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Conserved domains on  [gi|821389629|ref|XP_012387851|]
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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 821389629  51 RYVRHEDYQFCYSFRGRPGnkPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQ 130
Cdd:COG0596    5 RFVTVDGVRLHYREAGPDG--PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGH-GRSDKPAGGYTLDDLADDLAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 131 FVEclKLNKKPFHLIGTSMGGHVAGVYAAHYPSDVCSLSLVcpaglqystdNQFVQRLKElqesaavekiplipstpeem 210
Cdd:COG0596   82 LLD--ALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV----------DEVLAALAE-------------------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 211 semlqlcsyvrfrvpqqilqglvdvRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLA 290
Cdd:COG0596  130 -------------------------PLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLA 184
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 821389629 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 821389629  51 RYVRHEDYQFCYSFRGRPGnkPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQ 130
Cdd:COG0596    5 RFVTVDGVRLHYREAGPDG--PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGH-GRSDKPAGGYTLDDLADDLAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 131 FVEclKLNKKPFHLIGTSMGGHVAGVYAAHYPSDVCSLSLVcpaglqystdNQFVQRLKElqesaavekiplipstpeem 210
Cdd:COG0596   82 LLD--ALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV----------DEVLAALAE-------------------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 211 semlqlcsyvrfrvpqqilqglvdvRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLA 290
Cdd:COG0596  130 -------------------------PLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLA 184
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 821389629 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 821389629  62 YSFRGrPGNKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKp 141
Cdd:PRK14875 123 YLRLG-EGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGH-GASSKAVGAGSLDELAAAVLAFLDALGIERA- 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 142 fHLIGTSMGGHVAGVYAAHYPSDVCSLSLVCPAGLQYSTDNQFVQRLKELQESAAVEkiPLIpstpeemsEMLqlcsyvr 221
Cdd:PRK14875 200 -HLVGHSMGGAVALRLAARAPQRVASLTLIAPAGLGPEINGDYIDGFVAAESRRELK--PVL--------ELL------- 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 222 FRVPQQILQGLVD--VRiphnnfYRKL-----FLEIVSE------KSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADM 288
Cdd:PRK14875 262 FADPALVTRQMVEdlLK------YKRLdgvddALRALADalfaggRQRVDLRDRLASLAIPVLVIWGEQDRIIPAAHAQG 335
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 821389629 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 821389629   72 PSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGH-EGTTRSSLDDLSIDGQVKRIHQFVEclKLNKKPFHLIGTSM 149
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFgKSSRPKAQDDYRTDDLAEDLEYILE--ALGLEKVNLVGHSM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629  150 GGHVAGVYAAHYPSDVCSLSLVCPAGLQYSTDNQFVQRLKELQES-----AAVEKIPLIPSTPEEMSEmLQLCSYVRFRV 224
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFfdgfvADFAPNPLGRLVAKLLAL-LLLRLRLLKAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629  225 PQQILQGLVDVRIPHNN--FYRKLFLEIVSEKSRYSLHQNmdkIKVPTQIIWGKQDQVLDVSGADMLAKSIANCQVELLE 302
Cdd:pfam00561 158 PLLNKRFPSGDYALAKSlvTGALLFIETWSTELRAKFLGR---LDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIP 234
                         250
                  ....*....|.
gi 821389629  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 821389629   70 NKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDL--SIDGQVKRI-HQFVEclKLNKKPFHLIG 146
Cdd:TIGR03695   1 AKPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGH-GSSQSPSDIEryDFEEAAQLLlATLLD--QLGIEPFFLVG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629  147 TSMGGHVAGVYAAHYPSDVCSLSLV-CPAGLQ--------YSTDNQFVQRLkeLQESAAV-----EKIPLIpSTPEEMse 212
Cdd:TIGR03695  78 YSMGGRIALYYALQYPERVQGLILEsGSPGLQteeeraarRQNDEQLAQRF--EQEGLEAflddwYQQPLF-ASQKNL-- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629  213 mlqlcsyvrfrvPQQILQGLVDVRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMlAKS 292
Cdd:TIGR03695 153 ------------PPEQRQALRAERLANNPEGLAKMLRATGLGKQPSLWPKLQALKIPVLYLCGERDEKFVQIAKEM-QKL 219
                         250       260       270
                  ....*....|....*....|....*....|..
