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Conserved domains on  [gi|57528148|ref|NP_001009617|]
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mesoderm-specific transcript homolog protein [Rattus norvegicus]

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 2.48e-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: 106.62  E-value: 2.48e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148  45 TSGKFFTYKGLRIFYQDSvGVVGSPeiVVLLHGFPTSSYDWYKIWEGLTLRFhRVIALDFLGFGFSDKPRPHqYSIFEQA 124
Cdd:COG0596   2 STPRFVTVDGVRLHYREA-GPDGPP--VVLLHGLPGSSYEWRPLIPALAAGY-RVIAPDLRGHGRSDKPAGG-YTLDDLA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148 125 SIVESLLRHLGLQnrRINLLSHDYGDIVAQELLYRYKQNrsgrltIKSLCLSNggifpETHRplLLQKLLKDGGVLSPIL 204
Cdd:COG0596  77 DDLAALLDALGLE--RVVLVGHSMGGMVALELAARHPER------VAGLVLVD-----EVLA--ALAEPLRRPGLAPEAL 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148 205 TRLMNFFVfsrgltpvfgpytrpteseLWDMWAgirnndgnlvidsllqyinqrkkfrrrwvgALASVTIPIHFIYGPLD 284
Cdd:COG0596 142 AALLRALA-------------------RTDLRE------------------------------RLARITVPTLVIWGEKD 172

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 57528148 285 PINPyPEFLELYRKTLPRSTVSILDDhISHYPQLEDPMGFLNAYMGFINS 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 2.48e-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: 106.62  E-value: 2.48e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148  45 TSGKFFTYKGLRIFYQDSvGVVGSPeiVVLLHGFPTSSYDWYKIWEGLTLRFhRVIALDFLGFGFSDKPRPHqYSIFEQA 124
Cdd:COG0596   2 STPRFVTVDGVRLHYREA-GPDGPP--VVLLHGLPGSSYEWRPLIPALAAGY-RVIAPDLRGHGRSDKPAGG-YTLDDLA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148 125 SIVESLLRHLGLQnrRINLLSHDYGDIVAQELLYRYKQNrsgrltIKSLCLSNggifpETHRplLLQKLLKDGGVLSPIL 204
Cdd:COG0596  77 DDLAALLDALGLE--RVVLVGHSMGGMVALELAARHPER------VAGLVLVD-----EVLA--ALAEPLRRPGLAPEAL 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148 205 TRLMNFFVfsrgltpvfgpytrpteseLWDMWAgirnndgnlvidsllqyinqrkkfrrrwvgALASVTIPIHFIYGPLD 284
Cdd:COG0596 142 AALLRALA-------------------RTDLRE------------------------------RLARITVPTLVIWGEKD 172

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 57528148 285 PINPyPEFLELYRKTLPRSTVSILDDhISHYPQLEDPMGFLNAYMGFINS 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 3.94e-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: 87.95  E-value: 3.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148    72 VVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKPR-PHQYSIFEQASIVESLLRHLGLQnrRINLLSHDYGD 150
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKaQDDYRTDDLAEDLEYILEALGLE--KVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148   151 IVAQELLYRYKQNrsgrltIKSLCLSNGGIFPETHRPLLLQKLLKD----GGVLSPILTRLMNFFV-FSRGLTPVFGPYT 225
Cdd:pfam00561  81 LIALAYAAKYPDR------VKALVLLGALDPPHELDEADRFILALFpgffDGFVADFAPNPLGRLVaKLLALLLLRLRLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148   226 RPTESELWDMWAGIRNNDGNLVIDSLLQYINQRKKFRRRWVGALAsvtIPIHFIYGPLDPINPyPEFLELYRKTLPRSTV 305
Cdd:pfam00561 155 KALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLD---EPTLIIWGDQDPLVP-PQALEKLAQLFPNARL 230

                         250
                  ....*....|....*.
gi 57528148   306 sILDDHISHYPQLEDP 321
Cdd:pfam00561 231 -VVIPDAGHFAFLEGP 245
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 48-149 8.79e-13

