SitesBLAST
Comparing WP_013010412.1 NCBI__GCF_000025725.1:WP_013010412.1 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)
34% identity, 97% coverage: 7:243/244 of query aligns to 11:249/249 of P12282
- R14 (= R10) mutation R->A,K: No effect.; mutation to A: No activity; when associated with A-73.
- C44 (≠ G40) mutation to A: No effect.
- R73 (= R69) mutation to A: No effect. No activity; when associated with A-14.; mutation to K: Substantially reduced activity.
- C128 (≠ A124) mutation to A: No effect.; mutation to Y: No activity.
- D130 (≠ P126) mutation to A: No activity.; mutation to E: Substantially reduced activity.
- C142 (= C138) mutation to A: No effect.
- C172 (= C167) mutation to A: No zinc bound and no enzyme activity.
- C175 (= C170) mutation to A: No zinc bound and no enzyme activity.
- C187 (≠ W179) mutation to A: No effect.
- C231 (≠ M225) mutation to A: No effect.
- C244 (= C238) mutation to A: No zinc bound and almost no enzyme activity.
- C247 (= C241) mutation to A: No zinc bound and almost no enzyme activity.
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)
36% identity, 99% coverage: 2:242/244 of query aligns to 66:310/453 of Q9VLJ8
Sites not aligning to the query:
- 62 modified: Phosphothreonine
1jwbB Structure of the covalent acyl-adenylate form of the moeb-moad protein complex (see paper)
34% identity, 97% coverage: 7:242/244 of query aligns to 10:240/240 of 1jwbB
- active site: R13 (= R10), D129 (≠ P126)
- binding adenosine monophosphate: G37 (= G34), G39 (= G36), G40 (= G37), D61 (≠ H58), F62 (≠ Y59), K85 (≠ R82), L108 (≠ R105), C127 (≠ A124), T128 (≠ R125), D129 (≠ P126), N130 (= N127), V133 (≠ E130)
- binding zinc ion: C171 (= C167), C236 (= C238), C239 (= C241)
1jw9B Structure of the native moeb-moad protein complex (see paper)
34% identity, 97% coverage: 7:242/244 of query aligns to 10:240/240 of 1jw9B
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)
36% identity, 97% coverage: 6:242/244 of query aligns to 9:253/271 of Q72J02
- C192 (≠ W179) 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.
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)
33% identity, 98% coverage: 6:243/244 of query aligns to 11:250/270 of D4GSF3
- C188 (≠ W179) 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.
1zud3 Structure of this-thif protein complex (see paper)
34% identity, 98% coverage: 5:242/244 of query aligns to 6:239/240 of 1zud3
1zfnA Structural analysis of escherichia coli thif (see paper)
33% identity, 98% coverage: 5:242/244 of query aligns to 6:244/244 of 1zfnA
- active site: R11 (= R10), D127 (≠ P126)
- binding adenosine-5'-triphosphate: I34 (≠ G33), G35 (= G34), G37 (= G36), G38 (= G37), D59 (≠ H58), R70 (= R69), Q71 (= Q70), K83 (≠ R82), T126 (≠ R125), D127 (≠ P126), T131 (≠ E130)
- binding zinc ion: C169 (= C167), C172 (= C170), C240 (= C238), C243 (= C241)
P30138 Sulfur carrier protein ThiS adenylyltransferase; EC 2.7.7.73 from Escherichia coli (strain K12) (see 3 papers)
33% identity, 98% coverage: 5:242/244 of query aligns to 6:244/251 of P30138
- C169 (= C167) binding Zn(2+)
- C172 (= C170) binding Zn(2+)
- W174 (≠ V172) mutation to A: No adenylation of ThiS.
- C184 (≠ E181) mutation to S: No cross-link formed with ThiS. No effect on ThiS thiocarboxylate formation in vitro. Does not support growth.