gi 821389629  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 821389629  51 RYVRHEDYQFCYSFRGRPGnkPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQ 130
Cdd:COG0596    5 RFVTVDGVRLHYREAGPDG--PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGH-GRSDKPAGGYTLDDLADDLAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 131 FVEclKLNKKPFHLIGTSMGGHVAGVYAAHYPSDVCSLSLVcpaglqystdNQFVQRLKElqesaavekiplipstpeem 210
Cdd:COG0596   82 LLD--ALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV----------DEVLAALAE-------------------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 211 semlqlcsyvrfrvpqqilqglvdvRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLA 290
Cdd:COG0596  130 -------------------------PLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLA 184
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 821389629 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 821389629  62 YSFRGrPGNKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKp 141
Cdd:PRK14875 123 YLRLG-EGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGH-GASSKAVGAGSLDELAAAVLAFLDALGIERA- 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 142 fHLIGTSMGGHVAGVYAAHYPSDVCSLSLVCPAGLQYSTDNQFVQRLKELQESAAVEkiPLIpstpeemsEMLqlcsyvr 221
Cdd:PRK14875 200 -HLVGHSMGGAVALRLAARAPQRVASLTLIAPAGLGPEINGDYIDGFVAAESRRELK--PVL--------ELL------- 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 222 FRVPQQILQGLVD--VRiphnnfYRKL-----FLEIVSE------KSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADM 288
Cdd:PRK14875 262 FADPALVTRQMVEdlLK------YKRLdgvddALRALADalfaggRQRVDLRDRLASLAIPVLVIWGEQDRIIPAAHAQG 335
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 821389629 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 821389629   72 PSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGH-EGTTRSSLDDLSIDGQVKRIHQFVEclKLNKKPFHLIGTSM 149
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFgKSSRPKAQDDYRTDDLAEDLEYILE--ALGLEKVNLVGHSM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629  150 GGHVAGVYAAHYPSDVCSLSLVCPAGLQYSTDNQFVQRLKELQES-----AAVEKIPLIPSTPEEMSEmLQLCSYVRFRV 224
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFfdgfvADFAPNPLGRLVAKLLAL-LLLRLRLLKAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629  225 PQQILQGLVDVRIPHNN--FYRKLFLEIVSEKSRYSLHQNmdkIKVPTQIIWGKQDQVLDVSGADMLAKSIANCQVELLE 302
Cdd:pfam00561 158 PLLNKRFPSGDYALAKSlvTGALLFIETWSTELRAKFLGR---LDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIP 234
                         250
                  ....*....|.
gi 821389629  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 821389629  60 FCYSFRGRPGNKPSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGHEGTTRSSLDDLSIDGQVKRIHQFVECLK-L 137
Cdd:COG2267   17 RGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDALRaR 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 138 NKKPFHLIGTSMGGHVAGVYAAHYPSDVCSLSLVCPAglqYSTDnqfvqrlkelqesaavekiPLIPSTPEEMSEMLqlc 217
Cdd:COG2267   97 PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPA---YRAD-------------------PLLGPSARWLRALR--- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 218 syvrfrvpqqilqglvdvriphnnfyrklfleivseksrysLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSIA-NC 296
Cdd:COG2267  152 -----------------------------------------LAEALARIDVPVLVLHGGADRVVPPEAARRLAARLSpDV 190
                        250       260       270
                 ....*....|....*....|....*....|.
