), G238 (≠ A150), Y239 (≠ A151), V245 (= V160), P280 (vs. gap), R314 (= R221), G316 (≠ L223)
Sites not aligning to the query:
6om4A The structure of microcin c7 biosynthetic enzyme mccb in complex with n-formylated mcca (see paper)
26% identity, 87% coverage: 23:248/260 of query aligns to 107:345/345 of 6om4A
- binding 5'-O-[(S)-amino(hydroxy)phosphoryl]adenosine: G121 (= G37), D143 (= D59), K167 (= K83), N190 (≠ R106), I191 (≠ L107), S209 (≠ C125), A210 (≠ T126), D211 (= D127), H212 (≠ N128)
- binding pyrophosphate 2-: N151 (= N67), R154 (= R70), K167 (= K83)
- binding zinc ion: C254 (= C170), C257 (= C173), C340 (= C243), C343 (= C246)
- binding : I123 (≠ L39), S209 (≠ C125), A210 (≠ T126), D211 (= D127), N233 (≠ S148), A234 (≠ G149), G235 (≠ A150), Y236 (≠ A151), V237 (≠ I152), V261 (vs. gap), A262 (vs. gap), Y265 (≠ F175), R319 (= R221), G321 (≠ L223), W323 (≠ L225), Q332 (≠ V235)
Sites not aligning to the query:
Query Sequence
>WP_004313514.1 NCBI__GCF_000310185.1:WP_004313514.1
MNDDQLLRYSRHILLPEIDVEGQQALLDARALVVGAGGLGSPAAMYLAAAGVGTLVLADH
DTVDLTNLQRQIMHSADMVGLPKVASARATLHRLNPQTRLEPIQARLEGEALEAEVGRAD
VVLDCTDNFATRHAINRACVKHRKPLVSGAAIRFDGQVSVFDLRKPDSGCYHCLFPEGED
IEEVRCAVMGVFAPIVGIVGTIQAAEALKVLIGCGRTLDGRLLLLDGLSMEWRSVALGRD
PGCAVCGTARCAGAVESALR
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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