- C240 (= C238) binding Zn(2+)
- C243 (= C241) binding Zn(2+)
1jwaB Structure of the atp-bound moeb-moad protein complex (see paper)
32% identity, 93% coverage: 7:234/244 of query aligns to 10:217/217 of 1jwaB
- active site: R13 (= R10), D129 (≠ P126)
- binding adenosine-5'-triphosphate: G39 (= G36), G40 (= G37), D61 (≠ H58), F62 (≠ Y59), R72 (= R69), K85 (≠ R82), L108 (≠ R105), D129 (≠ P126), N130 (= N127), V133 (≠ E130)
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)
29% identity, 97% coverage: 5:241/244 of query aligns to 66:318/482 of O59954
- G82 (≠ K21) mutation to D: In cnxF21ts and cnxF24ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.
- G100 (= G39) mutation to S: In cnxF1285; impairs molybdopterin biosynthesis.
- R130 (= R69) mutation to Q: In cnxF200; impairs molybdopterin biosynthesis.
- C185 (≠ A124) mutation to Y: In cnxF472; impairs molybdopterin biosynthesis.
- E215 (≠ V154) mutation to K: In cnxF119; impairs molybdopterin biosynthesis.
- G264 (= G192) mutation to S: In cnxF142ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.
6yubB Crystal structure of uba4 from chaetomium thermophilum (see paper)
30% identity, 91% coverage: 6:226/244 of query aligns to 13:234/289 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)
29% identity, 98% coverage: 5:243/244 of query aligns to 44:291/440 of P38820
- C225 (≠ F184) 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.
6yubA Crystal structure of uba4 from chaetomium thermophilum (see paper)
30% identity, 91% coverage: 6:226/244 of query aligns to 12:235/423 of 6yubA
Sites not aligning to the query:
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)
30% identity, 98% coverage: 7:244/244 of query aligns to 62:303/460 of O95396
- 158:238 (vs. 103:183, 25% identical) Interaction with NFS1
- C239 (≠ F184) 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.
Q8VE47 Ubiquitin-like modifier-activating enzyme 5; Ubiquitin-activating enzyme 5; UFM1-activating enzyme from Mus musculus (Mouse) (see 2 papers)
27% identity, 95% coverage: 8:238/244 of query aligns to 51:301/403 of Q8VE47
- C248 (≠ L187) mutation C->S,A: Abolished ability to catalyze the first step in ufmylation.
Sites not aligning to the query:
- 340:344 WGIEL→LGIEA: Impaired ability to activate UFM1.
Q06624 DNA damage tolerance protein RHC31; RAD31 homolog from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
28% identity, 71% coverage: 2:175/244 of query aligns to 10:173/347 of Q06624
- K35 (≠ S29) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
6h77B E1 enzyme for ubiquitin like protein activation in complex with ubl (see paper)
27% identity, 97% coverage: 8:244/244 of query aligns to 18:271/302 of 6h77B
- binding adenosine-5'-triphosphate: G45 (= G34), G47 (= G36), G48 (= G37), D69 (≠ H58), Y70 (= Y59), D71 (≠ G60), N77 (= N66), R80 (= R69), K92 (≠ R82), N115 (= N107), I116 (≠ E108), D148 (≠ P126), N149 (= N127)
- binding zinc ion: C191 (= C167), C194 (= C170), C268 (= C241)
Sites not aligning to the query:
Q9GZZ9 Ubiquitin-like modifier-activating enzyme 5; Ubiquitin-activating enzyme 5; ThiFP1; UFM1-activating enzyme; Ubiquitin-activating enzyme E1 domain-containing protein 1 from Homo sapiens (Human) (see 13 papers)
28% identity, 95% coverage: 8:238/244 of query aligns to 53:303/404 of Q9GZZ9
- R55 (= R10) to H: in DEE44; reduces UFM1 activating enzyme activity; dbSNP:rs774318611
- M57 (≠ I12) to V: in DEE44; reduces UFM1 activating enzyme activity; reduces UFM1-DDRGK1 formation; dbSNP:rs532178791
- G83 (= G37) binding ATP
- D104 (≠ H58) binding ATP
- K127 (≠ R82) binding ATP
- N150 (= N107) binding ATP
- G168 (vs. gap) to E: in DEE44; abolishes UFM1 activating enzyme activity; dbSNP:rs886039761
- N184 (= N127) binding ATP
- R188 (= R131) mutation to A: Abolished ability to activate UFM1.
