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Conserved domains on  [gi|1034655657|ref|XP_016867707|]
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mesoderm-specific transcript homolog protein isoform X1 [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, ...
 36-325 9.36e-28

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: 9.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657  36 SSGKFFTYKGLRIFYQDSvGVVGSPeiVVLLHGFPTSSYDWYKIWEGLTLRFhRVIALDFLGFGFSDKPRPhHYSIFEQA 115
Cdd:COG0596     2 STPRFVTVDGVRLHYREA-GPDGPP--VVLLHGLPGSSYEWRPLIPALAAGY-RVIAPDLRGHGRSDKPAG-GYTLDDLA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657 116 SIVEALLRHLGLQnrRINLLSHDYGDIVAQELLYRYKQNrsgrltIKSLCLSNggifpETHRplLLQKLLKDGGVLSPIL 195
Cdd:COG0596    77 DDLAALLDALGLE--RVVLVGHSMGGMVALELAARHPER------VAGLVLVD-----EVLA--ALAEPLRRPGLAPEAL 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657 196 TRLMNFFVfsrgltpvfgpytrpseseLWDMWAgirnndgnlvidsllqyinqrkkfrrrwvgALASVTIPIHFIYGPLD 275
Cdd:COG0596   142 AALLRALA-------------------RTDLRE------------------------------RLARITVPTLVIWGEKD 172

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034655657 276 PVNPyPEFLELYRKTLPRSTVSILDDhISHYPQLEDPMGFLNAYMGFINS 325
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, ...
 36-325 9.36e-28

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: 9.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657  36 SSGKFFTYKGLRIFYQDSvGVVGSPeiVVLLHGFPTSSYDWYKIWEGLTLRFhRVIALDFLGFGFSDKPRPhHYSIFEQA 115
Cdd:COG0596     2 STPRFVTVDGVRLHYREA-GPDGPP--VVLLHGLPGSSYEWRPLIPALAAGY-RVIAPDLRGHGRSDKPAG-GYTLDDLA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657 116 SIVEALLRHLGLQnrRINLLSHDYGDIVAQELLYRYKQNrsgrltIKSLCLSNggifpETHRplLLQKLLKDGGVLSPIL 195
Cdd:COG0596    77 DDLAALLDALGLE--RVVLVGHSMGGMVALELAARHPER------VAGLVLVD-----EVLA--ALAEPLRRPGLAPEAL 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657 196 TRLMNFFVfsrgltpvfgpytrpseseLWDMWAgirnndgnlvidsllqyinqrkkfrrrwvgALASVTIPIHFIYGPLD 275
Cdd:COG0596   142 AALLRALA-------------------RTDLRE------------------------------RLARITVPTLVIWGEKD 172

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034655657 276 PVNPyPEFLELYRKTLPRSTVSILDDhISHYPQLEDPMGFLNAYMGFINS 325
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.
 63-312 7.05e-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: 7.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657  63 VVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKPR-PHHYSIFEQASIVEALLRHLGLQnrRINLLSHDYGD 141
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKaQDDYRTDDLAEDLEYILEALGLE--KVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657 142 IVAQELLYRYKQNrsgrltIKSLCLSNGGIFPETHRPLLLQKLLKD----GGVLSPILTRLMNFFV-FSRGLTPVFGPYT 216
Cdd:pfam00561  81 LIALAYAAKYPDR------VKALVLLGALDPPHELDEADRFILALFpgffDGFVADFAPNPLGRLVaKLLALLLLRLRLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657 217 RPSESELWDMWAGIRNNDGNLVIDSLLQYINQRKKFRRRWVGALAsvtIPIHFIYGPLDPVNPyPEFLELYRKTLPRSTV 296
Cdd:pfam00561 155 KALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLD---EPTLIIWGDQDPLVP-PQALEKLAQLFPNARL 230

                         250
                  ....*....|....*.
gi 1034655657 297 sILDDHISHYPQLEDP 312
Cdd:pfam00561 231 -VVIPDAGHFAFLEGP 245
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 39-140 2.86e-13

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 68.87  E-value: 2.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657  39 KFFTYKGLRIFYQDSvgvvGSPEIVVLLHGFPTSSYDWYKIWEGLTlRFHRVIALDFLGFGFSDKPrPHHYSIFEQASIV 118
Cdd:PRK03592   10 RRVEVLGSRMAYIET----GEGDPIVFLHGNPTSSYLWRNIIPHLA-GLGRCLAPDLIGMGASDKP-DIDYTFADHARYL 83

