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Conserved domains on  [gi|1831627243|ref|XP_033280570|]
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monoacylglycerol lipase ABHD6 [Orcinus orca]

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

 Zoom to residue level

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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, ...
 51-327 4.18e-40

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: 140.52  E-value: 4.18e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243  51 RYVRHEDYQFCYSFRGRPGnkPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQ 130
Cdd:COG0596     5 RFVTVDGVRLHYREAGPDG--PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGH-GRSDKPAGGYTLDDLADDLAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 131 FVEclKLNKKPFHLIGTSMGGHVAGVYAAHYPSDVCSLSLVcpaglqystdNQFVQRLKElqesaavekiplipstpeem 210
Cdd:COG0596    82 LLD--ALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV----------DEVLAALAE-------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 211 semlqlcsyvrfrvpqqilqglvdvRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLA 290
Cdd:COG0596   130 -------------------------PLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLA 184

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1831627243 291 KSIANCQVELLENCGHSVVMERPRKTAKLIVDFLASV 327
Cdd:COG0596   185 ELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 51-327 4.18e-40

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: 140.52  E-value: 4.18e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243  51 RYVRHEDYQFCYSFRGRPGnkPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQ 130
Cdd:COG0596     5 RFVTVDGVRLHYREAGPDG--PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGH-GRSDKPAGGYTLDDLADDLAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 131 FVEclKLNKKPFHLIGTSMGGHVAGVYAAHYPSDVCSLSLVcpaglqystdNQFVQRLKElqesaavekiplipstpeem 210
Cdd:COG0596    82 LLD--ALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV----------DEVLAALAE-------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 211 semlqlcsyvrfrvpqqilqglvdvRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLA 290
Cdd:COG0596   130 -------------------------PLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLA 184

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1831627243 291 KSIANCQVELLENCGHSVVMERPRKTAKLIVDFLASV 327
Cdd:COG0596   185 ELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 62-327 5.18e-30

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 117.35  E-value: 5.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243  62 YSFRGrPGNKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKp 141
Cdd:PRK14875  123 YLRLG-EGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGH-GASSKAVGAGSLDELAAAVLAFLDALGIERA- 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 142 fHLIGTSMGGHVAGVYAAHYPSDVCSLSLVCPAGLQYSTDNQFVQRLKELQESAAVEkiPLIpstpeemsEMLqlcsyvr 221
Cdd:PRK14875  200 -HLVGHSMGGAVALRLAARAPQRVASLTLIAPAGLGPEINGDYIDGFVAAESRRELK--PVL--------ELL------- 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 222 FRVPQQILQGLVD--VRiphnnfYRKL-----FLEIVSE------KSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADM 288
Cdd:PRK14875  262 FADPALVTRQMVEdlLK------YKRLdgvddALRALADalfaggRQRVDLRDRLASLAIPVLVIWGEQDRIIPAAHAQG 335

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1831627243 289 LAksiANCQVELLENCGHSVVMERPRKTAKLIVDFLASV 327
Cdd:PRK14875  336 LP---DGVAVHVLPGAGHMPQMEAAADVNRLLAEFLGKA 371
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 72-313 2.01e-27

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: 107.59  E-value: 2.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243  72 PSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGH-EGTTRSSLDDLSIDGQVKRIHQFVEclKLNKKPFHLIGTSM 149
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFgKSSRPKAQDDYRTDDLAEDLEYILE--ALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 150 GGHVAGVYAAHYPSDVCSLSLVCPAGLQYSTDNQFVQRLKELQES-----AAVEKIPLIPSTPEEMSEmLQLCSYVRFRV 224
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFfdgfvADFAPNPLGRLVAKLLAL-LLLRLRLLKAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 225 PQQILQGLVDVRIPHNN--FYRKLFLEIVSEKSRYSLHQNmdkIKVPTQIIWGKQDQVLDVSGADMLAKSIANCQVELLE 302
Cdd:pfam00561 158 PLLNKRFPSGDYALAKSlvTGALLFIETWSTELRAKFLGR---LDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIP 234

                         250
                  ....*....|.
gi 1831627243 303 NCGHSVVMERP 313
Cdd:pfam00561 235 DAGHFAFLEGP 245
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 70-324 5.82e-21

