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Conserved domains on  [gi|21356953|ref|NP_652068|]
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uncharacterized protein Dmel_CG5704, isoform A [Drosophila melanogaster]

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, ...
 32-301 4.38e-25

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: 100.85  E-value: 4.38e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953  32 RPILAIHGWLDNLGTFDRLIPLLPDYLGVLCIDLPGHGRSSHlpPGMYYSVYEYVFTIPLVMKEYGWSKVSLIGHSLGGV 111
Cdd:COG0596  24 PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK--PAGGYTLDDLADDLAALLDALGLERVVLVGHSMGGM 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953 112 LSFIYASLAPHTVDMIVsldillplrndidymdlsiekqLVNVERQKLGNYIEPPSYTHNQLGKVLAAGSFNSVSPELAK 191
Cdd:COG0596 102 VALELAARHPERVAGLV----------------------LVDEVLAALAEPLRRPGLAPEALAALLRALARTDLRERLAR 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953 192 hllhrqlaksklyperfyftrdirvkyyhyididdslgaemarriIKKPYLIIKGSLSPYLSVRNNEAisiLAKDNPHFE 271
Cdd:COG0596 160 ---------------------------------------------ITVPTLVIWGEKDPIVPPALARR---LAELLPNAE 191

                       250       260       270
                ....*....|....*....|....*....|
gi 21356953 272 FYEVENGTHHLHLHAAEECAGYIVPFIQHH 301
Cdd:COG0596 192 LVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 32-301 4.38e-25

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: 100.85  E-value: 4.38e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953  32 RPILAIHGWLDNLGTFDRLIPLLPDYLGVLCIDLPGHGRSSHlpPGMYYSVYEYVFTIPLVMKEYGWSKVSLIGHSLGGV 111
Cdd:COG0596  24 PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK--PAGGYTLDDLADDLAALLDALGLERVVLVGHSMGGM 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953 112 LSFIYASLAPHTVDMIVsldillplrndidymdlsiekqLVNVERQKLGNYIEPPSYTHNQLGKVLAAGSFNSVSPELAK 191
Cdd:COG0596 102 VALELAARHPERVAGLV----------------------LVDEVLAALAEPLRRPGLAPEALAALLRALARTDLRERLAR 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953 192 hllhrqlaksklyperfyftrdirvkyyhyididdslgaemarriIKKPYLIIKGSLSPYLSVRNNEAisiLAKDNPHFE 271
Cdd:COG0596 160 ---------------------------------------------ITVPTLVIWGEKDPIVPPALARR---LAELLPNAE 191

                       250       260       270
                ....*....|....*....|....*....|
gi 21356953 272 FYEVENGTHHLHLHAAEECAGYIVPFIQHH 301
Cdd:COG0596 192 LVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 33-284 1.15e-20

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: 89.49  E-value: 1.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953    33 PILAIHGWLDNLGTFDRLIPLLPDyLG--VLCIDLPGHGRSSHLPPGMYYSVYEYVFTIPLVMKEYGWSKVSLIGHSLGG 110
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALAR-DGfrVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953   111 VLSFIYASLAPHTVDMIVSLDILLPLrNDIDYMDLSIEKQLVNVERqklGNYIEPPSYTHNQLGKVLAAGSFNSvspela 190
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPP-HELDEADRFILALFPGFFD---GFVADFAPNPLGRLVAKLLALLLLR------ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953   191 kHLLHRQLAKSKLYPERFYFTRDIRVKYYH--YIDIDDSLGAEMARRIIKKPYLIIKGSLSPYLSvrnNEAISILAKDNP 268
Cdd:pfam00561 151 -LRLLKALPLLNKRFPSGDYALAKSLVTGAllFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVP---PQALEKLAQLFP 226

                         250
                  ....*....|....*.
gi 21356953   269 HFEFYEVENGTHHLHL 284
Cdd:pfam00561 227 NARLVVIPDAGHFAFL 242
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 33-124 5.80e-10

