NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1887096808|ref|NP_001287987|]
View 

sn-1-specific diacylglycerol lipase ABHD11 isoform 9 [Homo sapiens]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 11426811)

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

PubMed:  1409539|12369917

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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, ...
 58-145 1.27e-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: 88.90  E-value: 1.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096808  58 PAVVFLHGLFGSKTNFNSIAKILAQqtGRRVLTVDARNHGDSPHSP-DMSYEIMSQDLQDLLPQLGLVPCVVVGHSMGGK 136
Cdd:COG0596    24 PPVVLLHGLPGSSYEWRPLIPALAA--GYRVIAPDLRGHGRSDKPAgGYTLDDLADDLAALLDALGLERVVLVGHSMGGM 101


                  ....*....
gi 1887096808 137 TAMLLALQR 145
Cdd:COG0596   102 VALELAARH 110
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 58-145 1.27e-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: 88.90  E-value: 1.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096808  58 PAVVFLHGLFGSKTNFNSIAKILAQqtGRRVLTVDARNHGDSPHSP-DMSYEIMSQDLQDLLPQLGLVPCVVVGHSMGGK 136
Cdd:COG0596    24 PPVVLLHGLPGSSYEWRPLIPALAA--GYRVIAPDLRGHGRSDKPAgGYTLDDLADDLAALLDALGLERVVLVGHSMGGM 101


                  ....*....
gi 1887096808 137 TAMLLALQR 145
Cdd:COG0596   102 VALELAARH 110
PRK10673 PRK10673
esterase;
44-141 2.52e-22

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 89.02  E-value: 2.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096808  44 LPLSYRLLDGE---AALPaVVFLHGLFGSKTNFNSIAKILaqQTGRRVLTVDARNHGDSPHSPDMSYEIMSQDLQDLLPQ 120
Cdd:PRK10673    1 MKLNIRAQTAQnphNNSP-IVLVHGLFGSLDNLGVLARDL--VNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDA 77

                          90       100
                  ....*....|....*....|.
gi 1887096808 121 LGLVPCVVVGHSMGGKTAMLL 141
Cdd:PRK10673   78 LQIEKATFIGHSMGGKAVMAL 98
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 58-148 1.81e-15

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: 70.61  E-value: 1.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096808  58 PAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSPHSP---DMSYEIMSQDLQDLLPQLGLVPCVVVGHSMG 134
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARD-GFRVIALDLRGFGKSSRPKaqdDYRTDDLAEDLEYILEALGLEKVNLVGHSMG 79

                          90
                  ....*....|....
gi 1887096808 135 GKTAMLLALQRSQP 148
Cdd:pfam00561  80 GLIALAYAAKYPDR 93
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 107-143 7.94e-03

Lipase (class 3). 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: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 35.14  E-value: 7.94e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1887096808 107 YEIMSQDLQDLLPQLGLVPCVVVGHSMGGKTAMLLAL 143
Cdd:cd00519   111 YNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLAL 147
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 58-145 1.27e-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: 88.90  E-value: 1.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096808  58 PAVVFLHGLFGSKTNFNSIAKILAQqtGRRVLTVDARNHGDSPHSP-DMSYEIMSQDLQDLLPQLGLVPCVVVGHSMGGK 136
Cdd:COG0596    24 PPVVLLHGLPGSSYEWRPLIPALAA--GYRVIAPDLRGHGRSDKPAgGYTLDDLADDLAALLDALGLERVVLVGHSMGGM 101


                  ....*....
gi 1887096808 137 TAMLLALQR 145
Cdd:COG0596   102 VALELAARH 110
PRK10673 PRK10673
esterase;
44-141 2.52e-22

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 89.02  E-value: 2.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096808  44 LPLSYRLLDGE---AALPaVVFLHGLFGSKTNFNSIAKILaqQTGRRVLTVDARNHGDSPHSPDMSYEIMSQDLQDLLPQ 120
Cdd:PRK10673    1 MKLNIRAQTAQnphNNSP-IVLVHGLFGSLDNLGVLARDL--VNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDA 77

                          90       100
                  ....*....|....*....|.
gi 1887096808 121 LGLVPCVVVGHSMGGKTAMLL 141
Cdd:PRK10673   78 LQIEKATFIGHSMGGKAVMAL 98
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 58-148 1.81e-15

