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Conserved domains on  [gi|29294635|ref|NP_803490|]
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mesoderm-specific transcript homolog protein isoform b precursor [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 29294635  36 SSGKFFTYKGLRIFYQDSvGVVGSPeiVVLLHGFPTSSYDWYKIWEGLTLRFhRVIALDFLGFGFSDKPRPhHYSIFEQA 115
Cdd:COG0596   2 STPRFVTVDGVRLHYREA-GPDGPP--VVLLHGLPGSSYEWRPLIPALAAGY-RVIAPDLRGHGRSDKPAG-GYTLDDLA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294635 116 SIVEALLRHLGLQnrRINLLSHDYGDIVAQELLYRYKQNrsgrltIKSLCLSNggifpETHRplLLQKLLKDGGVLSPIL 195
Cdd:COG0596  77 DDLAALLDALGLE--RVVLVGHSMGGMVALELAARHPER------VAGLVLVD-----EVLA--ALAEPLRRPGLAPEAL 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294635 196 TRLMNFFVfsrgltpvfgpytrpseseLWDMWAgirnndgnlvidsllqyinqrkkfrrrwvgALASVTIPIHFIYGPLD 275
Cdd:COG0596 142 AALLRALA-------------------RTDLRE------------------------------RLARITVPTLVIWGEKD 172

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 29294635 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 29294635  36 SSGKFFTYKGLRIFYQDSvGVVGSPeiVVLLHGFPTSSYDWYKIWEGLTLRFhRVIALDFLGFGFSDKPRPhHYSIFEQA 115
Cdd:COG0596   2 STPRFVTVDGVRLHYREA-GPDGPP--VVLLHGLPGSSYEWRPLIPALAAGY-RVIAPDLRGHGRSDKPAG-GYTLDDLA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294635 116 SIVEALLRHLGLQnrRINLLSHDYGDIVAQELLYRYKQNrsgrltIKSLCLSNggifpETHRplLLQKLLKDGGVLSPIL 195
Cdd:COG0596  77 DDLAALLDALGLE--RVVLVGHSMGGMVALELAARHPER------VAGLVLVD-----EVLA--ALAEPLRRPGLAPEAL 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294635 196 TRLMNFFVfsrgltpvfgpytrpseseLWDMWAgirnndgnlvidsllqyinqrkkfrrrwvgALASVTIPIHFIYGPLD 275
Cdd:COG0596 142 AALLRALA-------------------RTDLRE------------------------------RLARITVPTLVIWGEKD 172

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 29294635 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 29294635    63 VVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKPR-PHHYSIFEQASIVEALLRHLGLQnrRINLLSHDYGD 141
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKaQDDYRTDDLAEDLEYILEALGLE--KVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294635   142 IVAQELLYRYKQNrsgrltIKSLCLSNGGIFPETHRPLLLQKLLKD----GGVLSPILTRLMNFFV-FSRGLTPVFGPYT 216
Cdd:pfam00561  81 LIALAYAAKYPDR------VKALVLLGALDPPHELDEADRFILALFpgffDGFVADFAPNPLGRLVaKLLALLLLRLRLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294635   217 RPSESELWDMWAGIRNNDGNLVIDSLLQYINQRKKFRRRWVGALAsvtIPIHFIYGPLDPVNPyPEFLELYRKTLPRSTV 296
Cdd:pfam00561 155 KALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLD---EPTLIIWGDQDPLVP-PQALEKLAQLFPNARL 230

                         250
                  ....*....|....*.
gi 29294635   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 29294635   39 KFFTYKGLRIFYQDSvgvvGSPEIVVLLHGFPTSSYDWYKIWEGLTlRFHRVIALDFLGFGFSDKPrPHHYSIFEQASIV 118
Cdd:PRK03592  10 RRVEVLGSRMAYIET----GEGDPIVFLHGNPTSSYLWRNIIPHLA-GLGRCLAPDLIGMGASDKP-DIDYTFADHARYL 83

