SitesBLAST
Comparing 6935922 FitnessBrowser__SB2B:6935922 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)
63% identity, 96% coverage: 6:250/254 of query aligns to 4:248/249 of P12282
- R14 (= R16) mutation R->A,K: No effect.; mutation to A: No activity; when associated with A-73.
- C44 (= C46) mutation to A: No effect.
- R73 (= R75) mutation to A: No effect. No activity; when associated with A-14.; mutation to K: Substantially reduced activity.
- C128 (= C130) mutation to A: No effect.; mutation to Y: No activity.
- D130 (= D132) mutation to A: No activity.; mutation to E: Substantially reduced activity.
- C142 (= C144) mutation to A: No effect.
- C172 (= C174) mutation to A: No zinc bound and no enzyme activity.
- C175 (= C177) mutation to A: No zinc bound and no enzyme activity.
- C187 (= C189) mutation to A: No effect.
- C231 (≠ M233) mutation to A: No effect.
- C244 (= C246) mutation to A: No zinc bound and almost no enzyme activity.
- C247 (= C249) mutation to A: No zinc bound and almost no enzyme activity.
1jwbB Structure of the covalent acyl-adenylate form of the moeb-moad protein complex (see paper)
61% identity, 96% coverage: 6:250/254 of query aligns to 3:240/240 of 1jwbB
- active site: R13 (= R16), D129 (= D132)
- binding adenosine monophosphate: G37 (= G40), G39 (= G42), G40 (= G43), D61 (= D64), F62 (= F65), K85 (= K88), L108 (≠ V111), C127 (= C130), T128 (= T131), D129 (= D132), N130 (= N133), V133 (= V136)
- binding zinc ion: C171 (= C174), C236 (= C246), C239 (= C249)
1jw9B Structure of the native moeb-moad protein complex (see paper)
61% identity, 96% coverage: 6:250/254 of query aligns to 3:240/240 of 1jw9B
1jwaB Structure of the atp-bound moeb-moad protein complex (see paper)
58% identity, 93% coverage: 6:242/254 of query aligns to 3:217/217 of 1jwaB
- active site: R13 (= R16), D129 (= D132)
- binding adenosine-5'-triphosphate: G39 (= G42), G40 (= G43), D61 (= D64), F62 (= F65), R72 (= R75), K85 (= K88), L108 (≠ V111), D129 (= D132), N130 (= N133), V133 (= V136)
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)
45% identity, 97% coverage: 6:251/254 of query aligns to 64:311/453 of Q9VLJ8
Sites not aligning to the query:
- 62 modified: Phosphothreonine
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)
45% identity, 98% coverage: 6:254/254 of query aligns to 61:324/482 of O59954
- G82 (= G27) mutation to D: In cnxF21ts and cnxF24ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.
- G100 (= G45) mutation to S: In cnxF1285; impairs molybdopterin biosynthesis.
- R130 (= R75) mutation to Q: In cnxF200; impairs molybdopterin biosynthesis.
- C185 (= C130) mutation to Y: In cnxF472; impairs molybdopterin biosynthesis.
- E215 (= E160) mutation to K: In cnxF119; impairs molybdopterin biosynthesis.
- G264 (= G200) mutation to S: In cnxF142ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.
P30138 Sulfur carrier protein ThiS adenylyltransferase; EC 2.7.7.73 from Escherichia coli (strain K12) (see 3 papers)
42% identity, 98% coverage: 6:253/254 of query aligns to 1:247/251 of P30138
- C169 (= C174) binding
- C172 (= C177) binding
- W174 (≠ A179) mutation to A: No adenylation of ThiS.
- C184 (= C189) mutation to S: No cross-link formed with ThiS. No effect on ThiS thiocarboxylate formation in vitro. Does not support growth.
- C240 (= C246) binding
- C243 (= C249) binding
1zfnA Structural analysis of escherichia coli thif (see paper)
42% identity, 96% coverage: 6:250/254 of query aligns to 1:244/244 of 1zfnA
- active site: R11 (= R16), D127 (= D132)
- binding adenosine-5'-triphosphate: I34 (= I39), G35 (= G40), G37 (= G42), G38 (= G43), D59 (= D64), R70 (= R75), Q71 (= Q76), K83 (= K88), T126 (= T131), D127 (= D132), T131 (≠ V136)
- binding zinc ion: C169 (= C174), C172 (= C177), C240 (= C246), C243 (= C249)
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)
46% identity, 89% coverage: 6:231/254 of query aligns to 55:281/460 of O95396
- 158:238 (vs. 109:188, 40% identical) Interaction with NFS1
- C239 (= C189) 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.
