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Conserved domains on  [gi|41053955|ref|NP_956231|]
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protein phosphatase methylesterase 1 [Danio rerio]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11427190)

alpha/beta hydrolase family protein 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:  12369917|19508187|37582413|31545554
SCOP:  3000102

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 68-210 4.34e-22

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: 93.14  E-value: 4.34e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955  68 SGSHGPVLLLLHGGGHSALSWAVFTSVICSRitCRVVAMDLRGHGDSKvKNPDDLSAETMAKDIGKVVEALygeNPPPIM 147
Cdd:COG0596  19 AGPDGPPVVLLHGLPGSSYEWRPLIPALAAG--YRVIAPDLRGHGRSD-KPAGGYTLDDLADDLAALLDAL---GLERVV 92

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41053955 148 IIGHSMGGAIAVHTAAANhvPSLL-GLCVIDvvegtamDALNSMQNFLRSRPKTFKSVENAIEW 210
Cdd:COG0596  93 LVGHSMGGMVALELAARH--PERVaGLVLVD-------EVLAALAEPLRRPGLAPEALAALLRA 147
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 73-353 8.23e-22

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: 92.95  E-value: 8.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955    73 PVLLLLHGGGHSALSWAVFTSVIcSRITCRVVAMDLRGHGDSKV-KNPDDLSAETMAKDIGKVVEALygeNPPPIMIIGH 151
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPAL-ARDGFRVIALDLRGFGKSSRpKAQDDYRTDDLAEDLEYILEAL---GLEKVNLVGH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955   152 SMGGAIAVHTAA--ANHVPSLLGLCVIDVVEGTAMDALNSMQNFLRSRPKTFKSVENAiewsvKSGQIRNVESARVSMVG 229
Cdd:pfam00561  77 SMGGLIALAYAAkyPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPN-----PLGRLVAKLLALLLLRL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955   230 QVKKCEEPLSspgvsksisegiieeeeedeeggesnhKRKKEDDQEIKKeSLYTWRIelskteKYWEGWF-KGLSSLFLS 308
Cdd:pfam00561 152 RLLKALPLLN---------------------------KRFPSGDYALAK-SLVTGAL------LFIETWStELRAKFLGR 197

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 41053955   309 CSVPKLLLLAGIDRLDKDLTIGQMQGKF---QMQVLPQCGHAVHEDAP 353
Cdd:pfam00561 198 LDEPTLIIWGDQDPLVPPQALEKLAQLFpnaRLVVIPDAGHFAFLEGP 245
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 68-210 4.34e-22

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: 93.14  E-value: 4.34e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955  68 SGSHGPVLLLLHGGGHSALSWAVFTSVICSRitCRVVAMDLRGHGDSKvKNPDDLSAETMAKDIGKVVEALygeNPPPIM 147
Cdd:COG0596  19 AGPDGPPVVLLHGLPGSSYEWRPLIPALAAG--YRVIAPDLRGHGRSD-KPAGGYTLDDLADDLAALLDAL---GLERVV 92

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41053955 148 IIGHSMGGAIAVHTAAANhvPSLL-GLCVIDvvegtamDALNSMQNFLRSRPKTFKSVENAIEW 210
Cdd:COG0596  93 LVGHSMGGMVALELAARH--PERVaGLVLVD-------EVLAALAEPLRRPGLAPEALAALLRA 147
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 73-353 8.23e-22

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: 92.95  E-value: 8.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955    73 PVLLLLHGGGHSALSWAVFTSVIcSRITCRVVAMDLRGHGDSKV-KNPDDLSAETMAKDIGKVVEALygeNPPPIMIIGH 151
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPAL-ARDGFRVIALDLRGFGKSSRpKAQDDYRTDDLAEDLEYILEAL---GLEKVNLVGH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955   152 SMGGAIAVHTAA--ANHVPSLLGLCVIDVVEGTAMDALNSMQNFLRSRPKTFKSVENAiewsvKSGQIRNVESARVSMVG 229
Cdd:pfam00561  77 SMGGLIALAYAAkyPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPN-----PLGRLVAKLLALLLLRL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955   230 QVKKCEEPLSspgvsksisegiieeeeedeeggesnhKRKKEDDQEIKKeSLYTWRIelskteKYWEGWF-KGLSSLFLS 308
Cdd:pfam00561 152 RLLKALPLLN---------------------------KRFPSGDYALAK-SLVTGAL------LFIETWStELRAKFLGR 197