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 274729 [Multi-domain]  Cd Length: 252  Bit Score: 90.35  E-value: 5.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243  70 NKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDL--SIDGQVKRI-HQFVEclKLNKKPFHLIG 146
Cdd:TIGR03695   1 AKPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGH-GSSQSPSDIEryDFEEAAQLLlATLLD--QLGIEPFFLVG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 147 TSMGGHVAGVYAAHYPSDVCSLSLV-CPAGLQ--------YSTDNQFVQRLkeLQESAAV-----EKIPLIpSTPEEMse 212
Cdd:TIGR03695  78 YSMGGRIALYYALQYPERVQGLILEsGSPGLQteeeraarRQNDEQLAQRF--EQEGLEAflddwYQQPLF-ASQKNL-- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 213 mlqlcsyvrfrvPQQILQGLVDVRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMlAKS 292
Cdd:TIGR03695 153 ------------PPEQRQALRAERLANNPEGLAKMLRATGLGKQPSLWPKLQALKIPVLYLCGERDEKFVQIAKEM-QKL 219

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1831627243 293 IANCQVELLENCGHSVVMERPRKTAKLIVDFL 324
Cdd:TIGR03695 220 IPNLTLHIIPNAGHNIHLENPEAFAKILLAFL 251
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 51-327 4.18e-40

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: 140.52  E-value: 4.18e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243  51 RYVRHEDYQFCYSFRGRPGnkPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQ 130
Cdd:COG0596     5 RFVTVDGVRLHYREAGPDG--PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGH-GRSDKPAGGYTLDDLADDLAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 131 FVEclKLNKKPFHLIGTSMGGHVAGVYAAHYPSDVCSLSLVcpaglqystdNQFVQRLKElqesaavekiplipstpeem 210
Cdd:COG0596    82 LLD--ALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV----------DEVLAALAE-------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 211 semlqlcsyvrfrvpqqilqglvdvRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLA 290
Cdd:COG0596   130 -------------------------PLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLA 184

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1831627243 291 KSIANCQVELLENCGHSVVMERPRKTAKLIVDFLASV 327
Cdd:COG0596   185 ELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 62-327 5.18e-30

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 117.35  E-value: 5.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243  62 YSFRGrPGNKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKp 141
Cdd:PRK14875  123 YLRLG-EGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGH-GASSKAVGAGSLDELAAAVLAFLDALGIERA- 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 142 fHLIGTSMGGHVAGVYAAHYPSDVCSLSLVCPAGLQYSTDNQFVQRLKELQESAAVEkiPLIpstpeemsEMLqlcsyvr 221
Cdd:PRK14875  200 -HLVGHSMGGAVALRLAARAPQRVASLTLIAPAGLGPEINGDYIDGFVAAESRRELK--PVL--------ELL------- 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 222 FRVPQQILQGLVD--VRiphnnfYRKL-----FLEIVSE------KSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADM 288
Cdd:PRK14875  262 FADPALVTRQMVEdlLK------YKRLdgvddALRALADalfaggRQRVDLRDRLASLAIPVLVIWGEQDRIIPAAHAQG 335

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1831627243 289 LAksiANCQVELLENCGHSVVMERPRKTAKLIVDFLASV 327
Cdd:PRK14875  336 LP---DGVAVHVLPGAGHMPQMEAAADVNRLLAEFLGKA 371
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 72-313 2.01e-27

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: 107.59  E-value: 2.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243  72 PSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGH-EGTTRSSLDDLSIDGQVKRIHQFVEclKLNKKPFHLIGTSM 149
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFgKSSRPKAQDDYRTDDLAEDLEYILE--ALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 150 GGHVAGVYAAHYPSDVCSLSLVCPAGLQYSTDNQFVQRLKELQES-----AAVEKIPLIPSTPEEMSEmLQLCSYVRFRV 224
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFfdgfvADFAPNPLGRLVAKLLAL-LLLRLRLLKAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 225 PQQILQGLVDVRIPHNN--FYRKLFLEIVSEKSRYSLHQNmdkIKVPTQIIWGKQDQVLDVSGADMLAKSIANCQVELLE 302
Cdd:pfam00561 158 PLLNKRFPSGDYALAKSlvTGALLFIETWSTELRAKFLGR---LDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIP 234