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 274729 [Multi-domain]  Cd Length: 252  Bit Score: 58.77  E-value: 5.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953    33 PILAIHGWLDNLGTFDRLIPLLPDYLGVLCIDLPGHGRSSHLppgMYYSVYEYVFTIPLVMKE----YGWSKVSLIGHSL 108
Cdd:TIGR03695   4 VLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSP---SDIERYDFEEAAQLLLATlldqLGIEPFFLVGYSM 80

                          90
                  ....*....|....*.
gi 21356953   109 GGVLSFIYASLAPHTV 124
Cdd:TIGR03695  81 GGRIALYYALQYPERV 96
PRK10673 PRK10673
esterase;
30-132 2.01e-09

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 57.43  E-value: 2.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953   30 NERPILAIHGW---LDNLGTFDRliPLLPDYlGVLCIDLPGHGRSSHLPPGMYYSVYEYVFTIplvMKEYGWSKVSLIGH 106
Cdd:PRK10673  15 NNSPIVLVHGLfgsLDNLGVLAR--DLVNDH-DIIQVDMRNHGLSPRDPVMNYPAMAQDLLDT---LDALQIEKATFIGH 88

                         90       100
                 ....*....|....*....|....*.
gi 21356953  107 SLGGVLSFIYASLAPHTVDMIVSLDI 132
Cdd:PRK10673  89 SMGGKAVMALTALAPDRIDKLVAIDI 114
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 32-301 4.38e-25

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: 100.85  E-value: 4.38e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953  32 RPILAIHGWLDNLGTFDRLIPLLPDYLGVLCIDLPGHGRSSHlpPGMYYSVYEYVFTIPLVMKEYGWSKVSLIGHSLGGV 111
Cdd:COG0596  24 PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK--PAGGYTLDDLADDLAALLDALGLERVVLVGHSMGGM 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953 112 LSFIYASLAPHTVDMIVsldillplrndidymdlsiekqLVNVERQKLGNYIEPPSYTHNQLGKVLAAGSFNSVSPELAK 191
Cdd:COG0596 102 VALELAARHPERVAGLV----------------------LVDEVLAALAEPLRRPGLAPEALAALLRALARTDLRERLAR 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953 192 hllhrqlaksklyperfyftrdirvkyyhyididdslgaemarriIKKPYLIIKGSLSPYLSVRNNEAisiLAKDNPHFE 271
Cdd:COG0596 160 ---------------------------------------------ITVPTLVIWGEKDPIVPPALARR---LAELLPNAE 191

                       250       260       270
                ....*....|....*....|....*....|
gi 21356953 272 FYEVENGTHHLHLHAAEECAGYIVPFIQHH 301
Cdd:COG0596 192 LVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 33-284 1.15e-20

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: 89.49  E-value: 1.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953    33 PILAIHGWLDNLGTFDRLIPLLPDyLG--VLCIDLPGHGRSSHLPPGMYYSVYEYVFTIPLVMKEYGWSKVSLIGHSLGG 110
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALAR-DGfrVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953   111 VLSFIYASLAPHTVDMIVSLDILLPLrNDIDYMDLSIEKQLVNVERqklGNYIEPPSYTHNQLGKVLAAGSFNSvspela 190
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPP-HELDEADRFILALFPGFFD---GFVADFAPNPLGRLVAKLLALLLLR------ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953   191 kHLLHRQLAKSKLYPERFYFTRDIRVKYYH--YIDIDDSLGAEMARRIIKKPYLIIKGSLSPYLSvrnNEAISILAKDNP 268
Cdd:pfam00561 151 -LRLLKALPLLNKRFPSGDYALAKSLVTGAllFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVP---PQALEKLAQLFP 226

                         250
                  ....*....|....*.
gi 21356953   269 HFEFYEVENGTHHLHL 284
Cdd:pfam00561 227 NARLVVIPDAGHFAFL 242
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
20-128 1.21e-12