- HIQ 215:217 (≠ YYF 156:158) mutation to AQA: Abolished ability to activate UFM1.
- C226 (= C167) binding Zn(2+)
- C229 (= C170) binding Zn(2+)
- APPL 230:233 (vs. gap) mutation APPL->RPPA,FPPA: Abolished interaction with UFM1.
- C250 (≠ L187) active site, Glycyl thioester intermediate; mutation to A: Abolished ability to activate UFM1.; mutation to S: Forms a stable intermediate complex.
- V260 (≠ S196) to M: in DEE44; reduces UFM1 activating enzyme activity; dbSNP:rs886039759
- K271 (= K204) mutation to D: Impaired ability to activate UFM1 via a trans-binding mechanism.
- D290 (≠ T227) mutation to K: Impaired homodimerization and ability to activate UFM1 via a trans-binding mechanism.
- C303 (= C238) binding Zn(2+)
Sites not aligning to the query:
- 246:404 natural variant: Missing (in SCAR24; delocalizes protein to the nucleus; activates degradation through the ubiquitin proteasome pathway; decreases protein stability; disrupts interaction with UFM1)
- 308 binding Zn(2+)
- 310 K → E: in SCAR24; does not affect cytoplasm localization; decreases protein stability; does not affect interaction with UFM1; dbSNP:rs886039762
- 334:346 UFM1-interacting sequence (UIS)
- 336 mutation H->A,D: Impaired ability to activate UFM1.
- 341 W→A: Abolished interaction with UFM1 and GABARAPL2.
- 342 G→A: Decreased interaction with UFM1 without affecting interaction with GABARAPL2.
- 343 I→A: Abolished interaction with UFM1 and decreased interaction with GABARAPL2.
- 343:345 IEL→AEA: Impaired ability to activate UFM1.
- 345 L→A: Abolished interaction with UFM1 and decreased interaction with GABARAPL2.
- 346 V→A: Abolished interaction with UFM1 and decreased interaction with GABARAPL2.
- 347:377 Linker
- 371 A → T: in DEE44; reduces UFM1 activating enzyme activity; reduces UFM1 activating enzyme activity; reduces UFM1-DDRGK1 formation; dbSNP:rs114925667
- 372 mutation Y->A,E: Strongly decreased ability to transfer UFM1 to UFC1.; Y→F: Does not affect ability to transfer UFM1 to UFC1.
- 389 D → Y: in DEE44; no effect on UFM1 activating enzyme activity; dbSNP:rs886039760
- 389:404 UFC1-binding sequence (UFC)
- 397 L→R: Abolished interaction with UFC1.
- 401 M→R: Abolished interaction with UFC1.
P20973 Ubiquitin-activating enzyme E1 1; EC 6.2.1.45 from Triticum aestivum (Wheat) (see paper)
31% identity, 58% coverage: 7:148/244 of query aligns to 444:592/1051 of P20973
Sites not aligning to the query:
- 626 active site, Glycyl thioester intermediate; C→A: Abolishes enzyme activity.
Query Sequence
>WP_013010412.1 NCBI__GCF_000025725.1:WP_013010412.1
MHDYYERYKRQIMLKDFGREKQDILKNSSVFIGGIGGLGGATAAYLASAGIGRMVISHYG
NLTESNMNRQHLMDVNRIGEPRIDIAVENILKINPDIELEMHNIRLNENKAEKFIEGCDV
AVSARPNFPERMAMNNACVKLGVPMIEAAMDDMVGYYFNIFPHETACLRCFVSEDVPDWK
ELGFGVLGAVSGTIGSLAAVEAVKIITKHGTPLKGKMMHIDFNTMRTITPKLKRNPDCPV
CGRR
Or try a new SitesBLAST search
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