SitesBLAST
Comparing 3608608 FitnessBrowser__Dino:3608608 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)
5f7qE Rok repressor lmo0178 from listeria monocytogenes bound to operator (see paper)
27% identity, 91% coverage: 28:403/414 of query aligns to 16:386/396 of 5f7qE
- binding zinc ion: H243 (= H259), C253 (= C269), C255 (= C271), C260 (= C276)
- binding : T32 (≠ M44), S43 (≠ G55), T44 (≠ S56), T67 (= T80), G68 (= G81), G68 (= G81), G69 (= G83), G69 (= G83), R70 (= R84), R70 (= R84), R71 (≠ P85), A72 (≠ P86), K73 (≠ V87)
Sites not aligning to the query:
1z05A Crystal structure of the rok family transcriptional regulator, homolog of e.Coli mlc protein.
30% identity, 78% coverage: 31:354/414 of query aligns to 11:333/396 of 1z05A
5f7rA Rok repressor lmo0178 from listeria monocytogenes bound to inducer (see paper)
27% identity, 74% coverage: 97:403/414 of query aligns to 2:302/306 of 5f7rA
- binding alpha-D-glucopyranose: K7 (≠ R102), E10 (≠ D105), G70 (= G168), N110 (≠ D207), N110 (≠ D207), S134 (≠ T231), V135 (≠ I232), G138 (= G235), L139 (≠ V236), G140 (= G237), E159 (= E256), H162 (= H259), E181 (= E278), E253 (≠ A354), W293 (= W394)
- binding zinc ion: H162 (= H259), C172 (= C269), C174 (= C271), C179 (= C276)
P50456 DNA-binding transcriptional repressor Mlc; Making large colonies protein; Membrane linked control from Escherichia coli (strain K12) (see 4 papers)
28% identity, 78% coverage: 30:351/414 of query aligns to 20:340/406 of P50456
- R52 (≠ S62) mutation to H: Shows increased expression and forms larger colonies.
- H86 (≠ Y97) mutation to R: Can be bound and inactivated by MtfA.
- F136 (≠ L149) mutation to A: Decreases association with PtsG EIIB domain.
- H247 (= H259) binding
- C257 (= C269) binding ; mutation to A: Strongly reduced activity; when associated with A-259.; mutation to S: Strongly reduced activity; when associated with S-259.
- C259 (= C271) binding ; mutation to A: Strongly reduced activity; when associated with A-257.; mutation to S: Strongly reduced activity; when associated with S-257.
- C264 (= C276) binding
- R306 (≠ A317) mutation to G: Forms dimers but not tetramers; when associated with G-310.
- L310 (≠ A321) mutation to G: Forms dimers but not tetramers; when associated with G-306.
1z6rA Crystal structure of mlc from escherichia coli (see paper)
26% identity, 78% coverage: 30:351/414 of query aligns to 9:316/382 of 1z6rA
2yi1A Crystal structure of n-acetylmannosamine kinase in complex with n- acetyl mannosamine 6-phosphate and adp. (see paper)
32% identity, 57% coverage: 119:353/414 of query aligns to 25:260/308 of 2yi1A
- binding adenosine-5'-diphosphate: T140 (≠ Q234), G189 (≠ D283), L216 (≠ E309)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G71 (≠ P167), G72 (= G168), R73 (≠ A169), S84 (= S180), T85 (≠ P181), L87 (= L183), N112 (= N206), D113 (= D207), G139 (≠ E233), T140 (≠ Q234), G141 (= G235), I142 (≠ V236), E162 (= E256), H165 (= H259), E184 (= E278)
- binding calcium ion: N112 (= N206), N115 (= N209), G144 (≠ M238), A161 (≠ L255)
- binding zinc ion: H165 (= H259), C175 (= C269), C177 (= C271), C182 (= C276)
Sites not aligning to the query:
2yhyA Structure of n-acetylmannosamine kinase in complex with n- acetylmannosamine and adp (see paper)
32% identity, 57% coverage: 119:353/414 of query aligns to 25:260/308 of 2yhyA
Sites not aligning to the query:
Q9Y223 Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase; UDP-GlcNAc-2-epimerase/ManAc kinase; EC 3.2.1.183; EC 2.7.1.60 from Homo sapiens (Human) (see 18 papers)
32% identity, 57% coverage: 119:354/414 of query aligns to 429:670/722 of Q9Y223
- I472 (≠ V164) to T: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to 50% of the wild-type activity; decreased N-acylmannosamine kinase activity; corresponding to less than 10% of wild-type activity
- G476 (= G168) binding ; binding
- R477 (≠ A169) binding ; binding
- T489 (≠ P181) binding ; binding
- N516 (= N206) binding ; binding
- D517 (= D207) active site; binding ; binding ; mutation D->A,N: Loss of N-acylmannosamine kinase activity. Decreased affinity for N-acyl-D-mannosamine. No effect on structure.
- N519 (= N209) to S: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs1554658910; mutation to S: Decreased N-acylmannosamine kinase activity.
