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Conserved domains on  [gi|1092638394|ref|WP_070583819|]
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alpha/beta fold hydrolase [Neisseria sp. HMSC072C05]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 4-98 1.07e-22

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


:

Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 87.96  E-value: 1.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394   4 IILLHGLHMHSWVMRPLAYLLEQEGFEVALFDYYSVLHSMNRHVEDLARWIDE---NHADETLHFVGHSLGGLVLRNFAA 80
Cdd:COG1075     8 VVLVHGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGSIEDSAEQLAAFVDAvlaATGAEKVDLVGHSMGGLVARYYLK 87

                          90       100
                  ....*....|....*....|
gi 1092638394  81 TY--PNKVsGRIVTMGTPHQ 98
Cdd:COG1075    88 RLggAAKV-ARVVTLGTPHH 106
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 4-199 7.83e-14

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: 67.72  E-value: 7.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394   4 IILLHGLHMHSWVMRPLAYLLeQEGFEVALFDYY--------SVLHSMNRHVEDLARWIDEnHADETLHFVGHSLGGLVL 75
Cdd:COG0596    26 VVLLHGLPGSSYEWRPLIPAL-AAGYRVIAPDLRghgrsdkpAGGYTLDDLADDLAALLDA-LGLERVVLVGHSMGGMVA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394  76 RNFAATYPNKVSgRIVTMGTPHQgsRAAQRVFNMGLQKPVLGGSYKGALDGGIPELPKGVELgsiagnkpyglgRVLGLH 155
Cdd:COG0596   104 LELAARHPERVA-GLVLVDEVLA--ALAEPLRRPGLAPEALAALLRALARTDLRERLARITV------------PTLVIW 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1092638394 156 GEHDGTVLVSET-----HCPNMRDHVVLPVSHSGMLFN-RKTAGQVVAFL 199
Cdd:COG0596   169 GEKDPIVPPALArrlaeLLPNAELVVLPGAGHFPPLEQpEAFAAALRDFL 218
 
Name Accession Description Interval E-value
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 4-98 1.07e-22

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 87.96  E-value: 1.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394   4 IILLHGLHMHSWVMRPLAYLLEQEGFEVALFDYYSVLHSMNRHVEDLARWIDE---NHADETLHFVGHSLGGLVLRNFAA 80
Cdd:COG1075     8 VVLVHGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGSIEDSAEQLAAFVDAvlaATGAEKVDLVGHSMGGLVARYYLK 87

                          90       100
                  ....*....|....*....|
gi 1092638394  81 TY--PNKVsGRIVTMGTPHQ 98
Cdd:COG1075    88 RLggAAKV-ARVVTLGTPHH 106
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 4-199 7.83e-14

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: 67.72  E-value: 7.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394   4 IILLHGLHMHSWVMRPLAYLLeQEGFEVALFDYY--------SVLHSMNRHVEDLARWIDEnHADETLHFVGHSLGGLVL 75
Cdd:COG0596    26 VVLLHGLPGSSYEWRPLIPAL-AAGYRVIAPDLRghgrsdkpAGGYTLDDLADDLAALLDA-LGLERVVLVGHSMGGMVA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394  76 RNFAATYPNKVSgRIVTMGTPHQgsRAAQRVFNMGLQKPVLGGSYKGALDGGIPELPKGVELgsiagnkpyglgRVLGLH 155
Cdd:COG0596   104 LELAARHPERVA-GLVLVDEVLA--ALAEPLRRPGLAPEALAALLRALARTDLRERLARITV------------PTLVIW 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1092638394 156 GEHDGTVLVSET-----HCPNMRDHVVLPVSHSGMLFN-RKTAGQVVAFL 199
Cdd:COG0596   169 GEKDPIVPPALArrlaeLLPNAELVVLPGAGHFPPLEQpEAFAAALRDFL 218
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 4-97 1.14e-12

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: 64.83  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394   4 IILLHGLHMHSWVMRPLAYLLEQEGFEVALFDYYSVLHSMNR------HVEDLARWIDENHA---DETLHFVGHSLGGLV 74
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPkaqddyRTDDLAEDLEYILEalgLEKVNLVGHSMGGLI 82

                          90       100
                  ....*....|....*....|...
gi 1092638394  75 LRNFAATYPNKVSgRIVTMGTPH 97
Cdd:pfam00561  83 ALAYAAKYPDRVK-ALVLLGALD 104
PLN02211 PLN02211
methyl indole-3-acetate methyltransferase
 5-86 1.34e-03

methyl indole-3-acetate methyltransferase


Pssm-ID: 215128  Cd Length: 273  Bit Score: 38.72  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394   5 ILLHGLHMHSWVMRPLAYLLEQEGFEVALFDYYSV---------LHSMNRHVEDLARWIDENHADETLHFVGHSLGGLVL 75
Cdd:PLN02211   22 VLIHGISGGSWCWYKIRCLMENSGYKVTCIDLKSAgidqsdadsVTTFDEYNKPLIDFLSSLPENEKVILVGHSAGGLSV 101

