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Conserved domains on  [gi|1586523015|gb|TBY95010|]
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carboxylesterase family protein [Rhizobium leguminosarum bv. viciae]

Protein Classification

carboxylesterase/lipase family protein( domain architecture ID 10006294)

carboxylesterase/lipase family protein similar to carboxylesterase, which catalyzes the hydrolysis of a carboxylic ester to form an alcohol and a carboxylate, and lipase, which hydrolyzes triglycerides into diglycerides and subsequently into monoglycerides and free fatty acids

CATH:  3.40.50.1820
EC:  3.1.1.-
Gene Ontology:  GO:0052689|GO:0016298
SCOP:  3000102

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
21-519 0e+00

Carboxylesterase type B [Lipid transport and metabolism];


:

Pssm-ID: 441873  Cd Length: 500  Bit Score: 531.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015  21 TFAPRLGAADDTVTIDSGMLKGERSGTVVSFKGIPYAAPPVGDLRWRNPRPMETWSGIKDARDFGPSCMQ-------TDD 93
Cdd:COG2272     3 RLLAAAAAAAPVVRTEAGRVRGVVEGGVRVFLGIPYAAPPVGELRWRAPQPVEPWTGVRDATEFGPACPQpprpgdpGGP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015  94 LPKSEDCLTLNVWTPVRRSRAPLPVMVWIYGGALAHG--NTPLYPGGQLAARKVVFVSMNYRMGRLGYFAHPALIKEApD 171
Cdd:COG2272    83 APGSEDCLYLNVWTPALAAGAKLPVMVWIHGGGFVSGsgSEPLYDGAALARRGVVVVTINYRLGALGFLALPALSGES-Y 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 172 EPVGNYGYMDQLAALKWVQQNIEAFGGDPKKVTIFGESAGGGSVMAHMISPLSRGLFRGAILQSPGLPAARaqstplsPL 251
Cdd:COG2272   162 GASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGLSVL-------TL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 252 KEAEKTALDYAASLGIngsDAGALTALRALSAEKLTEGASAedvlagMSTGEPVIGVSGAIIDGRFLLETPEAAFAAGRQ 331
Cdd:COG2272   235 AEAEAVGAAFAAALGV---APATLAALRALPAEELLAAQAA------LAAEGPGGLPFGPVVDGDVLPEDPLEAFAAGRA 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 332 APVPVIVGAND-------RDLGIGQAATKDDLFALL----GKHAAEARSLYDPTgqqTLDELKQQVLADKTLVEPSRHLA 400
Cdd:COG2272   306 ADVPLLIGTNRdegrlfaALLGDLGPLTAADYRAALrrrfGDDADEVLAAYPAA---SPAEALAALATDRVFRCPARRLA 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 401 DEMIRAGQPTWWYRFSYVAEALRNDPAwkGTLHGFEIPFTFDIPDALVKDKVTPADWAMATLASAYWVEFATSGDPNGGS 480
Cdd:COG2272   383 EAHAAAGAPVYLYRFDWRSPPLRGFGL--GAFHGAELPFVFGNLDAPALTGLTPADRALSDQMQAYWVNFARTGDPNGPG 460
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 1586523015 481 RPKWPHHDPFVHRVIDFTNHGVTFGADPLKLRLDLWQSY 519
Cdd:COG2272   461 LPEWPAYDPEDRAVMVFDAEPRVVNDPDAEERLDLWDGV 499
 
Name Accession Description Interval E-value
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
21-519 0e+00

