SitesBLAST
Comparing AZOBR_RS01090 FitnessBrowser__azobra:AZOBR_RS01090 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)
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)
54% identity, 99% coverage: 1:259/262 of query aligns to 1:261/271 of Q72J02
- C192 (= C190) 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)
53% identity, 94% coverage: 6:251/262 of query aligns to 8:249/270 of D4GSF3
- C188 (= C190) 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.
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, 98% coverage: 3:259/262 of query aligns to 64:318/453 of Q9VLJ8
Sites not aligning to the query:
- 62 modified: Phosphothreonine
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)
50% identity, 97% coverage: 7:259/262 of query aligns to 59:309/460 of O95396
- 158:238 (vs. 106:189, 52% identical) Interaction with NFS1
- C239 (= C190) 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.
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, 95% coverage: 7:256/262 of query aligns to 65:324/482 of O59954
- G82 (= G24) mutation to D: In cnxF21ts and cnxF24ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.
- G100 (= G42) mutation to S: In cnxF1285; impairs molybdopterin biosynthesis.
- R130 (= R72) mutation to Q: In cnxF200; impairs molybdopterin biosynthesis.
- C185 (≠ G127) mutation to Y: In cnxF472; impairs molybdopterin biosynthesis.
- E215 (≠ D157) mutation to K: In cnxF119; impairs molybdopterin biosynthesis.
- G264 (= G201) mutation to S: In cnxF142ts; temperature-sensitive mutant. Impairs molybdopterin biosynthesis.
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)
43% identity, 95% coverage: 7:256/262 of query aligns to 43:295/440 of P38820
- C225 (= C190) 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.
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)
42% identity, 95% coverage: 2:251/262 of query aligns to 3:248/249 of P12282
- R14 (= R13) mutation R->A,K: No effect.; mutation to A: No activity; when associated with A-73.
- C44 (≠ A43) mutation to A: No effect.
- R73 (= R72) mutation to A: No effect. No activity; when associated with A-14.; mutation to K: Substantially reduced activity.
- C128 (≠ G127) mutation to A: No effect.; mutation to Y: No activity.
- D130 (= D129) mutation to A: No activity.; mutation to E: Substantially reduced activity.
- C142 (= C141) mutation to A: No effect.
- C172 (= C173) mutation to A: No zinc bound and no enzyme activity.
- C175 (= C176) mutation to A: No zinc bound and no enzyme activity.
- C187 (= C190) mutation to A: No effect.
- C231 (≠ A234) mutation to A: No effect.
- C244 (= C247) mutation to A: No zinc bound and almost no enzyme activity.
- C247 (= C250) 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)
42% identity, 95% coverage: 2:251/262 of query aligns to 2:240/240 of 1jwbB
- active site: R13 (= R13), D129 (= D129)
- binding adenosine monophosphate: G37 (= G37), G39 (= G39), G40 (= G40), D61 (= D61), F62 (≠ D62), K85 (= K85), L108 (≠ R108), C127 (≠ G127), T128 (≠ S128), D129 (= D129), N130 (= N130), V133 (≠ T133)
- binding zinc ion: C171 (= C173), C236 (= C247), C239 (= C250)
1jw9B Structure of the native moeb-moad protein complex (see paper)
42% identity, 95% coverage: 2:251/262 of query aligns to 2:240/240 of 1jw9B
P30138 Sulfur carrier protein ThiS adenylyltransferase; EC 2.7.7.73 from Escherichia coli (strain K12) (see 3 papers)
39% identity, 95% coverage: 3:251/262 of query aligns to 1:244/251 of P30138
- C169 (= C173) binding
- C172 (= C176) binding
- W174 (≠ F178) mutation to A: No adenylation of ThiS.
- C184 (= C190) mutation to S: No cross-link formed with ThiS. No effect on ThiS thiocarboxylate formation in vitro. Does not support growth.
- C240 (= C247) binding
- C243 (= C250) binding
1zfnA Structural analysis of escherichia coli thif (see paper)
39% identity, 95% coverage: 3:251/262 of query aligns to 1:244/244 of 1zfnA
- active site: R11 (= R13), D127 (= D129)
- binding adenosine-5'-triphosphate: I34 (≠ V36), G35 (= G37), G37 (= G39), G38 (= G40), D59 (= D61), R70 (= R72), Q71 (= Q73), K83 (= K85), T126 (≠ S128), D127 (= D129), T131 (= T133)
- binding zinc ion: C169 (= C173), C172 (= C176), C240 (= C247), C243 (= C250)
1jwaB Structure of the atp-bound moeb-moad protein complex (see paper)
38% identity, 92% coverage: 2:243/262 of query aligns to 2:217/217 of 1jwaB
- active site: R13 (= R13), D129 (= D129)
- binding adenosine-5'-triphosphate: G39 (= G39), G40 (= G40), D61 (= D61), F62 (≠ D62), R72 (= R72), K85 (= K85), L108 (≠ R108), D129 (= D129), N130 (= N130), V133 (≠ T133)
