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Conserved domains on  [gi|44888974|sp|P33438|]
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RecName: Full=Glutactin; Flags: Precursor

Protein Classification

carboxylesterase/lipase family protein( domain architecture ID 10444481)

carboxylesterase/lipase family protein similar to carboxylesterase, which catalyzes the hydrolysis of a carboxylic ester to form an alcohol and a carboxylate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
58-579 2.37e-145

Carboxylesterase family;


:

Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 443.67  E-value: 2.37e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974     58 QEAVVQAPeVGQILGISGHKTIAnRPVNAFLGIRYGTVGGGLARFQAAQPI-GYQGRVNATVQSPNCAQFPELDRLRLSE 136
Cdd:pfam00135    1 DSPVVTTS-LGRVRGKRLKVDGG-KPVYAFLGIPYAEPPVGELRFQPPEPPePWTGVRDATKFGPRCPQNGDLTSPGSSG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974    137 SRGEnvDDCLTLDIYAPEGA----NQLPVLVFVHGEMLFDGGSEEAQPDYVLEK-DVLLVSINYRLAPFGFLSALTDELP 211
Cdd:pfam00135   79 LEGS--EDCLYLNVYTPKELkenkNKLPVMVWIHGGGFMFGSGSLYDGSYLAAEgDVIVVTINYRLGPLGFLSTGDDEAP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974    212 GNVALSDLQLALEWLQRNVVHFGGNAGQVTLVGQAGGATLAHALSLSGRAGNLFQQLILQSGTALNPYLIDNQPLDTLST 291
Cdd:pfam00135  157 GNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAIQSNARQRAKE 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974    292 FARLARCPPPSInpsaqglKPLYDCLARLPTSQLVAAFEQLLlqneHLGLTQLGGFKLVVGDplGFLPSHPASLATNSS- 370
Cdd:pfam00135  237 LAKLVGCPTSDS-------AELVECLRSKPAEELLDAQLKLL----VYGSVPFVPFGPVVDG--DFLPEHPEELLKSGNf 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974    371 LALPMIIGATKDASAFIVSRIYDQL----ARLQSRNVSDYIDVVLRHTappsehRLWKQWALREIFTPIQE--QTASLQT 444
Cdd:pfam00135  304 PKVPLLIGVTKDEGLLFAAYILDNVdilkALEEKLLRSLLIDLLYLLL------VDLPEEISAALREEYLDwgDRDDPET 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974    445 VAPGLLELSNYILYRAPVINSISQ-SYRSVPAYLYTFDYRGEHHRFghlsnPLPFGVDasLSDDSVYLFPYPPEASR-LN 522
Cdd:pfam00135  378 SRRALVELLTDYLFNCPVIRFADLhASRGTPVYMYSFDYRGSSLRY-----PKWVGVD--HGDELPYVFGTPFVGALlFT 450
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 44888974    523 PLDRSLSRALVTMWVNFATTGVPNPSSG--VWPQATSEYGPFLRFTNNQQ---SPLELDPHF 579
Cdd:pfam00135  451 EEDEKLSRKMMTYWTNFAKTGNPNGPEGlpKWPPYTDENGQYLSIDLEPRvkqGLKAERCAF 512
Casc1_N super family cl25546
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
681-717 6.39e-04

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


The actual alignment was detected with superfamily member pfam15927:

Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 41.96  E-value: 6.39e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 44888974    681 REQQDERIRQQREQEERLRQQREQEERLRQQRELEER 717
Cdd:pfam15927    2 RLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQ 38
 
Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
58-579 2.37e-145

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 443.67  E-value: 2.37e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974     58 QEAVVQAPeVGQILGISGHKTIAnRPVNAFLGIRYGTVGGGLARFQAAQPI-GYQGRVNATVQSPNCAQFPELDRLRLSE 136
Cdd:pfam00135    1 DSPVVTTS-LGRVRGKRLKVDGG-KPVYAFLGIPYAEPPVGELRFQPPEPPePWTGVRDATKFGPRCPQNGDLTSPGSSG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974    137 SRGEnvDDCLTLDIYAPEGA----NQLPVLVFVHGEMLFDGGSEEAQPDYVLEK-DVLLVSINYRLAPFGFLSALTDELP 211
Cdd:pfam00135   79 LEGS--EDCLYLNVYTPKELkenkNKLPVMVWIHGGGFMFGSGSLYDGSYLAAEgDVIVVTINYRLGPLGFLSTGDDEAP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974    212 GNVALSDLQLALEWLQRNVVHFGGNAGQVTLVGQAGGATLAHALSLSGRAGNLFQQLILQSGTALNPYLIDNQPLDTLST 291
Cdd:pfam00135  157 GNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAIQSNARQRAKE 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974    292 FARLARCPPPSInpsaqglKPLYDCLARLPTSQLVAAFEQLLlqneHLGLTQLGGFKLVVGDplGFLPSHPASLATNSS- 370
Cdd:pfam00135  237 LAKLVGCPTSDS-------AELVECLRSKPAEELLDAQLKLL----VYGSVPFVPFGPVVDG--DFLPEHPEELLKSGNf 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974    371 LALPMIIGATKDASAFIVSRIYDQL----ARLQSRNVSDYIDVVLRHTappsehRLWKQWALREIFTPIQE--QTASLQT 444
Cdd:pfam00135  304 PKVPLLIGVTKDEGLLFAAYILDNVdilkALEEKLLRSLLIDLLYLLL------VDLPEEISAALREEYLDwgDRDDPET 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974    445 VAPGLLELSNYILYRAPVINSISQ-SYRSVPAYLYTFDYRGEHHRFghlsnPLPFGVDasLSDDSVYLFPYPPEASR-LN 522
Cdd:pfam00135  378 SRRALVELLTDYLFNCPVIRFADLhASRGTPVYMYSFDYRGSSLRY-----PKWVGVD--HGDELPYVFGTPFVGALlFT 450
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 44888974    523 PLDRSLSRALVTMWVNFATTGVPNPSSG--VWPQATSEYGPFLRFTNNQQ---SPLELDPHF 579
Cdd:pfam00135  451 EEDEKLSRKMMTYWTNFAKTGNPNGPEGlpKWPPYTDENGQYLSIDLEPRvkqGLKAERCAF 512
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
83-558 7.62e-73

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: 249.94  E-value: 7.62e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974   83 PVNAFLGIRYGTVGGGLARFQAAQPI-GYQGRVNATVQSPNCAQ------FPELDRLRLSEsrgenvdDCLTLDIYAPEG 155
Cdd:cd00312   16 GVYSFLGIPYAEPPVGDLRFKEPQPYePWSDVLDATSYPPSCMQwdqlggGLWNAKLPGSE-------DCLYLNVYTPKN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974  156 A---NQLPVLVFVHGEMLFDGGSEEAQPDYVL--EKDVLLVSINYRLAPFGFLSALTDELPGNVALSDLQLALEWLQRNV 230
Cdd:cd00312   89 TkpgNSLPVMVWIHGGGFMFGSGSLYPGDGLAreGDNVIVVSINYRLGVLGFLSTGDIELPGNYGLKDQRLALKWVQDNI 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974  231 VHFGGNAGQVTLVGQAGGATLAHALSLSGRAGNLFQQLILQSGTALNPYLIDNQPLDTLSTFARLARCPppsiNPSAQGL 310
Cdd:cd00312  169 AAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSGSALSPWAIQENARGRAKRLARLLGCN----DTSSAEL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974  311 KplyDCLARLPTSQLVAAFEQLLLQNehlgLTQLGGFKLVV-GDplgFLPSHPASLATNSSLA-LPMIIGATKD-ASAFI 387
Cdd:cd00312  245 L---DCLRSKSAEELLDATRKLLLFS----YSPFLPFGPVVdGD---FIPDDPEELIKEGKFAkVPLIIGVTKDeGGYFA 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974  388 VS--------------RIYDQLARLQSRNVSDYIDVVLRHTAPPSEHRLWKQWALREIFTPiqeqtaslqtvapgllels 453
Cdd:cd00312  315 AMllnfdakliietndRWLELLPYLLFYADDALADKVLEKYPGDVDDSVESRKNLSDMLTD------------------- 375
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974  454 nyILYRAPVINSISQS--YRSVPAYLYTFDYRGEhhrFGHLSNPLPFGVDAslSDDSVYLFPYPPEASRLNPLDRSLSRA 531
Cdd:cd00312  376 --LLFKCPARYFLAQHrkAGGSPVYAYVFDHRSS---LSVGRWPPWLGTVH--GDEIFFVFGNPLLKEGLREEEEKLSRT 448
                        490       500
                 ....*....|....*....|....*....
gi 44888974  532 LVTMWVNFATTGVPNPSSG--VWPQATSE 558
Cdd:cd00312  449 MMKYWANFAKTGNPNTEGNlvVWPAYTSE 477
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
55-581 1.09e-68

