SitesBLAST
Comparing AZOBR_RS16895 FitnessBrowser__azobra:AZOBR_RS16895 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)
6z1mA Structure of an ancestral glycosidase (family 1) bound to heme (see paper)
46% identity, 91% coverage: 40:478/482 of query aligns to 3:423/423 of 6z1mA
- binding protoporphyrin ix containing fe: P164 (= P201), N165 (≠ S202), L194 (≠ Q231), L195 (≠ N232), L218 (= L257), L220 (= L259), N244 (= N283), F247 (≠ C286), K253 (≠ R292), Y256 (= Y295), L288 (≠ I319), R318 (≠ E371), Y323 (= Y376)
- binding magnesium ion: H346 (≠ Q401), K409 (≠ A464)
4ptwA Halothermothrix orenii beta-glucosidase a, 2-deoxy-2-fluoro-glucose complex (see paper)
46% identity, 91% coverage: 40:478/482 of query aligns to 3:445/445 of 4ptwA
- active site: R74 (= R111), H118 (= H155), E163 (= E200), V166 (= V203), N291 (= N325), Y293 (= Y327), E351 (= E385)
- binding 2-deoxy-2-fluoro-alpha-D-glucopyranose: Q17 (= Q54), H118 (= H155), E163 (= E200), Y293 (= Y327), E351 (= E385), W398 (= W432), E405 (= E439), W406 (= W440)
4ptvA Halothermothrix orenii beta-glucosidase a, thiocellobiose complex (see paper)
46% identity, 91% coverage: 40:478/482 of query aligns to 3:445/445 of 4ptvA
- active site: R74 (= R111), H118 (= H155), E163 (= E200), V166 (= V203), N291 (= N325), Y293 (= Y327), E351 (= E385)
- binding beta-D-glucopyranose: W324 (= W358), E405 (= E439), Y408 (≠ E442)
- binding 4-thio-beta-D-glucopyranose: Q17 (= Q54), H118 (= H155), E163 (= E200), Y293 (= Y327), E351 (= E385), W398 (= W432), E405 (= E439), W406 (= W440)
1uz1A Family 1 b-glucosidase from thermotoga maritima in complex with isofagomine lactam (see paper)
46% identity, 92% coverage: 37:478/482 of query aligns to 1:438/439 of 1uz1A
- active site: R75 (= R111), H119 (= H155), E164 (= E200), V167 (= V203), N290 (= N325), Y292 (= Y327), E345 (= E385)
- binding (3s,4r,5r)-3,4-dihydroxy-5-(hydroxymethyl)piperidin-2-one: Q18 (= Q54), H119 (= H155), N163 (= N199), E164 (= E200), Y292 (= Y327), E345 (= E385), W392 (= W432), E399 (= E439), W400 (= W440), F408 (= F448)
2cesA Beta-glucosidase from thermotoga maritima in complex with glucoimidazole (see paper)
46% identity, 92% coverage: 37:478/482 of query aligns to 1:439/440 of 2cesA
- active site: R75 (= R111), H119 (= H155), E164 (= E200), V167 (= V203), N291 (= N325), Y293 (= Y327), E346 (= E385)
- binding glucoimidazole: Q18 (= Q54), H119 (= H155), N163 (= N199), E164 (= E200), Y293 (= Y327), E346 (= E385), W393 (= W432), E400 (= E439), W401 (= W440), F409 (= F448)
2cbvA Beta-glucosidase from thermotoga maritima in complex with calystegine b2 (see paper)
46% identity, 92% coverage: 37:478/482 of query aligns to 1:441/443 of 2cbvA
- active site: R75 (= R111), H119 (= H155), E164 (= E200), V167 (= V203), N290 (= N325), Y292 (= Y327), E348 (= E385)
- binding calystegine b2: Q18 (= Q54), H119 (= H155), W120 (= W156), N163 (= N199), E164 (= E200), E348 (= E385), W395 (= W432), E402 (= E439), W403 (= W440)
1oimA Family 1 b-glucosidase from thermotoga maritima (see paper)
46% identity, 92% coverage: 37:478/482 of query aligns to 1:441/443 of 1oimA
- active site: R75 (= R111), H119 (= H155), E164 (= E200), V167 (= V203), N290 (= N325), Y292 (= Y327), E348 (= E385)
- binding 1-deoxynojirimycin: Q18 (= Q54), H119 (= H155), N163 (= N199), E164 (= E200), Y292 (= Y327), E348 (= E385), W395 (= W432), E402 (= E439), W403 (= W440)
2j7eA Beta-glucosidase from thermotoga maritima in complex with methyl acetate-substituted glucoimidazole (see paper)
46% identity, 92% coverage: 37:478/482 of query aligns to 1:435/436 of 2j7eA
- active site: R75 (= R111), H119 (= H155), E164 (= E200), V167 (= V203), N287 (= N325), Y289 (= Y327), E342 (= E385)
- binding methyl acetate-substituted glucoimidazole: Q18 (= Q54), H119 (= H155), N163 (= N199), E164 (= E200), N220 (≠ S258), Y289 (= Y327), E342 (= E385), W389 (= W432), E396 (= E439), W397 (= W440), F405 (= F448)
2j7fA Beta-glucosidase from thermotoga maritima in complex with carboxylate- substituted glucoimidazole (see paper)
46% identity, 92% coverage: 37:478/482 of query aligns to 1:434/435 of 2j7fA
- active site: R75 (= R111), H119 (= H155), E164 (= E200), V167 (= V203), N286 (= N325), Y288 (= Y327), E341 (= E385)
- binding carboxylate-substituted glucoimidazole: Q18 (= Q54), H119 (= H155), E164 (= E200), Y288 (= Y327), W314 (= W358), E341 (= E385), W388 (= W432), E395 (= E439), W396 (= W440), F404 (= F448)
2cetA Beta-glucosidase from thermotoga maritima in complex with phenethyl- substituted glucoimidazole (see paper)
46% identity, 92% coverage: 37:478/482 of query aligns to 1:434/435 of 2cetA
- active site: R75 (= R111), H119 (= H155), E164 (= E200), V167 (= V203), N286 (= N325), Y288 (= Y327), E341 (= E385)
- binding (5r,6r,7s,8s)-5-(hydroxymethyl)-2-(2-phenylethyl)-1,5,6,7,8,8a-hexahydroimidazo[1,2-a]pyridine-6,7,8-triol: Q18 (= Q54), H119 (= H155), E164 (= E200), Y288 (= Y327), E341 (= E385), W388 (= W432), E395 (= E439), W396 (= W440), F404 (= F448)
2j7gA Beta-glucosidase from thermotoga maritima in complex with methyl acetic acid-substituted glucoimidazole (see paper)
46% identity, 92% coverage: 37:478/482 of query aligns to 1:436/437 of 2j7gA
- active site: R75 (= R111), H119 (= H155), E164 (= E200), V167 (= V203), N288 (= N325), Y290 (= Y327), E343 (= E385)
- binding methyl acetic acid-substituted glucoimidazole: Q18 (= Q54), H119 (= H155), E164 (= E200), Y290 (= Y327), E343 (= E385), W390 (= W432), E397 (= E439), W398 (= W440), F406 (= F448)
2jalB Beta-glucosidase from thermotoga maritima in complex with cyclophellitol (see paper)
46% identity, 92% coverage: 37:478/482 of query aligns to 2:443/444 of 2jalB
- active site: R76 (= R111), H120 (= H155), E165 (= E200), V168 (= V203), N292 (= N325), Y294 (= Y327), E350 (= E385)
- binding calcium ion: D277 (≠ G310), E281 (≠ A314)
- binding (1r,2s,3s,4s,5r,6r)-6-(hydroxymethyl)cyclohexane-1,2,3,4,5-pentol: Q19 (= Q54), H120 (= H155), E165 (= E200), E350 (= E385), W397 (= W432), E404 (= E439), W405 (= W440), F413 (= F448)
1oifA Family 1 b-glucosidase from thermotoga maritima (see paper)
46% identity, 92% coverage: 37:478/482 of query aligns to 1:442/444 of 1oifA
- active site: R75 (= R111), H119 (= H155), E164 (= E200), V167 (= V203), N291 (= N325), Y293 (= Y327), E349 (= E385)
- binding 5-hydroxymethyl-3,4-dihydroxypiperidine: Q18 (= Q54), E164 (= E200), Y293 (= Y327), E349 (= E385), W396 (= W432), E403 (= E439), W404 (= W440), F412 (= F448)
5ossB Beta-glucosidase from thermotoga maritima in complex with gluco-1h- imidazole (see paper)
46% identity, 92% coverage: 37:478/482 of query aligns to 1:442/443 of 5ossB
- active site: R75 (= R111), H119 (= H155), E164 (= E200), V167 (= V203), N291 (= N325), Y293 (= Y327), E349 (= E385)
- binding (4~{S},5~{S},6~{R},7~{R})-7-(hydroxymethyl)-4,5,6,7-tetrahydro-1~{H}-benzimidazole-4,5,6-triol: Q18 (= Q54), H119 (= H155), E164 (= E200), Y293 (= Y327), E349 (= E385), W396 (= W432), E403 (= E439), W404 (= W440), F412 (= F448)
5n6tA Thermotoga maritima family 1 glycoside hydrolase complexed with a cyclophellitol analogue transition state mimic (see paper)
46% identity, 92% coverage: 37:478/482 of query aligns to 1:442/443 of 5n6tA
- active site: R75 (= R111), H119 (= H155), E164 (= E200), V167 (= V203), N291 (= N325), Y293 (= Y327), E349 (= E385)