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: 70.61  E-value: 1.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096808  58 PAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSPHSP---DMSYEIMSQDLQDLLPQLGLVPCVVVGHSMG 134
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARD-GFRVIALDLRGFGKSSRPKaqdDYRTDDLAEDLEYILEALGLEKVNLVGHSMG 79

                          90
                  ....*....|....
gi 1887096808 135 GKTAMLLALQRSQP 148
Cdd:pfam00561  80 GLIALAYAAKYPDR 93
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
48-149 2.60e-13

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 64.25  E-value: 2.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096808  48 YRLLDGEAALPAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSPHSPDM--SYEIMSQDLQ---DLLPQLG 122
Cdd:COG2267    19 RRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAA-GYAVLAFDLRGHGRSDGPRGHvdSFDDYVDDLRaalDALRARP 97

                          90       100
                  ....*....|....*....|....*..
gi 1887096808 123 LVPCVVVGHSMGGKTAMLLALQRSQPP 149
Cdd:COG2267    98 GLPVVLLGHSMGGLIALLYAARYPDRV 124
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 58-144 7.11e-12

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


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 60.62  E-value: 7.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096808  58 PAVVFLHGLFGSKTNFNSIAKILAQqtgRRVLTVDARNHGDSPHSPDMSYEIMSQDLQDLLPQLGLVPCVVVGHSMGGKT 137
Cdd:PRK11126    3 PWLVFLHGLLGSGQDWQPVGEALPD---YPRLYIDLPGHGGSAAISVDGFADVSRLLSQTLQSYNILPYWLVGYSLGGRI 79


                  ....*..
gi 1887096808 138 AMLLALQ 144
Cdd:PRK11126   80 AMYYACQ 86
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 53-147 1.60e-10

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 57.65  E-value: 1.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096808  53 GEAALPAVVFLHGLFGSKTN--FNsiakILAQQTGRRVLTVDARNHGDS-PHSPDMSYEIMSQDLQDLLPQLGLVPCVVV 129
Cdd:PRK14875  127 GEGDGTPVVLIHGFGGDLNNwlFN----HAALAAGRPVIALDLPGHGASsKAVGAGSLDELAAAVLAFLDALGIERAHLV 202

                          90
                  ....*....|....*...
gi 1887096808 130 GHSMGGKTAMLLALQRSQ 147
Cdd:PRK14875  203 GHSMGGAVALRLAARAPQ 220
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 52-148 3.85e-10

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 56.08  E-value: 3.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096808  52 DGEAALPAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSPHSP--DMSYEImsQDLQDLLPQLGLVPCV-- 127
Cdd:COG1073    32 GASKKYPAVVVAHGNGGVKEQRALYAQRLAEL-GFNVLAFDYRGYGESEGEPreEGSPER--RDARAAVDYLRTLPGVdp 108

                          90       100
                  ....*....|....*....|....*
gi 1887096808 128 ----VVGHSMGGKTAMLLALQRSQP 148
Cdd:COG1073   109 erigLLGISLGGGYALNAAATDPRV 133
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 59-148 4.06e-10

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: 56.07  E-value: 4.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096808  59 AVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSP----HSPdmSYEIMSQDLQDLLPQL----GLVPCVVVG 130
Cdd:pfam12146   6 VVVLVHGLGEHSGRYAHLADALAAQ-GFAVYAYDHRGHGRSDgkrgHVP--SFDDYVDDLDTFVDKIreehPGLPLFLLG 82

                          90
                  ....*....|....*...
gi 1887096808 131 HSMGGKTAMLLALQRSQP 148
Cdd:pfam12146  83 HSMGGLIAALYALRYPDK 100
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
52-146 3.72e-09

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 53.10  E-value: 3.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096808  52 DGEAALPAVVFLHGLFGSKTN-FNSIAKILAQQtGRRVLTVDARNHGDSPHSPdmsYEIMSQDLQ---DLLPQLGLVP-- 125
Cdd:COG1506    18 ADGKKYPVVVYVHGGPGSRDDsFLPLAQALASR-GYAVLAPDYRGYGESAGDW---GGDEVDDVLaaiDYLAARPYVDpd 93

                          90       100
                  ....*....|....*....|..
gi 1887096808 126 -CVVVGHSMGGKTAMLLALQRS 146
Cdd:COG1506    94 rIGIYGHSYGGYMALLAAARHP 115
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 60-135 1.56e-08

