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Conserved domains on  [gi|518891218|ref|WP_020047093|]
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alpha/beta hydrolase [Rhizobium leguminosarum]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11171394)

alpha/beta hydrolase catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  37582413|12369917|19508187

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 77-281 1.27e-89

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


:

Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 266.00  E-value: 1.27e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218   77 LLYLHGGGFVIGAPETHEDICRTLANMASAVVVSPDYRLAPEHPFPAAIDDCAATLVWMTEQADALGIDPLRILVAGDSA 156
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218  157 GGNLAAVVALLARDGQVPAVIGQVLIYPVTDQSQTSDSY--SRYQEDFGLTAAAMKWFRDHYLPDaASRSDWRASPLNVA 234
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYlaREFADGPLLTRAAMDWFWRLYLPG-ADRDDPLASPLFAS 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 518891218  235 SLAGVAPALLILAGHDVLFDEGAAYAERL-STEVKATTRTWPGQIHGF 281
Cdd:pfam07859 160 DLSGLPPALVVVAEFDPLRDEGEAYAERLrAAGVPVELIEYPGMPHGF 207
 
Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 77-281 1.27e-89

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 266.00  E-value: 1.27e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218   77 LLYLHGGGFVIGAPETHEDICRTLANMASAVVVSPDYRLAPEHPFPAAIDDCAATLVWMTEQADALGIDPLRILVAGDSA 156
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218  157 GGNLAAVVALLARDGQVPAVIGQVLIYPVTDQSQTSDSY--SRYQEDFGLTAAAMKWFRDHYLPDaASRSDWRASPLNVA 234
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYlaREFADGPLLTRAAMDWFWRLYLPG-ADRDDPLASPLFAS 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 518891218  235 SLAGVAPALLILAGHDVLFDEGAAYAERL-STEVKATTRTWPGQIHGF 281
Cdd:pfam07859 160 DLSGLPPALVVVAEFDPLRDEGEAYAERLrAAGVPVELIEYPGMPHGF 207
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
68-305 1.29e-67

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 210.11  E-value: 1.29e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218  68 AAPRQGAPALLYLHGGGFVIGAPETHEDICRTLANMASAVVVSPDYRLAPEHPFPAAIDDCAATLVWMTEQADALGIDPL 147
Cdd:COG0657    7 AGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELGIDPD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218 148 RILVAGDSAGGNLAAVVALLARDGQVPAVIGQVLIYPVTdqsqtsdsysryqedfgltaaamkwfrdhylpdaasrsDWR 227
Cdd:COG0657   87 RIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVL--------------------------------------DLT 128

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518891218 228 ASPLNvASLAGVAPALLILAGHDVLFDEGAAYAERLSTE-VKATTRTWPGQIHGFVSkRRAIPEGQEALEAIAAAWRAM 305
Cdd:COG0657  129 ASPLR-ADLAGLPPTLIVTGEADPLVDESEALAAALRAAgVPVELHVYPGGGHGFGL-LAGLPEARAALAEIAAFLRRA 205
PRK10162 PRK10162
acetyl esterase;
70-296 6.95e-37

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 134.08  E-value: 6.95e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218  70 PRQGAPA-LLYLHGGGFVIGAPETHEDICRTLANMASAVVVSPDYRLAPEHPFPAAIDDCAATLVWMTEQADALGIDPLR 148
Cdd:PRK10162  76 PQPDSQAtLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGINMSR 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218 149 ILVAGDSAGGNLAAVVALLARDGQVPA--VIGQVLIYPVTDQsQTSDSYSRYQEDF-GLTAAAMKWFRDHYLPDAASRSD 225
Cdd:PRK10162 156 IGFAGDSAGAMLALASALWLRDKQIDCgkVAGVLLWYGLYGL-RDSVSRRLLGGVWdGLTQQDLQMYEEAYLSNDADRES 234

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518891218 226 WRASPLNVASLAGVAPALLILAGHDVLFDEGAAYAERLSTEVKATT-RTWPGQIHGFVSKRRAIPEGQEALE 296
Cdd:PRK10162 235 PYYCLFNNDLTRDVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEfKLYPGTLHAFLHYSRMMDTADDALR 306
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 61-169 7.64e-09

Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.


