SitesBLAST
Comparing HSERO_RS19930 FitnessBrowser__HerbieS:HSERO_RS19930 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)
A0A0K2JL82 Nitrosuccinate lyase; EC 4.3.99.5 from Streptomyces cremeus (see paper)
39% identity, 95% coverage: 17:450/455 of query aligns to 34:472/476 of A0A0K2JL82
- N93 (≠ A76) mutation to A: Slight decrease in activity.
- D125 (= D108) mutation D->N,V: Almost loss of activity.
- R137 (≠ E120) binding
- R140 (= R123) binding
- R201 (≠ E185) binding
- H253 (= H227) mutation to A: Loss of activity.
- S302 (= S276) mutation to A: Loss of activity.
- K308 (= K282) binding ; mutation to A: Loss of activity.
- N310 (= N284) binding ; mutation to A: Loss of activity.
- R341 (= R315) mutation to A: Loss of activity.
5xnzA Crystal structure of cred complex with fumarate (see paper)
38% identity, 95% coverage: 17:446/455 of query aligns to 20:437/439 of 5xnzA
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
27% identity, 80% coverage: 14:375/455 of query aligns to 8:360/427 of 2x75A
Sites not aligning to the query:
Q9X0I0 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
24% identity, 92% coverage: 13:430/455 of query aligns to 8:413/431 of Q9X0I0
- H141 (≠ L153) active site, Proton donor/acceptor
P12047 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; Glutamyl--tRNA ligase regulatory factor; EC 4.3.2.2 from Bacillus subtilis (strain 168) (see paper)
27% identity, 80% coverage: 14:375/455 of query aligns to 9:361/431 of P12047
- H89 (= H101) mutation to Q: Abolishes enzyme activity.
- H141 (≠ L153) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ W226) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N284) mutation N->D,L: Abolishes enzyme activity.
- R301 (= R315) mutation R->K,Q: Abolishes enzyme activity.
5nx9D Crystal structure of neanderthal adenylosuccinate lyase (adsl) in complex with its products amp and fumarate (see paper)
28% identity, 71% coverage: 95:416/455 of query aligns to 94:426/477 of 5nx9D
- active site: T151 (= T152), H152 (≠ L153), S283 (= S277), K288 (= K282), E295 (≠ M289)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: T151 (= T152), H152 (≠ L153)
- binding adenosine monophosphate: S105 (= S106), Q234 (vs. gap), R296 (≠ I290), L324 (= L317), S327 (vs. gap), A328 (≠ G318), R331 (≠ Q321)
- binding fumaric acid: S105 (= S106), Q234 (vs. gap), S282 (= S276), S283 (= S277), K288 (= K282)
Sites not aligning to the query:
P30566 Adenylosuccinate lyase; ADSL; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Homo sapiens (Human) (see 13 papers)
28% identity, 71% coverage: 95:416/455 of query aligns to 101:433/484 of P30566
- Y114 (≠ D108) to H: in ADSLD; severe; total loss of activity; dbSNP:rs374259530
- R141 (= R135) to W: in ADSLD; severe; dbSNP:rs756210458
- H159 (≠ L153) active site, Proton donor/acceptor
- R190 (≠ A184) to Q: in ADSLD; moderate; dbSNP:rs28941471
- R194 (≠ L188) to C: in ADSLD; severe; reduces protein stability; dbSNP:rs1465152683
- K246 (≠ D231) to E: in ADSLD; moderate; strongly reduced catalytic activity; dbSNP:rs119450944
- D268 (= D253) to N: in ADSLD; severe; total loss of activity; dbSNP:rs746501563
- S289 (= S276) active site, Proton donor/acceptor
- R303 (≠ I290) to C: in ADSLD; mild; strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR; abolishes cooperativity; dbSNP:rs373458753
- L311 (vs. gap) to V: in ADSLD; severe; slightly reduced enzyme activity
- P318 (= P299) to L: in ADSLD; severe; dbSNP:rs202064195
- V364 (≠ I350) to M: in ADSLD; severe; dbSNP:rs370851726