1zud3 Structure of this-thif protein complex (see paper)
40% identity, 97% coverage: 6:251/254 of query aligns to 1:240/240 of 1zud3
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)
38% identity, 98% coverage: 3:250/254 of query aligns to 36:290/440 of P38820
- C225 (= C189) 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.
6yubB Crystal structure of uba4 from chaetomium thermophilum (see paper)
43% identity, 84% coverage: 2:214/254 of query aligns to 3:212/289 of 6yubB
Sites not aligning to the query:
6yubA Crystal structure of uba4 from chaetomium thermophilum (see paper)
43% identity, 84% coverage: 2:214/254 of query aligns to 2:213/423 of 6yubA
Sites not aligning to the query:
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)
42% identity, 96% coverage: 6:250/254 of query aligns to 5:249/270 of D4GSF3
- C188 (= C189) 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.
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)
38% identity, 96% coverage: 6:250/254 of query aligns to 3:253/271 of Q72J02
- C192 (= C189) 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.
3h9jA Crystal structure of e. Coli mccb + ampcpp + semet mcca (see paper)
27% identity, 96% coverage: 7:251/254 of query aligns to 85:339/339 of 3h9jA
- active site: R157 (= R75)
- binding diphosphomethylphosphonic acid adenosyl ester: G124 (= G42), G125 (= G43), D146 (= D64), D148 (= D66), R157 (= R75), K170 (= K88), N193 (≠ V111), I194 (≠ L112), A213 (= A122), D214 (= D123), H215 (= H124)
- binding zinc ion: C257 (= C174), C334 (= C246), C337 (= C249)
- binding : R313 (≠ L225), G315 (≠ M227)
3h5aC Crystal structure of e. Coli mccb (see paper)
27% identity, 96% coverage: 7:251/254 of query aligns to 85:348/358 of 3h5aC
3h5nA Crystal structure of e. Coli mccb + atp (see paper)
27% identity, 96% coverage: 7:250/254 of query aligns to 85:338/338 of 3h5nA
- active site: R157 (= R75)
- binding adenosine-5'-triphosphate: G124 (= G42), D146 (= D64), N154 (= N72), R157 (= R75), Q158 (= Q76), K170 (= K88), N193 (≠ V111), I194 (≠ L112), A213 (= A122), D214 (= D123), H215 (= H124)
- binding zinc ion: C257 (= C174), C260 (= C177), C334 (= C246), C337 (= C249)
3h5rA Crystal structure of e. Coli mccb + succinimide (see paper)
27% identity, 96% coverage: 7:251/254 of query aligns to 85:340/340 of 3h5rA
- active site: R157 (= R75)
- binding zinc ion: C257 (= C174), C260 (= C177), C335 (= C246), C338 (= C249)
- binding : I126 (≠ L44), S212 (vs. gap), A213 (= A122), A237 (= A154), G238 (≠ A155), Y239 (≠ A156), V245 (≠ M162), P280 (vs. gap), R314 (≠ L225), G316 (≠ M227)
Sites not aligning to the query:
6om4A The structure of microcin c7 biosynthetic enzyme mccb in complex with n-formylated mcca (see paper)
27% identity, 88% coverage: 28:251/254 of query aligns to 107:345/345 of 6om4A
- binding 5'-O-[(S)-amino(hydroxy)phosphoryl]adenosine: G121 (= G42), D143 (= D64), K167 (= K88), N190 (≠ V111), I191 (≠ L112), S209 (vs. gap), A210 (= A122), D211 (= D123), H212 (= H124)
- binding pyrophosphate 2-: N151 (= N72), R154 (= R75), K167 (= K88)
- binding zinc ion: C254 (= C174), C257 (= C177), C340 (= C246), C343 (= C249)
- binding : I123 (≠ L44), S209 (vs. gap), A210 (= A122), D211 (= D123), N233 (≠ S153), A234 (= A154), G235 (≠ A155), Y236 (≠ A156), V237 (≠ I157), V261 (≠ F178), A262 (= A179), Y265 (≠ F182), R319 (≠ L225), G321 (≠ M227), W323 (≠ D229), Q332 (≠ M238)
Sites not aligning to the query:
Query Sequence
>6935922 FitnessBrowser__SB2B:6935922
MTDDILSDTELLRYSRQISIKSMDIEGQEKLKQARVLVIGAGGLGCAAAQYLGVAGVGAM
TLVDFDTVELSNLQRQVLHRDNRIGMLKVESARLALNELNPHVQINPIGRVLDDPEMDAL
VADHSLVLDCTDNVAVRQQLNRACFAHKVPLVSAAAIRMEGMITVFDYAGDSPCYQCFAS
LFGEQQLTCVESGILAPVVGLMGCLQAVEAIKLIAGMGKPLLGRLLMVDAMTMEMRQMIL
PRQPNCPVCGGATV
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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