SitesBLAST
Comparing HSERO_RS00305 FitnessBrowser__HerbieS:HSERO_RS00305 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)
1cevA Arginase from bacillus caldovelox, native structure at ph 5.6 (see paper)
42% identity, 99% coverage: 1:300/302 of query aligns to 1:299/299 of 1cevA
- active site: H99 (= H97), D122 (= D124), H124 (= H126), D126 (= D128), H139 (= H141), D226 (= D227), D228 (= D229), E271 (= E272)
- binding manganese (ii) ion: H99 (= H97), D122 (= D124), D122 (= D124), H124 (= H126), D126 (= D128), D226 (= D227), D226 (= D227), D228 (= D229)
P53608 Arginase; EC 3.5.3.1 from Bacillus caldovelox (see paper)
42% identity, 99% coverage: 1:300/302 of query aligns to 1:299/299 of P53608
5cevA Arginase from bacillus caldevelox, l-lysine complex (see paper)
42% identity, 98% coverage: 4:300/302 of query aligns to 3:298/298 of 5cevA
- active site: H98 (= H97), D121 (= D124), H123 (= H126), D125 (= D128), H138 (= H141), D225 (= D227), D227 (= D229), E270 (= E272)
- binding guanidine: H251 (≠ Q253), E255 (= E257)
- binding lysine: S134 (≠ T137), H138 (= H141), E270 (= E272)
- binding manganese (ii) ion: H98 (= H97), D121 (= D124), D121 (= D124), H123 (= H126), D125 (= D128), D225 (= D227), D225 (= D227), D227 (= D229)
4cevA Arginase from bacillus caldevelox, l-ornithine complex (see paper)
42% identity, 98% coverage: 4:300/302 of query aligns to 3:298/298 of 4cevA
- active site: H98 (= H97), D121 (= D124), H123 (= H126), D125 (= D128), H138 (= H141), D225 (= D227), D227 (= D229), E270 (= E272)
- binding guanidine: H251 (≠ Q253), E255 (= E257)
- binding manganese (ii) ion: H98 (= H97), D121 (= D124), D121 (= D124), H123 (= H126), D125 (= D128), D225 (= D227), D225 (= D227), D227 (= D229)
- binding L-ornithine: H123 (= H126), D125 (= D128), S134 (≠ T137), H138 (= H141), D177 (= D180)
3cevA Arginase from bacillus caldevelox, complexed with l-arginine (see paper)
42% identity, 98% coverage: 4:300/302 of query aligns to 3:298/298 of 3cevA
- active site: H98 (= H97), D121 (= D124), H123 (= H126), D125 (= D128), H138 (= H141), D225 (= D227), D227 (= D229), E270 (= E272)
- binding arginine: H123 (= H126), D125 (= D128), S134 (≠ T137), H138 (= H141), D225 (= D227), H251 (≠ Q253), E255 (= E257), E270 (= E272), E295 (≠ K297), L297 (≠ T299)
- binding manganese (ii) ion: H98 (= H97), D121 (= D124), D125 (= D128), D225 (= D227)
2cevB Arginase from bacillus caldevelox, native structure at ph 8.5 (see paper)
42% identity, 98% coverage: 4:300/302 of query aligns to 3:298/298 of 2cevB
- active site: H98 (= H97), D121 (= D124), H123 (= H126), D125 (= D128), H138 (= H141), D225 (= D227), D227 (= D229), E270 (= E272)
- binding guanidine: H251 (≠ Q253), E255 (= E257)
- binding manganese (ii) ion: H98 (= H97), D121 (= D124), D121 (= D124), H123 (= H126), D125 (= D128), D225 (= D227), D225 (= D227), D227 (= D229)
6nfpD 1.7 angstrom resolution crystal structure of arginase from bacillus subtilis subsp. Subtilis str. 168
40% identity, 98% coverage: 4:300/302 of query aligns to 6:289/289 of 6nfpD
6nfpA 1.7 angstrom resolution crystal structure of arginase from bacillus subtilis subsp. Subtilis str. 168
40% identity, 98% coverage: 4:300/302 of query aligns to 3:292/292 of 6nfpA
6dktA Crystal structure of arginase from bacillus subtilis