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 66.18  E-value: 1.21e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953  20 HISGRWYGNRNE--RPILAIHGWLDNLGTFDRLIPLL--PDYlGVLCIDLPGHGRSSHlPPGMYYSVYEYVFTIPLVM-- 93
Cdd:COG2267  15 RLRGRRWRPAGSprGTVVLVHGLGEHSGRYAELAEALaaAGY-AVLAFDLRGHGRSDG-PRGHVDSFDDYVDDLRAALda 92

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 21356953  94 -KEYGWSKVSLIGHSLGGVLSFIYASLAPHTVDMIV 128
Cdd:COG2267  93 lRARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLV 128
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 33-124 5.80e-10

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 274729 [Multi-domain]  Cd Length: 252  Bit Score: 58.77  E-value: 5.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953    33 PILAIHGWLDNLGTFDRLIPLLPDYLGVLCIDLPGHGRSSHLppgMYYSVYEYVFTIPLVMKE----YGWSKVSLIGHSL 108
Cdd:TIGR03695   4 VLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSP---SDIERYDFEEAAQLLLATlldqLGIEPFFLVGYSM 80

                          90
                  ....*....|....*.
gi 21356953   109 GGVLSFIYASLAPHTV 124
Cdd:TIGR03695  81 GGRIALYYALQYPERV 96
PRK10673 PRK10673
esterase;
30-132 2.01e-09

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 57.43  E-value: 2.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953   30 NERPILAIHGW---LDNLGTFDRliPLLPDYlGVLCIDLPGHGRSSHLPPGMYYSVYEYVFTIplvMKEYGWSKVSLIGH 106
Cdd:PRK10673  15 NNSPIVLVHGLfgsLDNLGVLAR--DLVNDH-DIIQVDMRNHGLSPRDPVMNYPAMAQDLLDT---LDALQIEKATFIGH 88

                         90       100
                 ....*....|....*....|....*.
gi 21356953  107 SLGGVLSFIYASLAPHTVDMIVSLDI 132
Cdd:PRK10673  89 SMGGKAVMALTALAPDRIDKLVAIDI 114
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 34-122 7.73e-08

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 52.09  E-value: 7.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953    34 ILAIHGWLDnlgTFDRLIPLLPDYLGVLCIDLPGHGRSSHlPPGMYYSVYEYVFTIPLVMkeyGWSKVSLIGHSLGGVLS 113
Cdd:pfam12697   1 VVLVHGAGL---SAAPLAALLAAGVAVLAPDLPGHGSSSP-PPLDLADLADLAALLDELG---AARPVVLVGHSLGGAVA 73


                  ....*....
gi 21356953   114 FIYASLAPH 122
Cdd:pfam12697  74 LAAAAAALV 82
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 27-124 1.82e-07

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 52.25  E-value: 1.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953   27 GNRNERPILAIHGW---LDN-LGTFDRLIPLLPdylgVLCIDLPGHGRSSH-LPPGmyySVYEYVFTIPLVMKEYGWSKV 101
Cdd:PRK14875 127 GEGDGTPVVLIHGFggdLNNwLFNHAALAAGRP----VIALDLPGHGASSKaVGAG---SLDELAAAVLAFLDALGIERA 199

                         90       100
                 ....*....|....*....|...
gi 21356953  102 SLIGHSLGGVLSFIYASLAPHTV 124
Cdd:PRK14875 200 HLVGHSMGGAVALRLAARAPQRV 222
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 32-130 4.55e-06

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 44.82  E-value: 4.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953  32 RPILAIHGWLDNLGTFDRLIPLLPDyLG--VLCIDLPGHGRSShlpPGMYYSVYEYVFTiplVMKEYGWSKVSLIGHSLG 109
Cdd:COG1075   6 YPVVLVHGLGGSAASWAPLAPRLRA-AGypVYALNYPSTNGSI---EDSAEQLAAFVDA---VLAATGAEKVDLVGHSMG 78

                        90       100
                ....*....|....*....|...
gi 21356953 110 GVLSFIYASL--APHTVDMIVSL 130
Cdd:COG1075  79 GLVARYYLKRlgGAAKVARVVTL 101
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 37-130 1.12e-05

