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Conserved domains on  [gi|515743433|ref|WP_017176033|]
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MULTISPECIES: alpha/beta fold hydrolase [Staphylococcus]

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

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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, ...
 4-260 5.29e-34

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: 122.42  E-value: 5.29e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433   4 FTRKGGFTLNYNTMG-QGYPVVLVHTAFENASIFQNLAHALSKTFQVVLLDLRGHGYSDKP-RHIKFNEFADDIILLLDY 81
Cdd:COG0596    6 FVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPaGGYTLDDLADDLAALLDA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433  82 LYIDQAAFIGHEMGATIIAHLSKQYPEYVSSLTMINPtsiegelpeerLFRKYAHKIRNWNEDkqekfldkhryykhrkv 161
Cdd:COG0596   86 LGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDE-----------VLAALAEPLRRPGLA----------------- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433 162 nkflknvedtnsistKEETEAVDEVFKQRGIAEVFEYITKPTFIVASAYGERITSLESKEVADLIGNVHFEVYSKSSMYP 241
Cdd:COG0596  138 ---------------PEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFP 202

                        250
                 ....*....|....*....
gi 515743433 242 FEEEQEKFIHDVTPFIKKH 260
Cdd:COG0596  203 PLEQPEAFAAALRDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 4-260 5.29e-34

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: 122.42  E-value: 5.29e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433   4 FTRKGGFTLNYNTMG-QGYPVVLVHTAFENASIFQNLAHALSKTFQVVLLDLRGHGYSDKP-RHIKFNEFADDIILLLDY 81
Cdd:COG0596    6 FVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPaGGYTLDDLADDLAALLDA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433  82 LYIDQAAFIGHEMGATIIAHLSKQYPEYVSSLTMINPtsiegelpeerLFRKYAHKIRNWNEDkqekfldkhryykhrkv 161
Cdd:COG0596   86 LGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDE-----------VLAALAEPLRRPGLA----------------- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433 162 nkflknvedtnsistKEETEAVDEVFKQRGIAEVFEYITKPTFIVASAYGERITSLESKEVADLIGNVHFEVYSKSSMYP 241
Cdd:COG0596  138 ---------------PEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFP 202

                        250
                 ....*....|....*....
gi 515743433 242 FEEEQEKFIHDVTPFIKKH 260
Cdd:COG0596  203 PLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 21-245 1.28e-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: 1.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433   21 YPVVLVHTAFENASIFQNLAHALSKT-FQVVLLDLRGHGYSDKPRHIK---FNEFADDIILLLDYLYIDQAAFIGHEMGA 96
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPKAQDdyrTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433   97 TIIAHLSKQYPEYVSSLTMINPTSIEGELPEERLFRK----------YAHKIRNWNEDKQEKFLDKHRYY-----KHRKV 161
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILalfpgffdgfVADFAPNPLGRLVAKLLALLLLRlrllkALPLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433  162 NKFLKNVEDTNSISTKeeTEAVD--EVFKQRGIAEVFEYITKPTFIVASAYgERITSLESKEV-ADLIGNVHFEVYSKSS 238
Cdd:pfam00561 161 NKRFPSGDYALAKSLV--TGALLfiETWSTELRAKFLGRLDEPTLIIWGDQ-DPLVPPQALEKlAQLFPNARLVVIPDAG 237


                  ....*..
gi 515743433  239 MYPFEEE 245
Cdd:pfam00561 238 HFAFLEG 244
PRK10673 PRK10673
esterase;
22-117 4.43e-14

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 69.76  E-value: 4.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433  22 PVVLVHTAFENASIFQNLAHALSKTFQVVLLDLRGHGYSDKPRHIKFNEFADDIILLLDYLYIDQAAFIGHEMGATIIAH 101
Cdd:PRK10673  18 PIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQIEKATFIGHSMGGKAVMA 97

                         90
                 ....*....|....*.
gi 515743433 102 LSKQYPEYVSSLTMIN 117
Cdd:PRK10673  98 LTALAPDRIDKLVAID 113
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 18-116 1.21e-10

pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273783 [Multi-domain]  Cd Length: 245  Bit Score: 60.22  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433   18 GQGYP-VVLVHTAFENASIFQNLAHALSKTFQVVLLDLRGHGYSDKPRHIKFNEFADDIILLLDylyiDQAAFIGHEMGA 96
Cdd:TIGR01738   1 GQGNVhLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGFGPLSLADMAEAIAAQAP----DPAIWLGWSLGG 76

                          90       100
                  ....*....|....*....|
gi 515743433   97 TIIAHLSKQYPEYVSSLTMI 116
Cdd:TIGR01738  77 LVALHIAATHPDRVRALVTV 96
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 4-260 5.29e-34

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: 122.42  E-value: 5.29e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433   4 FTRKGGFTLNYNTMG-QGYPVVLVHTAFENASIFQNLAHALSKTFQVVLLDLRGHGYSDKP-RHIKFNEFADDIILLLDY 81
Cdd:COG0596    6 FVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPaGGYTLDDLADDLAALLDA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433  82 LYIDQAAFIGHEMGATIIAHLSKQYPEYVSSLTMINPtsiegelpeerLFRKYAHKIRNWNEDkqekfldkhryykhrkv 161
Cdd:COG0596   86 LGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDE-----------VLAALAEPLRRPGLA----------------- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433 162 nkflknvedtnsistKEETEAVDEVFKQRGIAEVFEYITKPTFIVASAYGERITSLESKEVADLIGNVHFEVYSKSSMYP 241
Cdd:COG0596  138 ---------------PEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFP 202

                        250
                 ....*....|....*....
gi 515743433 242 FEEEQEKFIHDVTPFIKKH 260
Cdd:COG0596  203 PLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 21-245 1.28e-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: 1.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433   21 YPVVLVHTAFENASIFQNLAHALSKT-FQVVLLDLRGHGYSDKPRHIK---FNEFADDIILLLDYLYIDQAAFIGHEMGA 96
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPKAQDdyrTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433   97 TIIAHLSKQYPEYVSSLTMINPTSIEGELPEERLFRK----------YAHKIRNWNEDKQEKFLDKHRYY-----KHRKV 161
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILalfpgffdgfVADFAPNPLGRLVAKLLALLLLRlrllkALPLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433  162 NKFLKNVEDTNSISTKeeTEAVD--EVFKQRGIAEVFEYITKPTFIVASAYgERITSLESKEV-ADLIGNVHFEVYSKSS 238
Cdd:pfam00561 161 NKRFPSGDYALAKSLV--TGALLfiETWSTELRAKFLGRLDEPTLIIWGDQ-DPLVPPQALEKlAQLFPNARLVVIPDAG 237


                  ....*..
gi 515743433  239 MYPFEEE 245
Cdd:pfam00561 238 HFAFLEG 244
PRK10673 PRK10673
esterase;
22-117 4.43e-14

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 69.76  E-value: 4.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433  22 PVVLVHTAFENASIFQNLAHALSKTFQVVLLDLRGHGYSDKPRHIKFNEFADDIILLLDYLYIDQAAFIGHEMGATIIAH 101
Cdd:PRK10673  18 PIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQIEKATFIGHSMGGKAVMA 97

                         90
                 ....*....|....*.
gi 515743433 102 LSKQYPEYVSSLTMIN 117
Cdd:PRK10673  98 LTALAPDRIDKLVAID 113
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 23-141 4.67e-14

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: 69.55  E-value: 4.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433   23 VVLVHTAFENASIFQNLAHALSKT-FQVVLLDLRGHGYSDKPR-HIK-FNEFADDIILLLDYL---YIDQAAFI-GHEMG 95
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALAAQgFAVYAYDHRGHGRSDGKRgHVPsFDDYVDDLDTFVDKIreeHPGLPLFLlGHSMG 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 515743433   96 ATIIAHLSKQYPEYVSSLTMINPtSIEGELPEERLFRKYAHKIRNW 141
Cdd:pfam12146  87 GLIAALYALRYPDKVDGLILSAP-ALKIKPYLAPPILKLLAKLLGK 131
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
4-125 3.54e-13

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 66.95  E-value: 3.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433   4 FTRKGGFTLNYNTM----GQGYPVVLVHTAFENASIFQNLAHALSKT-FQVVLLDLRGHGYSDKPR-HIK-FNEFADDII 76
Cdd:COG2267    8 LPTRDGLRLRGRRWrpagSPRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRgHVDsFDDYVDDLR 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 515743433  77 LLLDYL---YIDQAAFIGHEMGATIIAHLSKQYPEYVSSLTMINPTSIEGEL 125
Cdd:COG2267   88 AALDALrarPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPL 139
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 4-118 1.35e-11

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 63.81  E-value: 1.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433   4 FTRKGGFTLNYNTMGQGY--PVVLVHtAF---ENASIFqNLAhALSKTFQVVLLDLRGHGYSDKP-RHIKFNEFADDIIL 77
Cdd:PRK14875 113 KARIGGRTVRYLRLGEGDgtPVVLIH-GFggdLNNWLF-NHA-ALAAGRPVIALDLPGHGASSKAvGAGSLDELAAAVLA 189

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 515743433  78 LLDYLYIDQAAFIGHEMGATIIAHLSKQYPEYVSSLTMINP 118
Cdd:PRK14875 190 FLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
23-260 2.49e-11

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 61.88  E-value: 2.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433  23 VVLVH----TAFEnasiFQNLAHALSKT-FQVVLLDLRGHGYS-DKPRHIKFNEFADDIILLLDYL--YIDQAAFIGHEM 94
Cdd:COG1647   18 VLLLHgftgSPAE----MRPLAEALAKAgYTVYAPRLPGHGTSpEDLLKTTWEDWLEDVEEAYEILkaGYDKVIVIGLSM 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433  95 GATIIAHLSKQYPEyVSSLTMINPT-SIEGE-LPEERLFRKYAHKIRNWNEDKQEKFLDKHRYYKHRkvnkflknvedtn 172
Cdd:COG1647   94 GGLLALLLAARYPD-VAGLVLLSPAlKIDDPsAPLLPLLKYLARSLRGIGSDIEDPEVAEYAYDRTP------------- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433 173 sistkeeTEAVDEVFK-QRGIAEVFEYITKPTFIVasaYGER--ITSLES-KEVADLIG--NVHFEVYSKSS-MYPFEEE 245
Cdd:COG1647  160 -------LRALAELQRlIREVRRDLPKITAPTLII---QSRKdeVVPPESaRYIYERLGspDKELVWLEDSGhVITLDKD 229

                        250
                 ....*....|....*
gi 515743433 246 QEKFIHDVTPFIKKH 260
Cdd:COG1647  230 REEVAEEILDFLERL 244
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 18-116 1.21e-10

pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273783 [Multi-domain]  Cd Length: 245  Bit Score: 60.22  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433   18 GQGYP-VVLVHTAFENASIFQNLAHALSKTFQVVLLDLRGHGYSDKPRHIKFNEFADDIILLLDylyiDQAAFIGHEMGA 96
Cdd:TIGR01738   1 GQGNVhLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGFGPLSLADMAEAIAAQAP----DPAIWLGWSLGG 76

                          90       100
                  ....*....|....*....|
gi 515743433   97 TIIAHLSKQYPEYVSSLTMI 116
Cdd:TIGR01738  77 LVALHIAATHPDRVRALVTV 96
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 23-107 7.55e-09

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 54.40  E-value: 7.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433   23 VVLVHTAFENASifqNLAHALSKTFQVVLLDLRGHGYSDKPRHiKFNEFADDIILLLDYLYIDQAAFIGHEMGATIIAHL 102
Cdd:pfam12697   1 VVLVHGAGLSAA---PLAALLAAGVAVLAPDLPGHGSSSPPPL-DLADLADLAALLDELGAARPVVLVGHSLGGAVALAA 76


                  ....*
gi 515743433  103 SKQYP 107
Cdd:pfam12697  77 AAAAL 81
PLN02578 PLN02578
hydrolase
 9-141 8.15e-09

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 55.23  E-value: 8.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433   9 GFTLNYNTMGQGYPVVLVHtAFeNASIFQ---NLAHaLSKTFQVVLLDLRGHGYSDKPRhIKFNEF--ADDIILLLDYLY 83
Cdd:PLN02578  75 GHKIHYVVQGEGLPIVLIH-GF-GASAFHwryNIPE-LAKKYKVYALDLLGFGWSDKAL-IEYDAMvwRDQVADFVKEVV 150

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515743433  84 IDQAAFIGHEMGATIIAHLSKQYPEYVSSLTMINPT---------SIEGELPEERLFRKYA-HKIRNW 141
Cdd:PLN02578 151 KEPAVLVGNSLGGFTALSTAVGYPELVAGVALLNSAgqfgsesreKEEAIVVEETVLTRFVvKPLKEW 218
PRK05855 PRK05855
SDR family oxidoreductase;
2-96 6.23e-07

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 49.98  E-value: 6.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433   2 ELFTRKGGFTLNYNTMGQ--GYPVVLVHTAFENASIFQNLAHALSKTFQVVLLDLRGHGYSDKPRHI---KFNEFADDII 76
Cdd:PRK05855   5 RTVVSSDGVRLAVYEWGDpdRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRTaayTLARLADDFA 84

                         90       100
                 ....*....|....*....|.
gi 515743433  77 LLLDYLYIDQAA-FIGHEMGA 96
Cdd:PRK05855  85 AVIDAVSPDRPVhLLAHDWGS 105
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 21-118 7.19e-07

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 46.75  E-value: 7.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433  21 YPVVLVHTAFENASIFQNLAHALSKT-FQVVLLDlrghgYSDKPRHIKFN--EFADDIILLLDYLYIDQAAFIGHEMGAT 97
Cdd:COG1075    6 YPVVLVHGLGGSAASWAPLAPRLRAAgYPVYALN-----YPSTNGSIEDSaeQLAAFVDAVLAATGAEKVDLVGHSMGGL 80

                         90       100
                 ....*....|....*....|...
gi 515743433  98 IIAHLSKQY--PEYVSSLTMINP 118
Cdd:COG1075   81 VARYYLKRLggAAKVARVVTLGT 103
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 22-118 6.94e-06

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 46.80  E-value: 6.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433  22 PVVLVHTAFENASIFQNLAHALSKTFQVVLLDLRGHGYSDKPR-----HIKFNEFADDIILLLDYLYIDQAAFIGHEMGA 96
Cdd:PLN03084 129 PVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDKPQpgygfNYTLDEYVSSLESLIDELKSDKVSLVVQGYFS 208

                         90       100
                 ....*....|....*....|..
gi 515743433  97 TIIAHLSKQYPEYVSSLTMINP 118
Cdd:PLN03084 209 PPVVKYASAHPDKIKKLILLNP 230
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 9-119 7.14e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 43.19  E-value: 7.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433   9 GFTLNYNTMG-QGYPVVLVHTAFENASIFQNLAHALSKTFQVVLLDLRGHGYSDKPRHIK--------FNEFADDIILLL 79
Cdd:PLN02824  17 GYNIRYQRAGtSGPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKPNPRSappnsfytFETWGEQLNDFC 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 515743433  80 DYLYIDQAAFIGHEMGATIIAHLSKQYPEYVSSLTMINPT 119
Cdd:PLN02824  97 SDVVGDPAFVICNSVGGVVGLQAAVDAPELVRGVMLINIS 136
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 9-133 2.44e-04

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 41.52  E-value: 2.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433   9 GFTLNYNTMGQGYPVVLVHTAFENASIFQNLAHALSKTFQVVLLDLRGHGYSDKPR-HIKFNEFADDIILLLDYLYIDQA 87
Cdd:PRK03592  16 GSRMAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKPDiDYTFADHARYLDAWFDALGLDDV 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 515743433  88 AFIGHEMGATIIAHLSKQYPEYVSSL----TMINPTSIEgELPEE--RLFRK 133
Cdd:PRK03592  96 VLVGHDWGSALGFDWAARHPDRVRGIafmeAIVRPMTWD-DFPPAvrELFQA 146
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
18-108 2.76e-04

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


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 41.41  E-value: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433  18 GQGYPVVLVHTAFENASIF-QNLAHALSKT-FQVVLLDLRGHGYSdKPRHIKFNEFAddiilLLDYLYIDQAAfighemg 95
Cdd:COG4757   29 GPPRAVVLINPATGVPQRFyRPFARYLAERgFAVLTYDYRGIGLS-RPGSLRGFDAG-----YRDWGELDLPA------- 95

                         90
                 ....*....|...
gi 515743433  96 atIIAHLSKQYPE 108
Cdd:COG4757   96 --VLDALRARFPG 106
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 7-117 4.51e-04

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 40.98  E-value: 4.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433   7 KGGFTLNYNTMGQGY------PVVLVHtAFeNASI--FQNLAHALSKTFQVVLLDLRGHGYSDKPRHIKFN--EFADDII 76
Cdd:PLN02679  69 KGEYSINYLVKGSPEvtssgpPVLLVH-GF-GASIphWRRNIGVLAKNYTVYAIDLLGFGASDKPPGFSYTmeTWAELIL 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 515743433  77 LLLDYLYIDQAAFIGHEMG--ATIIAhLSKQYPEYVSSLTMIN 117
Cdd:PLN02679 147 DFLEEVVQKPTVLIGNSVGslACVIA-ASESTRDLVRGLVLLN 188
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 32-101 4.93e-04

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


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 40.61  E-value: 4.93e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515743433  32 NASIFQNLAHALSKTFQVVLLDL--RGHGYSDKPRHiKFNEFADDII-LLLDYL---YidqaAFIGHEMGAtIIAH 101
Cdd:COG3208   18 SASAYRPWAAALPPDIEVLAVQLpgRGDRLGEPPLT-SLEELADDLAeELAPLLdrpF----ALFGHSMGA-LLAF 87
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
14-116 6.26e-04

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 40.39  E-value: 6.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433  14 YNTMGQG-YPVVLVHTAFENASIFQNLAHALSKTFQVVLLDLRGHGYSDKPRHIKFNEFADDIILLLDylyiDQAAFIGH 92
Cdd:PRK10349   6 WQTKGQGnVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLADMAEAVLQQAP----DKAIWLGW 81

                         90       100
                 ....*....|....*....|....
gi 515743433  93 EMGATIIAHLSKQYPEYVSSLTMI 116
Cdd:PRK10349  82 SLGGLVASQIALTHPERVQALVTV 105
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 23-141 7.98e-04

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 40.56  E-value: 7.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433  23 VVLVH-----TAFENASIFQNLAHALSKTFQVVLLDLRGHGYSDKPrhikfnefADDIILLLDYL-YIDQAAF------- 89
Cdd:PLN03087 204 VLFIHgfissSAFWTETLFPNFSDAAKSTYRLFAVDLLGFGRSPKP--------ADSLYTLREHLeMIERSVLerykvks 275