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 41053955   309 CSVPKLLLLAGIDRLDKDLTIGQMQGKF---QMQVLPQCGHAVHEDAP 353
Cdd:pfam00561 198 LDEPTLIIWGDQDPLVPPQALEKLAQLFpnaRLVVIPDAGHFAFLEGP 245
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 75-359 9.18e-14

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 69.81  E-value: 9.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955    75 LLLLHGGGHSALSWAVFtsvicSRITCRVVAMDLRGHGDSkVKNPDDLSAetmAKDIGKVVEALygENPPPIMIIGHSMG 154
Cdd:pfam12697   1 VVLVHGAGLSAAPLAAL-----LAAGVAVLAPDLPGHGSS-SPPPLDLAD---LADLAALLDEL--GAARPVVLVGHSLG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955   155 GAIAVHTAAANHVPSLLglcvIDvvegtAMDALNSMQNFLRSRPKTFKSVENAIEWSVKsgqirnvESARVSMVGQVKKC 234
Cdd:pfam12697  70 GAVALAAAAAALVVGVL----VA-----PLAAPPGLLAALLALLARLGAALAAPAWLAA-------ESLARGFLDDLPAD 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955   235 EEplsspgvsksisegiieeeeedeeggesnhkrkkeddqeikkeslytWRIELSKTEKYWEGWFKGLSSLFLSCSVPkL 314
Cdd:pfam12697 134 AE-----------------------------------------------WAAALARLAALLAALALLPLAAWRDLPVP-V 165

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 41053955   315 LLLAGIDRLDKDLT--IGQMQGKFQMQVLPQCGHAVHEDaPEKVADA 359
Cdd:pfam12697 166 LVLAEEDRLVPELAqrLLAALAGARLVVLPGAGHLPLDD-PEEVAEA 211
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 72-174 1.57e-08

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 55.72  E-value: 1.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955   72 GPVLLLLHG-GG--------HSALSWAVftsvicsritcRVVAMDLRGHGDSkVKNPDDLSAETMAKDIGKVVEALygeN 142
Cdd:PRK14875 131 GTPVVLIHGfGGdlnnwlfnHAALAAGR-----------PVIALDLPGHGAS-SKAVGAGSLDELAAAVLAFLDAL---G 195

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 41053955  143 PPPIMIIGHSMGGAIAVhTAAANH---VPSLLGLC 174
Cdd:PRK14875 196 IERAHLVGHSMGGAVAL-RLAARApqrVASLTLIA 229
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 123-175 2.77e-04

Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 40.95  E-value: 2.77e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41053955 123 SAETMAKDIGKVVEALYGENPP-PIMIIGHSMGGAIAVHTAA--ANHVPSLLGLCV 175
Cdd:cd00741   6 AARSLANLVLPLLKSALAQYPDyKIHVTGHSLGGALAGLAGLdlRGRGLGRLVRVY 61
SH3_SH3RF_3 cd11783
Third Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), SH3RF3, and ...
 265-303 6.28e-03

Third Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), SH3RF3, and similar domains; SH3RF1 (or POSH) and SH3RF3 (or POSH2) are scaffold proteins that function as E3 ubiquitin-protein ligases. They contain an N-terminal RING finger domain and four SH3 domains. This model represents the third SH3 domain, located in the middle of SH3RF1 and SH3RF3, and similar domains. SH3RF1 plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF3 interacts with p21-activated kinase 2 (PAK2) and GTP-loaded Rac1. It may play a role in regulating JNK mediated apoptosis in certain conditions. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212717 [Multi-domain]  Cd Length: 55  Bit Score: 34.68  E-value: 6.28e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 41053955 265 NHKRKKEDDQEIKKESLYTwrielsKTEKYWEGWFKGLS 303
Cdd:cd11783   7 PYKPQKPDELELRKGEMYT------VTEKCQDGWFKGTS 39
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 68-210 4.34e-22