                          90
                  ....*....|.
gi 1092638394  76 RNFAATYPNKV 86
Cdd:PLN02211  102 TQAIHRFPKKI 112
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 36-96 6.79e-03

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: 35.94  E-value: 6.79e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092638394  36 YYSVLHSMNRHVEDLARWIDENHADETLHFVGHSLGG----LVLRNFAATYPNKVsGRIVTMGTP 96
Cdd:cd00741     3 FYKAARSLANLVLPLLKSALAQYPDYKIHVTGHSLGGalagLAGLDLRGRGLGRL-VRVYTFGPP 66
 
Name Accession Description Interval E-value
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 4-98 1.07e-22

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 87.96  E-value: 1.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394   4 IILLHGLHMHSWVMRPLAYLLEQEGFEVALFDYYSVLHSMNRHVEDLARWIDE---NHADETLHFVGHSLGGLVLRNFAA 80
Cdd:COG1075     8 VVLVHGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGSIEDSAEQLAAFVDAvlaATGAEKVDLVGHSMGGLVARYYLK 87

                          90       100
                  ....*....|....*....|
gi 1092638394  81 TY--PNKVsGRIVTMGTPHQ 98
Cdd:COG1075    88 RLggAAKV-ARVVTLGTPHH 106
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
4-168 8.33e-16

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 73.11  E-value: 8.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394   4 IILLHGLHMHSWVMRPLAYLLEQEGFEVALFDY---------YSVLHSMNRHVEDLARWIDE--NHADETLHFVGHSLGG 72
Cdd:COG2267    31 VVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLrghgrsdgpRGHVDSFDDYVDDLRAALDAlrARPGLPVVLLGHSMGG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394  73 LVLRNFAATYPNKVSGrIVTMGTPHqgsraaqrvfnmgLQKPVLGGSYKGALDGGIPELPKGVELgsiagnkpyglgRVL 152
Cdd:COG2267   111 LIALLYAARYPDRVAG-LVLLAPAY-------------RADPLLGPSARWLRALRLAEALARIDV------------PVL 164

                         170
                  ....*....|....*.
gi 1092638394 153 GLHGEHDGTVLVSETH 168
Cdd:COG2267   165 VLHGGADRVVPPEAAR 180
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 4-199 7.83e-14

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: 67.72  E-value: 7.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394   4 IILLHGLHMHSWVMRPLAYLLeQEGFEVALFDYY--------SVLHSMNRHVEDLARWIDEnHADETLHFVGHSLGGLVL 75
Cdd:COG0596    26 VVLLHGLPGSSYEWRPLIPAL-AAGYRVIAPDLRghgrsdkpAGGYTLDDLADDLAALLDA-LGLERVVLVGHSMGGMVA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394  76 RNFAATYPNKVSgRIVTMGTPHQgsRAAQRVFNMGLQKPVLGGSYKGALDGGIPELPKGVELgsiagnkpyglgRVLGLH 155
Cdd:COG0596   104 LELAARHPERVA-GLVLVDEVLA--ALAEPLRRPGLAPEALAALLRALARTDLRERLARITV------------PTLVIW 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1092638394 156 GEHDGTVLVSET-----HCPNMRDHVVLPVSHSGMLFN-RKTAGQVVAFL 199
Cdd:COG0596   169 GEKDPIVPPALArrlaeLLPNAELVVLPGAGHFPPLEQpEAFAAALRDFL 218
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 4-97 1.14e-12

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: 64.83  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394   4 IILLHGLHMHSWVMRPLAYLLEQEGFEVALFDYYSVLHSMNR------HVEDLARWIDENHA---DETLHFVGHSLGGLV 74
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPkaqddyRTDDLAEDLEYILEalgLEKVNLVGHSMGGLI 82

                          90       100
                  ....*....|....*....|...
gi 1092638394  75 LRNFAATYPNKVSgRIVTMGTPH 97
Cdd:pfam00561  83 ALAYAAKYPDRVK-ALVLLGALD 104
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 2-88 1.81e-11

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: 61.46  E-value: 1.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394   2 AKIILLHGLHMHSWVMRPLAYLLEQEGFEVALFDYY---------SVLHSMNRHVEDLARWID---ENHADETLHFVGHS 69
Cdd:pfam12146   5 AVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRghgrsdgkrGHVPSFDDYVDDLDTFVDkirEEHPGLPLFLLGHS 84