                         90       100
                 ....*....|....*....|..
gi 29294635  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 29294635  36 SSGKFFTYKGLRIFYQDSvGVVGSPeiVVLLHGFPTSSYDWYKIWEGLTLRFhRVIALDFLGFGFSDKPRPhHYSIFEQA 115
Cdd:COG0596   2 STPRFVTVDGVRLHYREA-GPDGPP--VVLLHGLPGSSYEWRPLIPALAAGY-RVIAPDLRGHGRSDKPAG-GYTLDDLA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294635 116 SIVEALLRHLGLQnrRINLLSHDYGDIVAQELLYRYKQNrsgrltIKSLCLSNggifpETHRplLLQKLLKDGGVLSPIL 195
Cdd:COG0596  77 DDLAALLDALGLE--RVVLVGHSMGGMVALELAARHPER------VAGLVLVD-----EVLA--ALAEPLRRPGLAPEAL 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294635 196 TRLMNFFVfsrgltpvfgpytrpseseLWDMWAgirnndgnlvidsllqyinqrkkfrrrwvgALASVTIPIHFIYGPLD 275
Cdd:COG0596 142 AALLRALA-------------------RTDLRE------------------------------RLARITVPTLVIWGEKD 172

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 29294635 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 29294635    63 VVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKPR-PHHYSIFEQASIVEALLRHLGLQnrRINLLSHDYGD 141
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKaQDDYRTDDLAEDLEYILEALGLE--KVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294635   142 IVAQELLYRYKQNrsgrltIKSLCLSNGGIFPETHRPLLLQKLLKD----GGVLSPILTRLMNFFV-FSRGLTPVFGPYT 216
Cdd:pfam00561  81 LIALAYAAKYPDR------VKALVLLGALDPPHELDEADRFILALFpgffDGFVADFAPNPLGRLVaKLLALLLLRLRLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294635   217 RPSESELWDMWAGIRNNDGNLVIDSLLQYINQRKKFRRRWVGALAsvtIPIHFIYGPLDPVNPyPEFLELYRKTLPRSTV 296
Cdd:pfam00561 155 KALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLD---EPTLIIWGDQDPLVP-PQALEKLAQLFPNARL 230

                         250
                  ....*....|....*.
gi 29294635   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 29294635   39 KFFTYKGLRIFYQDSvgvvGSPEIVVLLHGFPTSSYDWYKIWEGLTlRFHRVIALDFLGFGFSDKPrPHHYSIFEQASIV 118
Cdd:PRK03592  10 RRVEVLGSRMAYIET----GEGDPIVFLHGNPTSSYLWRNIIPHLA-GLGRCLAPDLIGMGASDKP-DIDYTFADHARYL 83

                         90       100
                 ....*....|....*....|..
gi 29294635  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 29294635   47 RIFYQDSvGVVGSPEiVVLLHGFPTSSYDWYKIWEGLTLRFHrVIALDFLGFGFSDKPRPHH---YSIFEQASIVEALlr 123
Cdd:PLN03084 116 RWFCVES-GSNNNPP-VLLIHGFPSQAYSYRKVLPVLSKNYH-AIAFDWLGFGFSDKPQPGYgfnYTLDEYVSSLESL-- 190

                         90       100
                 ....*....|....*....|..
gi 29294635  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 29294635   22 IPPPQLSPALHSWkssgkfFTYKGLRIFYQDSvgvvGSPEIVVLLHGFPTSSYDWYKIWEGLTLRFhRVIALDFLGFGFS 101
Cdd:PRK03204   6 TPDPQLYPFESRW------FDSSRGRIHYIDE----GTGPPILLCHGNPTWSFLYRDIIVALRDRF-RCVAPDYLGFGLS 74

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 29294635  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 29294635   46 LRIFYQDSVGVVGSPeiVVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKP-RPHHYSIFEQASIVEALLRH 124
Cdd:PRK00870  34 LRMHYVDEGPADGPP--VLLLHGEPSWSYLYRKMIPILAAAGHRVIAPDLIGFGRSDKPtRREDYTYARHVEWMRSWFEQ 111

                         90
                 ....*....|....*....
gi 29294635  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 29294635   23 PPPQLSPALHSWKssgkfftYKGLRIFYQDSVGvvgSPEIVVLLHGFPTSSYDWYKIWEGLTLRfHRVIALDFLGFGFSD 102
Cdd:PLN02824   2 VKPEPQVETRTWR-------WKGYNIRYQRAGT---SGPALVLVHGFGGNADHWRKNTPVLAKS-HRVYAIDLLGYGYSD 70