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: 93.14  E-value: 4.34e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955  68 SGSHGPVLLLLHGGGHSALSWAVFTSVICSRitCRVVAMDLRGHGDSKvKNPDDLSAETMAKDIGKVVEALygeNPPPIM 147
Cdd:COG0596  19 AGPDGPPVVLLHGLPGSSYEWRPLIPALAAG--YRVIAPDLRGHGRSD-KPAGGYTLDDLADDLAALLDAL---GLERVV 92

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41053955 148 IIGHSMGGAIAVHTAAANhvPSLL-GLCVIDvvegtamDALNSMQNFLRSRPKTFKSVENAIEW 210
Cdd:COG0596  93 LVGHSMGGMVALELAARH--PERVaGLVLVD-------EVLAALAEPLRRPGLAPEALAALLRA 147
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 73-353 8.23e-22

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: 92.95  E-value: 8.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955    73 PVLLLLHGGGHSALSWAVFTSVIcSRITCRVVAMDLRGHGDSKV-KNPDDLSAETMAKDIGKVVEALygeNPPPIMIIGH 151
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPAL-ARDGFRVIALDLRGFGKSSRpKAQDDYRTDDLAEDLEYILEAL---GLEKVNLVGH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955   152 SMGGAIAVHTAA--ANHVPSLLGLCVIDVVEGTAMDALNSMQNFLRSRPKTFKSVENAiewsvKSGQIRNVESARVSMVG 229
Cdd:pfam00561  77 SMGGLIALAYAAkyPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPN-----PLGRLVAKLLALLLLRL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955   230 QVKKCEEPLSspgvsksisegiieeeeedeeggesnhKRKKEDDQEIKKeSLYTWRIelskteKYWEGWF-KGLSSLFLS 308
Cdd:pfam00561 152 RLLKALPLLN---------------------------KRFPSGDYALAK-SLVTGAL------LFIETWStELRAKFLGR 197

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 41053955   309 CSVPKLLLLAGIDRLDKDLTIGQMQGKF---QMQVLPQCGHAVHEDAP 353
Cdd:pfam00561 198 LDEPTLIIWGDQDPLVPPQALEKLAQLFpnaRLVVIPDAGHFAFLEGP 245
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
68-166 2.22e-18

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 83.13  E-value: 2.22e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955  68 SGSHGPVLLLLHGGGHSALSWAVFTSVICSR-ItcRVVAMDLRGHGDSKVKNPDDLSAETMAKDIGKVVEALYGENPPPI 146
Cdd:COG2267  24 AGSPRGTVVLVHGLGEHSGRYAELAEALAAAgY--AVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDALRARPGLPV 101

                        90       100
                ....*....|....*....|
gi 41053955 147 MIIGHSMGGAIAVHTAAANH 166
Cdd:COG2267 102 VLLGHSMGGLIALLYAARYP 121
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 75-359 9.18e-14

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 69.81  E-value: 9.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955    75 LLLLHGGGHSALSWAVFtsvicSRITCRVVAMDLRGHGDSkVKNPDDLSAetmAKDIGKVVEALygENPPPIMIIGHSMG 154
Cdd:pfam12697   1 VVLVHGAGLSAAPLAAL-----LAAGVAVLAPDLPGHGSS-SPPPLDLAD---LADLAALLDEL--GAARPVVLVGHSLG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955   155 GAIAVHTAAANHVPSLLglcvIDvvegtAMDALNSMQNFLRSRPKTFKSVENAIEWSVKsgqirnvESARVSMVGQVKKC 234
Cdd:pfam12697  70 GAVALAAAAAALVVGVL----VA-----PLAAPPGLLAALLALLARLGAALAAPAWLAA-------ESLARGFLDDLPAD 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955   235 EEplsspgvsksisegiieeeeedeeggesnhkrkkeddqeikkeslytWRIELSKTEKYWEGWFKGLSSLFLSCSVPkL 314
Cdd:pfam12697 134 AE-----------------------------------------------WAAALARLAALLAALALLPLAAWRDLPVP-V 165