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 67.71  E-value: 8.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148   48 KFFTYKGLRIFYQDSvgvvGSPEIVVLLHGFPTSSYDWYKIWEGLTlRFHRVIALDFLGFGFSDKPrPHQYSIFEQASIV 127
Cdd:PRK03592  10 RRVEVLGSRMAYIET----GEGDPIVFLHGNPTSSYLWRNIIPHLA-GLGRCLAPDLIGMGASDKP-DIDYTFADHARYL 83

                         90       100
                 ....*....|....*....|..
gi 57528148  128 ESLLRHLGLqnRRINLLSHDYG 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 2.48e-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: 106.62  E-value: 2.48e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148  45 TSGKFFTYKGLRIFYQDSvGVVGSPeiVVLLHGFPTSSYDWYKIWEGLTLRFhRVIALDFLGFGFSDKPRPHqYSIFEQA 124
Cdd:COG0596   2 STPRFVTVDGVRLHYREA-GPDGPP--VVLLHGLPGSSYEWRPLIPALAAGY-RVIAPDLRGHGRSDKPAGG-YTLDDLA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148 125 SIVESLLRHLGLQnrRINLLSHDYGDIVAQELLYRYKQNrsgrltIKSLCLSNggifpETHRplLLQKLLKDGGVLSPIL 204
Cdd:COG0596  77 DDLAALLDALGLE--RVVLVGHSMGGMVALELAARHPER------VAGLVLVD-----EVLA--ALAEPLRRPGLAPEAL 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148 205 TRLMNFFVfsrgltpvfgpytrpteseLWDMWAgirnndgnlvidsllqyinqrkkfrrrwvgALASVTIPIHFIYGPLD 284
Cdd:COG0596 142 AALLRALA-------------------RTDLRE------------------------------RLARITVPTLVIWGEKD 172

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 57528148 285 PINPyPEFLELYRKTLPRSTVSILDDhISHYPQLEDPMGFLNAYMGFINS 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 3.94e-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: 87.95  E-value: 3.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148    72 VVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKPR-PHQYSIFEQASIVESLLRHLGLQnrRINLLSHDYGD 150
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKaQDDYRTDDLAEDLEYILEALGLE--KVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148   151 IVAQELLYRYKQNrsgrltIKSLCLSNGGIFPETHRPLLLQKLLKD----GGVLSPILTRLMNFFV-FSRGLTPVFGPYT 225
Cdd:pfam00561  81 LIALAYAAKYPDR------VKALVLLGALDPPHELDEADRFILALFpgffDGFVADFAPNPLGRLVaKLLALLLLRLRLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148   226 RPTESELWDMWAGIRNNDGNLVIDSLLQYINQRKKFRRRWVGALAsvtIPIHFIYGPLDPINPyPEFLELYRKTLPRSTV 305
Cdd:pfam00561 155 KALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLD---EPTLIIWGDQDPLVP-PQALEKLAQLFPNARL 230

                         250
                  ....*....|....*.
gi 57528148   306 sILDDHISHYPQLEDP 321
Cdd:pfam00561 231 -VVIPDAGHFAFLEGP 245
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 48-149 8.79e-13

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 67.71  E-value: 8.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148   48 KFFTYKGLRIFYQDSvgvvGSPEIVVLLHGFPTSSYDWYKIWEGLTlRFHRVIALDFLGFGFSDKPrPHQYSIFEQASIV 127
Cdd:PRK03592  10 RRVEVLGSRMAYIET----GEGDPIVFLHGNPTSSYLWRNIIPHLA-GLGRCLAPDLIGMGASDKP-DIDYTFADHARYL 83

                         90       100
                 ....*....|....*....|..
gi 57528148  128 ESLLRHLGLqnRRINLLSHDYG 149
Cdd:PRK03592  84 DAWFDALGL--DDVVLVGHDWG 103
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 56-154 4.87e-11

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 63.36  E-value: 4.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148   56 RIFYQDSvGVVGSPEiVVLLHGFPTSSYDWYKIWEGLTLRFHrVIALDFLGFGFSDKPRP---HQYSIFEQASIVESLlr 132
Cdd:PLN03084 116 RWFCVES-GSNNNPP-VLLIHGFPSQAYSYRKVLPVLSKNYH-AIAFDWLGFGFSDKPQPgygFNYTLDEYVSSLESL-- 190