- A524 (= A214) to V: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to less than 10% of wild-type activity; decreased N-acylmannosamine kinase activity; impaired homohexamers formation; dbSNP:rs764698870
- F528 (= F218) to C: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; retains 70% of wild-type activity; decreased N-acylmannosamine kinase activity; dbSNP:rs986773986; mutation to C: Decreased N-acylmannosamine kinase activity.
- G545 (= G235) binding
- E566 (= E256) binding
- H569 (= H259) binding ; binding ; binding
- V572 (= V262) to L: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; retains 70-80% of wild-type activity; decreased N-acylmannosamine kinase activity; corresponding to less than 10% of wild-type activity; does not affect homohexamers formation; dbSNP:rs121908632
- G576 (= G266) to E: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs121908625
- C579 (= C269) binding
- C581 (= C271) binding
- C586 (= C276) binding
- I587 (≠ L277) to T: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs748949603; mutation to T: Decreased N-acylmannosamine kinase activity.
- E588 (= E278) binding ; binding
- A630 (≠ Q314) to T: in NM; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
- A631 (= A315) to T: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; retains 80% of wild-type activity; decreased N-acylmannosamine kinase activity; retains 75% of wild-type activity; dbSNP:rs121908626; to V: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; retains 70% of wild-type activity; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs62541771; mutation A->V,T: Decreased N-acylmannosamine kinase activity.
Sites not aligning to the query:
- 13 C → S: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to 20% of wild-type activity; no effect on N-acylmannosamine kinase activity; dbSNP:rs1209266607
- 19 binding
- 23 binding
- 113 binding
- 132 H → Q: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to less than 10% of wild-type activity; impaired homohexamers formation
- 176 D → V: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to 20% of wild-type activity; no effect on N-acylmannosamine kinase activity; impaired homohexamers formation; dbSNP:rs139425890
- 177 R → C: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to less than 20% of wild-type activity; no effect on N-acylmannosamine kinase activity; impaired homohexamers formation; dbSNP:rs539332585
- 200 I → F: in NM; uncertain significance; decreased UDP-N-acetylglucosamine 2-epimerase activity; retains 90% of wild-type activity; decreased N-acylmannosamine kinase activity; retains 75% of wild-type activity; dbSNP:rs369328625
- 206 G → S: in NM; moderate phenotype with unusual involvement of quadriceps; dbSNP:rs766266918
- 220 binding
- 253 binding
- 259 binding
- 263 R → L: in SIALURIA; strong reduction of feedback inhibition by CMP-Neu5Ac; dbSNP:rs121908623
- 266 R → Q: in SIALURIA; abolishes feedback inhibition by CMP-Neu5Ac; dbSNP:rs121908622; R → W: in sialuria; dbSNP:rs121908621
- 271 binding
- 280 binding
- 281 binding
- 282 binding
- 301 binding
- 302 binding
- 303 C → V: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; retains 80% of wild-type activity; decreased N-acylmannosamine kinase activity; corresponding to 60% of wild-type activity; requires 2 nucleotide substitutions; dbSNP:rs121908633
- 307 binding
- 321 binding
- 331 V → A: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to 20% of wild-type activity; no effect on N-acylmannosamine kinase activity; impaired homohexamers formation
- 378 D → Y: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to 10-30% of wild-type activity; decreased N-acylmannosamine kinase activity; impaired homohexamers formation; dbSNP:rs199877522
- 413 binding
- 416 binding
- 417 binding
- 418 binding
- 420 binding
- 708 G → S: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; severely decreased; dbSNP:rs1554657922
- 712 M→T: Decreased N-acylmannosamine kinase activity.
O35826 Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase; UDP-GlcNAc-2-epimerase/ManAc kinase; EC 3.2.1.183; EC 2.7.1.60 from Rattus norvegicus (Rat) (see paper)
31% identity, 57% coverage: 119:354/414 of query aligns to 429:670/722 of O35826
Sites not aligning to the query:
- 1 UDP-N-acetylglucosamine 2-epimerase
- 49 H→A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Does not interfere with enzyme oligomerization.
- 110 H→A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Partial reduction of the dimerization process.
- 132 H→A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Partial reduction of the dimerization process.
- 155 H→A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Strong reduction of the dimerization process.
- 157 H→A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Strong reduction of the dimerization process.
- 406:722 N-acetylmannosamine kinase
- 413 mutation D->K,N: No effect on UDP-N-acetylglucosamine 2-epimerase activity. Does not affect feedback inhibition by CMP-Neu5Ac. Loss of N-acylmannosamine kinase activity. Does not interfere with oligomerization.
- 420 R→M: No effect on UDP-N-acetylglucosamine 2-epimerase activity. Does not affect feedback inhibition by CMP-Neu5Ac. Loss of N-acylmannosamine kinase activity. Does not interfere with oligomerization.
