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Conserved domains on  [gi|1175211850|ref|WP_081759757|]
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MULTISPECIES: alpha/beta hydrolase [Pseudoalteromonas]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11429202)

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
BD-FAE super family cl48589
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 72-252 2.14e-40

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.


The actual alignment was detected with superfamily member pfam20434:

Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 140.39  E-value: 2.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850  72 PNNNTVLPLIVLVHGGGWGSGS----PAILQTLAAKLAAKGFVVATPAYTLSDEAQYPASIHDIALATQWLKSNASRFHL 147
Cdd:pfam20434   7 KNAKGPYPVVIWIHGGGWNSGDkeadMGFMTNTVKALLKAGYAVASINYRLSTDAKFPAQIQDVKAAIRFLRANAAKYGI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850 148 NAEKLTLAGSSAGGQIAALLAYSH---------GKLLNQSASLAVNARVLINIDGLSDFTTPLALRYENDKNkavTSASK 218
Cdd:pfam20434  87 DTNKIALMGFSAGGHLALLAGLSNnnkefegnvGDYTPESSKESFKVNAVVDFYGPTDLLDMDSCGTHNDAK---SPETL 163

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1175211850 219 WLGGRYEEVPAIWQHASPINYISNTSPATLFING 252
Cdd:pfam20434 164 LLGAPPLENPDLAKSASPITYVDKNDPPFLIIHG 197
 
Name Accession Description Interval E-value
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 72-252 2.14e-40

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: 140.39  E-value: 2.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850  72 PNNNTVLPLIVLVHGGGWGSGS----PAILQTLAAKLAAKGFVVATPAYTLSDEAQYPASIHDIALATQWLKSNASRFHL 147
Cdd:pfam20434   7 KNAKGPYPVVIWIHGGGWNSGDkeadMGFMTNTVKALLKAGYAVASINYRLSTDAKFPAQIQDVKAAIRFLRANAAKYGI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850 148 NAEKLTLAGSSAGGQIAALLAYSH---------GKLLNQSASLAVNARVLINIDGLSDFTTPLALRYENDKNkavTSASK 218
Cdd:pfam20434  87 DTNKIALMGFSAGGHLALLAGLSNnnkefegnvGDYTPESSKESFKVNAVVDFYGPTDLLDMDSCGTHNDAK---SPETL 163

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1175211850 219 WLGGRYEEVPAIWQHASPINYISNTSPATLFING 252
Cdd:pfam20434 164 LLGAPPLENPDLAKSASPITYVDKNDPPFLIIHG 197
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
68-310 3.31e-38

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 134.23  E-value: 3.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850  68 TIIRPNNNT-VLPLIVLVHGGGWGSGSPAILQTLAAKLAA-KGFVVATPAYTLSDEAQYPASIHDIALATQWLKSNASRF 145
Cdd:COG0657     2 DVYRPAGAKgPLPVVVYFHGGGWVSGSKDTHDPLARRLAArAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850 146 HLNAEKLTLAGSSAGGQIAALLAYshgkLLNQSASLAVNArvLINIDGLSDFTtplalryendknkavtsaskwlggrye 225
Cdd:COG0657    82 GIDPDRIAVAGDSAGGHLAAALAL----RARDRGGPRPAA--QVLIYPVLDLT--------------------------- 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850 226 evpaiwqhASPINYISNTSPATLFINGGFARFYAGKKAVQEQLTERGITNKEHVFKEAPHCFWLFH--PWQNNTVELISE 303
Cdd:COG0657   129 --------ASPLRADLAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAglPEARAALAEIAA 200


                  ....*..
gi 1175211850 304 FINKQLA 310
Cdd:COG0657   201 FLRRALA 207
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 69-179 1.13e-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: 58.88  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850  69 IIRPNNNTV---LPLIVLVHGGGWGSGSPAILQTLAAKLAAKGFVVATPAYTLS-------DEAQYP--ASIHDIALATQ 136
Cdd:cd00312    83 VYTPKNTKPgnsLPVMVWIHGGGFMFGSGSLYPGDGLAREGDNVIVVSINYRLGvlgflstGDIELPgnYGLKDQRLALK 162

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1175211850 137 WLKSNASRFHLNAEKLTLAGSSAGGQ-IAALLAYSHGKLLNQSA 179
Cdd:cd00312   163 WVQDNIAAFGGDPDSVTIFGESAGGAsVSLLLLSPDSKGLFHRA 206
PRK10162 PRK10162
acetyl esterase;
81-164 1.93e-08

