SitesBLAST
Comparing CA265_RS15640 FitnessBrowser__Pedo557:CA265_RS15640 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)
5f7qE Rok repressor lmo0178 from listeria monocytogenes bound to operator (see paper)
28% identity, 97% coverage: 12:395/395 of query aligns to 16:391/396 of 5f7qE
- binding zinc ion: H243 (= H239), C253 (= C249), C255 (= C251), C260 (= C256)
- binding : T32 (= T28), S43 (≠ P39), T44 (≠ L40), T67 (= T63), G68 (= G64), G68 (= G64), G69 (= G65), G69 (= G65), R70 (= R66), R70 (= R66), R71 (= R67), A72 (≠ P68), K73 (≠ L69)
Sites not aligning to the query:
1z05A Crystal structure of the rok family transcriptional regulator, homolog of e.Coli mlc protein.
25% identity, 96% coverage: 15:395/395 of query aligns to 11:386/396 of 1z05A
2qm1B Crystal structure of glucokinase from enterococcus faecalis
31% identity, 69% coverage: 121:392/395 of query aligns to 49:323/325 of 2qm1B
5f7rA Rok repressor lmo0178 from listeria monocytogenes bound to inducer (see paper)
28% identity, 80% coverage: 80:394/395 of query aligns to 2:306/306 of 5f7rA
- binding alpha-D-glucopyranose: K7 (≠ A85), E10 (≠ Q88), G70 (= G149), N110 (≠ D187), N110 (≠ D187), S134 (≠ N211), V135 (≠ I212), G138 (= G215), L139 (≠ T216), G140 (= G217), E159 (= E236), H162 (= H239), E181 (= E258), E253 (≠ R340), W293 (≠ L381)
- binding zinc ion: H162 (= H239), C172 (= C249), C174 (= C251), C179 (= C256)
1z6rA Crystal structure of mlc from escherichia coli (see paper)
26% identity, 93% coverage: 26:394/395 of query aligns to 21:371/382 of 1z6rA
P50456 DNA-binding transcriptional repressor Mlc; Making large colonies protein; Membrane linked control from Escherichia coli (strain K12) (see 4 papers)
24% identity, 93% coverage: 26:394/395 of query aligns to 32:395/406 of P50456
- R52 (≠ N46) mutation to H: Shows increased expression and forms larger colonies.
- H86 (≠ R79) mutation to R: Can be bound and inactivated by MtfA.
- F136 (≠ I130) mutation to A: Decreases association with PtsG EIIB domain.
- H247 (= H239) binding
- C257 (= C249) binding ; mutation to A: Strongly reduced activity; when associated with A-259.; mutation to S: Strongly reduced activity; when associated with S-259.
- C259 (= C251) binding ; mutation to A: Strongly reduced activity; when associated with A-257.; mutation to S: Strongly reduced activity; when associated with S-257.
- C264 (= C256) binding
- R306 (≠ K303) mutation to G: Forms dimers but not tetramers; when associated with G-310.
- L310 (≠ V307) mutation to G: Forms dimers but not tetramers; when associated with G-306.
3vglA Crystal structure of a rok family glucokinase from streptomyces griseus in complex with glucose and amppnp (see paper)
27% identity, 68% coverage: 118:387/395 of query aligns to 35:308/312 of 3vglA
- binding phosphoaminophosphonic acid-adenylate ester: G130 (= G213), T131 (≠ W214), G180 (≠ L263), G214 (vs. gap), S218 (≠ L298), G260 (≠ R340), V261 (≠ G341), E264 (≠ A344)
- binding beta-D-glucopyranose: G65 (= G149), P78 (≠ M162), N103 (= N186), D104 (= D187), L133 (≠ T216), G134 (= G217), E153 (= E236), H156 (= H239), E175 (= E258)
- binding zinc ion: H156 (= H239), C166 (= C249), C168 (= C251), C173 (= C256)
Sites not aligning to the query:
3vgkB Crystal structure of a rok family glucokinase from streptomyces griseus (see paper)
27% identity, 68% coverage: 118:387/395 of query aligns to 35:308/312 of 3vgkB
2yi1A Crystal structure of n-acetylmannosamine kinase in complex with n- acetyl mannosamine 6-phosphate and adp. (see paper)
34% identity, 51% coverage: 140:339/395 of query aligns to 63:260/308 of 2yi1A
- binding adenosine-5'-diphosphate: T140 (≠ W214), G189 (≠ L263), L216 (≠ D295)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G71 (≠ P148), G72 (= G149), R73 (≠ F150), S84 (≠ N158), T85 (≠ Y159), L87 (≠ F161), N112 (= N186), D113 (= D187), G139 (= G213), T140 (≠ W214), G141 (= G215), I142 (≠ T216), E162 (= E236), H165 (= H239), E184 (= E258)
- binding calcium ion: N112 (= N186), N115 (≠ S189), G144 (≠ L218), A161 (≠ G235)
- binding zinc ion: H165 (= H239), C175 (= C249), C177 (= C251), C182 (= C256)
Sites not aligning to the query:
2yhyA Structure of n-acetylmannosamine kinase in complex with n- acetylmannosamine and adp (see paper)
34% identity, 51% coverage: 140:339/395 of query aligns to 63:260/308 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)
33% identity, 51% coverage: 140:339/395 of query aligns to 467:669/722 of Q9Y223
- I472 (= I145) 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 (= G149) binding ; binding
- R477 (≠ F150) binding ; binding
- T489 (≠ Y159) binding ; binding
- N516 (= N186) binding ; binding
- D517 (= D187) 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 (≠ S189) 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 (= A194) 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 (= F198) 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 (= G215) binding
- E566 (= E236) binding
- H569 (= H239) binding ; binding ; binding
- V572 (≠ L242) 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 (≠ N246) to E: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs121908625
- C579 (= C249) binding
- C581 (= C251) binding
- C586 (= C256) binding
- I587 (≠ L257) 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 (= E258) binding ; binding
- A630 (= A300) to T: in NM; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
- A631 (≠ V301) 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.