2yhwA High-resolution crystal structures of n-acetylmannosamine kinase: insights about substrate specificity, activity and inhibitor modelling. (see paper)
30% identity, 60% coverage: 119:367/414 of query aligns to 25:275/309 of 2yhwA
3vglA Crystal structure of a rok family glucokinase from streptomyces griseus in complex with glucose and amppnp (see paper)
31% identity, 56% coverage: 144:375/414 of query aligns to 39:281/312 of 3vglA
- binding phosphoaminophosphonic acid-adenylate ester: G130 (≠ E233), T131 (≠ Q234), G180 (≠ D283), G214 (vs. gap), S218 (vs. gap), G260 (≠ A354), V261 (≠ R355), E264 (≠ Y358)
- binding beta-D-glucopyranose: G65 (= G168), P78 (= P181), N103 (= N206), D104 (= D207), L133 (≠ V236), G134 (= G237), E153 (= E256), H156 (= H259), E175 (= E278)
- binding zinc ion: H156 (= H259), C166 (= C269), C168 (= C271), C173 (= C276)
Sites not aligning to the query:
3vgkB Crystal structure of a rok family glucokinase from streptomyces griseus (see paper)
31% identity, 56% coverage: 144:375/414 of query aligns to 39:281/312 of 3vgkB
3eo3A Crystal structure of the n-acetylmannosamine kinase domain of human gne protein (see paper)
37% identity, 39% coverage: 194:353/414 of query aligns to 75:240/288 of 3eo3A
2qm1B Crystal structure of glucokinase from enterococcus faecalis
27% identity, 67% coverage: 128:403/414 of query aligns to 41:320/325 of 2qm1B
7p9pAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
27% identity, 65% coverage: 136:403/414 of query aligns to 40:304/304 of 7p9pAAA
- binding phosphoaminophosphonic acid-adenylate ester: G133 (≠ E233), T134 (≠ Q234), G194 (≠ D283), E198 (≠ V287), A211 (= A305), G256 (= G353), G257 (≠ A354), N260 (≠ R357)
- binding zinc ion: H159 (= H259), C180 (= C269), C182 (= C271), C187 (= C276), E213 (≠ M307), H217 (≠ L311)
Sites not aligning to the query:
7p9lAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
27% identity, 65% coverage: 136:403/414 of query aligns to 39:303/303 of 7p9lAAA
- binding 2-acetamido-2-deoxy-6-O-phosphono-beta-D-glucopyranose: P66 (= P167), G67 (= G168), S79 (= S180), N105 (= N206), D106 (= D207), G132 (≠ E233), T133 (≠ Q234), G134 (= G235), V135 (= V236), G136 (= G237), E155 (= E256), H158 (= H259), D188 (≠ E278)
- binding zinc ion: H158 (= H259), C179 (= C269), C181 (= C271), C186 (= C276), E212 (≠ M307), H216 (≠ L311)
7p7wBBB Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
27% identity, 65% coverage: 136:403/414 of query aligns to 42:306/306 of 7p7wBBB
3vovB Crystal structure of rok hexokinase from thermus thermophilus (see paper)
37% identity, 46% coverage: 158:346/414 of query aligns to 57:236/298 of 3vovB
4db3A 1.95 angstrom resolution crystal structure of n-acetyl-d-glucosamine kinase from vibrio vulnificus.
25% identity, 71% coverage: 114:405/414 of query aligns to 14:311/311 of 4db3A
6jdbA Crystal structure of n-acetyl mannosmaine kinase in complex with mannac-6p and adp from haemophilus influenzae
30% identity, 40% coverage: 190:354/414 of query aligns to 86:241/290 of 6jdbA
- binding adenosine-5'-diphosphate: S129 (≠ E233), T130 (≠ Q234), P195 (≠ A301), K196 (≠ Q302), S241 (≠ A354)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: N102 (= N206), D103 (= D207), S129 (≠ E233), T130 (≠ Q234), H152 (≠ E256), H155 (= H259), E174 (= E278)
- binding zinc ion: H155 (= H259), C165 (= C269), C167 (= C271), C172 (= C276)
Sites not aligning to the query:
Query Sequence
>3608608 FitnessBrowser__Dino:3608608
MPEDAATRDTPGCGPMLPDSGRNAKPLRQAVFEHVRAAGHAPRMDIARALGISPGSVTTL
TSDLIEAGFLTEIAAPARETGRGRPPVALAVVPAARYVLGLRLSDEMHTVSLSDFSGTEL
ATAHRASQPGRYAVEALLTEMATLIDEVLAAAALPRDRVAALGVGLPGAVHHETGRVAWS
PILAGQDHALQAIIEDRFGLPAHLENDANVLTLAELWFGAGRAMQDFAVVTIEQGVGMGL
VLNNRLFRGAQGLGLELGHTKVQLDGALCRCGQRGCLEAYLADYALVREASTALDRDPRS
AQTAAAMLESLFDQAKAGNGAAKAIFQRAGRFLSLGLANVVQLFDPELIILSGARMRYDY
LYAEEVLAEMQRMTLHPATPRSRVEIHAWGDQVWARGATALALSAVTDALMGER
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