SitesBLAST
Comparing PfGW456L13_1584 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_1584 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)
57% identity, 98% coverage: 2:247/251 of query aligns to 4:248/249 of P12282
- R14 (= R12) mutation R->A,K: No effect.; mutation to A: No activity; when associated with A-73.
- C44 (≠ A42) mutation to A: No effect.
- R73 (= R71) mutation to A: No effect. No activity; when associated with A-14.; mutation to K: Substantially reduced activity.
- C128 (= C126) mutation to A: No effect.; mutation to Y: No activity.
- D130 (= D128) mutation to A: No activity.; mutation to E: Substantially reduced activity.
- C142 (= C140) mutation to A: No effect.
- C172 (= C171) mutation to A: No zinc bound and no enzyme activity.
- C175 (= C174) mutation to A: No zinc bound and no enzyme activity.
- C187 (= C186) mutation to A: No effect.
- C231 (≠ T230) 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.
1jwbB Structure of the covalent acyl-adenylate form of the moeb-moad protein complex (see paper)
55% identity, 98% coverage: 2:247/251 of query aligns to 3:240/240 of 1jwbB
- active site: R13 (= R12), D129 (= D128)
- binding adenosine monophosphate: G37 (= G36), G39 (= G38), G40 (= G39), D61 (= D60), F62 (= F61), K85 (= K84), L108 (≠ A107), C127 (= C126), T128 (≠ S127), D129 (= D128), N130 (= N129), V133 (≠ T132)
- binding zinc ion: C171 (= C171), C236 (= C243), C239 (= C246)
1jw9B Structure of the native moeb-moad protein complex (see paper)
55% identity, 98% coverage: 2:247/251 of query aligns to 3:240/240 of 1jw9B
1jwaB Structure of the atp-bound moeb-moad protein complex (see paper)
52% identity, 95% coverage: 2:239/251 of query aligns to 3:217/217 of 1jwaB
- active site: R13 (= R12), D129 (= D128)
- binding adenosine-5'-triphosphate: G39 (= G38), G40 (= G39), D61 (= D60), F62 (= F61), R72 (= R71), K85 (= K84), L108 (≠ A107), D129 (= D128), N130 (= N129), V133 (≠ T132)
P30138 Sulfur carrier protein ThiS adenylyltransferase; EC 2.7.7.73 from Escherichia coli (strain K12) (see 3 papers)
51% identity, 100% coverage: 2:251/251 of query aligns to 1:248/251 of P30138
- C169 (= C171) binding
- C172 (= C174) binding
- W174 (≠ Y176) 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
- C243 (= C246) binding
1zfnA Structural analysis of escherichia coli thif (see paper)
52% identity, 98% coverage: 2:247/251 of query aligns to 1:244/244 of 1zfnA
- active site: R11 (= R12), D127 (= D128)
- binding adenosine-5'-triphosphate: I34 (≠ V35), G35 (= G36), G37 (= G38), G38 (= G39), D59 (= D60), R70 (= R71), Q71 (= Q72), K83 (= K84), T126 (≠ S127), D127 (= D128), T131 (= T132)
- binding zinc ion: C169 (= C171), C172 (= C174), C240 (= C243), C243 (= C246)
1zud3 Structure of this-thif protein complex (see paper)
51% identity, 98% coverage: 2:247/251 of query aligns to 1:239/240 of 1zud3
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)
44% identity, 98% coverage: 2:246/251 of query aligns to 64:309/453 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)
43% identity, 98% coverage: 2:246/251 of query aligns to 61:318/482 of O59954
- G82 (= G23) mutation to D: In cnxF21ts and cnxF24ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.
- G100 (= G41) mutation to S: In cnxF1285; impairs molybdopterin biosynthesis.
- R130 (= R71) mutation to Q: In cnxF200; impairs molybdopterin biosynthesis.
- C185 (= C126) mutation to Y: In cnxF472; impairs molybdopterin biosynthesis.
- E215 (= E156) mutation to K: In cnxF119; impairs molybdopterin biosynthesis.
- G264 (= G197) mutation to S: In cnxF142ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.
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)
46% identity, 98% coverage: 2:247/251 of query aligns to 3:253/271 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.
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, 92% coverage: 2:232/251 of query aligns to 55:285/460 of O95396
- 158:238 (vs. 105:185, 43% 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.