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 49.44  E-value: 1.56e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1887096808  60 VVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVdarNHGDSPHSPDMSYEIMSQDLQDLLPQLGLVPCVVVGHSMGG 135
Cdd:COG1075     8 VVLVHGLGGSAASWAPLAPRLRAA-GYPVYAL---NYPSTNGSIEDSAEQLAAFVDAVLAATGAEKVDLVGHSMGG 79
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
52-147 1.59e-08

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 51.51  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096808  52 DGEAALPAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSPHSPDMSYEIMSQ--------DLQ---DLLPQ 120
Cdd:COG0412    24 AGGGPRPGVVVLHEIFGLNPHIRDVARRLAAA-GYVVLAPDLYGRGGPGDDPDEARALMGAldpellaaDLRaalDWLKA 102

                          90       100       110
                  ....*....|....*....|....*....|
gi 1887096808 121 LGLV---PCVVVGHSMGGKTAMLLALQRSQ 147
Cdd:COG0412   103 QPEVdagRVGVVGFCFGGGLALLAAARGPD 132
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
58-148 5.62e-08

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 49.94  E-value: 5.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096808  58 PAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSPHS-PDMSYEIMSQDLQDLLPQL--GLVPCVVVGHSMG 134
Cdd:COG1647    16 KGVLLLHGFTGSPAEMRPLAEALAKA-GYTVYAPRLPGHGTSPEDlLKTTWEDWLEDVEEAYEILkaGYDKVIVIGLSMG 94

                          90
                  ....*....|....
gi 1887096808 135 GKTAMLLALQRSQP 148
Cdd:COG1647    95 GLLALLLAARYPDV 108
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
48-150 3.62e-07

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 47.56  E-value: 3.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096808  48 YRLLDGEAALPAVVFLHG---LFGSKTNFNSIAKILAQQTGRRVLTVDARnhgdspHSPDMSYEIMSQDLQDLL------ 118
Cdd:COG0657     4 YRPAGAKGPLPVVVYFHGggwVSGSKDTHDPLARRLAARAGAAVVSVDYR------LAPEHPFPAALEDAYAALrwlran 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1887096808 119 -PQLGLVP--CVVVGHSMGGKTAMLLAL---QRSQPPP 150
Cdd:COG0657    78 aAELGIDPdrIAVAGDSAGGHLAAALALrarDRGGPRP 115
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 60-142 3.65e-07

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 47.47  E-value: 3.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096808  60 VVFLHGLFGSKTNFNSiakilAQQTGRRVLTVDARNHGDSPHSPDMSYEImsQDLQDLLPQLGLV-PCVVVGHSMGGKTA 138
Cdd:pfam12697   1 VVLVHGAGLSAAPLAA-----LLAAGVAVLAPDLPGHGSSSPPPLDLADL--ADLAALLDELGAArPVVLVGHSLGGAVA 73


                  ....
gi 1887096808 139 MLLA 142
Cdd:pfam12697  74 LAAA 77
PGAP1 pfam07819
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ...
 60-141 9.60e-07

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: 46.59  E-value: 9.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096808  60 VVFLHGLFGSKTNFNSIAKILAQQtgRRVLTVDARNHGDSP---HSPDMSYEIMSQDLQDLLPQLGLV------------ 124
Cdd:pfam07819   7 VLFIPGNAGSYKQVRSIASVAANL--YQVLRKLLQNDNGFHldfFSVDFNEELSAFHGRTLLDQAEYLndairyilslya 84

                          90       100
                  ....*....|....*....|....
gi 1887096808 125 -------PCVVVGHSMGGKTAMLL 141
Cdd:pfam07819  85 sgrpgptSVILIGHSMGGIVARAA 108
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
41-149 3.29e-06

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 45.10  E-value: 3.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096808  41 PRPLPLSYRL-------LDGEAALPAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVD-----------ARNHGDSPHS 102
Cdd:COG4188    39 DRPLPVDVWYpatapadAPAGGPFPLVVLSHGLGGSREGYAYLAEHLASH-GYVVAAPDhpgsnaadlsaALDGLADALD 117