                          90       100
                  ....*....|....*....|..
gi 1034655657 119 EALLRHLGLqnRRINLLSHDYG 140
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, ...
 36-325 9.36e-28

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: 9.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657  36 SSGKFFTYKGLRIFYQDSvGVVGSPeiVVLLHGFPTSSYDWYKIWEGLTLRFhRVIALDFLGFGFSDKPRPhHYSIFEQA 115
Cdd:COG0596     2 STPRFVTVDGVRLHYREA-GPDGPP--VVLLHGLPGSSYEWRPLIPALAAGY-RVIAPDLRGHGRSDKPAG-GYTLDDLA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657 116 SIVEALLRHLGLQnrRINLLSHDYGDIVAQELLYRYKQNrsgrltIKSLCLSNggifpETHRplLLQKLLKDGGVLSPIL 195
Cdd:COG0596    77 DDLAALLDALGLE--RVVLVGHSMGGMVALELAARHPER------VAGLVLVD-----EVLA--ALAEPLRRPGLAPEAL 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657 196 TRLMNFFVfsrgltpvfgpytrpseseLWDMWAgirnndgnlvidsllqyinqrkkfrrrwvgALASVTIPIHFIYGPLD 275
Cdd:COG0596   142 AALLRALA-------------------RTDLRE------------------------------RLARITVPTLVIWGEKD 172

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034655657 276 PVNPyPEFLELYRKTLPRSTVSILDDhISHYPQLEDPMGFLNAYMGFINS 325
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.
 63-312 7.05e-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: 7.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657  63 VVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKPR-PHHYSIFEQASIVEALLRHLGLQnrRINLLSHDYGD 141
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKaQDDYRTDDLAEDLEYILEALGLE--KVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657 142 IVAQELLYRYKQNrsgrltIKSLCLSNGGIFPETHRPLLLQKLLKD----GGVLSPILTRLMNFFV-FSRGLTPVFGPYT 216
Cdd:pfam00561  81 LIALAYAAKYPDR------VKALVLLGALDPPHELDEADRFILALFpgffDGFVADFAPNPLGRLVaKLLALLLLRLRLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657 217 RPSESELWDMWAGIRNNDGNLVIDSLLQYINQRKKFRRRWVGALAsvtIPIHFIYGPLDPVNPyPEFLELYRKTLPRSTV 296
Cdd:pfam00561 155 KALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLD---EPTLIIWGDQDPLVP-PQALEKLAQLFPNARL 230

                         250
                  ....*....|....*.
gi 1034655657 297 sILDDHISHYPQLEDP 312
Cdd:pfam00561 231 -VVIPDAGHFAFLEGP 245
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 39-140 2.86e-13

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 68.87  E-value: 2.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657  39 KFFTYKGLRIFYQDSvgvvGSPEIVVLLHGFPTSSYDWYKIWEGLTlRFHRVIALDFLGFGFSDKPrPHHYSIFEQASIV 118
Cdd:PRK03592   10 RRVEVLGSRMAYIET----GEGDPIVFLHGNPTSSYLWRNIIPHLA-GLGRCLAPDLIGMGASDKP-DIDYTFADHARYL 83

                          90       100
                  ....*....|....*....|..
gi 1034655657 119 EALLRHLGLqnRRINLLSHDYG 140
Cdd:PRK03592   84 DAWFDALGL--DDVVLVGHDWG 103
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 47-145 1.23e-10

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 61.82  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657  47 RIFYQDSvGVVGSPEiVVLLHGFPTSSYDWYKIWEGLTLRFHrVIALDFLGFGFSDKPRPHH---YSIFEQASIVEALlr 123
Cdd:PLN03084  116 RWFCVES-GSNNNPP-VLLIHGFPSQAYSYRKVLPVLSKNYH-AIAFDWLGFGFSDKPQPGYgfnYTLDEYVSSLESL-- 190

                          90       100
                  ....*....|....*....|..
gi 1034655657 124 hlglqnrrINLLSHDYGDIVAQ 145
Cdd:PLN03084  191 --------IDELKSDKVSLVVQ 204
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 22-140 1.92e-10

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 60.64  E-value: 1.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657  22 IPPPQLSPALHSWkssgkfFTYKGLRIFYQDSvgvvGSPEIVVLLHGFPTSSYDWYKIWEGLTLRFhRVIALDFLGFGFS 101
Cdd:PRK03204    6 TPDPQLYPFESRW------FDSSRGRIHYIDE----GTGPPILLCHGNPTWSFLYRDIIVALRDRF-RCVAPDYLGFGLS 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1034655657 102 DKPRPHHYSIFEQASIVEALLRHLGLQNrrINLLSHDYG 140
Cdd:PRK03204   75 ERPSGFGYQIDEHARVIGEFVDHLGLDR--YLSMGQDWG 111
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 46-143 8.75e-09

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 55.74  E-value: 8.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657  46 LRIFYQDSVGVVGSPeiVVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKP-RPHHYSIFEQASIVEALLRH 124
Cdd:PRK00870   34 LRMHYVDEGPADGPP--VLLLHGEPSWSYLYRKMIPILAAAGHRVIAPDLIGFGRSDKPtRREDYTYARHVEWMRSWFEQ 111

                          90
                  ....*....|....*....
gi 1034655657 125 LGLQNrrINLLSHDYGDIV 143
Cdd:PRK00870  112 LDLTD--VTLVCQDWGGLI 128
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 23-106 1.26e-08

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 55.13  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657  23 PPPQLSPALHSWKssgkfftYKGLRIFYQDSVGvvgSPEIVVLLHGFPTSSYDWYKIWEGLTLRfHRVIALDFLGFGFSD 102
Cdd:PLN02824    2 VKPEPQVETRTWR-------WKGYNIRYQRAGT---SGPALVLVHGFGGNADHWRKNTPVLAKS-HRVYAIDLLGYGYSD 70


                  ....
gi 1034655657 103 KPRP 106
Cdd:PLN02824   71 KPNP 74
PLN02578 PLN02578
hydrolase
 12-103 3.93e-08

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 54.08  E-value: 3.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657  12 AVPLLAAYLHIPPPQLSPALHSWKSSGKFFTYKGLRIFYqdsvgVV---GSPeiVVLLHGFPTSSYDW-YKIWEglTLRF 87
Cdd:PLN02578   42 GVSVMGSSSASQSVQGLERLPFKKEGYNFWTWRGHKIHY-----VVqgeGLP--IVLIHGFGASAFHWrYNIPE--LAKK 112

                          90
                  ....*....|....*.
gi 1034655657  88 HRVIALDFLGFGFSDK 103
Cdd:PLN02578  113 YKVYALDLLGFGWSDK 128
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
35-151 4.57e-08

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 52.70  E-value: 4.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657  35 KSSGKFFTYKGLRIFYQDSVGVVGSPEIVVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKPRPHHYSIFEQ 114
Cdd:COG2267     3 RRLVTLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDY 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034655657 115 ASIVEALLRHLGLQ-NRRINLLSHDYGDIVAQELLYRY 151
Cdd:COG2267    83 VDDLRAALDALRARpGLPVVLLGHSMGGLIALLYAARY 120
PRK05855 PRK05855
SDR family oxidoreductase;
45-150 6.13e-07

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 50.75  E-value: 6.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657  45 GLRIfyqdSVGVVGSPE--IVVLLHGFPTSSYDWYKIWEGLTLRFHrVIALDFLGFGFSDKPRPHH-YSIFEQASIVEAL 121
Cdd:PRK05855   12 GVRL----AVYEWGDPDrpTVVLVHGYPDNHEVWDGVAPLLADRFR-VVAYDVRGAGRSSAPKRTAaYTLARLADDFAAV 86

                          90       100
                  ....*....|....*....|....*....
gi 1034655657 122 LRHLGlQNRRINLLSHDYGDIVAQELLYR 150
Cdd:PRK05855   87 IDAVS-PDRPVHLLAHDWGSIQGWEAVTR 114
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 63-152 9.62e-06

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: 9.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657  63 VVLLHGFPTSSYDWykiwEGLTLRFHRVIALDFLGFGFSDkPRPHHYSIFEQasiVEALLRHLGLQNRRInLLSHDYGDI 142
Cdd:pfam12697   1 VVLVHGAGLSAAPL----AALLAAGVAVLAPDLPGHGSSS-PPPLDLADLAD---LAALLDELGAARPVV-LVGHSLGGA 71

                          90
                  ....*....|
gi 1034655657 143 VAQELLYRYK 152
Cdd:pfam12697  72 VALAAAAAAL 81
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 32-166 1.82e-05

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 45.95  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657  32 HSWKSSGKfftyKGLRIFYQDSVGVvGSPEIVVLLHGFPTSSYDWYkiwEGLTLRF-------HRVIALDFLGFGFSDKP 104
Cdd:PLN03087  178 TSWLSSSN----ESLFVHVQQPKDN-KAKEDVLFIHGFISSSAFWT---ETLFPNFsdaakstYRLFAVDLLGFGRSPKP 249

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034655657 105 RPHHYSIFEQASIVE-ALLRHLGLqnRRINLLSHDYGDIVAQELLYRYKQnrsgrlTIKSLCL 166
Cdd:PLN03087  250 ADSLYTLREHLEMIErSVLERYKV--KSFHIVAHSLGCILALALAVKHPG------AVKSLTL 304
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 58-192 5.26e-04

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 41.47  E-value: 5.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657  58 GSPEIVVLLHGFPTSSYDWYKIWEGLTlRFHRVIALDFLGFGFSDKpRPHHYSIFEQASIVEALLRHLGLQnrRINLLSH 137
Cdd:PRK14875  129 GDGTPVVLIHGFGGDLNNWLFNHAALA-AGRPVIALDLPGHGASSK-AVGAGSLDELAAAVLAFLDALGIE--RAHLVGH 204

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034655657 138 DYGDIVAQELLyrykQNRSGRltIKSLCL-SNGGIFPE-------------THRPL--LLQKLLKDGGVLS 192
Cdd:PRK14875  205 SMGGAVALRLA----ARAPQR--VASLTLiAPAGLGPEingdyidgfvaaeSRRELkpVLELLFADPALVT 269
PRK08775 PRK08775
homoserine O-succinyltransferase;
46-163 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 1034655657  46 LRIFYQdSVGVVGSPEIVVL--------LHGFPTSSYD-WykiWEGLT-------LRFHRVIALDFLGfgfSDKPRPHHY 109
Cdd:PRK08775   46 LRLRYE-LIGPAGAPVVFVAggisahrhVAATATFPEKgW---WEGLVgsgraldPARFRLLAFDFIG---ADGSLDVPI 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034655657 110 SIFEQASIVEALLRHLGLQnRRINLLSHDYGDIVAQELLYRYKQnRSGRLTIKS 163
Cdd:PRK08775  119 DTADQADAIALLLDALGIA-RLHAFVGYSYGALVGLQFASRHPA-RVRTLVVVS 170
DUF1057 pfam06342
Alpha/beta hydrolase of unknown function (DUF1057); This family consists of several ...
 50-140 3.27e-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: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657  50 YQDSVGVVGSPEIVVLLHGFPTSSYDWYKI---WEGLTLRFhrvIALDFLGFGFSDKPRPHHYSIFEQASIVEALLRHLG 126
Cdd:pfam06342  25 YEDSLTSGSPFGTVVAFHGSPGSHNDFKYIrskFEDLNIRF---IGVNYPGFEFTTGYPGQSHTNQERNSYSKALLEELE 101

                          90
                  ....*....|....
gi 1034655657 127 LQNRRInLLSHDYG 140
Cdd:pfam06342 102 LKGKLI-IMGHSRG 114
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 62-198 5.39e-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: 37.58  E-value: 5.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657  62 IVVLLHGFpTSSYDWY-KIWEGLTLRFHRVIALDFLGFGFSDKPRPHHYSIFEQASIVEALLRHLGLQNRRIN--LLSHD 138
Cdd:pfam12146   6 VVVLVHGL-GEHSGRYaHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPlfLLGHS 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034655657 139 YGDIVAQELLYRYKQNrsgrltIKSLCLSNGGIFPETHRPLLLQKLLkdGGVLSPILTRL 198
Cdd:pfam12146  85 MGGLIAALYALRYPDK------VDGLILSAPALKIKPYLAPPILKLL--AKLLGKLFPRL 136
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 39-111 5.39e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 38.28  E-value: 5.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034655657  39 KFFTYKGL-RIFY--QDSVGVVGSPEIVVLLHGFPTSSYDWYKIWEGLTlRFHRVIALDFLGFGFSDKPRPHHYSI 111
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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