1zud3 Structure of this-thif protein complex (see paper)
38% identity, 95% coverage: 3:251/262 of query aligns to 1:239/240 of 1zud3
6yubA Crystal structure of uba4 from chaetomium thermophilum (see paper)
38% identity, 81% coverage: 3:213/262 of query aligns to 6:211/423 of 6yubA
Sites not aligning to the query:
6yubB Crystal structure of uba4 from chaetomium thermophilum (see paper)
37% identity, 81% coverage: 2:213/262 of query aligns to 6:210/289 of 6yubB
Sites not aligning to the query:
O42939 Ubiquitin-activating enzyme E1-like; Pmt3-activating enzyme subunit 2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
32% identity, 75% coverage: 31:227/262 of query aligns to 26:224/628 of O42939
Sites not aligning to the query:
- 559 modified: Phosphoserine
- 563 modified: Phosphoserine
3kydB Human sumo e1~sumo1-amp tetrahedral intermediate mimic (see paper)
34% identity, 63% coverage: 26:191/262 of query aligns to 10:171/477 of 3kydB
- active site: D114 (= D129), C170 (= C190), T171 (≠ S191)
- binding 5'-{[(3-aminopropyl)sulfonyl]amino}-5'-deoxyadenosine: I25 (≠ L41), D45 (= D61), L46 (≠ D62), K69 (= K85), S92 (≠ T107), I93 (≠ R108), L113 (≠ S128), D114 (= D129), N115 (= N130), C170 (= C190)
- binding zinc ion: C155 (= C173), C158 (= C176)
Sites not aligning to the query:
3kycB Human sumo e1 complex with a sumo1-amp mimic (see paper)
34% identity, 63% coverage: 26:191/262 of query aligns to 9:170/548 of 3kycB
- active site: D113 (= D129), C169 (= C190), T170 (≠ S191)
- binding 5'-deoxy-5'-(sulfamoylamino)adenosine: G22 (= G39), G23 (= G40), D44 (= D61), L45 (≠ D62), K68 (= K85), S91 (≠ T107), I92 (≠ R108), L112 (≠ S128), D113 (= D129), N114 (= N130)
- binding zinc ion: C154 (= C173), C157 (= C176)
Sites not aligning to the query:
6xoiB Structure of sumo1-ml00752641 adduct bound to sae (see paper)
34% identity, 59% coverage: 26:179/262 of query aligns to 6:157/403 of 6xoiB
- active site: D110 (= D129)
- binding [(1R,2R,3S,4R)-4-{[5-(1-benzyl-1H-pyrazole-3-carbonyl)pyrimidin-4-yl]amino}-2,3-dihydroxycyclopentyl]methyl sulfamate: G20 (= G40), D41 (= D61), L42 (≠ D62), K65 (= K85), S88 (≠ T107), I89 (≠ R108), A108 (≠ G127), L109 (≠ S128), D110 (= D129), N111 (= N130)
- binding zinc ion: C151 (= C173), C154 (= C176)
Sites not aligning to the query:
Q9UBT2 SUMO-activating enzyme subunit 2; Anthracycline-associated resistance ARX; Ubiquitin-like 1-activating enzyme E1B; Ubiquitin-like modifier-activating enzyme 2; EC 2.3.2.- from Homo sapiens (Human) (see 8 papers)
34% identity, 63% coverage: 26:191/262 of query aligns to 13:174/640 of Q9UBT2
- G24 (= G37) to V: in ACCES; loss of function; does not rescue the abnormal phenotype in a zebrafish disease model; dbSNP:rs2075211884
- GAGGIG 24:29 (≠ GAGGLG 37:42) binding
- D48 (= D61) binding
- N56 (= N69) mutation to A: Abolishes ATP-dependent activation of SUMO proteins.
- NLNR 56:59 (≠ NLQR 69:72) binding
- L57 (= L70) mutation to A: Strongly reduces ATP-dependent activation of SUMO proteins.
- R59 (= R72) mutation to A: Strongly reduces ATP-dependent activation of SUMO proteins.
- K72 (= K85) binding ; mutation to A: Abolishes ATP-dependent activation of SUMO proteins.
- SI 95:96 (≠ TR 107:108) binding
- D117 (= D129) mutation to A: Abolishes ATP-dependent activation of SUMO proteins.
- DNRAAR 117:122 (≠ DNFATR 129:134) binding
- R122 (= R134) to G: in ACCES; loss of function; does not rescue the abnormal phenotype in a zebrafish disease model
- C173 (= C190) active site, Glycyl thioester intermediate; mutation to A: Loss of enzyme activity.
- T174 (≠ S191) mutation to A: Slightly reduced enzyme activity.
Sites not aligning to the query:
- 184 H→Q: No effect on enzyme activity.
- 235 I→A: Strongly reduced interaction with UBE2I; when associated with A-238.
- 238 I→A: Strongly reduced interaction with UBE2I; when associated with A-235.
- 307 L → R: in dbSNP:rs1043062
- 483 E → K: in ACCES; loss of function; does not rescue the abnormal phenotype in a zebrafish disease model; dbSNP:rs2075619600
- 484 mutation Missing: Strongly reduced interaction with UBE2I.
- 485 G→GGGG: Strongly reduced interaction with UBE2I.
Query Sequence
>AZOBR_RS01090 FitnessBrowser__azobra:AZOBR_RS01090
MDFTDTQLHRYSRHIILPEVGGIGQEALLRARVLVVGAGGLGAPLLLYLAAAGVGTIGVI
DDDTVDLSNLQRQVIHDESSLGVPKVESAAARIRALNPDVAVEVHKTRLTKDNALDLIGR
YDIVADGSDNFATRFLLNDACYFAKKTLVSAAILRFDGQVSTFKAHLGDPHPCYRCLFPE
PPPRGLVPSCSEGGVLGALAGFVGSLQTTEVLKEIMGIGEGLSGSLMMLDTLHASFQRIT
VRRDPDCPLCGTHPTIHDLSAH
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