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 54.72  E-value: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850  81 IVLVHGGGWGSGS----PAILQTLAAKlaaKGFVVATPAYTLSDEAQYPASIHDIALATQWLKSNASRFHLNAEKLTLAG 156
Cdd:PRK10162   84 LFYLHGGGFILGNldthDRIMRLLASY---SGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGINMSRIGFAG 160


                  ....*...
gi 1175211850 157 SSAGGQIA 164
Cdd:PRK10162  161 DSAGAMLA 168
 
Name Accession Description Interval E-value
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 72-252 2.14e-40

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: 140.39  E-value: 2.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850  72 PNNNTVLPLIVLVHGGGWGSGS----PAILQTLAAKLAAKGFVVATPAYTLSDEAQYPASIHDIALATQWLKSNASRFHL 147
Cdd:pfam20434   7 KNAKGPYPVVIWIHGGGWNSGDkeadMGFMTNTVKALLKAGYAVASINYRLSTDAKFPAQIQDVKAAIRFLRANAAKYGI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850 148 NAEKLTLAGSSAGGQIAALLAYSH---------GKLLNQSASLAVNARVLINIDGLSDFTTPLALRYENDKNkavTSASK 218
Cdd:pfam20434  87 DTNKIALMGFSAGGHLALLAGLSNnnkefegnvGDYTPESSKESFKVNAVVDFYGPTDLLDMDSCGTHNDAK---SPETL 163

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1175211850 219 WLGGRYEEVPAIWQHASPINYISNTSPATLFING 252
Cdd:pfam20434 164 LLGAPPLENPDLAKSASPITYVDKNDPPFLIIHG 197
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
68-310 3.31e-38

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 134.23  E-value: 3.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850  68 TIIRPNNNT-VLPLIVLVHGGGWGSGSPAILQTLAAKLAA-KGFVVATPAYTLSDEAQYPASIHDIALATQWLKSNASRF 145
Cdd:COG0657     2 DVYRPAGAKgPLPVVVYFHGGGWVSGSKDTHDPLARRLAArAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850 146 HLNAEKLTLAGSSAGGQIAALLAYshgkLLNQSASLAVNArvLINIDGLSDFTtplalryendknkavtsaskwlggrye 225
Cdd:COG0657    82 GIDPDRIAVAGDSAGGHLAAALAL----RARDRGGPRPAA--QVLIYPVLDLT--------------------------- 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850 226 evpaiwqhASPINYISNTSPATLFINGGFARFYAGKKAVQEQLTERGITNKEHVFKEAPHCFWLFH--PWQNNTVELISE 303
Cdd:COG0657   129 --------ASPLRADLAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAglPEARAALAEIAA 200


                  ....*..
gi 1175211850 304 FINKQLA 310
Cdd:COG0657   201 FLRRALA 207
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 81-288 6.22e-21

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: 88.81  E-value: 6.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850  81 IVLVHGGGWGSGSPAILQTLAAKLAAK-GFVVATPAYTLSDEAQYPASIHDIALATQWLKSNASRFHLNAEKLTLAGSSA 159
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEaGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850 160 GGQIAALLAyshgkLLNQSASL-AVNARVLINidGLSDFTT--PLALRYENDKNKAVTSAS------KWLGGRYEEVPAi 230
Cdd:pfam07859  81 GGNLAAAVA-----LRARDEGLpKPAGQVLIY--PGTDLRTesPSYLAREFADGPLLTRAAmdwfwrLYLPGADRDDPL- 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1175211850 231 wqhASPInYISNTS--PATLFINGGF------ARFYAgkkavqEQLTERGITNKEHVFKEAPHCFW 288
Cdd:pfam07859 153 ---ASPL-FASDLSglPPALVVVAEFdplrdeGEAYA------ERLRAAGVPVELIEYPGMPHGFH 208
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
68-309 1.28e-18