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515743433  90 ---IGHEMGATIIAHLSKQYPEYVSSLTMINPTSI---EGELPEERLFRKYAHKiRNW 141
Cdd:PLN03087 276 fhiVAHSLGCILALALAVKHPGAVKSLTLLAPPYYpvpKGVQATQYVMRKVAPR-RVW 332
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
18-168 1.20e-03

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 39.23  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433  18 GQGYPVVL-VHTAFENAS-IFQNLAHALSKT-FQVVLLDLRGHGYSDKPRHikfNEFADDIILLLDYL----YIDQA--A 88
Cdd:COG1506   20 GKKYPVVVyVHGGPGSRDdSFLPLAQALASRgYAVLAPDYRGYGESAGDWG---GDEVDDVLAAIDYLaarpYVDPDriG 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433  89 FIGHEMGATIIAHLSKQYPEYVSSLTMINPTSiegelpeerLFRKYAHKIRNWNEDKQEKFLDKHRYYKHRKVNKFLKNV 168
Cdd:COG1506   97 IYGHSYGGYMALLAAARHPDRFKAAVALAGVS---------DLRSYYGTTREYTERLMGGPWEDPEAYAARSPLAYADKL 167
Ndr pfam03096
Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, ...
 70-120 1.95e-03

Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, and Ndr3. Their similarity was previously noted. The precise molecular and cellular function of members of this family is still unknown. Yet, they are known to be involved in cellular differentiation events. The Ndr1 group was the first to be discovered. Their expression is repressed by the proto-oncogenes N-myc and c-myc, and in line with this observation, Ndr1 protein expression is down-regulated in neoplastic cells, and is reactivated when differentiation is induced by chemicals such as retinoic acid. Ndr2 and Ndr3 expression is not under the control of N-myc or c-myc. Ndr1 expression is also activated by several chemicals: tunicamycin and homocysteine induce Ndr1 in human umbilical endothelial cells; nickel induces Ndr1 in several cell types. Members of this family are found in wide variety of multicellular eukaryotes, including an Ndr1 type protein in Helianthus annuus (sunflower), known as Sf21. Interestingly, the highest scoring matches in the noise are all alpha/beta hydrolases pfam00561, suggesting that this family may have an enzymatic function (Bateman A pers. obs.).


Pssm-ID: 397285 [Multi-domain]  Cd Length: 285  Bit Score: 38.87  E-value: 1.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 515743433   70 EFADDIILLLDYLYIDQAAFIGHEMGATIIAHLSKQYPEYVSSLTMINPTS 120
Cdd:pfam03096  84 DLADMLPVVLDHFRLKSVIGMGVGAGAYILARFALKHPERVEGLVLINPTP 134
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 22-116 2.99e-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: 38.14  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433   22 PVVLVHTAFENASIFQNLAHALSKTFQVVLLDLRGHGYSDKPrhikfnefADDIILLLDYlYIDQA---------AFIGH 92
Cdd:pfam00975   2 PLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPP--------LNSIEALADE-YAEALrqiqpegpyALFGH 72

                          90       100
                  ....*....|....*....|....*..
gi 515743433   93 EMGATI---IAHLSKQYPEYVSSLTMI 116
Cdd:pfam00975  73 SMGGMLafeVARRLERQGEAVRSLFLS 99
PHA02857 PHA02857
monoglyceride lipase; Provisional
 21-118 8.34e-03

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 36.79  E-value: 8.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743433  21 YPVVLV---HTAFENASIFQNLAHALSK-TFQVVLLDLRGHGYSDKPRHI--KFNEFADDII---LLLDYLYIDQAAFI- 90
Cdd:PHA02857  23 YPKALVfisHGAGEHSGRYEELAENISSlGILVFSHDHIGHGRSNGEKMMidDFGVYVRDVVqhvVTIKSTYPGVPVFLl 102

                         90       100
                 ....*....|....*....|....*...
gi 515743433  91 GHEMGATIIAHLSKQYPEYVSSLTMINP 118
Cdd:PHA02857 103 GHSMGATISILAAYKNPNLFTAMILMSP 130
 
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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