                 ....
gi 29294635  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 29294635   12 AVPLLAAYLHIPPPQLSPALHSWKSSGKFFTYKGLRIFYqdsvgVV---GSPeiVVLLHGFPTSSYDW-YKIWEglTLRF 87
Cdd:PLN02578  42 GVSVMGSSSASQSVQGLERLPFKKEGYNFWTWRGHKIHY-----VVqgeGLP--IVLIHGFGASAFHWrYNIPE--LAKK 112

                         90
                 ....*....|....*.
gi 29294635   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 29294635  35 KSSGKFFTYKGLRIFYQDSVGVVGSPEIVVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKPRPHHYSIFEQ 114
Cdd:COG2267   3 RRLVTLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDY 82

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 29294635 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 29294635   45 GLRIfyqdSVGVVGSPE--IVVLLHGFPTSSYDWYKIWEGLTLRFHrVIALDFLGFGFSDKPRPHH-YSIFEQASIVEAL 121
Cdd:PRK05855  12 GVRL----AVYEWGDPDrpTVVLVHGYPDNHEVWDGVAPLLADRFR-VVAYDVRGAGRSSAPKRTAaYTLARLADDFAAV 86

                         90       100
                 ....*....|....*....|....*....
gi 29294635  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 29294635    63 VVLLHGFPTSSYDWykiwEGLTLRFHRVIALDFLGFGFSDkPRPHHYSIFEQasiVEALLRHLGLQNRRInLLSHDYGDI 142
Cdd:pfam12697   1 VVLVHGAGLSAAPL----AALLAAGVAVLAPDLPGHGSSS-PPPLDLADLAD---LAALLDELGAARPVV-LVGHSLGGA 71

                          90
                  ....*....|
gi 29294635   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 29294635   32 HSWKSSGKfftyKGLRIFYQDSVGVvGSPEIVVLLHGFPTSSYDWYkiwEGLTLRF-------HRVIALDFLGFGFSDKP 104
Cdd:PLN03087 178 TSWLSSSN----ESLFVHVQQPKDN-KAKEDVLFIHGFISSSAFWT---ETLFPNFsdaakstYRLFAVDLLGFGRSPKP 249

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29294635  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 29294635   58 GSPEIVVLLHGFPTSSYDWYKIWEGLTlRFHRVIALDFLGFGFSDKpRPHHYSIFEQASIVEALLRHLGLQnrRINLLSH 137
Cdd:PRK14875 129 GDGTPVVLIHGFGGDLNNWLFNHAALA-AGRPVIALDLPGHGASSK-AVGAGSLDELAAAVLAFLDALGIE--RAHLVGH 204

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29294635  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 29294635   46 LRIFYQdSVGVVGSPEIVVL--------LHGFPTSSYD-WykiWEGLT-------LRFHRVIALDFLGfgfSDKPRPHHY 109
Cdd:PRK08775  46 LRLRYE-LIGPAGAPVVFVAggisahrhVAATATFPEKgW---WEGLVgsgraldPARFRLLAFDFIG---ADGSLDVPI 118

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 29294635  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 29294635    50 YQDSVGVVGSPEIVVLLHGFPTSSYDWYKI---WEGLTLRFhrvIALDFLGFGFSDKPRPHHYSIFEQASIVEALLRHLG 126
Cdd:pfam06342  25 YEDSLTSGSPFGTVVAFHGSPGSHNDFKYIrskFEDLNIRF---IGVNYPGFEFTTGYPGQSHTNQERNSYSKALLEELE 101

                          90
                  ....*....|....
gi 29294635   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 29294635    62 IVVLLHGFpTSSYDWY-KIWEGLTLRFHRVIALDFLGFGFSDKPRPHHYSIFEQASIVEALLRHLGLQNRRIN--LLSHD 138
Cdd:pfam12146   6 VVVLVHGL-GEHSGRYaHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPlfLLGHS 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 29294635   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 29294635   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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