                          90
                  ....*....|....*....
gi 1092638394  70 LGGLVLRNFAATYPNKVSG 88
Cdd:pfam12146  85 MGGLIAALYALRYPDKVDG 103
Palm_thioest pfam02089
Palmitoyl protein thioesterase;
4-99 1.14e-07

Palmitoyl protein thioesterase;


Pssm-ID: 460441 [Multi-domain]  Cd Length: 248  Bit Score: 50.70  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394   4 IILLHGL--HMHSWVMRPLAYLLEQE--GFEV---ALFDYY------SVLHSMNRHVEDLARWIDENHADETLHFVGHSL 70
Cdd:pfam02089   2 VVIWHGLgdSCASPGMQSLAELIKEAhpGTYVhsiDIGDGPsedrkaSFFGNMNEQVEAVCEQLKPELPANGFNAIGFSQ 81

                          90       100
                  ....*....|....*....|....*....
gi 1092638394  71 GGLVLRNFAATYPNKVSGRIVTMGTPHQG 99
Cdd:pfam02089  82 GGLFLRGLVERCPDPPVHNLISLGGPHMG 110
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
4-76 4.51e-06

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


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 46.29  E-value: 4.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394   4 IILLHGL--HMHSWVMRPLAYLLEQEGFEVALFDYYSvlHS--MNR-----H---VEDL---ARWIDENHADETLHFVGH 68
Cdd:COG0429    64 VVLLHGLegSSDSHYARGLARALYARGWDVVRLNFRG--CGgePNLlprlyHsgdTEDLvwvLAHLRARYPYAPLYAVGF 141


                  ....*....
gi 1092638394  69 SLGG-LVLR 76
Cdd:COG0429   142 SLGGnLLLK 150
DUF676 pfam05057
Putative serine esterase (DUF676); This family of proteins are probably serine esterase type ...
 4-112 3.85e-04

Putative serine esterase (DUF676); This family of proteins are probably serine esterase type enzymes with an alpha/beta hydrolase fold.


Pssm-ID: 309968  Cd Length: 212  Bit Score: 40.17  E-value: 3.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394   4 IILLHGLHMHSWVMRPLAYLLEQE---------GFEVALFDYYSVLHSM-NRHVEDLARWIDENHADETLHFVGHSLGGL 73
Cdd:pfam05057   8 VVLVHGLWGNSADMEYVAEQLEKKlpdelivflMSSNNVSKTFKGIDVMgERLANEVLEFVQDGSDGKKISFVGHSLGGL 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1092638394  74 VLRnFAATY----PNKVSGRI--------VTMGTPHQGSRAAQRVFNMGLQ 112
Cdd:pfam05057  88 IAR-YAIGKlydkAMTFKGFFkglepmnfITLASPHLGVLGNSPLINWGLW 137
COG4814 COG4814
Uncharacterized conserved protein with an alpha/beta hydrolase fold [Function unknown];
65-147 4.05e-04

Uncharacterized conserved protein with an alpha/beta hydrolase fold [Function unknown];


Pssm-ID: 443842  Cd Length: 286  Bit Score: 40.31  E-value: 4.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394  65 FVGHSLGGLVLRNFAATYPNKVS----GRIVTMGTPhqgsraaqrvFNmGLQKPVLGGSYKGALDGGIPE---------- 130
Cdd:COG4814   138 AVGHSMGGLALTYYLEKYGNDKSlpklNKLVTIGGP----------FN-GIENEDNNNLTDLLADGKPKPktqaykdlik 206

                          90       100
                  ....*....|....*....|.
gi 1092638394 131 ----LPKGVELGSIAGNKPYG 147
Cdd:COG4814   207 nrdkFPKNLQVLNIAGDLNDG 227
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
4-96 7.19e-04

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 39.54  E-value: 7.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394   4 IILLHGLHMHSWVMRPLAYLLEQEGFEVALFDYYSvlHSmnRHVEDLAR-----WIDEnhADETLHF----------VGH 68
Cdd:COG1647    18 VLLLHGFTGSPAEMRPLAEALAKAGYTVYAPRLPG--HG--TSPEDLLKttwedWLED--VEEAYEIlkagydkvivIGL 91

                          90       100
                  ....*....|....*....|....*...
gi 1092638394  69 SLGGLVLRNFAATYPNkVSGrIVTMGTP 96
Cdd:COG1647    92 SMGGLLALLLAARYPD-VAG-LVLLSPA 117
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 4-83 1.19e-03

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 38.61  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394   4 IILLHGLHMHSWVMRPLAYlleqEGFEVALFDYYSVLHSMNRH-----VEDLARWIDENHADETLHFVGHSLGGLVLRNF 78
Cdd:pfam12697   1 VVLVHGAGLSAAPLAALLA----AGVAVLAPDLPGHGSSSPPPldladLADLAALLDELGAARPVVLVGHSLGGAVALAA 76


