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Conserved domains on  [gi|356582507|ref|NP_001239222|]
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mesoderm-specific transcript protein isoform 1 [Mus musculus]

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 4.36e-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: 105.85  E-value: 4.36e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507  36 TSGKFFTYKGLRIFYQDSvGVVGSPeiVVLLHGFPTSSYDWYKIWEGLTLRFhRVIALDFLGFGFSDKPRPHqYSIFEQA 115
Cdd:COG0596    2 STPRFVTVDGVRLHYREA-GPDGPP--VVLLHGLPGSSYEWRPLIPALAAGY-RVIAPDLRGHGRSDKPAGG-YTLDDLA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507 116 SIVESLLRHLGLQnrRINLLSHDYGDIVAQELLYRYKQNrsgrltIKSLCLSNggifpETHRplLLQKLLKDGGVLSPIL 195
Cdd:COG0596   77 DDLAALLDALGLE--RVVLVGHSMGGMVALELAARHPER------VAGLVLVD-----EVLA--ALAEPLRRPGLAPEAL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507 196 TRLMNFFVfsrgltpvfgpytrpteseLWDMWAvirnndgnlvidsllqyinqrkkfrrrwvgALASVSIPIHFIYGPLD 275
Cdd:COG0596  142 AALLRALA-------------------RTDLRE------------------------------RLARITVPTLVIWGEKD 172

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 356582507 276 PINPyPEFLELYRKTLPRSTVSILDDhISHYPQLEDPMGFLNAYMGFINS 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 4.36e-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: 105.85  E-value: 4.36e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507  36 TSGKFFTYKGLRIFYQDSvGVVGSPeiVVLLHGFPTSSYDWYKIWEGLTLRFhRVIALDFLGFGFSDKPRPHqYSIFEQA 115
Cdd:COG0596    2 STPRFVTVDGVRLHYREA-GPDGPP--VVLLHGLPGSSYEWRPLIPALAAGY-RVIAPDLRGHGRSDKPAGG-YTLDDLA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507 116 SIVESLLRHLGLQnrRINLLSHDYGDIVAQELLYRYKQNrsgrltIKSLCLSNggifpETHRplLLQKLLKDGGVLSPIL 195
Cdd:COG0596   77 DDLAALLDALGLE--RVVLVGHSMGGMVALELAARHPER------VAGLVLVD-----EVLA--ALAEPLRRPGLAPEAL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507 196 TRLMNFFVfsrgltpvfgpytrpteseLWDMWAvirnndgnlvidsllqyinqrkkfrrrwvgALASVSIPIHFIYGPLD 275
Cdd:COG0596  142 AALLRALA-------------------RTDLRE------------------------------RLARITVPTLVIWGEKD 172

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 356582507 276 PINPyPEFLELYRKTLPRSTVSILDDhISHYPQLEDPMGFLNAYMGFINS 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 6.27e-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: 87.17  E-value: 6.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507   63 VVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKPR-PHQYSIFEQASIVESLLRHLGLQnrRINLLSHDYGD 141
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKaQDDYRTDDLAEDLEYILEALGLE--KVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507  142 IVAQELLYRYKQNrsgrltIKSLCLSNGGIFPETHRPLLLQKLLKD----GGVLSPILTRLMNFFV-FSRGLTPVFGPYT 216
Cdd:pfam00561  81 LIALAYAAKYPDR------VKALVLLGALDPPHELDEADRFILALFpgffDGFVADFAPNPLGRLVaKLLALLLLRLRLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507  217 RPTESELWDMWAVIRNNDGNLVIDSLLQYINQRKKFRRRWVGALasvSIPIHFIYGPLDPINPyPEFLELYRKTLPRSTV 296
Cdd:pfam00561 155 KALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRL---DEPTLIIWGDQDPLVP-PQALEKLAQLFPNARL 230

                         250
                  ....*....|....*.
gi 356582507  297 sILDDHISHYPQLEDP 312
Cdd:pfam00561 231 -VVIPDAGHFAFLEGP 245
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 39-140 8.17e-13