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096808 103 P--------DMSY-----EIMSQDLQDLLPQLGLVPCVVVGHSMGGKTAMLLALQRSQPP 149
Cdd:COG4188   118 PeelwerplDLSFvldqlLALNKSDPPLAGRLDLDRIGVIGHSLGGYTALALAGARLDFA 177
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 60-146 5.98e-06

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 44.85  E-value: 5.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096808   60 VVFLHGLFGSKTNFNSIAKILAQQTgrRVLTVDARNHGDSP---------HSPDMSYEIMSQDLQDLLPQLGLVPCVVVG 130
Cdd:PLN02980  1374 VLFLHGFLGTGEDWIPIMKAISGSA--RCISIDLPGHGGSKiqnhaketqTEPTLSVELVADLLYKLIEHITPGKVTLVG 1451

                           90
                   ....*....|....*.
gi 1887096808  131 HSMGGKTAMLLALQRS 146
Cdd:PLN02980  1452 YSMGARIALYMALRFS 1467
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
45-146 2.52e-05

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


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 42.56  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096808  45 PLSYRLLDGEAALPAVVFLHGLFGSKTNF-NSIAKILAQQtGRRVLTVDARNHGDS-PHSP---DMSY-EIMSQD----- 113
Cdd:COG4757    19 PLAARLFPPAGPPRAVVLINPATGVPQRFyRPFARYLAER-GFAVLTYDYRGIGLSrPGSLrgfDAGYrDWGELDlpavl 97

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1887096808 114 --LQDLLPQLglvPCVVVGHSMGGktaMLLALQRS 146
Cdd:COG4757    98 daLRARFPGL---PLLLVGHSLGG---QLLGLAPN 126
PRK10566 PRK10566
esterase; Provisional
 56-139 3.69e-05

esterase; Provisional


Pssm-ID: 182555 [Multi-domain]  Cd Length: 249  Bit Score: 41.90  E-value: 3.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096808  56 ALPAVVFLHGLFGSKTNFNSIAKILAqQTGRRVLTVDARNH-----GDSPHSPDMSYEIMSQDLQDL------LPQLGLV 124
Cdd:PRK10566   26 PLPTVFFYHGFTSSKLVYSYFAVALA-QAGFRVIMPDAPMHgarfsGDEARRLNHFWQILLQNMQEFptlraaIREEGWL 104

                          90
                  ....*....|....*...
gi 1887096808 125 P---CVVVGHSMGGKTAM 139
Cdd:PRK10566  105 LddrLAVGGASMGGMTAL 122
Lipase_3 pfam01764
Lipase (class 3);
107-143 2.87e-03

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 35.70  E-value: 2.87e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1887096808 107 YEIMSQDLQDLLPQLGLVPCVVVGHSMGGKTAMLLAL 143
Cdd:pfam01764  46 REQVLAELKRLLEKYPDYSIVVTGHSLGGALASLAAL 82
Chlorophyllase pfam07224
Chlorophyllase; This family consists of several plant specific Chlorophyllase proteins (EC:3.1. ...
 39-143 7.14e-03

Chlorophyllase; This family consists of several plant specific Chlorophyllase proteins (EC:3.1.1.14). Chlorophyllase (Chlase) is the first enzyme involved in chlorophyll (Chl) degradation and catalyzes the hydrolysis of ester bond to yield chlorophyllide and phytol.


Pssm-ID: 254111  Cd Length: 307  Bit Score: 35.59  E-value: 7.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096808  39 AEPRPLPLSYRLLDGEaaLPAVVFLHGLFGSKTN----FNSIAK----ILAQQTGRRVLTVDARNHGDSPHSpdmSYEIM 110
Cdd:pfam07224  30 PPPKPLIIITPKEAGT--YPVVLFLHGTMLSNEFyslfFNHIAShgfiVVAPQLYRLFPPPSQQDEIDSAAE---VANWL 104

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1887096808 111 SQDLQDLLP---QLGLVPCVVVGHSMGGKTAMLLAL 143
Cdd:pfam07224 105 PLGLQVVLPtgvEANLSKLALSGHSRGGKTAFALAL 140
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 107-143 7.94e-03

Lipase (class 3). 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: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 35.14  E-value: 7.94e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1887096808 107 YEIMSQDLQDLLPQLGLVPCVVVGHSMGGKTAMLLAL 143
Cdd:cd00519   111 YNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLAL 147
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH