SitesBLAST
Comparing GFF3638 FitnessBrowser__Phaeo:GFF3638 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, 96% coverage: 13:398/404 of query aligns to 11:396/396 of 5f7qE
- binding zinc ion: H243 (= H250), C253 (= C260), C255 (= C262), C260 (= C267)
- binding : K12 (≠ R14), N15 (≠ S17), T32 (≠ I34), S43 (≠ A45), T44 (= T46), T67 (≠ R69), G68 (= G70), G68 (= G70), G69 (≠ A71), G69 (≠ A71), R70 (≠ K72), R70 (≠ K72), R71 (= R73), A72 (≠ G74), K73 (≠ R75)
Sites not aligning to the query:
1z05A Crystal structure of the rok family transcriptional regulator, homolog of e.Coli mlc protein.
28% identity, 90% coverage: 20:384/404 of query aligns to 10:378/396 of 1z05A
P50456 DNA-binding transcriptional repressor Mlc; Making large colonies protein; Membrane linked control from Escherichia coli (strain K12) (see 4 papers)
27% identity, 83% coverage: 1:336/404 of query aligns to 1:340/406 of P50456
- R52 (≠ A52) mutation to H: Shows increased expression and forms larger colonies.
- H86 (= H88) mutation to R: Can be bound and inactivated by MtfA.
- F136 (≠ C140) mutation to A: Decreases association with PtsG EIIB domain.
- H247 (= H250) binding
- C257 (= C260) binding ; mutation to A: Strongly reduced activity; when associated with A-259.; mutation to S: Strongly reduced activity; when associated with S-259.
- C259 (= C262) binding ; mutation to A: Strongly reduced activity; when associated with A-257.; mutation to S: Strongly reduced activity; when associated with S-257.
- C264 (= C267) binding
- R306 (≠ E302) mutation to G: Forms dimers but not tetramers; when associated with G-310.
- L310 (≠ M306) mutation to G: Forms dimers but not tetramers; when associated with G-306.
5f7rA Rok repressor lmo0178 from listeria monocytogenes bound to inducer (see paper)
28% identity, 75% coverage: 89:391/404 of query aligns to 3:305/306 of 5f7rA
- binding alpha-D-glucopyranose: K7 (= K93), E10 (≠ H96), G70 (= G159), N110 (≠ D198), N110 (≠ D198), S134 (≠ T222), V135 (= V223), G138 (= G226), L139 (≠ V227), G140 (= G228), E159 (= E247), H162 (= H250), E181 (= E269), E253 (≠ A339), W293 (= W379)
- binding zinc ion: H162 (= H250), C172 (= C260), C174 (= C262), C179 (= C267)
1z6rA Crystal structure of mlc from escherichia coli (see paper)
26% identity, 80% coverage: 12:336/404 of query aligns to 1:316/382 of 1z6rA
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, 62% coverage: 98:346/404 of query aligns to 406:676/722 of O35826
- D413 (= D105) 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.
- R420 (vs. gap) mutation to 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.
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
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, 62% coverage: 98:346/404 of query aligns to 406:676/722 of Q9Y223
- D413 (= D105) binding
- G416 (= G108) binding
- T417 (= T109) binding
- N418 (≠ E110) binding
- R420 (vs. gap) binding
- I472 (= I155) 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 (= G159) binding ; binding
- R477 (≠ V160) binding ; binding
- T489 (≠ S172) binding ; binding
- N516 (= N197) binding ; binding
- D517 (= D198) 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 (= N200) 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 (= A205) 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 (= F209) 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 (= G226) binding
- E566 (= E247) binding
- H569 (= H250) binding ; binding ; binding
- V572 (= V253) 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 (= G257) to E: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs121908625
- C579 (= C260) binding
- C581 (= C262) binding
- C586 (= C267) binding
- I587 (≠ L268) 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 (= E269) binding ; binding
- A630 (= A299) to T: in NM; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
- A631 (≠ V300) 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
- 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)
31% identity, 61% coverage: 99:346/404 of query aligns to 3:268/309 of 2yhwA
2yi1A Crystal structure of n-acetylmannosamine kinase in complex with n- acetyl mannosamine 6-phosphate and adp. (see paper)
32% identity, 61% coverage: 99:346/404 of query aligns to 3:267/308 of 2yi1A