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 67.71  E-value: 8.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507  39 KFFTYKGLRIFYQDSvgvvGSPEIVVLLHGFPTSSYDWYKIWEGLTlRFHRVIALDFLGFGFSDKPrPHQYSIFEQASIV 118
Cdd:PRK03592  10 RRVEVLGSRMAYIET----GEGDPIVFLHGNPTSSYLWRNIIPHLA-GLGRCLAPDLIGMGASDKP-DIDYTFADHARYL 83

                         90       100
                 ....*....|....*....|..
gi 356582507 119 ESLLRHLGLqnRRINLLSHDYG 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 4.36e-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: 105.85  E-value: 4.36e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507  36 TSGKFFTYKGLRIFYQDSvGVVGSPeiVVLLHGFPTSSYDWYKIWEGLTLRFhRVIALDFLGFGFSDKPRPHqYSIFEQA 115
Cdd:COG0596    2 STPRFVTVDGVRLHYREA-GPDGPP--VVLLHGLPGSSYEWRPLIPALAAGY-RVIAPDLRGHGRSDKPAGG-YTLDDLA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507 116 SIVESLLRHLGLQnrRINLLSHDYGDIVAQELLYRYKQNrsgrltIKSLCLSNggifpETHRplLLQKLLKDGGVLSPIL 195
Cdd:COG0596   77 DDLAALLDALGLE--RVVLVGHSMGGMVALELAARHPER------VAGLVLVD-----EVLA--ALAEPLRRPGLAPEAL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507 196 TRLMNFFVfsrgltpvfgpytrpteseLWDMWAvirnndgnlvidsllqyinqrkkfrrrwvgALASVSIPIHFIYGPLD 275
Cdd:COG0596  142 AALLRALA-------------------RTDLRE------------------------------RLARITVPTLVIWGEKD 172

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 356582507 276 PINPyPEFLELYRKTLPRSTVSILDDhISHYPQLEDPMGFLNAYMGFINS 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 6.27e-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: 87.17  E-value: 6.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507   63 VVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKPR-PHQYSIFEQASIVESLLRHLGLQnrRINLLSHDYGD 141
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKaQDDYRTDDLAEDLEYILEALGLE--KVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507  142 IVAQELLYRYKQNrsgrltIKSLCLSNGGIFPETHRPLLLQKLLKD----GGVLSPILTRLMNFFV-FSRGLTPVFGPYT 216
Cdd:pfam00561  81 LIALAYAAKYPDR------VKALVLLGALDPPHELDEADRFILALFpgffDGFVADFAPNPLGRLVaKLLALLLLRLRLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507  217 RPTESELWDMWAVIRNNDGNLVIDSLLQYINQRKKFRRRWVGALasvSIPIHFIYGPLDPINPyPEFLELYRKTLPRSTV 296
Cdd:pfam00561 155 KALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRL---DEPTLIIWGDQDPLVP-PQALEKLAQLFPNARL 230

                         250
                  ....*....|....*.
gi 356582507  297 sILDDHISHYPQLEDP 312
Cdd:pfam00561 231 -VVIPDAGHFAFLEGP 245
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 39-140 8.17e-13

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 67.71  E-value: 8.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507  39 KFFTYKGLRIFYQDSvgvvGSPEIVVLLHGFPTSSYDWYKIWEGLTlRFHRVIALDFLGFGFSDKPrPHQYSIFEQASIV 118
Cdd:PRK03592  10 RRVEVLGSRMAYIET----GEGDPIVFLHGNPTSSYLWRNIIPHLA-GLGRCLAPDLIGMGASDKP-DIDYTFADHARYL 83

                         90       100
                 ....*....|....*....|..
gi 356582507 119 ESLLRHLGLqnRRINLLSHDYG 140
Cdd:PRK03592  84 DAWFDALGL--DDVVLVGHDWG 103
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 47-145 4.80e-11

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 62.98  E-value: 4.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507  47 RIFYQDSvGVVGSPEiVVLLHGFPTSSYDWYKIWEGLTLRFHrVIALDFLGFGFSDKPRP---HQYSIFEQASIVESLlr 123
Cdd:PLN03084 116 RWFCVES-GSNNNPP-VLLIHGFPSQAYSYRKVLPVLSKNYH-AIAFDWLGFGFSDKPQPgygFNYTLDEYVSSLESL-- 190