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 83.14  E-value: 1.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850  68 TIIRPNNNTVLPLIVLVHGGGWGSGSPAILqtLAAKLAAKGFVVATPAYT---LSDEAQYPASIHDIALATQWLksnASR 144
Cdd:COG1506    13 WLYLPADGKKYPVVVYVHGGPGSRDDSFLP--LAQALASRGYAVLAPDYRgygESAGDWGGDEVDDVLAAIDYL---AAR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850 145 FHLNAEKLTLAGSSAGGQIAALLAYSHGKLLnqsaslavnaRVLINIDGLSDFTTPLALRYEndknkavtsASKWLGGRY 224
Cdd:COG1506    88 PYVDPDRIGIYGHSYGGYMALLAAARHPDRF----------KAAVALAGVSDLRSYYGTTRE---------YTERLMGGP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850 225 EEVPAIWQHASPINYISNTSPATLFINGG---FARFYAGKKAVQEqLTERGITNKEHVFKEAPHCFwlFHPWQNNTVELI 301
Cdd:COG1506   149 WEDPEAYAARSPLAYADKLKTPLLLIHGEaddRVPPEQAERLYEA-LKKAGKPVELLVYPGEGHGF--SGAGAPDYLERI 225


                  ....*...
gi 1175211850 302 SEFINKQL 309
Cdd:COG1506   226 LDFLDRHL 233
COesterase pfam00135
Carboxylesterase family;
72-171 1.48e-13

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 70.80  E-value: 1.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850  72 PNNNTVLPLIVLVHGGG--WGSGSPAILQTLAAKLaakGFVVATPAY---------TLSDEAQYPASIHDIALATQWLKS 140
Cdd:pfam00135  97 KENKNKLPVMVWIHGGGfmFGSGSLYDGSYLAAEG---DVIVVTINYrlgplgflsTGDDEAPGNYGLLDQVLALRWVQE 173

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1175211850 141 NASRFHLNAEKLTLAGSSAGGQIAALLAYSH 171
Cdd:pfam00135 174 NIASFGGDPNRVTLFGESAGAASVSLLLLSP 204
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 69-179 1.13e-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: 58.88  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850  69 IIRPNNNTV---LPLIVLVHGGGWGSGSPAILQTLAAKLAAKGFVVATPAYTLS-------DEAQYP--ASIHDIALATQ 136
Cdd:cd00312    83 VYTPKNTKPgnsLPVMVWIHGGGFMFGSGSLYPGDGLAREGDNVIVVSINYRLGvlgflstGDIELPgnYGLKDQRLALK 162

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1175211850 137 WLKSNASRFHLNAEKLTLAGSSAGGQ-IAALLAYSHGKLLNQSA 179
Cdd:cd00312   163 WVQDNIAAFGGDPDSVTIFGESAGGAsVSLLLLSPDSKGLFHRA 206
PRK10162 PRK10162
acetyl esterase;
81-164 1.93e-08

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 54.72  E-value: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850  81 IVLVHGGGWGSGS----PAILQTLAAKlaaKGFVVATPAYTLSDEAQYPASIHDIALATQWLKSNASRFHLNAEKLTLAG 156
Cdd:PRK10162   84 LFYLHGGGFILGNldthDRIMRLLASY---SGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGINMSRIGFAG 160


                  ....*...
gi 1175211850 157 SSAGGQIA 164
Cdd:PRK10162  161 DSAGAMLA 168
PLN00021 PLN00021
chlorophyllase
 47-206 4.62e-08

chlorophyllase


Pssm-ID: 177659  Cd Length: 313  Bit Score: 53.51  E-value: 4.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850  47 PISNLNVEQHTYPGKLRSqsITIIRPNNNTVLPLIVLVHGGGWgsgSPAILQTLAAKLAAKGFVVATPA-YTLSDeaqyP 125
Cdd:PLN00021   23 PVELITVDESSRPSPPKP--LLVATPSEAGTYPVLLFLHGYLL---YNSFYSQLLQHIASHGFIVVAPQlYTLAG----P 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850 126 ASIHDIALA---TQWLKSNASRF-----HLNAEKLTLAGSSAGGQIAALLAYSHGKllnqsASLAVNARVLINID----- 192
Cdd:PLN00021   94 DGTDEIKDAaavINWLSSGLAAVlpegvRPDLSKLALAGHSRGGKTAFALALGKAA-----VSLPLKFSALIGLDpvdgt 168

                         170
                  ....*....|....
gi 1175211850 193 GLSDFTTPLALRYE 206
Cdd:PLN00021  169 SKGKQTPPPVLTYA 182
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
68-168 6.36e-08

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 52.28  E-value: 6.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850  68 TIIRPNNNTVLPLIVLVHGggWGSGSPAILQtLAAKLAAKGFVVATP-------AYTLSDEAQYPAS-------IHDIAL 133
Cdd:COG0412    19 YLARPAGGGPRPGVVVLHE--IFGLNPHIRD-VARRLAAAGYVVLAPdlygrggPGDDPDEARALMGaldpellAADLRA 95

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1175211850 134 ATQWLKSNASrfhLNAEKLTLAGSSAGGQIAALLA 168
Cdd:COG0412    96 ALDWLKAQPE---VDAGRVGVVGFCFGGGLALLAA 127
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 79-307 1.54e-07

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 51.16  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850  79 PLIVLVHGGGwgsGSPAILQTLAAKLAAKGFVVA--TPAYTLSDEAQYPASIHDIALAT-QWLKsnasrfHLNAEKLTLA 155
Cdd:COG0596    24 PPVVLLHGLP---GSSYEWRPLIPALAAGYRVIApdLRGHGRSDKPAGGYTLDDLADDLaALLD------ALGLERVVLV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850 156 GSSAGGQIAALLAYSHGKLLnqsASLavnarVLINiDGLSDFTTPLALRYENDknKAVTSASKWLGGryeevPAIWQHAS 235
Cdd:COG0596    95 GHSMGGMVALELAARHPERV---AGL-----VLVD-EVLAALAEPLRRPGLAP--EALAALLRALAR-----TDLRERLA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1175211850 236 PInyisnTSPaTLFINGGFARFYAgkKAVQEQLTERgITNKE-HVFKEAPHCFWLFHPwqNNTVELISEFINK 307
Cdd:COG0596   159 RI-----TVP-TLVIWGEKDPIVP--PALARRLAEL-LPNAElVVLPGAGHFPPLEQP--EAFAAALRDFLAR 220
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
78-168 1.75e-07

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 52.03  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850  78 LPLIVLVHGGGwgsGSPAILQTLAAKLAAKGFVVATPAYTLSDEAQYPASI----------------HDI-ALATQWLKS 140
Cdd:COG4188    62 FPLVVLSHGLG---GSREGYAYLAEHLASHGYVVAAPDHPGSNAADLSAALdgladaldpeelwerpLDLsFVLDQLLAL 138

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1175211850 141 NAS----RFHLNAEKLTLAGSSAGGQIAALLA 168
Cdd:COG4188   139 NKSdpplAGRLDLDRIGVIGHSLGGYTALALA 170
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
79-175 8.66e-07

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 48.84  E-value: 8.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850  79 PLIVLVHGGGWGSGSpaiLQTLAAKLAAKGFVVAT---PAYTLSDEAQ-----YPASIHDIALATQWLKSNASRfhlnae 150
Cdd:COG2267    29 GTVVLVHGLGEHSGR---YAELAEALAAAGYAVLAfdlRGHGRSDGPRghvdsFDDYVDDLRAALDALRARPGL------ 99

                          90       100
                  ....*....|....*....|....*
gi 1175211850 151 KLTLAGSSAGGQIAALLAYSHGKLL 175
Cdd:COG2267   100 PVVLLGHSMGGLIALLYAARYPDRV 124
YpfH COG0400
Predicted esterase [General function prediction only];
79-175 8.85e-07

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 48.75  E-value: 8.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850  79 PLIVLVHGGGwgsGSPAILQTLAAKLAAKGFVVATPA------------YTLS------DEAQYPASIHDIAlatQWLKS 140
Cdd:COG0400     6 PLVVLLHGYG---GDEEDLLPLAPELALPGAAVLAPRapvpegpggrawFDLSflegreDEEGLAAAAEALA---AFIDE 79

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1175211850 141 NASRFHLNAEKLTLAGSSAGGQIAALLAYSHGKLL 175
Cdd:COG0400    80 LEARYGIDPERIVLAGFSQGAAMALSLALRRPELL 114
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
43-181 1.20e-05

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 46.38  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850  43 PDDSPISNLNVEQHTYPGKL--RSQSITIIRP----NNNTVLPLIVLVHGGGWGSGS-------PAILQTLAAKLAAKGF 109
Cdd:COG2382    71 TDDKDVPHGTVETVTYPSKAlgRTRRVWVYLPpgydNPGKKYPVLYLLDGGGGDEQDwfdqgrlPTILDNLIAAGKIPPM 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850 110 VVATPAYTLSDEAQYPASIHDiALAT-------QWLKSNAsRFHLNAEKLTLAGSSAGGQIAALLAYSH----GKLLNQS 178
Cdd:COG2382   151 IVVMPDGGDGGDRGTEGPGND-AFERflaeeliPFVEKNY-RVSADPEHRAIAGLSMGGLAALYAALRHpdlfGYVGSFS 228


                  ...
gi 1175211850 179 ASL 181
Cdd:COG2382   229 GSF 231
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 81-172 6.02e-05

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 41.35  E-value: 6.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850  81 IVLVHggGWGsGSPAILQTLAAKLAAKGFVVATPaytlsdeaQYPASIHDIALATQWLKS--NASRFHLNAEKLTLAGSS 158
Cdd:COG1075     8 VVLVH--GLG-GSAASWAPLAPRLRAAGYPVYAL--------NYPSTNGSIEDSAEQLAAfvDAVLAATGAEKVDLVGHS 76

                          90
                  ....*....|....
gi 1175211850 159 AGGQIAALLAYSHG 172
Cdd:COG1075    77 MGGLVARYYLKRLG 90
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
104-309 5.70e-04

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 40.29  E-value: 5.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850 104 LAAKGFVVATPAYTLSDE-------------AQYPASihDIALATQWLksnASRFHLNAEKLTLAGSSAGGQIAALLAYS 170
Cdd:pfam00326  10 LADRGYVVAIANGRGSGGygeafhdagkgdlGQNEFD--DFIAAAEYL---IEQGYTDPDRLAIWGGSYGGYLTGAALNQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850 171 HGKLLnqsaslavnaRVLINIDGLSDfttplALRYEndknkavTSASKWLGGRYEEVPAIWQH------ASPINYISNT- 243
Cdd:pfam00326  85 RPDLF----------KAAVAHVPVVD-----WLAYM-------SDTSLPFTERYMEWGNPWDNeegydyLSPYSPADNVk 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1175211850 244 -SPATLFINGGF---------ARFYAgkkavqeQLTERGITNKEHVFKEAPHCFwLFHPWQNNTVELISEFINKQL 309
Cdd:pfam00326 143 vYPPLLLIHGLLddrvppwqsLKLVA-------ALQRKGVPFLLLIFPDEGHGI-GKPRNKVEEYARELAFLLEYL 210
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
81-228 6.88e-04

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 40.31  E-value: 6.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850  81 IVLVHGGgwgSGSPAILQTLAAKLAAKGFVVATPAY-----TLSDEAQYPAS--IHDIALATQWLKSnasrfhlNAEKLT 153
Cdd:COG1647    18 VLLLHGF---TGSPAEMRPLAEALAKAGYTVYAPRLpghgtSPEDLLKTTWEdwLEDVEEAYEILKA-------GYDKVI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850 154 LAGSSAGGQIAALLAYSHGKLlnqSASLAVNArvLINIDGLSDFTTPLA------LRYENDKNKAVTSASKWlggrYEEV 227
Cdd:COG1647    88 VIGLSMGGLLALLLAARYPDV---AGLVLLSP--ALKIDDPSAPLLPLLkylarsLRGIGSDIEDPEVAEYA----YDRT 158


                  .
gi 1175211850 228 P 228
Cdd:COG1647   159 P 159
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 78-168 2.94e-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: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850  78 LPLIVLVHGGGwgsGSPAILQTLA--AKLA-AKGFVVATPAYTLSDEAQY---------------PASIHDIalaTQWLk 139
Cdd:COG3509    53 LPLVVALHGCG---GSAADFAAGTglNALAdREGFIVVYPEGTGRAPGRCwnwfdgrdqrrgrddVAFIAAL---VDDL- 125

                          90       100
                  ....*....|....*....|....*....
gi 1175211850 140 snASRFHLNAEKLTLAGSSAGGQIAALLA 168
Cdd:COG3509   126 --AARYGIDPKRVYVTGLSAGGAMAYRLA 152
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 79-171 4.59e-03

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


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 37.87  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175211850  79 PLIVLVHGGGWGSGSPAILQTLAAKLAAKGFVVATPAYTLSDEAQYPASIHDIALAtQWLksNASRFHLNAEKLTLAGSS 158
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLA-EDL--EYILEALGLEKVNLVGHS 77

                          90
                  ....*....|...
gi 1175211850 159 AGGQIAALLAYSH 171
Cdd:pfam00561  78 MGGLIALAYAAKY 90
 
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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