                         90       100
                 ....*....|....*....|..
gi 57528148  133 hlglqnrrINLLSHDYGDIVAQ 154
Cdd:PLN03084 191 --------IDELKSDKVSLVVQ 204
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 31-149 1.16e-10

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 61.41  E-value: 1.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148   31 IPPPQLSPALHSWktsgkfFTYKGLRIFYQDSvgvvGSPEIVVLLHGFPTSSYDWYKIWEGLTLRFhRVIALDFLGFGFS 110
Cdd:PRK03204   6 TPDPQLYPFESRW------FDSSRGRIHYIDE----GTGPPILLCHGNPTWSFLYRDIIVALRDRF-RCVAPDYLGFGLS 74

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 57528148  111 DKPRPHQYSIFEQASIVESLLRHLGLQNrrINLLSHDYG 149
Cdd:PRK03204  75 ERPSGFGYQIDEHARVIGEFVDHLGLDR--YLSMGQDWG 111
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 70-152 5.37e-09

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 56.52  E-value: 5.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148   70 EIVVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKP-RPHQYSIFEQASIVESLLRHLGLQNrrINLLSHDY 148
Cdd:PRK00870  47 PPVLLLHGEPSWSYLYRKMIPILAAAGHRVIAPDLIGFGRSDKPtRREDYTYARHVEWMRSWFEQLDLTD--VTLVCQDW 124


                 ....
gi 57528148  149 GDIV 152
Cdd:PRK00870 125 GGLI 128
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 32-117 1.23e-08

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 55.51  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148   32 PPPQLSPALHSWKtsgkfftYKGLRIFYQDSVGvvgSPEIVVLLHGFPTSSYDWYKIWEGLTLRfHRVIALDFLGFGFSD 111
Cdd:PLN02824   2 VKPEPQVETRTWR-------WKGYNIRYQRAGT---SGPALVLVHGFGGNADHWRKNTPVLAKS-HRVYAIDLLGYGYSD 70


                 ....*.
gi 57528148  112 KPRPHQ 117
Cdd:PLN02824  71 KPNPRS 76
PLN02578 PLN02578
hydrolase
 21-112 4.88e-08

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 53.69  E-value: 4.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148   21 AVPLLAAYLHIPPPQLSPALHSWKTSGKFFTYKGLRIFYqdsvgVV---GSPeiVVLLHGFPTSSYDW-YKIWEglTLRF 96
Cdd:PLN02578  42 GVSVMGSSSASQSVQGLERLPFKKEGYNFWTWRGHKIHY-----VVqgeGLP--IVLIHGFGASAFHWrYNIPE--LAKK 112

                         90
                 ....*....|....*.
gi 57528148   97 HRVIALDFLGFGFSDK 112
Cdd:PLN02578 113 YKVYALDLLGFGWSDK 128
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
44-160 1.78e-07

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 51.16  E-value: 1.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148  44 KTSGKFFTYKGLRIFYQDSVGVVGSPEIVVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKPRPHQYSIFEQ 123
Cdd:COG2267   3 RRLVTLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDY 82

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 57528148 124 ASIVESLLRHLGLQ-NRRINLLSHDYGDIVAQELLYRY 160
Cdd:COG2267  83 VDDLRAALDALRARpGLPVVLLGHSMGGLIALLYAARY 120
PRK05855 PRK05855
SDR family oxidoreductase;
54-159 1.40e-06

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 49.59  E-value: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148   54 GLRIfyqdSVGVVGSPE--IVVLLHGFPTSSYDWYKIWEGLTLRFHrVIALDFLGFGFSDKPRP-HQYSIFEQASIVESL 130
Cdd:PRK05855  12 GVRL----AVYEWGDPDrpTVVLVHGYPDNHEVWDGVAPLLADRFR-VVAYDVRGAGRSSAPKRtAAYTLARLADDFAAV 86

                         90       100
                 ....*....|....*....|....*....
gi 57528148  131 LRHLGlQNRRINLLSHDYGDIVAQELLYR 159
Cdd:PRK05855  87 IDAVS-PDRPVHLLAHDWGSIQGWEAVTR 114
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 41-175 2.46e-06