                         90       100
                 ....*....|....*....|..
gi 356582507 124 hlglqnrrINLLSHDYGDIVAQ 145
Cdd:PLN03084 191 --------IDELKSDKVSLVVQ 204
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 22-140 1.13e-10

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 61.41  E-value: 1.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507  22 IPPPQLSPALHSWktsgkfFTYKGLRIFYQDSvgvvGSPEIVVLLHGFPTSSYDWYKIWEGLTLRFhRVIALDFLGFGFS 101
Cdd:PRK03204   6 TPDPQLYPFESRW------FDSSRGRIHYIDE----GTGPPILLCHGNPTWSFLYRDIIVALRDRF-RCVAPDYLGFGLS 74

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 356582507 102 DKPRPHQYSIFEQASIVESLLRHLGLQNrrINLLSHDYG 140
Cdd:PRK03204  75 ERPSGFGYQIDEHARVIGEFVDHLGLDR--YLSMGQDWG 111
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 61-143 4.77e-09

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 56.52  E-value: 4.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507  61 EIVVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKP-RPHQYSIFEQASIVESLLRHLGLQNrrINLLSHDY 139
Cdd:PRK00870  47 PPVLLLHGEPSWSYLYRKMIPILAAAGHRVIAPDLIGFGRSDKPtRREDYTYARHVEWMRSWFEQLDLTD--VTLVCQDW 124


                 ....
gi 356582507 140 GDIV 143
Cdd:PRK00870 125 GGLI 128
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 23-108 1.16e-08

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 55.51  E-value: 1.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507  23 PPPQLSPALHSWKtsgkfftYKGLRIFYQDSVGvvgSPEIVVLLHGFPTSSYDWYKIWEGLTLRfHRVIALDFLGFGFSD 102
Cdd:PLN02824   2 VKPEPQVETRTWR-------WKGYNIRYQRAGT---SGPALVLVHGFGGNADHWRKNTPVLAKS-HRVYAIDLLGYGYSD 70


                 ....*.
gi 356582507 103 KPRPHQ 108
Cdd:PLN02824  71 KPNPRS 76
PLN02578 PLN02578
hydrolase
 12-103 4.93e-08

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 53.69  E-value: 4.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507  12 AVPLLAAYLHIPPPQLSPALHSWKTSGKFFTYKGLRIFYqdsvgVV---GSPeiVVLLHGFPTSSYDW-YKIWEglTLRF 87
Cdd:PLN02578  42 GVSVMGSSSASQSVQGLERLPFKKEGYNFWTWRGHKIHY-----VVqgeGLP--IVLIHGFGASAFHWrYNIPE--LAKK 112

                         90
                 ....*....|....*.
gi 356582507  88 HRVIALDFLGFGFSDK 103
Cdd:PLN02578 113 YKVYALDLLGFGWSDK 128
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
35-151 1.73e-07

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 51.16  E-value: 1.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507  35 KTSGKFFTYKGLRIFYQDSVGVVGSPEIVVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKPRPHQYSIFEQ 114
Cdd:COG2267    3 RRLVTLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDY 82

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 356582507 115 ASIVESLLRHLGLQ-NRRINLLSHDYGDIVAQELLYRY 151
Cdd:COG2267   83 VDDLRAALDALRARpGLPVVLLGHSMGGLIALLYAARY 120
PRK05855 PRK05855
SDR family oxidoreductase;
45-150 1.32e-06

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 49.59  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507  45 GLRIfyqdSVGVVGSPE--IVVLLHGFPTSSYDWYKIWEGLTLRFHrVIALDFLGFGFSDKPRP-HQYSIFEQASIVESL 121
Cdd:PRK05855  12 GVRL----AVYEWGDPDrpTVVLVHGYPDNHEVWDGVAPLLADRFR-VVAYDVRGAGRSSAPKRtAAYTLARLADDFAAV 86

                         90       100
                 ....*....|....*....|....*....
gi 356582507 122 LRHLGlQNRRINLLSHDYGDIVAQELLYR 150
Cdd:PRK05855  87 IDAVS-PDRPVHLLAHDWGSIQGWEAVTR 114
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 32-166 2.63e-06