6yubA Crystal structure of uba4 from chaetomium thermophilum (see paper)
42% identity, 84% coverage: 2:211/251 of query aligns to 6:213/423 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)
44% identity, 98% coverage: 2:247/251 of query aligns to 5:249/270 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.
6yubB Crystal structure of uba4 from chaetomium thermophilum (see paper)
42% identity, 84% coverage: 2:211/251 of query aligns to 7:212/289 of 6yubB
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)
36% identity, 97% coverage: 5:247/251 of query aligns to 42:290/440 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.
3h5aC Crystal structure of e. Coli mccb (see paper)
29% identity, 98% coverage: 3:249/251 of query aligns to 85:349/358 of 3h5aC
3h5nA Crystal structure of e. Coli mccb + atp (see paper)
27% identity, 98% coverage: 3:247/251 of query aligns to 85:338/338 of 3h5nA
- active site: R157 (= R71)
- binding adenosine-5'-triphosphate: G124 (= G38), D146 (= D60), N154 (= N68), R157 (= R71), Q158 (= Q72), K170 (= K84), N193 (≠ A107), I194 (≠ L108), A213 (≠ S127), D214 (= D128), H215 (≠ N129)
- binding zinc ion: C257 (= C171), C260 (= C174), C334 (= C243), C337 (= C246)
3h9jA Crystal structure of e. Coli mccb + ampcpp + semet mcca (see paper)
27% identity, 98% coverage: 3:247/251 of query aligns to 85:338/339 of 3h9jA
- active site: R157 (= R71)
- binding diphosphomethylphosphonic acid adenosyl ester: G124 (= G38), G125 (= G39), D146 (= D60), D148 (= D62), R157 (= R71), K170 (= K84), N193 (≠ A107), I194 (≠ L108), A213 (≠ S127), D214 (= D128), H215 (≠ N129)
- binding zinc ion: C257 (= C171), C334 (= C243), C337 (= C246)
- binding : R313 (≠ L222), G315 (≠ L224)
3h5rA Crystal structure of e. Coli mccb + succinimide (see paper)
28% identity, 98% coverage: 3:247/251 of query aligns to 85:339/340 of 3h5rA
- active site: R157 (= R71)
- binding zinc ion: C257 (= C171), C260 (= C174), C335 (= C243), C338 (= C246)
- binding : I126 (≠ L40), S212 (≠ C126), A213 (≠ S127), A237 (≠ G150), G238 (≠ A151), Y239 (≠ A152), V245 (= V161), P280 (≠ A189), R314 (≠ L222), G316 (≠ L224)
Sites not aligning to the query:
6om4A The structure of microcin c7 biosynthetic enzyme mccb in complex with n-formylated mcca (see paper)
28% identity, 89% coverage: 24:247/251 of query aligns to 107:344/345 of 6om4A
- binding 5'-O-[(S)-amino(hydroxy)phosphoryl]adenosine: G121 (= G38), D143 (= D60), K167 (= K84), N190 (≠ A107), I191 (≠ L108), S209 (≠ C126), A210 (≠ S127), D211 (= D128), H212 (≠ N129)
- binding pyrophosphate 2-: N151 (= N68), R154 (= R71), K167 (= K84)
- binding zinc ion: C254 (= C171), C257 (= C174), C340 (= C243), C343 (= C246)
- binding : I123 (≠ L40), S209 (≠ C126), A210 (≠ S127), D211 (= D128), N233 (≠ S149), A234 (≠ G150), G235 (≠ A151), Y236 (≠ A152), V237 (≠ I153), V261 (vs. gap), A262 (vs. gap), Y265 (= Y176), R319 (≠ L222), G321 (≠ L224), W323 (≠ D226), Q332 (≠ L235)
Sites not aligning to the query:
Query Sequence
>PfGW456L13_1584 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_1584
VLNDQELLRYSRQILLQHIDIDGQLRLKESRVLIVGLGGLGAPVALYLAAAGVGELHLAD
FDTVDLTNLQRQIIHDTDSVGMTKVDSAIKRLTAINPEIQLIAHRAALDEDSLAAVVARV
DLVLDCSDNFSTREAVNAACVAAGKPLVSGAAIRLEGQLSVFDPRRPESPCYHCLYGHGS
EAELTCSEAGVVGPLVGLVGSLQALEALKLLAGFGEPLVGRLLLIDALGTRFRELRVKRD
PGCSVCGPKHA
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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