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 531.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015  21 TFAPRLGAADDTVTIDSGMLKGERSGTVVSFKGIPYAAPPVGDLRWRNPRPMETWSGIKDARDFGPSCMQ-------TDD 93
Cdd:COG2272     3 RLLAAAAAAAPVVRTEAGRVRGVVEGGVRVFLGIPYAAPPVGELRWRAPQPVEPWTGVRDATEFGPACPQpprpgdpGGP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015  94 LPKSEDCLTLNVWTPVRRSRAPLPVMVWIYGGALAHG--NTPLYPGGQLAARKVVFVSMNYRMGRLGYFAHPALIKEApD 171
Cdd:COG2272    83 APGSEDCLYLNVWTPALAAGAKLPVMVWIHGGGFVSGsgSEPLYDGAALARRGVVVVTINYRLGALGFLALPALSGES-Y 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 172 EPVGNYGYMDQLAALKWVQQNIEAFGGDPKKVTIFGESAGGGSVMAHMISPLSRGLFRGAILQSPGLPAARaqstplsPL 251
Cdd:COG2272   162 GASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGLSVL-------TL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 252 KEAEKTALDYAASLGIngsDAGALTALRALSAEKLTEGASAedvlagMSTGEPVIGVSGAIIDGRFLLETPEAAFAAGRQ 331
Cdd:COG2272   235 AEAEAVGAAFAAALGV---APATLAALRALPAEELLAAQAA------LAAEGPGGLPFGPVVDGDVLPEDPLEAFAAGRA 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 332 APVPVIVGAND-------RDLGIGQAATKDDLFALL----GKHAAEARSLYDPTgqqTLDELKQQVLADKTLVEPSRHLA 400
Cdd:COG2272   306 ADVPLLIGTNRdegrlfaALLGDLGPLTAADYRAALrrrfGDDADEVLAAYPAA---SPAEALAALATDRVFRCPARRLA 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 401 DEMIRAGQPTWWYRFSYVAEALRNDPAwkGTLHGFEIPFTFDIPDALVKDKVTPADWAMATLASAYWVEFATSGDPNGGS 480
Cdd:COG2272   383 EAHAAAGAPVYLYRFDWRSPPLRGFGL--GAFHGAELPFVFGNLDAPALTGLTPADRALSDQMQAYWVNFARTGDPNGPG 460
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 1586523015 481 RPKWPHHDPFVHRVIDFTNHGVTFGADPLKLRLDLWQSY 519
Cdd:COG2272   461 LPEWPAYDPEDRAVMVFDAEPRVVNDPDAEERLDLWDGV 499
COesterase pfam00135
Carboxylesterase family;
32-485 1.14e-130

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 389.74  E-value: 1.14e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015  32 TVTIDSGMLKG-----ERSGTVVSFKGIPYAAPPVGDLRWRNPRPMETWSGIKDARDFGPSCMQTDDL--------PKSE 98
Cdd:pfam00135   4 VVTTSLGRVRGkrlkvDGGKPVYAFLGIPYAEPPVGELRFQPPEPPEPWTGVRDATKFGPRCPQNGDLtspgssglEGSE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015  99 DCLTLNVWTPVRRSRAP--LPVMVWIYGGALAHGNTPLYPGGQLAAR-KVVFVSMNYRMGRLGYFAhpALIKEAPdepvG 175
Cdd:pfam00135  84 DCLYLNVYTPKELKENKnkLPVMVWIHGGGFMFGSGSLYDGSYLAAEgDVIVVTINYRLGPLGFLS--TGDDEAP----G 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 176 NYGYMDQLAALKWVQQNIEAFGGDPKKVTIFGESAGGGSVMAHMISPLSRGLFRGAILQSPglpaaraqsTPLSPL---K 252
Cdd:pfam00135 158 NYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSG---------SALSPWaiqS 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 253 EAEKTALDYAASLGINGSDAGALTA-LRALSAEKLTegasaeDVLAGMSTGEPVIGVSGA-IIDGRFLLETPEAAFAAGR 330
Cdd:pfam00135 229 NARQRAKELAKLVGCPTSDSAELVEcLRSKPAEELL------DAQLKLLVYGSVPFVPFGpVVDGDFLPEHPEELLKSGN 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 331 QAPVPVIVGAN-----------DRDLGIGQAATKDDLFALLGKHAAEARSLYDPTGQQTL-----DELK----------- 383
Cdd:pfam00135 303 FPKVPLLIGVTkdegllfaayiLDNVDILKALEEKLLRSLLIDLLYLLLVDLPEEISAALreeylDWGDrddpetsrral 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 384 QQVLADKTLVEPSRHLADEMIRAGQPTWWYRFSYVAEALRnDPAWKGTLHGFEIPFTFDIPdALVKDKVTPADWAMATLA 463
Cdd:pfam00135 383 VELLTDYLFNCPVIRFADLHASRGTPVYMYSFDYRGSSLR-YPKWVGVDHGDELPYVFGTP-FVGALLFTEEDEKLSRKM 460
                         490       500
                  ....*....|....*....|...
gi 1586523015 464 SAYWVEFATSGDPNGGSR-PKWP 485
Cdd:pfam00135 461 MTYWTNFAKTGNPNGPEGlPKWP 483
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
32-485 3.96e-124

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: 372.44  E-value: 3.96e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015  32 TVTIDSGMLKGERSGTVVSFKGIPYAAPPVGDLRWRNPRPMETWSGIKDARDFGPSCMQTDD---------LPKSEDCLT 102
Cdd:cd00312     1 LVVTPNGKVRGVDEGGVYSFLGIPYAEPPVGDLRFKEPQPYEPWSDVLDATSYPPSCMQWDQlggglwnakLPGSEDCLY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 103 LNVWTP-VRRSRAPLPVMVWIYGGALAHGNTPLYPGGQLAAR--KVVFVSMNYRMGRLGYFAHPAliKEAPdepvGNYGY 179
Cdd:cd00312    81 LNVYTPkNTKPGNSLPVMVWIHGGGFMFGSGSLYPGDGLAREgdNVIVVSINYRLGVLGFLSTGD--IELP----GNYGL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 180 MDQLAALKWVQQNIEAFGGDPKKVTIFGESAGGGSVMAHMISPLSRGLFRGAILQS-PGLPaaraqstPLSPLKEAEKTA 258
Cdd:cd00312   155 KDQRLALKWVQDNIAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSgSALS-------PWAIQENARGRA 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 259 LDYAASLGINGSDAGAL-TALRALSAEKLTEgasAEDVLAGMSTGEPVIgvSGAIIDGRFLLETPEAAFAAGRQAPVPVI 337
Cdd:cd00312   228 KRLARLLGCNDTSSAELlDCLRSKSAEELLD---ATRKLLLFSYSPFLP--FGPVVDGDFIPDDPEELIKEGKFAKVPLI 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 338 VGANdRDLGI--------GQAATKDDLFALLGKHAAEarSLYDPtGQQTLDELKQQVLADKTLVEPSRHLADEMI----- 404
Cdd:cd00312   303 IGVT-KDEGGyfaamllnFDAKLIIETNDRWLELLPY--LLFYA-DDALADKVLEKYPGDVDDSVESRKNLSDMLtdllf 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 405 -------------RAGQPTWWYRFSYVAE-ALRNDPAWKGTLHGFEIPFTFDIPDALVKDkvTPADWAMATLASAYWVEF 470
Cdd:cd00312   379 kcparyflaqhrkAGGSPVYAYVFDHRSSlSVGRWPPWLGTVHGDEIFFVFGNPLLKEGL--REEEEKLSRTMMKYWANF 456
                         490
                  ....*....|....*.
gi 1586523015 471 ATSGDPNG-GSRPKWP 485
Cdd:cd00312   457 AKTGNPNTeGNLVVWP 472
 
Name Accession Description Interval E-value
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
21-519 0e+00

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 531.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015  21 TFAPRLGAADDTVTIDSGMLKGERSGTVVSFKGIPYAAPPVGDLRWRNPRPMETWSGIKDARDFGPSCMQ-------TDD 93
Cdd:COG2272     3 RLLAAAAAAAPVVRTEAGRVRGVVEGGVRVFLGIPYAAPPVGELRWRAPQPVEPWTGVRDATEFGPACPQpprpgdpGGP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015  94 LPKSEDCLTLNVWTPVRRSRAPLPVMVWIYGGALAHG--NTPLYPGGQLAARKVVFVSMNYRMGRLGYFAHPALIKEApD 171
Cdd:COG2272    83 APGSEDCLYLNVWTPALAAGAKLPVMVWIHGGGFVSGsgSEPLYDGAALARRGVVVVTINYRLGALGFLALPALSGES-Y 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 172 EPVGNYGYMDQLAALKWVQQNIEAFGGDPKKVTIFGESAGGGSVMAHMISPLSRGLFRGAILQSPGLPAARaqstplsPL 251
Cdd:COG2272   162 GASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGLSVL-------TL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 252 KEAEKTALDYAASLGIngsDAGALTALRALSAEKLTEGASAedvlagMSTGEPVIGVSGAIIDGRFLLETPEAAFAAGRQ 331
Cdd:COG2272   235 AEAEAVGAAFAAALGV---APATLAALRALPAEELLAAQAA------LAAEGPGGLPFGPVVDGDVLPEDPLEAFAAGRA 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 332 APVPVIVGAND-------RDLGIGQAATKDDLFALL----GKHAAEARSLYDPTgqqTLDELKQQVLADKTLVEPSRHLA 400
Cdd:COG2272   306 ADVPLLIGTNRdegrlfaALLGDLGPLTAADYRAALrrrfGDDADEVLAAYPAA---SPAEALAALATDRVFRCPARRLA 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 401 DEMIRAGQPTWWYRFSYVAEALRNDPAwkGTLHGFEIPFTFDIPDALVKDKVTPADWAMATLASAYWVEFATSGDPNGGS 480
Cdd:COG2272   383 EAHAAAGAPVYLYRFDWRSPPLRGFGL--GAFHGAELPFVFGNLDAPALTGLTPADRALSDQMQAYWVNFARTGDPNGPG 460
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 1586523015 481 RPKWPHHDPFVHRVIDFTNHGVTFGADPLKLRLDLWQSY 519
Cdd:COG2272   461 LPEWPAYDPEDRAVMVFDAEPRVVNDPDAEERLDLWDGV 499
COesterase pfam00135
Carboxylesterase family;
32-485 1.14e-130