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 48.65  E-value: 2.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507  32 HSWKTSGKfftyKGLRIFYQDSVGVvGSPEIVVLLHGFPTSSYDWYkiwEGLTLRF-------HRVIALDFLGFGFSDKP 104
Cdd:PLN03087 178 TSWLSSSN----ESLFVHVQQPKDN-KAKEDVLFIHGFISSSAFWT---ETLFPNFsdaakstYRLFAVDLLGFGRSPKP 249

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356582507 105 RPHQYSIFEQASIVE-SLLRHLGLqnRRINLLSHDYGDIVAQELLYRYKQnrsgrlTIKSLCL 166
Cdd:PLN03087 250 ADSLYTLREHLEMIErSVLERYKV--KSFHIVAHSLGCILALALAVKHPG------AVKSLTL 304
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 63-152 2.88e-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: 44.39  E-value: 2.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507   63 VVLLHGFPTSSYDWykiwEGLTLRFHRVIALDFLGFGFSDKPRPHqysiFEQASIVESLLRHLGLQNRRInLLSHDYGDI 142
Cdd:pfam12697   1 VVLVHGAGLSAAPL----AALLAAGVAVLAPDLPGHGSSSPPPLD----LADLADLAALLDELGAARPVV-LVGHSLGGA 71

                          90
                  ....*....|
gi 356582507  143 VAQELLYRYK 152
Cdd:pfam12697  72 VALAAAAAAL 81
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 58-192 2.32e-03

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 39.16  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507  58 GSPEIVVLLHGFPTSSYDWYKIWEGLTlRFHRVIALDFLGFGFSDKpRPHQYSIFEQASIVESLLRHLGLQnrRINLLSH 137
Cdd:PRK14875 129 GDGTPVVLIHGFGGDLNNWLFNHAALA-AGRPVIALDLPGHGASSK-AVGAGSLDELAAAVLAFLDALGIE--RAHLVGH 204

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356582507 138 DYGDIVAQELLyrykQNRSGRltIKSLCL-SNGGIFPE-------------THRPL--LLQKLLKDGGVLS 192
Cdd:PRK14875 205 SMGGAVALRLA----ARAPQR--VASLTLiAPAGLGPEingdyidgfvaaeSRRELkpVLELLFADPALVT 269
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 39-111 4.21e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 38.67  E-value: 4.21e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356582507  39 KFFTYKGL-RIFY--QDSVGVVGSPEIVVLLHGFPTSSYDWYKIWEGLTlRFHRVIALDFLGFGFSDKPRPHQYSI 111
Cdd:PLN02679  64 KKWKWKGEySINYlvKGSPEVTSSGPPVLLVHGFGASIPHWRRNIGVLA-KNYTVYAIDLLGFGASDKPPGFSYTM 138
PRK08775 PRK08775
homoserine O-succinyltransferase;
46-163 4.93e-03

homoserine O-succinyltransferase;


Pssm-ID: 181553 [Multi-domain]  Cd Length: 343  Bit Score: 38.23  E-value: 4.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507  46 LRIFYQdSVGVVGSPEIVVL--------LHGFPTSSYD-WykiWEGLT-------LRFHRVIALDFLGfgfSDKPRPHQY 109
Cdd:PRK08775  46 LRLRYE-LIGPAGAPVVFVAggisahrhVAATATFPEKgW---WEGLVgsgraldPARFRLLAFDFIG---ADGSLDVPI 118

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 356582507 110 SIFEQASIVESLLRHLGLQnRRINLLSHDYGDIVAQELLYRYKQnRSGRLTIKS 163
Cdd:PRK08775 119 DTADQADAIALLLDALGIA-RLHAFVGYSYGALVGLQFASRHPA-RVRTLVVVS 170
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 62-198 8.95e-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: 37.19  E-value: 8.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507   62 IVVLLHGFpTSSYDWY-KIWEGLTLRFHRVIALDFLGFGFSDKPRPHQYSIFEQASIVESLLRHLGLQNRRIN--LLSHD 138
Cdd:pfam12146   6 VVVLVHGL-GEHSGRYaHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPlfLLGHS 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582507  139 YGDIVAQELLYRYKQNrsgrltIKSLCLSNGGIFPETHRPLLLQKLLkdGGVLSPILTRL 198
Cdd:pfam12146  85 MGGLIAALYALRYPDK------VDGLILSAPALKIKPYLAPPILKLL--AKLLGKLFPRL 136
 
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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