- R374 (≠ D360) to W: in ADSLD; severe; dbSNP:rs376533026
- S395 (≠ G380) to R: in ADSLD; severe
- R396 (= R381) to C: in ADSLD; severe; abolishes cooperativity and reduces enzyme activity; dbSNP:rs755492501; to H: in ADSLD; severe; abolishes cooperativity and reduces enzyme activity; dbSNP:rs763542069
- D422 (≠ V405) to Y: in ADSLD; moderate; dbSNP:rs119450943
- L423 (= L406) to V: in ADSLD; moderate
- R426 (≠ A409) to H: in ADSLD; severe; most frequent mutation; dbSNP:rs119450941
- D430 (= D413) to N: in ADSLD; mild; dbSNP:rs554254383
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine; A → V: in ADSLD; severe; dbSNP:rs143083947
- 3 A → V: in ADSLD; severe
- 26 M → L: in ADSLD; severe; dbSNP:rs1311171245
- 72 I → V: in ADSLD; severe
- 100 P → A: in ADSLD; moderate; dbSNP:rs119450942
- 438 S → P: in ADSLD; severe; dbSNP:rs119450940
- 447 S → P: in ADSLD; severe; dbSNP:rs777821034
- 450 T → S: in ADSLD; moderate; dbSNP:rs372895468
- 452 R → P: in ADSLD; severe
5nxaB Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
28% identity, 69% coverage: 103:416/455 of query aligns to 40:364/415 of 5nxaB
- active site: T89 (= T152), H90 (≠ L153), S221 (= S277), K226 (= K282), E233 (≠ M289)
- binding aminoimidazole 4-carboxamide ribonucleotide: M230 (≠ V286), R234 (≠ I290)
- binding fumaric acid: S220 (= S276), S221 (= S277), M223 (= M279), K226 (= K282), N228 (= N284)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: S43 (= S106), T89 (= T152), H90 (≠ L153), Q172 (vs. gap), L262 (= L317), S265 (vs. gap), A266 (≠ G318), R269 (≠ Q321)
Sites not aligning to the query:
Q05911 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
28% identity, 66% coverage: 96:397/455 of query aligns to 99:409/482 of Q05911
- K196 (≠ G193) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
5eytA Crystal structure of adenylosuccinate lyase from schistosoma mansoni in complex with amp (see paper)
25% identity, 68% coverage: 88:398/455 of query aligns to 86:401/472 of 5eytA
Sites not aligning to the query:
4eeiB Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with amp and succinate
24% identity, 57% coverage: 92:350/455 of query aligns to 80:324/423 of 4eeiB
Sites not aligning to the query:
5hw2A Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with fumaric acid
24% identity, 57% coverage: 92:350/455 of query aligns to 80:324/419 of 5hw2A
Sites not aligning to the query:
4efcA Crystal structure of adenylosuccinate lyase from trypanosoma brucei, tb427tmp.160.5560
31% identity, 45% coverage: 81:286/455 of query aligns to 104:309/452 of 4efcA
Sites not aligning to the query:
- active site: 96, 312
- binding adenosine monophosphate: 18, 19, 95, 96, 97, 313, 339, 341, 344, 345, 348
5nxaA Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
26% identity, 71% coverage: 95:416/455 of query aligns to 94:413/464 of 5nxaA
- active site: T151 (= T152), H152 (≠ L153), K275 (= K282), E282 (≠ M289)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: T104 (= T105), S105 (= S106), Q234 (vs. gap), K275 (= K282), R283 (≠ I290), L311 (= L317), S314 (vs. gap), A315 (≠ G318), R318 (≠ Q321)
Sites not aligning to the query:
5nxaC Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
27% identity, 65% coverage: 95:391/455 of query aligns to 93:379/418 of 5nxaC
- active site: T150 (= T152), H151 (≠ L153), K276 (= K282), E283 (≠ M289)
- binding aminoimidazole 4-carboxamide ribonucleotide: Q233 (vs. gap), L312 (= L317), S315 (vs. gap), A316 (≠ G318), R319 (≠ Q321)