Pssm-ID: 238191 [Multi-domain]  Cd Length: 493  Bit Score: 56.57  E-value: 7.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218  61 LKIWRGR-AAPRQGAPALLYLHGGGFVIGAPET--HEDICRTLANMasaVVVSPDYRLAP---------EHPFPAAIDDC 128
Cdd:cd00312   81 LNVYTPKnTKPGNSLPVMVWIHGGGFMFGSGSLypGDGLAREGDNV---IVVSINYRLGVlgflstgdiELPGNYGLKDQ 157

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 518891218 129 AATLVWMTEQADALGIDPLRILVAGDSAGGnlAAVVALLAR 169
Cdd:cd00312  158 RLALKWVQDNIAAFGGDPDSVTIFGESAGG--ASVSLLLLS 196
 
Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 77-281 1.27e-89

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 266.00  E-value: 1.27e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218   77 LLYLHGGGFVIGAPETHEDICRTLANMASAVVVSPDYRLAPEHPFPAAIDDCAATLVWMTEQADALGIDPLRILVAGDSA 156
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218  157 GGNLAAVVALLARDGQVPAVIGQVLIYPVTDQSQTSDSY--SRYQEDFGLTAAAMKWFRDHYLPDaASRSDWRASPLNVA 234
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYlaREFADGPLLTRAAMDWFWRLYLPG-ADRDDPLASPLFAS 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 518891218  235 SLAGVAPALLILAGHDVLFDEGAAYAERL-STEVKATTRTWPGQIHGF 281
Cdd:pfam07859 160 DLSGLPPALVVVAEFDPLRDEGEAYAERLrAAGVPVELIEYPGMPHGF 207
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
68-305 1.29e-67

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 210.11  E-value: 1.29e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218  68 AAPRQGAPALLYLHGGGFVIGAPETHEDICRTLANMASAVVVSPDYRLAPEHPFPAAIDDCAATLVWMTEQADALGIDPL 147
Cdd:COG0657    7 AGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELGIDPD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218 148 RILVAGDSAGGNLAAVVALLARDGQVPAVIGQVLIYPVTdqsqtsdsysryqedfgltaaamkwfrdhylpdaasrsDWR 227
Cdd:COG0657   87 RIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVL--------------------------------------DLT 128

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518891218 228 ASPLNvASLAGVAPALLILAGHDVLFDEGAAYAERLSTE-VKATTRTWPGQIHGFVSkRRAIPEGQEALEAIAAAWRAM 305
Cdd:COG0657  129 ASPLR-ADLAGLPPTLIVTGEADPLVDESEALAAALRAAgVPVELHVYPGGGHGFGL-LAGLPEARAALAEIAAFLRRA 205
PRK10162 PRK10162
acetyl esterase;
70-296 6.95e-37

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 134.08  E-value: 6.95e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218  70 PRQGAPA-LLYLHGGGFVIGAPETHEDICRTLANMASAVVVSPDYRLAPEHPFPAAIDDCAATLVWMTEQADALGIDPLR 148
Cdd:PRK10162  76 PQPDSQAtLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGINMSR 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218 149 ILVAGDSAGGNLAAVVALLARDGQVPA--VIGQVLIYPVTDQsQTSDSYSRYQEDF-GLTAAAMKWFRDHYLPDAASRSD 225
Cdd:PRK10162 156 IGFAGDSAGAMLALASALWLRDKQIDCgkVAGVLLWYGLYGL-RDSVSRRLLGGVWdGLTQQDLQMYEEAYLSNDADRES 234

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518891218 226 WRASPLNVASLAGVAPALLILAGHDVLFDEGAAYAERLSTEVKATT-RTWPGQIHGFVSKRRAIPEGQEALE 296
Cdd:PRK10162 235 PYYCLFNNDLTRDVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEfKLYPGTLHAFLHYSRMMDTADDALR 306
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 75-167 2.08e-20