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 49.04  E-value: 2.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148   41 HSWKTSGKfftyKGLRIFYQDSVGVvGSPEIVVLLHGFPTSSYDWYkiwEGLTLRF-------HRVIALDFLGFGFSDKP 113
Cdd:PLN03087 178 TSWLSSSN----ESLFVHVQQPKDN-KAKEDVLFIHGFISSSAFWT---ETLFPNFsdaakstYRLFAVDLLGFGRSPKP 249

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57528148  114 RPHQYSIFEQASIVE-SLLRHLGLqnRRINLLSHDYGDIVAQELLYRYKQnrsgrlTIKSLCL 175
Cdd:PLN03087 250 ADSLYTLREHLEMIErSVLERYKV--KSFHIVAHSLGCILALALAVKHPG------AVKSLTL 304
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 72-161 2.81e-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: 2.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148    72 VVLLHGFPTSSYDWykiwEGLTLRFHRVIALDFLGFGFSDKPRPHqysiFEQASIVESLLRHLGLQNRRInLLSHDYGDI 151
Cdd:pfam12697   1 VVLVHGAGLSAAPL----AALLAAGVAVLAPDLPGHGSSSPPPLD----LADLADLAALLDELGAARPVV-LVGHSLGGA 71

                          90
                  ....*....|
gi 57528148   152 VAQELLYRYK 161
Cdd:pfam12697  72 VALAAAAAAL 81
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 67-201 2.43e-03

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 39.16  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148   67 GSPEIVVLLHGFPTSSYDWYKIWEGLTlRFHRVIALDFLGFGFSDKpRPHQYSIFEQASIVESLLRHLGLQnrRINLLSH 146
Cdd:PRK14875 129 GDGTPVVLIHGFGGDLNNWLFNHAALA-AGRPVIALDLPGHGASSK-AVGAGSLDELAAAVLAFLDALGIE--RAHLVGH 204

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57528148  147 DYGDIVAQELLyrykQNRSGRltIKSLCL-SNGGIFPE-------------THRPL--LLQKLLKDGGVLS 201
Cdd:PRK14875 205 SMGGAVALRLA----ARAPQR--VASLTLiAPAGLGPEingdyidgfvaaeSRRELkpVLELLFADPALVT 269
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 48-120 4.32e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 38.67  E-value: 4.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57528148   48 KFFTYKGL-RIFY--QDSVGVVGSPEIVVLLHGFPTSSYDWYKIWEGLTlRFHRVIALDFLGFGFSDKPRPHQYSI 120
Cdd:PLN02679  64 KKWKWKGEySINYlvKGSPEVTSSGPPVLLVHGFGASIPHWRRNIGVLA-KNYTVYAIDLLGFGASDKPPGFSYTM 138
PRK08775 PRK08775
homoserine O-succinyltransferase;
55-172 4.76e-03

homoserine O-succinyltransferase;


Pssm-ID: 181553 [Multi-domain]  Cd Length: 343  Bit Score: 38.23  E-value: 4.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148   55 LRIFYQdSVGVVGSPEIVVL--------LHGFPTSSYD-WykiWEGLT-------LRFHRVIALDFLGfgfSDKPRPHQY 118
Cdd:PRK08775  46 LRLRYE-LIGPAGAPVVFVAggisahrhVAATATFPEKgW---WEGLVgsgraldPARFRLLAFDFIG---ADGSLDVPI 118

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 57528148  119 SIFEQASIVESLLRHLGLQnRRINLLSHDYGDIVAQELLYRYKQnRSGRLTIKS 172
Cdd:PRK08775 119 DTADQADAIALLLDALGIA-RLHAFVGYSYGALVGLQFASRHPA-RVRTLVVVS 170
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 71-207 9.08e-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: 9.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148    71 IVVLLHGFpTSSYDWY-KIWEGLTLRFHRVIALDFLGFGFSDKPRPHQYSIFEQASIVESLLRHLGLQNRRIN--LLSHD 147
Cdd:pfam12146   6 VVVLVHGL-GEHSGRYaHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPlfLLGHS 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528148   148 YGDIVAQELLYRYKQNrsgrltIKSLCLSNGGIFPETHRPLLLQKLLkdGGVLSPILTRL 207
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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