                         250
                  ....*....|.
gi 1831627243 303 NCGHSVVMERP 313
Cdd:pfam00561 235 DAGHFAFLEGP 245
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
60-326 1.24e-24

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 99.69  E-value: 1.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243  60 FCYSFRGRPGNKPSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGHEGTTRSSLDDLSIDGQVKRIHQFVECLK-L 137
Cdd:COG2267    17 RGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDALRaR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 138 NKKPFHLIGTSMGGHVAGVYAAHYPSDVCSLSLVCPAglqYSTDnqfvqrlkelqesaavekiPLIPSTPEEMSEMLqlc 217
Cdd:COG2267    97 PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPA---YRAD-------------------PLLGPSARWLRALR--- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 218 syvrfrvpqqilqglvdvriphnnfyrklfleivseksrysLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSIA-NC 296
Cdd:COG2267   152 -----------------------------------------LAEALARIDVPVLVLHGGADRVVPPEAARRLAARLSpDV 190

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1831627243 297 QVELLENCGHSVVMERPRKTA-KLIVDFLAS 326
Cdd:COG2267   191 ELVLLPGARHELLNEPAREEVlAAILAWLER 221
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
68-329 8.27e-22

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 92.31  E-value: 8.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243  68 PGNKPSILMLHGFSAHKdmwlSVVKFLPKNLH-----LVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKPF 142
Cdd:COG1647    12 EGGRKGVLLLHGFTGSP----AEMRPLAEALAkagytVYAPRLPGH-GTSPEDLLKTTWEDWLEDVEEAYEILKAGYDKV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 143 HLIGTSMGGHVAGVYAAHYPsDVCSLSLVCPAgLQYSTDNQFVQRLKELqesaAVEKIPLIPSTPEEmsemLQLCSYVRF 222
Cdd:COG1647    87 IVIGLSMGGLLALLLAARYP-DVAGLVLLSPA-LKIDDPSAPLLPLLKY----LARSLRGIGSDIED----PEVAEYAYD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 223 RVPQQILQglvdvriphnNFYRklFLEIVSEksryslhqNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSIANCQVEL-- 300
Cdd:COG1647   157 RTPLRALA----------ELQR--LIREVRR--------DLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELvw 216

                         250       260       270
                  ....*....|....*....|....*....|
gi 1831627243 301 LENCGHSVVMERPRKT-AKLIVDFLASVHS 329
Cdd:COG1647   217 LEDSGHVITLDKDREEvAEEILDFLERLAA 246
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 70-324 5.82e-21

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 274729 [Multi-domain]  Cd Length: 252  Bit Score: 90.35  E-value: 5.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243  70 NKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDL--SIDGQVKRI-HQFVEclKLNKKPFHLIG 146
Cdd:TIGR03695   1 AKPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGH-GSSQSPSDIEryDFEEAAQLLlATLLD--QLGIEPFFLVG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 147 TSMGGHVAGVYAAHYPSDVCSLSLV-CPAGLQ--------YSTDNQFVQRLkeLQESAAV-----EKIPLIpSTPEEMse 212
Cdd:TIGR03695  78 YSMGGRIALYYALQYPERVQGLILEsGSPGLQteeeraarRQNDEQLAQRF--EQEGLEAflddwYQQPLF-ASQKNL-- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 213 mlqlcsyvrfrvPQQILQGLVDVRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMlAKS 292
Cdd:TIGR03695 153 ------------PPEQRQALRAERLANNPEGLAKMLRATGLGKQPSLWPKLQALKIPVLYLCGERDEKFVQIAKEM-QKL 219

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1831627243 293 IANCQVELLENCGHSVVMERPRKTAKLIVDFL 324
Cdd:TIGR03695 220 IPNLTLHIIPNAGHNIHLENPEAFAKILLAFL 251
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 74-319 3.10e-11

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 62.11  E-value: 3.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243  74 ILMLHGFSAHKDmwlSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSidgQVKRIHQFVECLKlNKKPFHLIGTSMGGHV 153
Cdd:pfam12697   1 VVLVHGAGLSAA---PLAALLAAGVAVLAPDLPGH-GSSSPPPLDLA---DLADLAALLDELG-AARPVVLVGHSLGGAV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 154 AGVYAAHYPSDVCslsLVCPAGLQYSTDNQFVQRLKELQESAAVEKIPLIPSTPEEMSEMLQLCSYVRFRVPQQILQGLV 233
Cdd:pfam12697  73 ALAAAAAALVVGV---LVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALLAA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 234 DVRIPHNNFyrklfleivseksryslhqnmDKIKVPTQIIWGkQDQVLDvSGADMLAKSIANCQVELLENCGHSvVMERP 313
Cdd:pfam12697 150 LALLPLAAW---------------------RDLPVPVLVLAE-EDRLVP-ELAQRLLAALAGARLVVLPGAGHL-PLDDP 205


                  ....*.
gi 1831627243 314 RKTAKL 319
Cdd:pfam12697 206 EEVAEA 211
PLN02578 PLN02578
hydrolase
 9-326 1.15e-10

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 61.78  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243   9 FVIAGGTLAIPILAFVASFLLWP-SALIRI-------YYWYWRralGMQVRYVRHedyqfcysfrgrpGNKPSILMLHGF 80
Cdd:PLN02578   32 IFIFGGIVASGVSVMGSSSASQSvQGLERLpfkkegyNFWTWR---GHKIHYVVQ-------------GEGLPIVLIHGF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243  81 SAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLddLSIDGQVKRiHQFVECLK-LNKKPFHLIGTSMGGHVAGVYAA 159
Cdd:PLN02578   96 GASAFHWRYNIPELAKKYKVYALDLLGF-GWSDKAL--IEYDAMVWR-DQVADFVKeVVKEPAVLVGNSLGGFTALSTAV 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 160 HYPSDVCSLSLVCPAGlqystdnQFVQRLKELQESAAVEKIPLIPSTPEEMSEMLQ----LCSYVRFRVPQQILQGLVDV 235
Cdd:PLN02578  172 GYPELVAGVALLNSAG-------QFGSESREKEEAIVVEETVLTRFVVKPLKEWFQrvvlGFLFWQAKQPSRIESVLKSV 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 236 RIPHNN---------------------FYRkLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSIA 294
Cdd:PLN02578  245 YKDKSNvddylvesitepaadpnagevYYR-LMSRFLFNQSRYTLDSLLSKLSCPLLLLWGDLDPWVGPAKAEKIKAFYP 323

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1831627243 295 NCQVELLEnCGHSVVMERPRKTAKLIVDFLAS 326
Cdd:PLN02578  324 DTTLVNLQ-AGHCPHDEVPEQVNKALLEWLSS 354
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 71-312 1.21e-10

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: 60.69  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243  71 KPSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGH---EGTTR--SSLDDLsidgqVKRIHQFVECLKLN--KKPF 142
Cdd:pfam12146   4 RAVVVLVHGLGEHSGRYAHLADALAAQgFAVYAYDHRGHgrsDGKRGhvPSFDDY-----VDDLDTFVDKIREEhpGLPL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 143 HLIGTSMGGHVAGVYAAHYPSDVCSLSLVCPA-GLQYSTDNQFVQRLKELQESAAVEKIPLIPSTPEEMS---EMLQLC- 217
Cdd:pfam12146  79 FLLGHSMGGLIAALYALRYPDKVDGLILSAPAlKIKPYLAPPILKLLAKLLGKLFPRLRVPNNLLPDSLSrdpEVVAAYa 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 218 --SYVRFRVPQQILQGLVDVRIphnnfyrklfleivseksrySLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSI-- 293
Cdd:pfam12146 159 adPLVHGGISARTLYELLDAGE--------------------RLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAgs 218

                         250
                  ....*....|....*....
gi 1831627243 294 ANCQVELLENCGHSVVMER 312
Cdd:pfam12146 219 TDKTLKLYPGLYHELLNEP 237
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
 62-325 2.33e-10

3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]


Pssm-ID: 131480 [Multi-domain]  Cd Length: 251  Bit Score: 60.06  E-value: 2.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243  62 YSFRGRPGNKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGH----EGTTRSSLDDLSIDgqvkrihqfVECL-- 135
Cdd:TIGR02427   4 YRLDGAADGAPVLVFINSLGTDLRMWDPVLPALTPDFRVLRYDKRGHglsdAPEGPYSIEDLADD---------VLALld 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 136 KLNKKPFHLIGTSMGGHVAGVYAAHYPSDVCSLSLVCPAGlQYSTDNQFVQRLkelqesAAVEKiplipstpEEMSEMLQ 215
Cdd:TIGR02427  75 HLGIERAVFCGLSLGGLIAQGLAARRPDRVRALVLSNTAA-KIGTPESWNARI------AAVRA--------EGLAALAD 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 216 lCSYVRFRVPqqilqglvDVRIPHN---NFYRKLFLEivSEKSRYSLH----QNMD------KIKVPTQIIWGKQDQVLD 282
Cdd:TIGR02427 140 -AVLERWFTP--------GFREAHParlDLYRNMLVR--QPPDGYAGCcaaiRDADfrdrlgAIAVPTLCIAGDQDGSTP 208

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1831627243 283 VSGADMLAKSIANCQVELLENCGHSVVMERPRKTAKLIVDFLA 325
Cdd:TIGR02427 209 PELVREIADLVPGARFAEIRGAGHIPCVEQPEAFNAALRDFLR 251
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 47-313 1.11e-08

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 56.07  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243  47 GMQVRYVRHEDYQFCY----SFRGRPgNKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHEGTTRSSLDDLSID 122
Cdd:PLN02894   78 GSKVRWFRSASNEPRFintvTFDSKE-DAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTCKSTE 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 123 -GQVKRIHQFVECLKL-NKKPFHLIGTSMGGHVAGVYAAHYPSDVCSLSLVCPAGlqystdnqfvqrlkelqesaaveki 200
Cdd:PLN02894  157 eTEAWFIDSFEEWRKAkNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAG------------------------- 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 201 plIPSTPEEMSEMLqlcsyVRFR----------------VPQQILQGL-----------VDVRIPHNN------------ 241
Cdd:PLN02894  212 --FSSESDDKSEWL-----TKFRatwkgavlnhlwesnfTPQKIIRGLgpwgpnlvrryTTARFGAHStgdilseeeskl 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 242 ----FYRKLFLEIVSEK-----------SRYSLHQNMDKIKVPTQIIWGKQDQvLDVSGADMLAKSI-ANCQVELLENCG 305
Cdd:PLN02894  285 ltdyVYHTLAAKASGELclkyifsfgafARKPLLESASEWKVPTTFIYGRHDW-MNYEGAVEARKRMkVPCEIIRVPQGG 363


                  ....*...
gi 1831627243 306 HSVVMERP 313
Cdd:PLN02894  364 HFVFLDNP 371
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 72-323 1.26e-08

pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273783 [Multi-domain]  Cd Length: 245  Bit Score: 54.82  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243  72 PSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHEGTTrsSLDDLSIDGQVKRIHQFVEclklnkKPFHLIGTSMGG 151
Cdd:TIGR01738   5 VHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSR--GFGPLSLADMAEAIAAQAP------DPAIWLGWSLGG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 152 HVAGVYAAHYPSDVCSLSLVC-----------PAGLQYSTDNQFVQRLK-ELQESaaVEKIPLIPS--TPEEMSEMLQLC 217
Cdd:TIGR01738  77 LVALHIAATHPDRVRALVTVAsspcfsaredwPEGIKPDVLTGFQQQLSdDYQRT--IERFLALQTlgTPTARQDARALK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 218 SYVRFR-VPQ-QILQGLVDVriphnnfyrklfleivseKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSIAN 295
Cdd:TIGR01738 155 QTLLARpTPNvQVLQAGLEI------------------LATVDLRQPLQNISVPFLRLYGYLDGLVPAKVVPMLDKLAPH 216

                         250       260
                  ....*....|....*....|....*...
gi 1831627243 296 CQVELLENCGHSVVMERPRKTAKLIVDF 323
Cdd:TIGR01738 217 SELYIFAKAAHAPFLSHAEAFCALLVAF 244
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
68-325 2.60e-08

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 53.87  E-value: 2.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243  68 PGNKPSILMLHGFSAHKD-MWLSVVKFLPKN-LHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKPFHLI 145
Cdd:COG1506    20 GKKYPVVVYVHGGPGSRDdSFLPLAQALASRgYAVLAPDYRGY-GESAGDWGGDEVDDVLAAIDYLAARPYVDPDRIGIY 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 146 GTSMGGHVAGVYAAHYPSDVCSLSLVCPA---GLQYSTDNQFVQRLKElqesaavekiplipsTPEEMSEMLQlcsyvrf 222
Cdd:COG1506    99 GHSYGGYMALLAAARHPDRFKAAVALAGVsdlRSYYGTTREYTERLMG---------------GPWEDPEAYA------- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 223 rvpqqilqglvdvriphnnfyrklfleivseksRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSI--ANCQVEL 300
Cdd:COG1506   157 ---------------------------------ARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALkkAGKPVEL 203

                         250       260
                  ....*....|....*....|....*..
gi 1831627243 301 L--ENCGHSVVMERPRKTAKLIVDFLA 325
Cdd:COG1506   204 LvyPGEGHGFSGAGAPDYLERILDFLD 230
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 70-160 4.19e-08

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 53.30  E-value: 4.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243  70 NKPSILMLHGFSAHKDMWLSVVKFLPKNlHLVCVDMPGHeGTTRssldDLSIDGQVKRIHQFVECLK-LNKKPFHLIGTS 148
Cdd:PRK11126    1 GLPWLVFLHGLLGSGQDWQPVGEALPDY-PRLYIDLPGH-GGSA----AISVDGFADVSRLLSQTLQsYNILPYWLVGYS 74

                          90
                  ....*....|..
gi 1831627243 149 MGGHVAGVYAAH 160
Cdd:PRK11126   75 LGGRIAMYYACQ 86
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 62-324 8.67e-07

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 49.53  E-value: 8.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243  62 YSFRGRPGNKPSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGH---EGTTRSSLDDLSIDgqvkrIHQFVEclKL 137
Cdd:COG1073    28 YLPAGASKKYPAVVVAHGNGGVKEQRALYAQRLAELgFNVLAFDYRGYgesEGEPREEGSPERRD-----ARAAVD--YL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 138 NKKPFH------LIGTSMGGHVAGVYAAHYPsDVCSLSLVCPAglqystdNQFVQRLKELQESAAVEKIPLIPSTPeems 211
Cdd:COG1073   101 RTLPGVdperigLLGISLGGGYALNAAATDP-RVKAVILDSPF-------TSLEDLAAQRAKEARGAYLPGVPYLP---- 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243 212 emlqlcsyvrfrvpqqilqglvdvRIPHNNFYRKLFleivseksrYSLHQnMDKIKVPTQIIWGKQDQVldVS---GADM 288
Cdd:COG1073   169 ------------------------NVRLASLLNDEF---------DPLAK-IEKISRPLLFIHGEKDEA--VPfymSEDL 212

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1831627243 289 LAKSIANCQVELLENCGHSVVMERPRKTA-KLIVDFL 324
Cdd:COG1073   213 YEAAAEPKELLIVPGAGHVDLYDRPEEEYfDKLAEFF 249
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 67-161 1.81e-04

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 40.20  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831627243  67 RPGNKPsILMLHGFSAHKDMWLSVVKFLPKNLHLVC-VDMPGHEGTTRSSLDDLsiDGQVKRIHQfveclKLNKKPFHLI 145
Cdd:COG1075     2 AATRYP-VVLVHGLGGSAASWAPLAPRLRAAGYPVYaLNYPSTNGSIEDSAEQL--AAFVDAVLA-----ATGAEKVDLV 73

                          90
                  ....*....|....*.
gi 1831627243 146 GTSMGGHVAGVYAAHY 161
Cdd:COG1075    74 GHSMGGLVARYYLKRL 89
 
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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