- binding adenosine-5'-diphosphate: G11 (≠ E107), T13 (= T109), N14 (≠ E110), R16 (vs. gap), T140 (≠ H225), G189 (≠ D274), L216 (= L296), V261 (≠ A339)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G12 (= G108), G71 (≠ A158), G72 (= G159), R73 (≠ V160), S84 (= S171), T85 (≠ S172), L87 (= L174), N112 (= N197), D113 (= D198), G139 (≠ E224), T140 (≠ H225), G141 (= G226), I142 (≠ V227), E162 (= E247), H165 (= H250), E184 (= E269)
- binding calcium ion: N112 (= N197), N115 (= N200), G144 (≠ M229), A161 (= A246)
- binding zinc ion: H165 (= H250), C175 (= C260), C177 (= C262), C182 (= C267)
2yhyA Structure of n-acetylmannosamine kinase in complex with n- acetylmannosamine and adp (see paper)
32% identity, 61% coverage: 99:346/404 of query aligns to 3:267/308 of 2yhyA
- binding adenosine-5'-diphosphate: G11 (≠ E107), G12 (= G108), T13 (= T109), N14 (≠ E110), R16 (vs. gap), T140 (≠ H225), G189 (≠ D274), L216 (= L296), V261 (≠ A339)
- binding calcium ion: N112 (= N197), N115 (= N200), G144 (≠ M229), A161 (= A246)
- binding zinc ion: H165 (= H250), C175 (= C260), C177 (= C262), C182 (= C267)
3vglA Crystal structure of a rok family glucokinase from streptomyces griseus in complex with glucose and amppnp (see paper)
30% identity, 67% coverage: 91:360/404 of query aligns to 5:281/312 of 3vglA
- binding phosphoaminophosphonic acid-adenylate ester: G9 (≠ S95), T11 (≠ H97), K12 (≠ A98), G130 (≠ E224), T131 (≠ H225), G180 (≠ D274), G214 (vs. gap), S218 (≠ Y297), G260 (≠ A339), V261 (≠ Q340), E264 (≠ F343)
- binding beta-D-glucopyranose: G65 (= G159), P78 (≠ S172), N103 (= N197), D104 (= D198), L133 (≠ V227), G134 (= G228), E153 (= E247), H156 (= H250), E175 (= E269)
- binding zinc ion: H156 (= H250), C166 (= C260), C168 (= C262), C173 (= C267)
3vgkB Crystal structure of a rok family glucokinase from streptomyces griseus (see paper)
30% identity, 67% coverage: 91:360/404 of query aligns to 5:281/312 of 3vgkB
3eo3A Crystal structure of the n-acetylmannosamine kinase domain of human gne protein (see paper)
38% identity, 41% coverage: 180:346/404 of query aligns to 70:247/288 of 3eo3A
2qm1B Crystal structure of glucokinase from enterococcus faecalis
25% identity, 64% coverage: 132:389/404 of query aligns to 50:321/325 of 2qm1B
3vovB Crystal structure of rok hexokinase from thermus thermophilus (see paper)
35% identity, 44% coverage: 153:331/404 of query aligns to 61:236/298 of 3vovB
6jdbA Crystal structure of n-acetyl mannosmaine kinase in complex with mannac-6p and adp from haemophilus influenzae
29% identity, 61% coverage: 102:347/404 of query aligns to 4:250/290 of 6jdbA
- binding adenosine-5'-diphosphate: K12 (≠ E110), S129 (≠ E224), T130 (≠ H225), P195 (≠ L293), K196 (≠ A294), S241 (≠ A339)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: T62 (≠ V153), G63 (= G154), A72 (≠ S173), L73 (= L174), N74 (= N175), N77 (= N178), N102 (= N197), D103 (= D198), S129 (≠ E224), T130 (≠ H225), H152 (≠ E247), H155 (= H250), E174 (= E269)
- binding zinc ion: H155 (= H250), C165 (= C260), C167 (= C262), C172 (= C267)
6jdcA Crystal structure of n-acetyl mannosmaine kinase in complex with mannac from haemophilus influenzae
28% identity, 54% coverage: 130:347/404 of query aligns to 34:230/269 of 6jdcA
2gupA Structural genomics, the crystal structure of a rok family protein from streptococcus pneumoniae tigr4 in complex with sucrose
27% identity, 53% coverage: 124:339/404 of query aligns to 32:233/289 of 2gupA
Sites not aligning to the query:
6jdoA Crystal structure of n-acetyl mannosmaine kinase with amp-pnp from pasteurella multocida
28% identity, 43% coverage: 172:346/404 of query aligns to 72:250/293 of 6jdoA
6jdhA Crystal structure of n-acetyl mannosmaine kinase from pasteurella multocida
28% identity, 43% coverage: 172:346/404 of query aligns to 72:250/293 of 6jdhA
Query Sequence
>GFF3638 FitnessBrowser__Phaeo:GFF3638
MVKSDRLSHSGELRESSRLQVFDTIRAAGQIARIDIAQITRISPATVTAITAELLAAGLI
EEVSPDTVRGAKRGRPRVALKIRGSAHHIAGLKLSHHAITTLITDFEGTELISHEMPLRG
GQMSPESLCEKIVEALDQSCAKGGLTRTQISGVGIGMAGVMDAERNFIYWSSSLNVRNID
LGSALKSHLSMPVFIDNDANLVAKAEHLFGEGDTRSNFVVVTVEHGVGMGIVIDNQIYRG
ARGCGAEFGHIKVQLEGALCQCGQRGCLEAYVGDYALLREANITSGVERHKDLASLYAAV
AEGDMMAQSILDRAGRMFAMGLANIVNIFDPQMIVLAGAQLAFGYLSSDKVVEEMRRWVV
QVDGPLPEVRVHGWGNQMWAKGAAAYAIEEVSALTIREVASHAG
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