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 41053955   315 LLLAGIDRLDKDLT--IGQMQGKFQMQVLPQCGHAVHEDaPEKVADA 359
Cdd:pfam12697 166 LVLAEEDRLVPELAqrLLAALAGARLVVLPGAGHLPLDD-PEEVAEA 211
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 74-173 1.25e-09

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 57.99  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955    74 VLLLLHGGG-HS-----------ALSWAVFtsvicsritcrvvAMDLRGHGDSK-----VKNPDDlsaetMAKDIGKVVE 136
Cdd:pfam12146   6 VVVLVHGLGeHSgryahladalaAQGFAVY-------------AYDHRGHGRSDgkrghVPSFDD-----YVDDLDTFVD 67

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 41053955   137 ALYGENP-PPIMIIGHSMGGAIAVHtAAANHVPSLLGL 173
Cdd:pfam12146  68 KIREEHPgLPLFLLGHSMGGLIAAL-YALRYPDKVDGL 104
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 72-174 1.57e-08

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 55.72  E-value: 1.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955   72 GPVLLLLHG-GG--------HSALSWAVftsvicsritcRVVAMDLRGHGDSkVKNPDDLSAETMAKDIGKVVEALygeN 142
Cdd:PRK14875 131 GTPVVLIHGfGGdlnnwlfnHAALAAGR-----------PVIALDLPGHGAS-SKAVGAGSLDELAAAVLAFLDAL---G 195

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 41053955  143 PPPIMIIGHSMGGAIAVhTAAANH---VPSLLGLC 174
Cdd:PRK14875 196 IERAHLVGHSMGGAVAL-RLAARApqrVASLTLIA 229
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
73-163 3.15e-08

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 53.87  E-value: 3.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955  73 PVLLLLHGGGHSAL-SWAVFTSVICSRiTCRVVAMDLRGHGDSKVKNPDDlsaetMAKDIGKVVEALYGE---NPPPIMI 148
Cdd:COG1506  24 PVVVYVHGGPGSRDdSFLPLAQALASR-GYAVLAPDYRGYGESAGDWGGD-----EVDDVLAAIDYLAARpyvDPDRIGI 97

                        90
                ....*....|....*
gi 41053955 149 IGHSMGGAIAVHTAA 163
Cdd:COG1506  98 YGHSYGGYMALLAAA 112
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 67-175 2.46e-07

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 51.01  E-value: 2.46e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955  67 SSGSHGPVLLLLH--GGGHSA-LSWAVFTSvicSRItcRVVAMDLRGHGDSkvknpddlSAETMAKDIGKVVEALYGENP 143
Cdd:COG3208   1 PRPDARLRLFCFPyaGGSASAyRPWAAALP---PDI--EVLAVQLPGRGDR--------LGEPPLTSLEELADDLAEELA 67

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 41053955 144 P----PIMIIGHSMGGAIAVHTAA---ANHVPSLLGLCV 175
Cdd:COG3208  68 PlldrPFALFGHSMGALLAFELARrleRRGRPLPAHLFV 106
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 45-162 3.01e-07

2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 52.55  E-value: 3.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955    45 ETIEDVEVEVENDNSKDTFRIYSSGSH--GPVLLLLHGGGHSALSWAVFTSVICSriTCRVVAMDLRGHGDSKVKNPDDL 122
Cdd:PLN02980 1342 EQVRTYELRVDVDGFSCLIKVHEVGQNaeGSVVLFLHGFLGTGEDWIPIMKAISG--SARCISIDLPGHGGSKIQNHAKE 1419

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 41053955   123 SAETMAKDIGKVVEALYGE----NPPPIMIIGHSMGGAIAVHTA 162
Cdd:PLN02980 1420 TQTEPTLSVELVADLLYKLiehiTPGKVTLVGYSMGARIALYMA 1463
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
101-176 2.73e-06