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 389.74  E-value: 1.14e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015  32 TVTIDSGMLKG-----ERSGTVVSFKGIPYAAPPVGDLRWRNPRPMETWSGIKDARDFGPSCMQTDDL--------PKSE 98
Cdd:pfam00135   4 VVTTSLGRVRGkrlkvDGGKPVYAFLGIPYAEPPVGELRFQPPEPPEPWTGVRDATKFGPRCPQNGDLtspgssglEGSE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015  99 DCLTLNVWTPVRRSRAP--LPVMVWIYGGALAHGNTPLYPGGQLAAR-KVVFVSMNYRMGRLGYFAhpALIKEAPdepvG 175
Cdd:pfam00135  84 DCLYLNVYTPKELKENKnkLPVMVWIHGGGFMFGSGSLYDGSYLAAEgDVIVVTINYRLGPLGFLS--TGDDEAP----G 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 176 NYGYMDQLAALKWVQQNIEAFGGDPKKVTIFGESAGGGSVMAHMISPLSRGLFRGAILQSPglpaaraqsTPLSPL---K 252
Cdd:pfam00135 158 NYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSG---------SALSPWaiqS 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 253 EAEKTALDYAASLGINGSDAGALTA-LRALSAEKLTegasaeDVLAGMSTGEPVIGVSGA-IIDGRFLLETPEAAFAAGR 330
Cdd:pfam00135 229 NARQRAKELAKLVGCPTSDSAELVEcLRSKPAEELL------DAQLKLLVYGSVPFVPFGpVVDGDFLPEHPEELLKSGN 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 331 QAPVPVIVGAN-----------DRDLGIGQAATKDDLFALLGKHAAEARSLYDPTGQQTL-----DELK----------- 383
Cdd:pfam00135 303 FPKVPLLIGVTkdegllfaayiLDNVDILKALEEKLLRSLLIDLLYLLLVDLPEEISAALreeylDWGDrddpetsrral 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 384 QQVLADKTLVEPSRHLADEMIRAGQPTWWYRFSYVAEALRnDPAWKGTLHGFEIPFTFDIPdALVKDKVTPADWAMATLA 463
Cdd:pfam00135 383 VELLTDYLFNCPVIRFADLHASRGTPVYMYSFDYRGSSLR-YPKWVGVDHGDELPYVFGTP-FVGALLFTEEDEKLSRKM 460
                         490       500
                  ....*....|....*....|...
gi 1586523015 464 SAYWVEFATSGDPNGGSR-PKWP 485
Cdd:pfam00135 461 MTYWTNFAKTGNPNGPEGlPKWP 483
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
32-485 3.96e-124

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: 372.44  E-value: 3.96e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015  32 TVTIDSGMLKGERSGTVVSFKGIPYAAPPVGDLRWRNPRPMETWSGIKDARDFGPSCMQTDD---------LPKSEDCLT 102
Cdd:cd00312     1 LVVTPNGKVRGVDEGGVYSFLGIPYAEPPVGDLRFKEPQPYEPWSDVLDATSYPPSCMQWDQlggglwnakLPGSEDCLY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 103 LNVWTP-VRRSRAPLPVMVWIYGGALAHGNTPLYPGGQLAAR--KVVFVSMNYRMGRLGYFAHPAliKEAPdepvGNYGY 179
Cdd:cd00312    81 LNVYTPkNTKPGNSLPVMVWIHGGGFMFGSGSLYPGDGLAREgdNVIVVSINYRLGVLGFLSTGD--IELP----GNYGL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 180 MDQLAALKWVQQNIEAFGGDPKKVTIFGESAGGGSVMAHMISPLSRGLFRGAILQS-PGLPaaraqstPLSPLKEAEKTA 258
Cdd:cd00312   155 KDQRLALKWVQDNIAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSgSALS-------PWAIQENARGRA 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 259 LDYAASLGINGSDAGAL-TALRALSAEKLTEgasAEDVLAGMSTGEPVIgvSGAIIDGRFLLETPEAAFAAGRQAPVPVI 337
Cdd:cd00312   228 KRLARLLGCNDTSSAELlDCLRSKSAEELLD---ATRKLLLFSYSPFLP--FGPVVDGDFIPDDPEELIKEGKFAKVPLI 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 338 VGANdRDLGI--------GQAATKDDLFALLGKHAAEarSLYDPtGQQTLDELKQQVLADKTLVEPSRHLADEMI----- 404
Cdd:cd00312   303 IGVT-KDEGGyfaamllnFDAKLIIETNDRWLELLPY--LLFYA-DDALADKVLEKYPGDVDDSVESRKNLSDMLtdllf 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 405 -------------RAGQPTWWYRFSYVAE-ALRNDPAWKGTLHGFEIPFTFDIPDALVKDkvTPADWAMATLASAYWVEF 470
Cdd:cd00312   379 kcparyflaqhrkAGGSPVYAYVFDHRSSlSVGRWPPWLGTVHGDEIFFVFGNPLLKEGL--REEEEKLSRTMMKYWANF 456
                         490
                  ....*....|....*.
gi 1586523015 471 ATSGDPNG-GSRPKWP 485
Cdd:cd00312   457 AKTGNPNTeGNLVVWP 472
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
105-238 2.17e-14

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 72.21  E-value: 2.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 105 VWTPvRRSRAPLPVMVWIYGGALAHGNTPLYPG--GQLAARK-VVFVSMNYRMgrlgyfahpalikeAPDepvgnYGYMD 181
Cdd:COG0657     3 VYRP-AGAKGPLPVVVYFHGGGWVSGSKDTHDPlaRRLAARAgAAVVSVDYRL--------------APE-----HPFPA 62
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586523015 182 QL----AALKWVQQNIEAFGGDPKKVTIFGESAGGG--SVMAHMISPLSRGLFRGAILQSPGL 238
Cdd:COG0657    63 ALedayAALRWLRANAAELGIDPDRIAVAGDSAGGHlaAALALRARDRGGPRPAAQVLIYPVL 125
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
119-238 4.33e-10

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: 59.53  E-value: 4.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 119 MVWIYGGALAHGNTPLYPG--GQLAAR-KVVFVSMNYRMgrlgyfahpalikeAPDEPvgnY--GYMDQLAALKWVQQNI 193
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRlcRRLAAEaGAVVVSVDYRL--------------APEHP---FpaAYDDAYAALRWLAEQA 63
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1586523015 194 EAFGGDPKKVTIFGESAGGG--SVMAHMISPLSRGLFRGAILQSPGL 238
Cdd:pfam07859  64 AELGADPSRIAVAGDSAGGNlaAAVALRARDEGLPKPAGQVLIYPGT 110
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
114-212 4.86e-09

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: 56.42  E-value: 4.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015 114 APLPVMVWIYGGALAHGN----TPLYP--GGQLAARKVVFVSMNYRMGRLGYFahPALIKeapdepvgnygymDQLAALK 187
Cdd:pfam20434  11 GPYPVVIWIHGGGWNSGDkeadMGFMTntVKALLKAGYAVASINYRLSTDAKF--PAQIQ-------------DVKAAIR 75
                          90       100
                  ....*....|....*....|....*
gi 1586523015 188 WVQQNIEAFGGDPKKVTIFGESAGG 212
Cdd:pfam20434  76 FLRANAAKYGIDTNKIALMGFSAGG 100
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
96-236 7.58e-09

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 56.18  E-value: 7.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586523015  96 KSEDCLTLNVWTPVRRSRAPLPVMVWIYGGALAHGNTPLYPGGQLAARKVVFVSMNYRmgrlGYfahpalikeapDEPVG 175
Cdd:COG1506     3 KSADGTTLPGWLYLPADGKKYPVVVYVHGGPGSRDDSFLPLAQALASRGYAVLAPDYR----GY-----------GESAG 67
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586523015 176 NYG---YMDQLAALKWVQQNIEAfggDPKKVTIFGESAGGGSVMahMISPLSRGLFRGAILQSP 236
Cdd:COG1506    68 DWGgdeVDDVLAAIDYLAARPYV---DPDRIGIYGHSYGGYMAL--LAAARHPDRFKAAVALAG 126
 
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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