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Conserved domains on  [gi|29294639|ref|NP_002393|]
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mesoderm-specific transcript homolog protein isoform a [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

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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, ...
 45-334 1.10e-27

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: 107.78  E-value: 1.10e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639  45 SSGKFFTYKGLRIFYQDSvGVVGSPeiVVLLHGFPTSSYDWYKIWEGLTLRFhRVIALDFLGFGFSDKPRPhHYSIFEQA 124
Cdd:COG0596   2 STPRFVTVDGVRLHYREA-GPDGPP--VVLLHGLPGSSYEWRPLIPALAAGY-RVIAPDLRGHGRSDKPAG-GYTLDDLA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639 125 SIVEALLRHLGLQnrRINLLSHDYGDIVAQELLYRYKQNrsgrltIKSLCLSNggifpETHRplLLQKLLKDGGVLSPIL 204
Cdd:COG0596  77 DDLAALLDALGLE--RVVLVGHSMGGMVALELAARHPER------VAGLVLVD-----EVLA--ALAEPLRRPGLAPEAL 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639 205 TRLMNFFVfsrgltpvfgpytrpseseLWDMWAgirnndgnlvidsllqyinqrkkfrrrwvgALASVTIPIHFIYGPLD 284
Cdd:COG0596 142 AALLRALA-------------------RTDLRE------------------------------RLARITVPTLVIWGEKD 172

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 29294639 285 PVNPyPEFLELYRKTLPRSTVSILDDhISHYPQLEDPMGFLNAYMGFINS 334
Cdd:COG0596 173 PIVP-PALARRLAELLPNAELVVLPG-AGHFPPLEQPEAFAAALRDFLAR 220
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 45-334 1.10e-27

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: 107.78  E-value: 1.10e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639  45 SSGKFFTYKGLRIFYQDSvGVVGSPeiVVLLHGFPTSSYDWYKIWEGLTLRFhRVIALDFLGFGFSDKPRPhHYSIFEQA 124
Cdd:COG0596   2 STPRFVTVDGVRLHYREA-GPDGPP--VVLLHGLPGSSYEWRPLIPALAAGY-RVIAPDLRGHGRSDKPAG-GYTLDDLA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639 125 SIVEALLRHLGLQnrRINLLSHDYGDIVAQELLYRYKQNrsgrltIKSLCLSNggifpETHRplLLQKLLKDGGVLSPIL 204
Cdd:COG0596  77 DDLAALLDALGLE--RVVLVGHSMGGMVALELAARHPER------VAGLVLVD-----EVLA--ALAEPLRRPGLAPEAL 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639 205 TRLMNFFVfsrgltpvfgpytrpseseLWDMWAgirnndgnlvidsllqyinqrkkfrrrwvgALASVTIPIHFIYGPLD 284
Cdd:COG0596 142 AALLRALA-------------------RTDLRE------------------------------RLARITVPTLVIWGEKD 172

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 29294639 285 PVNPyPEFLELYRKTLPRSTVSILDDhISHYPQLEDPMGFLNAYMGFINS 334
Cdd:COG0596 173 PIVP-PALARRLAELLPNAELVVLPG-AGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 72-321 8.30e-21

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: 89.87  E-value: 8.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639    72 VVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKPR-PHHYSIFEQASIVEALLRHLGLQnrRINLLSHDYGD 150
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKaQDDYRTDDLAEDLEYILEALGLE--KVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639   151 IVAQELLYRYKQNrsgrltIKSLCLSNGGIFPETHRPLLLQKLLKD----GGVLSPILTRLMNFFV-FSRGLTPVFGPYT 225
Cdd:pfam00561  81 LIALAYAAKYPDR------VKALVLLGALDPPHELDEADRFILALFpgffDGFVADFAPNPLGRLVaKLLALLLLRLRLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639   226 RPSESELWDMWAGIRNNDGNLVIDSLLQYINQRKKFRRRWVGALAsvtIPIHFIYGPLDPVNPyPEFLELYRKTLPRSTV 305
Cdd:pfam00561 155 KALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLD---EPTLIIWGDQDPLVP-PQALEKLAQLFPNARL 230

                         250
                  ....*....|....*.
gi 29294639   306 sILDDHISHYPQLEDP 321
Cdd:pfam00561 231 -VVIPDAGHFAFLEGP 245
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 48-149 2.62e-13

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 69.25  E-value: 2.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639   48 KFFTYKGLRIFYQDSvgvvGSPEIVVLLHGFPTSSYDWYKIWEGLTlRFHRVIALDFLGFGFSDKPrPHHYSIFEQASIV 127
Cdd:PRK03592  10 RRVEVLGSRMAYIET----GEGDPIVFLHGNPTSSYLWRNIIPHLA-GLGRCLAPDLIGMGASDKP-DIDYTFADHARYL 83

                         90       100
                 ....*....|....*....|..
gi 29294639  128 EALLRHLGLqnRRINLLSHDYG 149
Cdd:PRK03592  84 DAWFDALGL--DDVVLVGHDWG 103
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 45-334 1.10e-27

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: 107.78  E-value: 1.10e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639  45 SSGKFFTYKGLRIFYQDSvGVVGSPeiVVLLHGFPTSSYDWYKIWEGLTLRFhRVIALDFLGFGFSDKPRPhHYSIFEQA 124
Cdd:COG0596   2 STPRFVTVDGVRLHYREA-GPDGPP--VVLLHGLPGSSYEWRPLIPALAAGY-RVIAPDLRGHGRSDKPAG-GYTLDDLA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639 125 SIVEALLRHLGLQnrRINLLSHDYGDIVAQELLYRYKQNrsgrltIKSLCLSNggifpETHRplLLQKLLKDGGVLSPIL 204
Cdd:COG0596  77 DDLAALLDALGLE--RVVLVGHSMGGMVALELAARHPER------VAGLVLVD-----EVLA--ALAEPLRRPGLAPEAL 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639 205 TRLMNFFVfsrgltpvfgpytrpseseLWDMWAgirnndgnlvidsllqyinqrkkfrrrwvgALASVTIPIHFIYGPLD 284
Cdd:COG0596 142 AALLRALA-------------------RTDLRE------------------------------RLARITVPTLVIWGEKD 172

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 29294639 285 PVNPyPEFLELYRKTLPRSTVSILDDhISHYPQLEDPMGFLNAYMGFINS 334
Cdd:COG0596 173 PIVP-PALARRLAELLPNAELVVLPG-AGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 72-321 8.30e-21

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: 89.87  E-value: 8.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639    72 VVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKPR-PHHYSIFEQASIVEALLRHLGLQnrRINLLSHDYGD 150
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKaQDDYRTDDLAEDLEYILEALGLE--KVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639   151 IVAQELLYRYKQNrsgrltIKSLCLSNGGIFPETHRPLLLQKLLKD----GGVLSPILTRLMNFFV-FSRGLTPVFGPYT 225
Cdd:pfam00561  81 LIALAYAAKYPDR------VKALVLLGALDPPHELDEADRFILALFpgffDGFVADFAPNPLGRLVaKLLALLLLRLRLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639   226 RPSESELWDMWAGIRNNDGNLVIDSLLQYINQRKKFRRRWVGALAsvtIPIHFIYGPLDPVNPyPEFLELYRKTLPRSTV 305
Cdd:pfam00561 155 KALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLD---EPTLIIWGDQDPLVP-PQALEKLAQLFPNARL 230

                         250
                  ....*....|....*.
gi 29294639   306 sILDDHISHYPQLEDP 321
Cdd:pfam00561 231 -VVIPDAGHFAFLEGP 245
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 48-149 2.62e-13

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 69.25  E-value: 2.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639   48 KFFTYKGLRIFYQDSvgvvGSPEIVVLLHGFPTSSYDWYKIWEGLTlRFHRVIALDFLGFGFSDKPrPHHYSIFEQASIV 127
Cdd:PRK03592  10 RRVEVLGSRMAYIET----GEGDPIVFLHGNPTSSYLWRNIIPHLA-GLGRCLAPDLIGMGASDKP-DIDYTFADHARYL 83

                         90       100
                 ....*....|....*....|..
gi 29294639  128 EALLRHLGLqnRRINLLSHDYG 149
Cdd:PRK03592  84 DAWFDALGL--DDVVLVGHDWG 103
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 56-154 1.28e-10

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 61.82  E-value: 1.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639   56 RIFYQDSvGVVGSPEiVVLLHGFPTSSYDWYKIWEGLTLRFHrVIALDFLGFGFSDKPRPHH---YSIFEQASIVEALlr 132
Cdd:PLN03084 116 RWFCVES-GSNNNPP-VLLIHGFPSQAYSYRKVLPVLSKNYH-AIAFDWLGFGFSDKPQPGYgfnYTLDEYVSSLESL-- 190

                         90       100
                 ....*....|....*....|..
gi 29294639  133 hlglqnrrINLLSHDYGDIVAQ 154
Cdd:PLN03084 191 --------IDELKSDKVSLVVQ 204
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 31-149 1.70e-10

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 61.03  E-value: 1.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639   31 IPPPQLSPALHSWkssgkfFTYKGLRIFYQDSvgvvGSPEIVVLLHGFPTSSYDWYKIWEGLTLRFhRVIALDFLGFGFS 110
Cdd:PRK03204   6 TPDPQLYPFESRW------FDSSRGRIHYIDE----GTGPPILLCHGNPTWSFLYRDIIVALRDRF-RCVAPDYLGFGLS 74

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 29294639  111 DKPRPHHYSIFEQASIVEALLRHLGLQNrrINLLSHDYG 149
Cdd:PRK03204  75 ERPSGFGYQIDEHARVIGEFVDHLGLDR--YLSMGQDWG 111
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 55-152 9.21e-09

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 55.74  E-value: 9.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639   55 LRIFYQDSVGVVGSPeiVVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKP-RPHHYSIFEQASIVEALLRH 133
Cdd:PRK00870  34 LRMHYVDEGPADGPP--VLLLHGEPSWSYLYRKMIPILAAAGHRVIAPDLIGFGRSDKPtRREDYTYARHVEWMRSWFEQ 111

                         90
                 ....*....|....*....
gi 29294639  134 LGLQNrrINLLSHDYGDIV 152
Cdd:PRK00870 112 LDLTD--VTLVCQDWGGLI 128
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 32-115 1.40e-08

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 55.13  E-value: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639   32 PPPQLSPALHSWKssgkfftYKGLRIFYQDSVGvvgSPEIVVLLHGFPTSSYDWYKIWEGLTLRfHRVIALDFLGFGFSD 111
Cdd:PLN02824   2 VKPEPQVETRTWR-------WKGYNIRYQRAGT---SGPALVLVHGFGGNADHWRKNTPVLAKS-HRVYAIDLLGYGYSD 70


                 ....
gi 29294639  112 KPRP 115
Cdd:PLN02824  71 KPNP 74
PLN02578 PLN02578
hydrolase
 21-112 4.34e-08

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 54.08  E-value: 4.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639   21 AVPLLAAYLHIPPPQLSPALHSWKSSGKFFTYKGLRIFYqdsvgVV---GSPeiVVLLHGFPTSSYDW-YKIWEglTLRF 96
Cdd:PLN02578  42 GVSVMGSSSASQSVQGLERLPFKKEGYNFWTWRGHKIHY-----VVqgeGLP--IVLIHGFGASAFHWrYNIPE--LAKK 112

                         90
                 ....*....|....*.
gi 29294639   97 HRVIALDFLGFGFSDK 112
Cdd:PLN02578 113 YKVYALDLLGFGWSDK 128
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
44-160 4.71e-08

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 52.70  E-value: 4.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639  44 KSSGKFFTYKGLRIFYQDSVGVVGSPEIVVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKPRPHHYSIFEQ 123
Cdd:COG2267   3 RRLVTLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDY 82

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 29294639 124 ASIVEALLRHLGLQ-NRRINLLSHDYGDIVAQELLYRY 160
Cdd:COG2267  83 VDDLRAALDALRARpGLPVVLLGHSMGGLIALLYAARY 120
PRK05855 PRK05855
SDR family oxidoreductase;
54-159 6.48e-07

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 50.75  E-value: 6.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639   54 GLRIfyqdSVGVVGSPE--IVVLLHGFPTSSYDWYKIWEGLTLRFHrVIALDFLGFGFSDKPRPHH-YSIFEQASIVEAL 130
Cdd:PRK05855  12 GVRL----AVYEWGDPDrpTVVLVHGYPDNHEVWDGVAPLLADRFR-VVAYDVRGAGRSSAPKRTAaYTLARLADDFAAV 86

                         90       100
                 ....*....|....*....|....*....
gi 29294639  131 LRHLGlQNRRINLLSHDYGDIVAQELLYR 159
Cdd:PRK05855  87 IDAVS-PDRPVHLLAHDWGSIQGWEAVTR 114
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 72-161 1.07e-05

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 45.93  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639    72 VVLLHGFPTSSYDWykiwEGLTLRFHRVIALDFLGFGFSDkPRPHHYSIFEQasiVEALLRHLGLQNRRInLLSHDYGDI 151
Cdd:pfam12697   1 VVLVHGAGLSAAPL----AALLAAGVAVLAPDLPGHGSSS-PPPLDLADLAD---LAALLDELGAARPVV-LVGHSLGGA 71

                          90
                  ....*....|
gi 29294639   152 VAQELLYRYK 161
Cdd:pfam12697  72 VALAAAAAAL 81
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 41-175 1.89e-05

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 45.95  E-value: 1.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639   41 HSWKSSGKfftyKGLRIFYQDSVGVvGSPEIVVLLHGFPTSSYDWYkiwEGLTLRF-------HRVIALDFLGFGFSDKP 113
Cdd:PLN03087 178 TSWLSSSN----ESLFVHVQQPKDN-KAKEDVLFIHGFISSSAFWT---ETLFPNFsdaakstYRLFAVDLLGFGRSPKP 249

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29294639  114 RPHHYSIFEQASIVE-ALLRHLGLqnRRINLLSHDYGDIVAQELLYRYKQnrsgrlTIKSLCL 175
Cdd:PLN03087 250 ADSLYTLREHLEMIErSVLERYKV--KSFHIVAHSLGCILALALAVKHPG------AVKSLTL 304
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 67-201 5.52e-04

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 41.47  E-value: 5.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639   67 GSPEIVVLLHGFPTSSYDWYKIWEGLTlRFHRVIALDFLGFGFSDKpRPHHYSIFEQASIVEALLRHLGLQnrRINLLSH 146
Cdd:PRK14875 129 GDGTPVVLIHGFGGDLNNWLFNHAALA-AGRPVIALDLPGHGASSK-AVGAGSLDELAAAVLAFLDALGIE--RAHLVGH 204

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29294639  147 DYGDIVAQELLyrykQNRSGRltIKSLCL-SNGGIFPE-------------THRPL--LLQKLLKDGGVLS 201
Cdd:PRK14875 205 SMGGAVALRLA----ARAPQR--VASLTLiAPAGLGPEingdyidgfvaaeSRRELkpVLELLFADPALVT 269
PRK08775 PRK08775
homoserine O-succinyltransferase;
55-172 1.79e-03

homoserine O-succinyltransferase;


Pssm-ID: 181553 [Multi-domain]  Cd Length: 343  Bit Score: 39.77  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639   55 LRIFYQdSVGVVGSPEIVVL--------LHGFPTSSYD-WykiWEGLT-------LRFHRVIALDFLGfgfSDKPRPHHY 118
Cdd:PRK08775  46 LRLRYE-LIGPAGAPVVFVAggisahrhVAATATFPEKgW---WEGLVgsgraldPARFRLLAFDFIG---ADGSLDVPI 118

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 29294639  119 SIFEQASIVEALLRHLGLQnRRINLLSHDYGDIVAQELLYRYKQnRSGRLTIKS 172
Cdd:PRK08775 119 DTADQADAIALLLDALGIA-RLHAFVGYSYGALVGLQFASRHPA-RVRTLVVVS 170
DUF1057 pfam06342
Alpha/beta hydrolase of unknown function (DUF1057); This family consists of several ...
 59-149 3.47e-03

Alpha/beta hydrolase of unknown function (DUF1057); This family consists of several Caenorhabditis elegans specific proteins of unknown function. Members of this family have an alpha/beta hydrolase fold.


Pssm-ID: 115027  Cd Length: 297  Bit Score: 38.58  E-value: 3.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639    59 YQDSVGVVGSPEIVVLLHGFPTSSYDWYKI---WEGLTLRFhrvIALDFLGFGFSDKPRPHHYSIFEQASIVEALLRHLG 135
Cdd:pfam06342  25 YEDSLTSGSPFGTVVAFHGSPGSHNDFKYIrskFEDLNIRF---IGVNYPGFEFTTGYPGQSHTNQERNSYSKALLEELE 101

                          90
                  ....*....|....
gi 29294639   136 LQNRRInLLSHDYG 149
Cdd:pfam06342 102 LKGKLI-IMGHSRG 114
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 71-207 5.41e-03

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: 37.96  E-value: 5.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639    71 IVVLLHGFpTSSYDWY-KIWEGLTLRFHRVIALDFLGFGFSDKPRPHHYSIFEQASIVEALLRHLGLQNRRIN--LLSHD 147
Cdd:pfam12146   6 VVVLVHGL-GEHSGRYaHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPlfLLGHS 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294639   148 YGDIVAQELLYRYKQNrsgrltIKSLCLSNGGIFPETHRPLLLQKLLkdGGVLSPILTRL 207
Cdd:pfam12146  85 MGGLIAALYALRYPDK------VDGLILSAPALKIKPYLAPPILKLL--AKLLGKLFPRL 136
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 48-120 5.89e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 38.28  E-value: 5.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29294639   48 KFFTYKGL-RIFY--QDSVGVVGSPEIVVLLHGFPTSSYDWYKIWEGLTlRFHRVIALDFLGFGFSDKPRPHHYSI 120
Cdd:PLN02679  64 KKWKWKGEySINYlvKGSPEVTSSGPPVLLVHGFGASIPHWRRNIGVLA-KNYTVYAIDLLGFGASDKPPGFSYTM 138
 
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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