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 48.01  E-value: 2.73e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41053955 101 CRVVAMDLRGHGDSkvknPDDLSAETmAKD-IGKVVEALY--GENPPPIMIIGHSMGGAIAVHTAAanHVPSLLGLCVI 176
Cdd:COG1647  43 YTVYAPRLPGHGTS----PEDLLKTT-WEDwLEDVEEAYEilKAGYDKVIVIGLSMGGLLALLLAA--RYPDVAGLVLL 114
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 64-214 2.73e-06

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 48.58  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955   64 RIYSSGSHGPVLLLLHGGGHSALSWAVFTSVICSRitCRVVAMDLRGHGDSKVKNPDDLSA------ETMAKDIGKVVEA 137
Cdd:PLN02824  21 RYQRAGTSGPALVLVHGFGGNADHWRKNTPVLAKS--HRVYAIDLLGYGYSDKPNPRSAPPnsfytfETWGEQLNDFCSD 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955  138 LYGEnppPIMIIGHSMGGAIAVHtAAANHVPSLLGLCVIDVvegtAMDALN-------------SMQNFLRSRP---KTF 201
Cdd:PLN02824  99 VVGD---PAFVICNSVGGVVGLQ-AAVDAPELVRGVMLINI----SLRGLHikkqpwlgrpfikAFQNLLRETAvgkAFF 170

                        170
                 ....*....|...
gi 41053955  202 KSVenAIEWSVKS 214
Cdd:PLN02824 171 KSV--ATPETVKN 181
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 73-173 1.12e-05

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 43.66  E-value: 1.12e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955  73 PVLLLlHGGGHSALSWAVFTSVICSRITCrVVAMDLrghgdskvkNPDDLSAETMAKDIGKVVEALYGENP-PPIMIIGH 151
Cdd:COG1075   7 PVVLV-HGLGGSAASWAPLAPRLRAAGYP-VYALNY---------PSTNGSIEDSAEQLAAFVDAVLAATGaEKVDLVGH 75

                        90       100
                ....*....|....*....|....*.
gi 41053955 152 SMGGAIA----VHTAAANHVPSLLGL 173
Cdd:COG1075  76 SMGGLVAryylKRLGGAAKVARVVTL 101
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
64-170 1.64e-05

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 45.25  E-value: 1.64e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955  64 RIYS---SGSHGPVLLLLHGGGHSALSWAVFTSViCSRIT----CRVVAMDLRghgdskvknpddLSAE----TMAKDIG 132
Cdd:COG0657   2 DVYRpagAKGPLPVVVYFHGGGWVSGSKDTHDPL-ARRLAaragAAVVSVDYR------------LAPEhpfpAALEDAY 68

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 41053955 133 KVVEAL------YGENPPPIMIIGHSMGGAIAVHTAAANHVPSL 170
Cdd:COG0657  69 AALRWLranaaeLGIDPDRIAVAGDSAGGHLAAALALRARDRGG 112
PLN02578 PLN02578
hydrolase
 72-212 2.66e-05

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 45.60  E-value: 2.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955   72 GPVLLLLHGGGHSALSWAVFTSVICSriTCRVVAMDLRGHGDSKvKNPDDLSAETMAKDIGKVVEALYGEnppPIMIIGH 151
Cdd:PLN02578  86 GLPIVLIHGFGASAFHWRYNIPELAK--KYKVYALDLLGFGWSD-KALIEYDAMVWRDQVADFVKEVVKE---PAVLVGN 159

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41053955  152 SMGGAIAVHTAAANHvpsllglcviDVVEGTAMdaLNS---MQNFLRSRPKTFKSVENAIEWSV 212
Cdd:PLN02578 160 SLGGFTALSTAVGYP----------ELVAGVAL--LNSagqFGSESREKEEAIVVEETVLTRFV 211
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
70-199 3.09e-05

Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 45.52  E-value: 3.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955  70 SHGPVLLLLHG-GGHSALSWAVFTSVICSRITCRVVAMDLRGHGDSKVKNP----DDLSAetmakDIGKVVEALYGENPP 144
Cdd:COG0429  59 PSKPLVVLLHGlEGSSDSHYARGLARALYARGWDVVRLNFRGCGGEPNLLPrlyhSGDTE-----DLVWVLAHLRARYPY 133

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41053955 145 -PIMIIGHSMGGAIAVHTAA--ANHVPSLLGLCVI----DVVEgtAMDALNS------MQNFLRS-RPK 199
Cdd:COG0429 134 aPLYAVGFSLGGNLLLKYLGeqGDDAPPLKAAVAVspplDLAA--SADRLERgfnrlyQRYFLRSlKRK 200
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
46-165 3.10e-05

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 44.57  E-value: 3.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955  46 TIEDVEVEVENDNSKDTFRIY-SSGSHGPVLLLLHG-GGHSALSWAVftsviCSRIT---CRVVAMDLRGHGDSkVKNPD 120
Cdd:COG0412   2 TTETVTIPTPDGVTLPGYLARpAGGGPRPGVVVLHEiFGLNPHIRDV-----ARRLAaagYVVLAPDLYGRGGP-GDDPD 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41053955 121 D-------LSAETMAKDIGKVVEALYGE---NPPPIMIIGHSMGGAIAVHTAAAN 165
Cdd:COG0412  76 EaralmgaLDPELLAADLRAALDWLKAQpevDAGRVGVVGFCFGGGLALLAAARG 130
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
101-167 3.44e-05

Predicted alpha/beta hydrolase [General function prediction only];


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 45.26  E-value: 3.44e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41053955 101 CRVVAMDLRGHGDSKVKNPDDLSA---ETMAKDIGKVVEALYGENPP-PIMIIGHSMGGAIAVHTAAANHV 167
Cdd:COG4757  60 FAVLTYDYRGIGLSRPGSLRGFDAgyrDWGELDLPAVLDALRARFPGlPLLLVGHSLGGQLLGLAPNAERV 130
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 72-181 6.12e-05

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 44.06  E-value: 6.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955   72 GPVLLLLHGGGHSALSWavfTSVICSRITCRVVAMDLRGHGDSKVKNPDDLsaETMAKDIGKVVEAlYGENPppIMIIGH 151
Cdd:PRK11126   2 LPWLVFLHGLLGSGQDW---QPVGEALPDYPRLYIDLPGHGGSAAISVDGF--ADVSRLLSQTLQS-YNILP--YWLVGY 73

                         90       100       110
                 ....*....|....*....|....*....|
gi 41053955  152 SMGGAIAVHTAAANHVPSLLGLCvidvVEG 181
Cdd:PRK11126  74 SLGGRIAMYYACQGLAGGLCGLI----VEG 99
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 123-175 2.77e-04

Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 40.95  E-value: 2.77e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41053955 123 SAETMAKDIGKVVEALYGENPP-PIMIIGHSMGGAIAVHTAA--ANHVPSLLGLCV 175
Cdd:cd00741   6 AARSLANLVLPLLKSALAQYPDyKIHVTGHSLGGALAGLAGLdlRGRGLGRLVRVY 61
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 73-163 3.54e-04

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 41.82  E-value: 3.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955  73 PVLLLLHGGG----HSALSWAVFTSvicsritcR---VVAMDLRGHGDSK-----VKNPDDLSAETMAKdigkVVEALYG 140
Cdd:COG1073  38 PAVVVAHGNGgvkeQRALYAQRLAE--------LgfnVLAFDYRGYGESEgepreEGSPERRDARAAVD----YLRTLPG 105

                        90       100
                ....*....|....*....|...
gi 41053955 141 ENPPPIMIIGHSMGGAIAVHTAA 163
Cdd:COG1073 106 VDPERIGLLGISLGGGYALNAAA 128
PRK10673 PRK10673
esterase;
103-178 4.39e-04