40% identity, 98% coverage: 4:300/302 of query aligns to 3:283/283 of 6dktA
6nbkA Crystal structure of arginase from bacillus cereus
39% identity, 98% coverage: 2:298/302 of query aligns to 1:287/289 of 6nbkA
2ef5A Crystal structure of the arginase from thermus thermophilus
43% identity, 99% coverage: 2:300/302 of query aligns to 1:273/273 of 2ef5A
- active site: H80 (= H97), D102 (= D124), H104 (= H126), D106 (= D128), H118 (= H141), D200 (= D227), D202 (= D229), E245 (= E272)
- binding lysine: P9 (= P10), D15 (≠ S16), M16 (= M22), S19 (≠ A25)
- binding manganese (ii) ion: H80 (= H97), D102 (= D124), D102 (= D124), H104 (= H126), D106 (= D128), D200 (= D227), D200 (= D227), D202 (= D229)
6dktE Crystal structure of arginase from bacillus subtilis
37% identity, 98% coverage: 4:300/302 of query aligns to 3:268/268 of 6dktE
1hq5A Crystal structure of the binuclear manganese metalloenzyme arginase complexed with s-(2-boronoethyl)-l-cysteine, an l-arginine analogue (see paper)
36% identity, 97% coverage: 4:296/302 of query aligns to 3:300/308 of 1hq5A
- active site: H96 (= H97), D119 (= D124), H121 (= H126), D123 (= D128), H136 (= H141), D227 (= D227), D229 (= D229), E272 (= E272)
- binding manganese (ii) ion: H96 (= H97), D119 (= D124), D119 (= D124), H121 (= H126), D123 (= D128), D227 (= D227), D227 (= D227), D229 (= D229)
- binding s-2-(boronoethyl)-l-cysteine: D119 (= D124), H121 (= H126), D123 (= D128), S132 (≠ T137), H136 (= H141), D178 (= D180), D227 (= D227), D229 (= D229), E272 (= E272)
1d3vA Crystal structure of the binuclear manganese metalloenzyme arginase complexed with 2(s)-amino-6-boronohexanoic acid, an l-arginine analog (see paper)
36% identity, 97% coverage: 4:296/302 of query aligns to 3:300/308 of 1d3vA
- active site: H96 (= H97), D119 (= D124), H121 (= H126), D123 (= D128), H136 (= H141), D227 (= D227), D229 (= D229), E272 (= E272)
- binding 2(s)-amino-6-boronohexanoic acid: H96 (= H97), D119 (= D124), H121 (= H126), D123 (= D128), N125 (= N130), S132 (≠ T137), H136 (= H141), D227 (= D227)
- binding manganese (ii) ion: H96 (= H97), D119 (= D124), D119 (= D124), H121 (= H126), D123 (= D128), D227 (= D227), D227 (= D227), D229 (= D229)
P07824 Arginase-1; Liver-type arginase; Type I arginase; EC 3.5.3.1 from Rattus norvegicus (Rat) (see 7 papers)
36% identity, 97% coverage: 4:296/302 of query aligns to 8:305/323 of P07824
- H101 (= H97) binding ; mutation to E: Reduced catalytic activity. No effect on manganese binding.
- D124 (= D124) binding ; binding
- H126 (= H126) binding
- D128 (= D128) binding ; mutation D->E,N: Reduced manganese binding and strongly reduced catalytic activity.
- H141 (= H141) mutation H->A,C,D: Strongly reduced catalytic activity. Minor effect on affinity for arginine.; mutation to N: Reduced affinity for arginine and reduced catalytic activity.
- D232 (= D227) binding ; binding ; mutation to A: Loss of one manganese ion and strongly reduced catalytic activity.; mutation to C: Reduced manganese binding and strongly reduced catalytic activity.
- D234 (= D229) binding ; mutation D->A,E,H: Reduced manganese binding and strongly reduced catalytic activity.
- G235 (≠ F230) mutation to A: 56% of wild-type activity.; mutation to R: Loss of manganese-binding and activity.