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: 45.96  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953    37 IHGWLDNLGTFDRLIPLLPDYLGVLCIDLPGHGRSSHLPPgmyysvyeyvFTIPLV---MKEYGWSKVSLIGHSLGGVLS 113
Cdd:TIGR01738  10 IHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGFGP----------LSLADMaeaIAAQAPDPAIWLGWSLGGLVA 79

                          90
                  ....*....|....*..
gi 21356953   114 FIYASLAPHTVDMIVSL 130
Cdd:TIGR01738  80 LHIAATHPDRVRALVTV 96
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 34-129 1.49e-05

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: 45.67  E-value: 1.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953    34 ILAIHGWLDNLGTFDRLIPLL--PDYlGVLCIDLPGHGRSshlPPGMYY--SVYEYV-----FtIPLVMKEYGWSKVSLI 104
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALaaQGF-AVYAYDHRGHGRS---DGKRGHvpSFDDYVddldtF-VDKIREEHPGLPLFLL 81

                          90       100
                  ....*....|....*....|....*.
gi 21356953   105 GHSLGGVLSFIYASLAPHTVD-MIVS 129
Cdd:pfam12146  82 GHSMGGLIAALYALRYPDKVDgLILS 107
bchO_mg_che_rel TIGR03056
putative magnesium chelatase accessory protein; Members of this family belong to the alpha ...
 34-131 2.17e-05

putative magnesium chelatase accessory protein; Members of this family belong to the alpha/beta fold family hydrolases (pfam00561). Members are found in bacterial genomes if and only if they encoded for anoxygenic photosynthetic systems similar to that of Rhodobacter capsulatus and other alpha-Proteobacteria. Members often are encoded in the same operon as subunits of the protoporphyrin IX magnesium chelatase, and were once designated BchO. No literature supports a role as an actual subunit of magnesium chelatase, but an accessory role is possible, as suggested by placement by its probable hydrolase activity. [Energy metabolism, Photosynthesis]


Pssm-ID: 132100  Cd Length: 278  Bit Score: 45.27  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953    34 ILAIHGWLDNLGTFDRLIPLLPDYLGVLCIDLPGHGRSShlppgmyySVYEYVFTIPLVMKEY-------GWSKVSLIGH 106
Cdd:TIGR03056  31 LLLLHGTGASTHSWRDLMPPLARSFRVVAPDLPGHGFTR--------APFRFRFTLPSMAEDLsalcaaeGLSPDGVIGH 102

                          90       100
                  ....*....|....*....|....*
gi 21356953   107 SLGGVLSFIYASLAPHTVDMIVSLD 131
Cdd:TIGR03056 103 SAGAAIALRLALDGPVTPRMVVGIN 127
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 50-117 3.40e-05

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


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 44.44  E-value: 3.40e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21356953   50 LIPLLPDYlGVLCIDLPGHGRSSHLPPGMYYSVYEYVFTIplvMKEYGWSKVSLIGHSLGGVLSFIYA 117
Cdd:PRK11126  21 VGEALPDY-PRLYIDLPGHGGSAAISVDGFADVSRLLSQT---LQSYNILPYWLVGYSLGGRIAMYYA 84
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
30-118 1.42e-04

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 42.62  E-value: 1.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953  30 NERPILAIHGWLDNLGTFDRLipllPDYLG-----VLCIDLPGHGRS----SHLPPGMYYSVYEYVFTIplvMKEyGWSK 100
Cdd:COG1647  14 GRKGVLLLHGFTGSPAEMRPL----AEALAkagytVYAPRLPGHGTSpedlLKTTWEDWLEDVEEAYEI---LKA-GYDK 85

                        90
                ....*....|....*...
gi 21356953 101 VSLIGHSLGGVLSFIYAS 118
Cdd:COG1647  86 VIVIGLSMGGLLALLLAA 103
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
21-130 5.10e-04