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 41.64  E-value: 4.39e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41053955  103 VVAMDLRGHGDSKVKNPDDLSAetMAKDIGKVVEALygeNPPPIMIIGHSMGGAIAVH-TAAAnhvPSLL-GLCVIDV 178
Cdd:PRK10673  45 IIQVDMRNHGLSPRDPVMNYPA--MAQDLLDTLDAL---QIEKATFIGHSMGGKAVMAlTALA---PDRIdKLVAIDI 114
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 74-171 1.82e-03

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 39.88  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955   74 VLLLLHGGGHSALSWAVFTSVICSritCR--VVAMDLRGHGDSKVKNPDDLSAETMAKDIGKVVEALYGENPP-PIMIIG 150
Cdd:PLN02652 138 ILIIIHGLNEHSGRYLHFAKQLTS---CGfgVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAFLEKIRSENPGvPCFLFG 214

                         90       100
                 ....*....|....*....|.
gi 41053955  151 HSMGGAIAVHTAAANHVPSLL 171
Cdd:PLN02652 215 HSTGGAVVLKAASYPSIEDKL 235
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 73-164 2.48e-03

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 38.91  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955    73 PVLLLLHGGGHSALSWAVFTSVIcsRITCRVVAMDLRGHGDSkvknpddlsaETMAKDIGKVVEALYGE-----NPPPIM 147
Cdd:pfam00975   1 RPLFCFPPAGGSASSFRSLARRL--PPPAEVLAVQYPGRGRG----------EPPLNSIEALADEYAEAlrqiqPEGPYA 68

                          90
                  ....*....|....*..
gi 41053955   148 IIGHSMGGAIAVHTAAA 164
Cdd:pfam00975  69 LFGHSMGGMLAFEVARR 85
PRK05855 PRK05855
SDR family oxidoreductase;
72-154 2.91e-03

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 39.58  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955   72 GPVLLLLHGGGHSALSWAVFTSVICSRItcRVVAMDLRGHGDSKVknPDDLSAETMAK---DIGKVVEALygeNPP-PIM 147
Cdd:PRK05855  25 RPTVVLVHGYPDNHEVWDGVAPLLADRF--RVVAYDVRGAGRSSA--PKRTAAYTLARladDFAAVIDAV---SPDrPVH 97


                 ....*..
gi 41053955  148 IIGHSMG 154
Cdd:PRK05855  98 LLAHDWG 104
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
73-165 3.82e-03

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 38.66  E-value: 3.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053955  73 PVLLLLHGGGHSALSWAVFTSVicSRITCR----VVAMDlRGHG----DSKVKNPDDLSAETM-AKDIGKVVEALYG--E 141
Cdd:COG0627  34 PVLYLLHGLTGTHENWTRKTGA--QRLAAElgviVVMPD-GGQAsfyvDWTQGPAGHYRWETYlTEELPPLIEANFPvsA 110

                        90       100
                ....*....|....*....|....
gi 41053955 142 NPPPIMIIGHSMGGAIAVHTAAAN 165
Cdd:COG0627 111 DRERRAIAGLSMGGHGALTLALRH 134
SH3_SH3RF_3 cd11783
Third Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), SH3RF3, and ...
 265-303 6.28e-03

Third Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), SH3RF3, and similar domains; SH3RF1 (or POSH) and SH3RF3 (or POSH2) are scaffold proteins that function as E3 ubiquitin-protein ligases. They contain an N-terminal RING finger domain and four SH3 domains. This model represents the third SH3 domain, located in the middle of SH3RF1 and SH3RF3, and similar domains. SH3RF1 plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF3 interacts with p21-activated kinase 2 (PAK2) and GTP-loaded Rac1. It may play a role in regulating JNK mediated apoptosis in certain conditions. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212717 [Multi-domain]  Cd Length: 55  Bit Score: 34.68  E-value: 6.28e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 41053955 265 NHKRKKEDDQEIKKESLYTwrielsKTEKYWEGWFKGLS 303
Cdd:cd11783   7 PYKPQKPDELELRKGEMYT------VTEKCQDGWFKGTS 39
 
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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