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 87.24  E-value: 2.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218   75 PALLYLHGGGFVIGAPETHED-ICRTLANMASA--VVVSPDYRLAPEHPFPAAIDDCAATLVWMTEQADALGIDPLRILV 151
Cdd:pfam20434  14 PVVIWIHGGGWNSGDKEADMGfMTNTVKALLKAgyAVASINYRLSTDAKFPAQIQDVKAAIRFLRANAAKYGIDTNKIAL 93

                          90
                  ....*....|....*.
gi 518891218  152 AGDSAGGNLAAVVALL 167
Cdd:pfam20434  94 MGFSAGGHLALLAGLS 109
COesterase pfam00135
Carboxylesterase family;
60-167 2.65e-11

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 63.87  E-value: 2.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218   60 RLKIW--RGRAAPRQGAPALLYLHGGGFVIGAPETHEDicRTLANMASAVVVSPDYRLAP---------EHPFPAAIDDC 128
Cdd:pfam00135  87 YLNVYtpKELKENKNKLPVMVWIHGGGFMFGSGSLYDG--SYLAAEGDVIVVTINYRLGPlgflstgddEAPGNYGLLDQ 164

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 518891218  129 AATLVWMTEQADALGIDPLRILVAGDSAGgnlAAVVALL 167
Cdd:pfam00135 165 VLALRWVQENIASFGGDPNRVTLFGESAG---AASVSLL 200
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
56-297 3.12e-11

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 61.96  E-value: 3.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218  56 AGGIRLKIWRGRAAPRQGAPALLYLHGGgfvigaPETHEDICRTLAN-MASA--VVVSPDYR---LAPEHPFPAAIDDCA 129
Cdd:COG1506    5 ADGTTLPGWLYLPADGKKYPVVVYVHGG------PGSRDDSFLPLAQaLASRgyAVLAPDYRgygESAGDWGGDEVDDVL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218 130 ATLVWMTEQADalgIDPLRILVAGDSAGGNLAAvvALLARDGQVPAVIgqVLIYPVTDQSQTSDSYSRYQEdfgltaaam 209
Cdd:COG1506   79 AAIDYLAARPY---VDPDRIGIYGHSYGGYMAL--LAAARHPDRFKAA--VALAGVSDLRSYYGTTREYTE--------- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218 210 kwfRDHYLPDAASRSDWRASPLNVAslAGVAPALLILAGHD---VLFDEGAAYAERL-STEVKATTRTWPGQIHGFVskR 285
Cdd:COG1506  143 ---RLMGGPWEDPEAYAARSPLAYA--DKLKTPLLLIHGEAddrVPPEQAERLYEALkKAGKPVELLVYPGEGHGFS--G 215

                        250
                 ....*....|..
gi 518891218 286 RAIPEGQEALEA 297
Cdd:COG1506  216 AGAPDYLERILD 227
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 61-169 7.64e-09

Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.


Pssm-ID: 238191 [Multi-domain]  Cd Length: 493  Bit Score: 56.57  E-value: 7.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218  61 LKIWRGR-AAPRQGAPALLYLHGGGFVIGAPET--HEDICRTLANMasaVVVSPDYRLAP---------EHPFPAAIDDC 128
Cdd:cd00312   81 LNVYTPKnTKPGNSLPVMVWIHGGGFMFGSGSLypGDGLAREGDNV---IVVSINYRLGVlgflstgdiELPGNYGLKDQ 157

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 518891218 129 AATLVWMTEQADALGIDPLRILVAGDSAGGnlAAVVALLAR 169
Cdd:cd00312  158 RLALKWVQDNIAAFGGDPDSVTIFGESAGG--ASVSLLLLS 196
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
61-168 7.90e-08

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 53.35  E-value: 7.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218  61 LKIWRGRAAPRQGAPALLYLHGGGFVIGApeTHEDICRTlANMAS--AVVVSPDYRL------------APEHPFPA--A 124
Cdd:COG2272   92 LNVWTPALAAGAKLPVMVWIHGGGFVSGS--GSEPLYDG-AALARrgVVVVTINYRLgalgflalpalsGESYGASGnyG 168

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 518891218 125 IDDCAATLVWMTEQADALGIDPLRILVAGDSAGGnlAAVVALLA 168
Cdd:COG2272  169 LLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGA--ASVAALLA 210
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
56-300 5.18e-04

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 40.76  E-value: 5.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218  56 AGGIRLKIWRGRAAPRQGaPALLYLHGGGfviGAPETHEDICRTLANmASAVVVSPDYR----LAPEHPFPAAIDDCAAT 131
Cdd:COG2267   11 RDGLRLRGRRWRPAGSPR-GTVVLVHGLG---EHSGRYAELAEALAA-AGYAVLAFDLRghgrSDGPRGHVDSFDDYVDD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218 132 LVWMTEQADALGidPLRILVAGDSAGGnLAAVVALLARDGQVPAVigqVLIYPvtdqsqtsdsysRYQEDfGLTAAAMKW 211
Cdd:COG2267   86 LRAALDALRARP--GLPVVLLGHSMGG-LIALLYAARYPDRVAGL---VLLAP------------AYRAD-PLLGPSARW 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218 212 FRDHYLPDAASRSDwrasplnvaslagvAPALLILAGHDVLFD--EGAAYAERLSTEVkaTTRTWPGQIHGFVSKrraiP 289
Cdd:COG2267  147 LRALRLAEALARID--------------VPVLVLHGGADRVVPpeAARRLAARLSPDV--ELVLLPGARHELLNE----P 206

                        250
                 ....*....|.
gi 518891218 290 EGQEALEAIAA 300
Cdd:COG2267  207 AREEVLAAILA 217
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 67-170 2.30e-03

Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 38.83  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218  67 RAAPRQGAPALLYLHGGGfviGAPETHEDICR--TLANMASAVVVSPD-YRLAPEHPF--------PAAIDDcAATLVWM 135
Cdd:COG3509   46 GYDGGAPLPLVVALHGCG---GSAADFAAGTGlnALADREGFIVVYPEgTGRAPGRCWnwfdgrdqRRGRDD-VAFIAAL 121

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 518891218 136 TEQADA-LGIDPLRILVAGDSAGGNLAAVVALLARD 170
Cdd:COG3509  122 VDDLAArYGIDPKRVYVTGLSAGGAMAYRLACEYPD 157
Say1_Mug180 pfam10340
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ...
 75-230 2.81e-03

Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) and fission yeast Mug180. Say1 is a a membrane-anchored deacetylase required for the deacetylation of acetylated sterols. It is involved in the resistance to eugenol and pregnenolone toxicity. Mug180 has a role in meiosis.


Pssm-ID: 313549  Cd Length: 374  Bit Score: 39.05  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218   75 PALLYLHGGGFVIGAPETHEDICRTLANMASAV-VVSPDYRLAPEHP----FPAAIDDCAATLVWMTEqadALGIDplRI 149
Cdd:pfam10340 123 PILLYYHGGGFALKLIPVTLVFLNNLGKYFPDMaILVSDYTVTANCPqsytYPLQVLQCLAVYDYLTL---TKGCK--NV 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518891218  150 LVAGDSAGGNLAAVVAL-LARDGQVPAVIGQVLIYP---VTDQSQTSDSYsrYQEDFGLTAAAMK---WFRDHYLPDAAS 222
Cdd:pfam10340 198 TLMGDSAGGNLVLNILLyLHKCNKVVLPKKAIAISPwlnLTDRNEKEKEY--MKANDKLDGLCYKglnMFGKLYVPNVEP 275


                  ....*...
gi 518891218  223 RSDWRASP 230
Cdd:pfam10340 276 EESLFTDP 283
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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