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 40.77  E-value: 5.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953  21 ISGRWYGNRNERP---ILAIHGWLDN-LGTFDRLIPLLPDyLG--VLCIDLPGHGRSSHLPPGMYY----SVYEYVFTIP 90
Cdd:COG1506  10 LPGWLYLPADGKKypvVVYVHGGPGSrDDSFLPLAQALAS-RGyaVLAPDYRGYGESAGDWGGDEVddvlAAIDYLAARP 88

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 21356953  91 LVMKEygwsKVSLIGHSLGGVLSFIYASLAPHTVDMIVSL 130
Cdd:COG1506  89 YVDPD----RIGIYGHSYGGYMALLAAARHPDRFKAAVAL 124
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 24-135 8.83e-04

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 40.63  E-value: 8.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953   24 RWY----GNRNERPILAIHGWLDNLGTFDRLIPLLPDYLGVLCIDLPGHGRSSHLPP--GMYYSVYEYVFTIPLVMKEYG 97
Cdd:PLN03084 116 RWFcvesGSNNNPPVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDKPQPgyGFNYTLDEYVSSLESLIDELK 195

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 21356953   98 WSKVSLI--GHSLGGVLSfiYASLAPhtvDMIVSLDILLP 135
Cdd:PLN03084 196 SDKVSLVvqGYFSPPVVK--YASAHP---DKIKKLILLNP 230
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 33-121 1.35e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 40.21  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953   33 PILAIHGWLDNLGTFDRLIPLLPDYLGVLCIDLPGHGrSSHLPPGMYYSVYEYVFTIPLVMKEYGWSKVSLIGHSLGGVL 112
Cdd:PLN02679  90 PVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFG-ASDKPPGFSYTMETWAELILDFLEEVVQKPTVLIGNSVGSLA 168


                 ....*....
gi 21356953  113 SFIYASLAP 121
Cdd:PLN02679 169 CVIAASEST 177
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 28-109 1.63e-03

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 40.23  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953    28 NRNERPILAIHGWLdnlGTFDRLIPLLPDYLG---VLCIDLPGHGRSSHLPPGmYYSVYEYVFTIPLV-------MKEYG 97
Cdd:PLN02980 1368 NAEGSVVLFLHGFL---GTGEDWIPIMKAISGsarCISIDLPGHGGSKIQNHA-KETQTEPTLSVELVadllyklIEHIT 1443

                          90
                  ....*....|..
gi 21356953    98 WSKVSLIGHSLG 109
Cdd:PLN02980 1444 PGKVTLVGYSMG 1455
PRK05855 PRK05855
SDR family oxidoreductase;
26-111 2.02e-03

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 39.96  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953   26 YGNrNERP-ILAIHGWLDNLGTFDRLIPLLPDYLGVLCIDLPGHGRSSHLPPGMYYSVYEYVFTIPLVMKEYGWSK-VSL 103
Cdd:PRK05855  20 WGD-PDRPtVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVIDAVSPDRpVHL 98


                 ....*...
gi 21356953  104 IGHSLGGV 111
Cdd:PRK05855  99 LAHDWGSI 106
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 46-114 3.79e-03

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


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 38.29  E-value: 3.79e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21356953  46 TFDRLIPLLPDYLGVLCIDLPGHGRSSHLPPgmYYSVYEYVFTIPLVMKEYGWSKVSLIGHSLGGVLSF 114
Cdd:COG3208  21 AYRPWAAALPPDIEVLAVQLPGRGDRLGEPP--LTSLEELADDLAEELAPLLDRPFALFGHSMGALLAF 87
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 47-119 6.06e-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: 37.37  E-value: 6.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356953    47 FDRLIPLLPDYLGVLCIDLPGHGRSSHLPPGMYYSVYEYVFTI-------PLVmkeygwskvsLIGHSLGGVLSFIYASL 119
Cdd:pfam00975  16 FRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADEYAEALrqiqpegPYA----------LFGHSMGGMLAFEVARR 85
 
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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