2yhwA High-resolution crystal structures of n-acetylmannosamine kinase: insights about substrate specificity, activity and inhibitor modelling. (see paper)
33% identity, 51% coverage: 140:339/395 of query aligns to 63:261/309 of 2yhwA
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)
32% identity, 51% coverage: 140:339/395 of query aligns to 467:669/722 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.
3eo3A Crystal structure of the n-acetylmannosamine kinase domain of human gne protein (see paper)
32% identity, 46% coverage: 157:339/395 of query aligns to 58:240/288 of 3eo3A
P32718 D-allose kinase; Allokinase; EC 2.7.1.55 from Escherichia coli (strain K12) (see paper)
29% identity, 50% coverage: 142:339/395 of query aligns to 66:246/309 of P32718
- A73 (≠ G149) mutation to G: 60-fold increase in catalytic efficiency for glucose phosphorylation. 45-fold increase in D-glucose affinity. No change in catalytic efficiency for D-allose phosphorylation.
- F145 (≠ L218) mutation to L: 10-fold increase in catalytic efficiency for glucose phosphorylation. Slight increase in catalytic efficiency for D-allose phosphorylation.
Q93LQ8 Beta-glucoside kinase; EC 2.7.1.85 from Klebsiella pneumoniae (see paper)
24% identity, 50% coverage: 142:339/395 of query aligns to 56:242/297 of Q93LQ8
- D103 (= D187) mutation to G: Loss of catalytic activity.
- G131 (= G215) mutation to A: Loss of catalytic activity.
- G133 (= G217) mutation to A: Loss of catalytic activity.
Sites not aligning to the query:
- 7 D→G: Loss of catalytic activity.
- 9 G→A: Loss of catalytic activity.
3vovB Crystal structure of rok hexokinase from thermus thermophilus (see paper)
28% identity, 48% coverage: 143:332/395 of query aligns to 61:236/298 of 3vovB
2gupA Structural genomics, the crystal structure of a rok family protein from streptococcus pneumoniae tigr4 in complex with sucrose
34% identity, 30% coverage: 135:253/395 of query aligns to 47:171/289 of 2gupA
Sites not aligning to the query:
7p9lAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
32% identity, 29% coverage: 143:258/395 of query aligns to 61:188/303 of 7p9lAAA
- binding 2-acetamido-2-deoxy-6-O-phosphono-beta-D-glucopyranose: P66 (= P148), G67 (= G149), S79 (= S160), N105 (= N186), D106 (= D187), G132 (= G213), T133 (≠ W214), G134 (= G215), V135 (≠ T216), G136 (= G217), E155 (= E236), H158 (= H239), D188 (≠ E258)
- binding zinc ion: H158 (= H239), C179 (= C249), C181 (= C251), C186 (= C256)
Sites not aligning to the query:
7p9pAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
32% identity, 29% coverage: 143:258/395 of query aligns to 62:189/304 of 7p9pAAA
Sites not aligning to the query:
Query Sequence
>CA265_RS15640 FitnessBrowser__Pedo557:CA265_RS15640
MSATIKKAQRLRADIIKLLYYKKKSSLTDLSKRTKKSLPLITSTVNALIEDGLIIEQGLA
PSTGGRRPLNFLLNPDYKRYIIAVAMDQLTSQLTIYDLSNHQVLPTQVIDLDMTQSKSAD
TLIEFIDHCIKKSTIDKENLLGIGIGMPGFVNAEKGMNYSFMQVENDISLQDYLAKKLRL
PVYIDNDSSLIALAELNFGEARNLKDVLVVNIGWGTGLGMIINGKLYRGSSGYAGEFSHI
PLSNSNTLCSCGKRGCLEVETSLLVMVQKAEEAVKNGEETSLKTLFNDKSKSHVDHFLNA
VVKQDPVAISILADAAFQIGKGLATLIHIMNPERIVLSGRGAKAGKMLLPPIQQAINEFC
IPRVAEQTEIKCSSLSDEAELLAAASLMVENSLFE
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