                  ....*
gi 1092638394  79 AATYP 83
Cdd:pfam12697  77 AAAAL 81
PLN02211 PLN02211
methyl indole-3-acetate methyltransferase
 5-86 1.34e-03

methyl indole-3-acetate methyltransferase


Pssm-ID: 215128  Cd Length: 273  Bit Score: 38.72  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394   5 ILLHGLHMHSWVMRPLAYLLEQEGFEVALFDYYSV---------LHSMNRHVEDLARWIDENHADETLHFVGHSLGGLVL 75
Cdd:PLN02211   22 VLIHGISGGSWCWYKIRCLMENSGYKVTCIDLKSAgidqsdadsVTTFDEYNKPLIDFLSSLPENEKVILVGHSAGGLSV 101

                          90
                  ....*....|.
gi 1092638394  76 RNFAATYPNKV 86
Cdd:PLN02211  102 TQAIHRFPKKI 112
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
18-95 1.86e-03

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


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 38.33  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394  18 RPLA-YLLEQeGFEVALFDY---------------YSVLHSMNRHVEDLARWIDENHADETLHFVGHSLGGLVLRnfAAT 81
Cdd:COG4757    49 RPFArYLAER-GFAVLTYDYrgiglsrpgslrgfdAGYRDWGELDLPAVLDALRARFPGLPLLLVGHSLGGQLLG--LAP 125

                          90
                  ....*....|....
gi 1092638394  82 YPNKVSgRIVTMGT 95
Cdd:COG4757   126 NAERVD-RLVTVAS 138
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
4-168 6.40e-03

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 36.53  E-value: 6.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394   4 IILLHGL-HMHSWVMRPLAYLLEQEGFEVALFDY----YSVLHSMNRHVEDLARWID----ENHADET-LHFVGHSLGGL 73
Cdd:COG1506    26 VVYVHGGpGSRDDSFLPLAQALASRGYAVLAPDYrgygESAGDWGGDEVDDVLAAIDylaaRPYVDPDrIGIYGHSYGGY 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394  74 VLRNFAATYPNKVSGrIVTMGTphqgsraaqrVFNMGLQKPVLGGsYKGALDGGIPELPKGVELGSIAG-----NKPygl 148
Cdd:COG1506   106 MALLAAARHPDRFKA-AVALAG----------VSDLRSYYGTTRE-YTERLMGGPWEDPEAYAARSPLAyadklKTP--- 170

                         170       180
                  ....*....|....*....|
gi 1092638394 149 grVLGLHGEHDGTVLVSETH 168
Cdd:COG1506   171 --LLLIHGEADDRVPPEQAE 188
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
48-108 6.68e-03

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 36.66  E-value: 6.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092638394  48 EDLARWIDENHADETLHFVGHSLGG----LVLRNFAATYPNKVSgRIVTMGTPHQGSRAAQRVFN 108
Cdd:COG3675    75 ELLEDALRPLSPGKRLYVTGHSLGGalatLAAADLERNYIFPVR-GLYTFGQPRVGDRSFAKYYN 138
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 36-96 6.79e-03

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: 35.94  E-value: 6.79e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092638394  36 YYSVLHSMNRHVEDLARWIDENHADETLHFVGHSLGG----LVLRNFAATYPNKVsGRIVTMGTP 96
Cdd:cd00741     3 FYKAARSLANLVLPLLKSALAQYPDYKIHVTGHSLGGalagLAGLDLRGRGLGRL-VRVYTFGPP 66
PGAP1 pfam07819
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ...
 34-142 9.66e-03

PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an endoplasmic reticulum membrane protein with a catalytic serine containing motif that is conserved in a number of lipases. PGAP1 functions as a GPI inositol-deacylase; this deacylation is important for the efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi body. This entry also includes Tgl2, a mitochondria protein that serves as a triacylglycerol lipase in budding yeasts.


Pssm-ID: 369540  Cd Length: 233  Bit Score: 35.80  E-value: 9.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092638394  34 FDYYSV----------LHSMNRH---VEDLARWI-----DENHADETLHFVGHSLGGLVLRnFAATYPNKVSGR---IVT 92
Cdd:pfam07819  46 LDFFSVdfneelsafhGRTLLDQaeyLNDAIRYIlslyaSGRPGPTSVILIGHSMGGIVAR-AALTLPNYIPQSvntIIT 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1092638394  93 MGTPHQGSRAAQRVFNMGLQKPVLGGSYKGALDGGIPELpKGVELGSIAG 142
Cdd:pfam07819 125 LSSPHAKPPLTFDGDILKFYERLNAFWRKLYNDGDSNNL-SNVLLVSITG 173
 
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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