- binding fumaric acid: T103 (= T105), S104 (= S106), Q233 (vs. gap)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: T150 (= T152), H151 (≠ L153), K276 (= K282), R284 (≠ I290)
Sites not aligning to the query:
5nx9C Crystal structure of neanderthal adenylosuccinate lyase (adsl) in complex with its products amp and fumarate (see paper)
26% identity, 71% coverage: 95:416/455 of query aligns to 93:402/441 of 5nx9C
- active site: T150 (= T152), H151 (≠ L153), E280 (≠ M289)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: T103 (= T105), S104 (= S106), Q233 (vs. gap), M277 (≠ V286), R281 (≠ I290), L309 (= L317), S312 (vs. gap), A313 (≠ G318), R316 (≠ Q321)
- binding fumaric acid: T150 (= T152), H151 (≠ L153)
Sites not aligning to the query:
2ptrA Crystal structure of escherichia coli adenylosuccinate lyase mutant h171a with bound adenylosuccinate substrate (see paper)
27% identity, 41% coverage: 100:287/455 of query aligns to 117:306/454 of 2ptrA
- active site: T170 (= T152), A171 (≠ L153), K301 (= K282)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: T122 (= T105), S123 (= S106), Q247 (vs. gap), S295 (= S276), S296 (= S277), M298 (= M279), K301 (= K282), N303 (= N284)
Sites not aligning to the query:
- active site: 91, 308
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: 15, 16, 91, 92, 309, 335, 337, 340, 341, 344
5vkwB Crystal structure of adenylosuccinate lyase ade13 from candida albicans
27% identity, 66% coverage: 96:397/455 of query aligns to 99:402/469 of 5vkwB
Sites not aligning to the query:
2ptqA Crystal structure of escherichia coli adenylosuccinate lyase mutant h171n with bound amp and fumarate (see paper)
27% identity, 41% coverage: 100:287/455 of query aligns to 117:306/459 of 2ptqA
- active site: T170 (= T152), N171 (≠ L153), S296 (= S277), K301 (= K282)
- binding adenosine monophosphate: Q247 (vs. gap)
- binding fumaric acid: T122 (= T105), S123 (= S106), Q247 (vs. gap), S295 (= S276), S296 (= S277), M298 (= M279), K301 (= K282), N303 (= N284)
Sites not aligning to the query:
- active site: 91, 308
- binding adenosine monophosphate: 15, 16, 90, 91, 309, 335, 337, 340, 341, 344
- binding fumaric acid: 91
P0AB89 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Escherichia coli (strain K12) (see 2 papers)
26% identity, 41% coverage: 100:287/455 of query aligns to 117:306/456 of P0AB89
- TS 122:123 (= TS 105:106) binding ; binding
- H171 (≠ L153) mutation H->A,N: Reduces catalytic activity about 500-fold.
- Q247 (vs. gap) binding ; binding ; binding
- S295 (= S276) mutation to A: Reduces catalytic activity about 1000-fold.
- S296 (= S277) binding ; binding
- KVN 301:303 (≠ KRN 282:284) binding ; binding
Sites not aligning to the query:
- 15:16 binding ; binding
- 90:92 binding ; binding
- 91 binding
- 94 modified: N6-acetyllysine
- 309 binding ; binding
- 335 binding ; binding
- 340:344 binding ; binding
- 366 modified: N6-acetyllysine
Query Sequence
>HSERO_RS19930 FitnessBrowser__HerbieS:HSERO_RS19930
MSVSIFDSFLTTSEMIAVFDDQAVVQAMLRFEQVLAEAQAAEGVIPDAAARAIASVCRAP
LYDIPALIVAGRRAGALAIPLVKELQRTVALYSEEAATHVHWGSTSQDVLDTAMVLVTRE
ALRLVEGELEQLSRRLLDLAQSHLDTPVLARTLMQPAQVTSLGLKFCNWAAPLLRSRAQL
QALAERALQLQLGGAVGTLTVLGEKGPAVAARMAAALELKTPEAAWHTQRDQWIRLGAEM
AVLAGSLGKIATDLSLMAQGEIAELAEPSGNGRGGSSAMPHKRNPVSSMIALAAAARAPQ
QAAALLAAMSQQHERGLGNWQAELAEWPALFLGVHGALRALNDAFAGLVIDAPRMLRNID
ALQGLVFAESASIALAGVIGRPRAHSLLEQLTRKAVADGAQLVDVLVDAVQADAQLRKEI
DLPMLRGLFDPVQATRPARRIAEGQLEHLRTLLAQ
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