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 238.63  E-value: 1.09e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974   55 AQPQEAVVQAPEvGQILGIsghktiANRPVNAFLGIRYG--TVGGglARFQAAQP-IGYQGRVNATVQSPNCAQFPELDR 131
Cdd:COG2272    8 AAAAAPVVRTEA-GRVRGV------VEGGVRVFLGIPYAapPVGE--LRWRAPQPvEPWTGVRDATEFGPACPQPPRPGD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974  132 LRLSESRGEnvdDCLTLDIYAPEGANQ--LPVLVFVHGEMLFDGGSeeAQPDY---VL-EKDVLLVSINYRLAPFGFL-- 203
Cdd:COG2272   79 PGGPAPGSE---DCLYLNVWTPALAAGakLPVMVWIHGGGFVSGSG--SEPLYdgaALaRRGVVVVTINYRLGALGFLal 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974  204 SALTDE---LPGNVALSDLQLALEWLQRNVVHFGGNAGQVTLVGQAGGATLAHALSLSGRAGNLFQQLILQSGTALNPYl 280
Cdd:COG2272  154 PALSGEsygASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGLSVL- 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974  281 idnqPLDTL----STFARLARCPPPSInpsaqglkplyDCLARLPTSQLVAAFEQLLLQNEhlgltQLGGFKLVVGDPlg 356
Cdd:COG2272  233 ----TLAEAeavgAAFAAALGVAPATL-----------AALRALPAEELLAAQAALAAEGP-----GGLPFGPVVDGD-- 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974  357 FLPSHP-ASLATNSSLALPMIIGATKD-ASAFIVsriydqlarlqsrnvsdyidvVLRHTAPPSEHRLWKqwALREIFTP 434
Cdd:COG2272  291 VLPEDPlEAFAAGRAADVPLLIGTNRDeGRLFAA---------------------LLGDLGPLTAADYRA--ALRRRFGD 347
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974  435 IQEQTASL---QTVAPGLLELSNYILYRAPVINSI-SQSYRSVPAYLYTFDYRGEHHRfghlsnPLPFGvdASLSDDSVY 510
Cdd:COG2272  348 DADEVLAAypaASPAEALAALATDRVFRCPARRLAeAHAAAGAPVYLYRFDWRSPPLR------GFGLG--AFHGAELPF 419
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 44888974  511 LFPYP--PEASRLNPLDRSLSRALVTMWVNFATTGVPN-PSSGVWPQATSEYGPFLRFtnNQQSPLELDPHFGE 581
Cdd:COG2272  420 VFGNLdaPALTGLTPADRALSDQMQAYWVNFARTGDPNgPGLPEWPAYDPEDRAVMVF--DAEPRVVNDPDAEE 491
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
681-717 6.39e-04

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 41.96  E-value: 6.39e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 44888974    681 REQQDERIRQQREQEERLRQQREQEERLRQQRELEER 717
Cdd:pfam15927    2 RLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQ 38
 
Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
58-579 2.37e-145

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 443.67  E-value: 2.37e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974     58 QEAVVQAPeVGQILGISGHKTIAnRPVNAFLGIRYGTVGGGLARFQAAQPI-GYQGRVNATVQSPNCAQFPELDRLRLSE 136
Cdd:pfam00135    1 DSPVVTTS-LGRVRGKRLKVDGG-KPVYAFLGIPYAEPPVGELRFQPPEPPePWTGVRDATKFGPRCPQNGDLTSPGSSG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974    137 SRGEnvDDCLTLDIYAPEGA----NQLPVLVFVHGEMLFDGGSEEAQPDYVLEK-DVLLVSINYRLAPFGFLSALTDELP 211
Cdd:pfam00135   79 LEGS--EDCLYLNVYTPKELkenkNKLPVMVWIHGGGFMFGSGSLYDGSYLAAEgDVIVVTINYRLGPLGFLSTGDDEAP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974    212 GNVALSDLQLALEWLQRNVVHFGGNAGQVTLVGQAGGATLAHALSLSGRAGNLFQQLILQSGTALNPYLIDNQPLDTLST 291
Cdd:pfam00135  157 GNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAIQSNARQRAKE 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974    292 FARLARCPPPSInpsaqglKPLYDCLARLPTSQLVAAFEQLLlqneHLGLTQLGGFKLVVGDplGFLPSHPASLATNSS- 370
Cdd:pfam00135  237 LAKLVGCPTSDS-------AELVECLRSKPAEELLDAQLKLL----VYGSVPFVPFGPVVDG--DFLPEHPEELLKSGNf 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974    371 LALPMIIGATKDASAFIVSRIYDQL----ARLQSRNVSDYIDVVLRHTappsehRLWKQWALREIFTPIQE--QTASLQT 444
Cdd:pfam00135  304 PKVPLLIGVTKDEGLLFAAYILDNVdilkALEEKLLRSLLIDLLYLLL------VDLPEEISAALREEYLDwgDRDDPET 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974    445 VAPGLLELSNYILYRAPVINSISQ-SYRSVPAYLYTFDYRGEHHRFghlsnPLPFGVDasLSDDSVYLFPYPPEASR-LN 522
Cdd:pfam00135  378 SRRALVELLTDYLFNCPVIRFADLhASRGTPVYMYSFDYRGSSLRY-----PKWVGVD--HGDELPYVFGTPFVGALlFT 450
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 44888974    523 PLDRSLSRALVTMWVNFATTGVPNPSSG--VWPQATSEYGPFLRFTNNQQ---SPLELDPHF 579
Cdd:pfam00135  451 EEDEKLSRKMMTYWTNFAKTGNPNGPEGlpKWPPYTDENGQYLSIDLEPRvkqGLKAERCAF 512
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
83-558 7.62e-73

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: 249.94  E-value: 7.62e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974   83 PVNAFLGIRYGTVGGGLARFQAAQPI-GYQGRVNATVQSPNCAQ------FPELDRLRLSEsrgenvdDCLTLDIYAPEG 155
Cdd:cd00312   16 GVYSFLGIPYAEPPVGDLRFKEPQPYePWSDVLDATSYPPSCMQwdqlggGLWNAKLPGSE-------DCLYLNVYTPKN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974  156 A---NQLPVLVFVHGEMLFDGGSEEAQPDYVL--EKDVLLVSINYRLAPFGFLSALTDELPGNVALSDLQLALEWLQRNV 230
Cdd:cd00312   89 TkpgNSLPVMVWIHGGGFMFGSGSLYPGDGLAreGDNVIVVSINYRLGVLGFLSTGDIELPGNYGLKDQRLALKWVQDNI 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974  231 VHFGGNAGQVTLVGQAGGATLAHALSLSGRAGNLFQQLILQSGTALNPYLIDNQPLDTLSTFARLARCPppsiNPSAQGL 310
Cdd:cd00312  169 AAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSGSALSPWAIQENARGRAKRLARLLGCN----DTSSAEL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974  311 KplyDCLARLPTSQLVAAFEQLLLQNehlgLTQLGGFKLVV-GDplgFLPSHPASLATNSSLA-LPMIIGATKD-ASAFI 387
Cdd:cd00312  245 L---DCLRSKSAEELLDATRKLLLFS----YSPFLPFGPVVdGD---FIPDDPEELIKEGKFAkVPLIIGVTKDeGGYFA 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974  388 VS--------------RIYDQLARLQSRNVSDYIDVVLRHTAPPSEHRLWKQWALREIFTPiqeqtaslqtvapgllels 453
Cdd:cd00312  315 AMllnfdakliietndRWLELLPYLLFYADDALADKVLEKYPGDVDDSVESRKNLSDMLTD------------------- 375
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974  454 nyILYRAPVINSISQS--YRSVPAYLYTFDYRGEhhrFGHLSNPLPFGVDAslSDDSVYLFPYPPEASRLNPLDRSLSRA 531
Cdd:cd00312  376 --LLFKCPARYFLAQHrkAGGSPVYAYVFDHRSS---LSVGRWPPWLGTVH--GDEIFFVFGNPLLKEGLREEEEKLSRT 448
                        490       500
                 ....*....|....*....|....*....
gi 44888974  532 LVTMWVNFATTGVPNPSSG--VWPQATSE 558
Cdd:cd00312  449 MMKYWANFAKTGNPNTEGNlvVWPAYTSE 477
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
55-581 1.09e-68

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 238.63  E-value: 1.09e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974   55 AQPQEAVVQAPEvGQILGIsghktiANRPVNAFLGIRYG--TVGGglARFQAAQP-IGYQGRVNATVQSPNCAQFPELDR 131
Cdd:COG2272    8 AAAAAPVVRTEA-GRVRGV------VEGGVRVFLGIPYAapPVGE--LRWRAPQPvEPWTGVRDATEFGPACPQPPRPGD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974  132 LRLSESRGEnvdDCLTLDIYAPEGANQ--LPVLVFVHGEMLFDGGSeeAQPDY---VL-EKDVLLVSINYRLAPFGFL-- 203
Cdd:COG2272   79 PGGPAPGSE---DCLYLNVWTPALAAGakLPVMVWIHGGGFVSGSG--SEPLYdgaALaRRGVVVVTINYRLGALGFLal 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974  204 SALTDE---LPGNVALSDLQLALEWLQRNVVHFGGNAGQVTLVGQAGGATLAHALSLSGRAGNLFQQLILQSGTALNPYl 280
Cdd:COG2272  154 PALSGEsygASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGLSVL- 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974  281 idnqPLDTL----STFARLARCPPPSInpsaqglkplyDCLARLPTSQLVAAFEQLLLQNEhlgltQLGGFKLVVGDPlg 356
Cdd:COG2272  233 ----TLAEAeavgAAFAAALGVAPATL-----------AALRALPAEELLAAQAALAAEGP-----GGLPFGPVVDGD-- 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974  357 FLPSHP-ASLATNSSLALPMIIGATKD-ASAFIVsriydqlarlqsrnvsdyidvVLRHTAPPSEHRLWKqwALREIFTP 434
Cdd:COG2272  291 VLPEDPlEAFAAGRAADVPLLIGTNRDeGRLFAA---------------------LLGDLGPLTAADYRA--ALRRRFGD 347
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974  435 IQEQTASL---QTVAPGLLELSNYILYRAPVINSI-SQSYRSVPAYLYTFDYRGEHHRfghlsnPLPFGvdASLSDDSVY 510
Cdd:COG2272  348 DADEVLAAypaASPAEALAALATDRVFRCPARRLAeAHAAAGAPVYLYRFDWRSPPLR------GFGLG--AFHGAELPF 419
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 44888974  511 LFPYP--PEASRLNPLDRSLSRALVTMWVNFATTGVPN-PSSGVWPQATSEYGPFLRFtnNQQSPLELDPHFGE 581
Cdd:COG2272  420 VFGNLdaPALTGLTPADRALSDQMQAYWVNFARTGDPNgPGLPEWPAYDPEDRAVMVF--DAEPRVVNDPDAEE 491
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
149-300 1.23e-12

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 67.98  E-value: 1.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974  149 DIYAPEGANQ-LPVLVFVHGemlfdGG-----SEEAQP---DYVLEKDVLLVSINYRLAPfgflsaltdELPGNVALSDL 219
Cdd:COG0657    2 DVYRPAGAKGpLPVVVYFHG-----GGwvsgsKDTHDPlarRLAARAGAAVVSVDYRLAP---------EHPFPAALEDA 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974  220 QLALEWLQRNVVHFGGNAGQVTLVGQAGGATLAHALSLSGR--AGNLFQQLILQSGtalnPYLIDNQPLdtlstFARLAR 297
Cdd:COG0657   68 YAALRWLRANAAELGIDPDRIAVAGDSAGGHLAAALALRARdrGGPRPAAQVLIYP----VLDLTASPL-----RADLAG 138

                 ...
gi 44888974  298 CPP 300
Cdd:COG0657  139 LPP 141
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
148-263 2.27e-06

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: 49.49  E-value: 2.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974    148 LDIYAPEGA-NQLPVLVFVHGEMLFdGGSEEAQPDYV-------LEKDVLLVSINYRL---APFgflsaltdelPGnvAL 216
Cdd:pfam20434    1 LDIYLPKNAkGPYPVVIWIHGGGWN-SGDKEADMGFMtntvkalLKAGYAVASINYRLstdAKF----------PA--QI 67
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 44888974    217 SDLQLALEWLQRNVVHFGGNAGQVTLVGQAGGATLAhalSLSGRAGN 263
Cdd:pfam20434   68 QDVKAAIRFLRANAAKYGIDTNKIALMGFSAGGHLA---LLAGLSNN 111
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
162-278 3.13e-06

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: 49.13  E-value: 3.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888974    162 LVFVHGE--MLFDGGSEEAQP-DYVLEKDVLLVSINYRLAP-FGFLSALTDelpgnvALSdlqlALEWLQRNVVHFGGNA 237
Cdd:pfam07859    1 LVYFHGGgfVLGSADTHDRLCrRLAAEAGAVVVSVDYRLAPeHPFPAAYDD------AYA----ALRWLAEQAAELGADP 70
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 44888974    238 GQVTLVGQAGGATLAHALSLSGRAGNLFQ---QLILQSGTALNP 278
Cdd:pfam07859   71 SRIAVAGDSAGGNLAAAVALRARDEGLPKpagQVLIYPGTDLRT 114
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
681-717 6.39e-04

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 41.96  E-value: 6.39e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 44888974    681 REQQDERIRQQREQEERLRQQREQEERLRQQRELEER 717
Cdd:pfam15927    2 RLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQ 38
Pinin_SDK_memA pfam04696
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ...
677-717 1.77e-03

pinin/SDK/memA/ protein conserved region; Members of this family have very varied localizations within the eukaryotic cell. pinin is known to localize at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque. SDK2/3 is a dynamically localized nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions.


Pssm-ID: 461396 [Multi-domain]  Cd Length: 130  Bit Score: 39.58  E-value: 1.77e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 44888974    677 QQEPREQQDERIRQQREQ-EERLRQQREQ--EERLRQQRELEER 717
Cdd:pfam04696   35 RAEIEKRLEEKAKQEKEElEERKREEREElfEERRAEQIELRAL 78
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
677-717 9.45e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 39.93  E-value: 9.45e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 44888974    677 QQEPREQQD------ERIRQQREQEERLRQQREQEERLRQqrELEER 717
Cdd:pfam15709  364 QQEQLERAEkmreelELEQQRRFEEIRLRKQRLEEERQRQ--EEEER 408
 
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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