- binding [(1~{R},2~{R},3~{R},4~{S},5~{R},6~{S})-3,4,5-tris(oxidanyl)-7-oxabicyclo[4.1.0]heptan-2-yl]methanediazonium: Q18 (= Q54), H119 (= H155), N163 (= N199), E164 (= E200), Y293 (= Y327), E349 (= E385), W396 (= W432), E403 (= E439), W404 (= W440), F412 (= F448)
5n6sA Thermotoga maritima family 1 glycoside hydrolase complexed with carba- cyclophellitol transition state mimic (see paper)
46% identity, 92% coverage: 37:478/482 of query aligns to 1:442/443 of 5n6sA
- active site: R75 (= R111), H119 (= H155), E164 (= E200), V167 (= V203), N291 (= N325), Y293 (= Y327), E349 (= E385)
- binding azanylidene-[4-[[(1~{S},2~{R},3~{R},4~{R},5~{S},6~{S},7~{S})-2-(hydroxymethyl)-3,4,5-tris(oxidanyl)-7-bicyclo[4.1.0]heptanyl]carbonylamino]butylimino]azanium: Q18 (= Q54), H119 (= H155), W120 (= W156), N163 (= N199), E164 (= E200), W166 (≠ S202), V167 (= V203), E349 (= E385), W396 (= W432), E403 (= E439), W404 (= W440), F412 (= F448)
2wc4A Structure of family 1 beta-glucosidase from thermotoga maritima in complex with 3-imino-2-thia-(+)-castanospermine (see paper)
46% identity, 92% coverage: 37:478/482 of query aligns to 1:442/443 of 2wc4A
- active site: R75 (= R111), H119 (= H155), E164 (= E200), V167 (= V203), N291 (= N325), Y293 (= Y327), E349 (= E385)
- binding (3Z,5S,6R,7S,8R,8aS)-3-(octylimino)hexahydro[1,3]thiazolo[3,4-a]pyridine-5,6,7,8-tetrol: Q18 (= Q54), H119 (= H155), N163 (= N199), E164 (= E200), Y293 (= Y327), W322 (= W358), E349 (= E385), W396 (= W432), E403 (= E439), W404 (= W440), F412 (= F448)
2wbgA Structure of family 1 beta-glucosidase from thermotoga maritima in complex with 3-imino-2-oxa-(+)-castanospermine (see paper)
46% identity, 92% coverage: 37:478/482 of query aligns to 1:442/443 of 2wbgA
- active site: R75 (= R111), H119 (= H155), E164 (= E200), V167 (= V203), N291 (= N325), Y293 (= Y327), E349 (= E385)
- binding (3Z,5S,6R,7S,8R,8aR)-3-(octylimino)hexahydro[1,3]oxazolo[3,4-a]pyridine-5,6,7,8-tetrol: Q18 (= Q54), H119 (= H155), N163 (= N199), E164 (= E200), Y293 (= Y327), H296 (≠ M330), W322 (= W358), E349 (= E385), W396 (= W432), E403 (= E439), W404 (= W440)
2j79A Beta-glucosidase from thermotoga maritima in complex with galacto- hydroximolactam (see paper)
46% identity, 92% coverage: 37:478/482 of query aligns to 1:436/437 of 2j79A
- active site: R75 (= R111), H119 (= H155), E164 (= E200), V167 (= V203), N288 (= N325), Y290 (= Y327), E343 (= E385)
- binding (2e,3r,4r,5r,6s)-3,4,5-trihydroxy-6-(hydroxymethyl)-2-piperidinone: Q18 (= Q54), H119 (= H155), E164 (= E200), Y290 (= Y327), E343 (= E385), W390 (= W432), E397 (= E439), W398 (= W440), F406 (= F448)
2cbuA Beta-glucosidase from thermotoga maritima in complex with castanospermine (see paper)
46% identity, 92% coverage: 37:478/482 of query aligns to 1:438/440 of 2cbuA
- active site: R75 (= R111), H119 (= H155), E164 (= E200), V167 (= V203), N289 (= N325), Y291 (= Y327), E345 (= E385)
- binding castanospermine: Q18 (= Q54), H119 (= H155), N163 (= N199), E164 (= E200), Y291 (= Y327), W318 (= W358), E345 (= E385), W392 (= W432), E399 (= E439), W400 (= W440), F408 (= F448)
Query Sequence
>AZOBR_RS16895 FitnessBrowser__azobra:AZOBR_RS16895
MRRRSFLKAAAATGLAASAGAFLTTRRAAVAQPSEVLAAFPDKFVWGASTSSYQIEGAVT
AGGRGPSVWDTFSHSFGKVANGDTGDVACDHYNRYAEDVDLMAKAGMNAYRFSVAWPRVQ
PTGTGPANAEGLDFYDRLTDALLAKGIAPWPCLYHWDLPQALQDRGGWTNRDIAGWFTDY
AQLVAARIGDRAKHWTMLNEPSVHAIFGHGLGGHAPGMTGKGNYFKAIHHQNLAQGMALK
ALRAAGGAKGWQLGTVLSLQPVWPVGGLDANYAASLMWDAVWNRACLDPLLRGEYPELLR
DGFAPLVKAGDLEAIRQPIDFLGINYYSRMHQQPDPAGLFGTGYGSPPEGTPTTGMGWPV
EPDGIAEILIELKQEYGNPPVYVMENGAAYPEQTGPKGFVQDNDRISYLRRHILAGHQAL
EEGVDLRGWFVWSLLDNFEWAEGYQRRFGLIEVDRQTLERRPKASYHWYADVIRKKGVPT
SA
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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