1t4tA Arginase-dinor-noha complex (see paper)
36% identity, 97% coverage: 4:296/302 of query aligns to 3:300/314 of 1t4tA
- active site: H96 (= H97), D119 (= D124), H121 (= H126), D123 (= D128), H136 (= H141), D227 (= D227), D229 (= D229), E272 (= E272)
- binding 3-{[(e)-amino(hydroxyimino)methyl]amino}alanine: H121 (= H126), D123 (= D128), N125 (= N130), D178 (= D180), T241 (= T241)
- binding manganese (ii) ion: H96 (= H97), D119 (= D124), D119 (= D124), H121 (= H126), D123 (= D128), D227 (= D227), D227 (= D227), D229 (= D229)
1t4sA Arginase-l-valine complex (see paper)
36% identity, 97% coverage: 4:296/302 of query aligns to 3:300/314 of 1t4sA
- active site: H96 (= H97), D119 (= D124), H121 (= H126), D123 (= D128), H136 (= H141), D227 (= D227), D229 (= D229), E272 (= E272)
- binding manganese (ii) ion: H96 (= H97), D119 (= D124), D119 (= D124), H121 (= H126), D123 (= D128), D227 (= D227), D227 (= D227), D229 (= D229)
- binding valine: H121 (= H126), S132 (≠ T137), H136 (= H141), D178 (= D180)
1t4rA Arginase-descarboxy-nor-noha complex (see paper)
36% identity, 97% coverage: 4:296/302 of query aligns to 3:300/314 of 1t4rA
- active site: H96 (= H97), D119 (= D124), H121 (= H126), D123 (= D128), H136 (= H141), D227 (= D227), D229 (= D229), E272 (= E272)
- binding 3-{[(e)-amino(hydroxyimino)methyl]amino}propan-1-aminium: H121 (= H126), D123 (= D128), H136 (= H141), T241 (= T241)
- binding manganese (ii) ion: H96 (= H97), D119 (= D124), D119 (= D124), H121 (= H126), D123 (= D128), D227 (= D227), D227 (= D227), D229 (= D229)
1t4pA Arginase-dehydro-abh complex (see paper)
36% identity, 97% coverage: 4:296/302 of query aligns to 3:300/314 of 1t4pA
- active site: H96 (= H97), D119 (= D124), H121 (= H126), D123 (= D128), H136 (= H141), D227 (= D227), D229 (= D229), E272 (= E272)
- binding [(1e,5s)-5-amino-5-carboxypent-1-enyl](trihydroxy)borate(1-): D119 (= D124), H121 (= H126), D123 (= D128), H136 (= H141), G137 (= G142), D178 (= D180), D227 (= D227), D229 (= D229), E272 (= E272)
- binding manganese (ii) ion: H96 (= H97), D119 (= D124), D119 (= D124), H121 (= H126), D123 (= D128), D227 (= D227), D227 (= D227), D229 (= D229)
1r1oA Amino acid sulfonamides as transition-state analogue inhibitors of arginase (see paper)
36% identity, 97% coverage: 4:296/302 of query aligns to 3:300/314 of 1r1oA
- active site: H96 (= H97), D119 (= D124), H121 (= H126), D123 (= D128), H136 (= H141), D227 (= D227), D229 (= D229), E272 (= E272)
- binding manganese (ii) ion: H96 (= H97), D119 (= D124), D119 (= D124), H121 (= H126), D123 (= D128), D227 (= D227), D227 (= D227), D229 (= D229)
- binding s-[2-(aminosulfonyl)ethyl]-d-cysteine: D119 (= D124), H121 (= H126), D123 (= D128), D178 (= D180), D227 (= D227), E272 (= E272)
Query Sequence
>HSERO_RS00305 FitnessBrowser__HerbieS:HSERO_RS00305
MNRIRMMGAPTDVGASRRGASMAPAALRVAELQRGLQQHGLDVIDGGDLAGPANPQQPPV
QGLRHLEQVVQWNQTVHEAVAQCLADGELPLLMGGDHALAVGSIAAVAAHCRSQGKELRV
LWLDAHADANTSQSTPTGNIHGMPVACLLGVGPAALTAIGGQTPALQPQQICQVGIRSVD
REEKRHLRELGVRVFDMRHIDEYGMRQTMEEALAGVGPQTHLHVSFDVDFLDAALAPGVG
TAVPGGPTYREAQLCMEMIADTGALASLDVMELNPACDVRNQTAELVVDLVESLFGKSTL
IR
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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