gi 821389629 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 821389629  68 PGNKPSILMLHGFSAHKdmwlSVVKFLPKNLH-----LVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKPF 142
Cdd:COG1647   12 EGGRKGVLLLHGFTGSP----AEMRPLAEALAkagytVYAPRLPGH-GTSPEDLLKTTWEDWLEDVEEAYEILKAGYDKV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 143 HLIGTSMGGHVAGVYAAHYPsDVCSLSLVCPAgLQYSTDNQFVQRLKELqesaAVEKIPLIPSTPEEmsemLQLCSYVRF 222
Cdd:COG1647   87 IVIGLSMGGLLALLLAARYP-DVAGLVLLSPA-LKIDDPSAPLLPLLKY----LARSLRGIGSDIED----PEVAEYAYD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 223 RVPQQILQglvdvriphnNFYRklFLEIVSEksryslhqNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSIANCQVEL-- 300
Cdd:COG1647  157 RTPLRALA----------ELQR--LIREVRR--------DLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELvw 216
                        250       260       270
                 ....*....|....*....|....*....|
gi 821389629 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 821389629   70 NKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDL--SIDGQVKRI-HQFVEclKLNKKPFHLIG 146
Cdd:TIGR03695   1 AKPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGH-GSSQSPSDIEryDFEEAAQLLlATLLD--QLGIEPFFLVG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629  147 TSMGGHVAGVYAAHYPSDVCSLSLV-CPAGLQ--------YSTDNQFVQRLkeLQESAAV-----EKIPLIpSTPEEMse 212
Cdd:TIGR03695  78 YSMGGRIALYYALQYPERVQGLILEsGSPGLQteeeraarRQNDEQLAQRF--EQEGLEAflddwYQQPLF-ASQKNL-- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629  213 mlqlcsyvrfrvPQQILQGLVDVRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMlAKS 292
Cdd:TIGR03695 153 ------------PPEQRQALRAERLANNPEGLAKMLRATGLGKQPSLWPKLQALKIPVLYLCGERDEKFVQIAKEM-QKL 219
                         250       260       270
                  ....*....|....*....|....*....|..
gi 821389629  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 821389629   74 ILMLHGFSAHKDmwlSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSidgQVKRIHQFVECLKlNKKPFHLIGTSMGGHV 153
Cdd:pfam12697   1 VVLVHGAGLSAA---PLAALLAAGVAVLAPDLPGH-GSSSPPPLDLA---DLADLAALLDELG-AARPVVLVGHSLGGAV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629  154 AGVYAAHYPSDVCslsLVCPAGLQYSTDNQFVQRLKELQESAAVEKIPLIPSTPEEMSEMLQLCSYVRFRVPQQILQGLV 233
Cdd:pfam12697  73 ALAAAAAALVVGV---LVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALLAA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629  234 DVRIPHNNFyrklfleivseksryslhqnmDKIKVPTQIIWGkQDQVLDvSGADMLAKSIANCQVELLENCGHSvVMERP 313
Cdd:pfam12697 150 LALLPLAAW---------------------RDLPVPVLVLAE-EDRLVP-ELAQRLLAALAGARLVVLPGAGHL-PLDDP 205

                  ....*.
gi 821389629  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 821389629   9 FVIAGGTLAIPILAFVASFLLWP-SALIRI-------YYWYWRralGMQVRYVRHedyqfcysfrgrpGNKPSILMLHGF 80
Cdd:PLN02578  32 IFIFGGIVASGVSVMGSSSASQSvQGLERLpfkkegyNFWTWR---GHKIHYVVQ-------------GEGLPIVLIHGF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629  81 SAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLddLSIDGQVKRiHQFVECLK-LNKKPFHLIGTSMGGHVAGVYAA 159
Cdd:PLN02578  96 GASAFHWRYNIPELAKKYKVYALDLLGF-GWSDKAL--IEYDAMVWR-DQVADFVKeVVKEPAVLVGNSLGGFTALSTAV 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 160 HYPSDVCSLSLVCPAGlqystdnQFVQRLKELQESAAVEKIPLIPSTPEEMSEMLQ----LCSYVRFRVPQQILQGLVDV 235
Cdd:PLN02578 172 GYPELVAGVALLNSAG-------QFGSESREKEEAIVVEETVLTRFVVKPLKEWFQrvvlGFLFWQAKQPSRIESVLKSV 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 236 RIPHNN---------------------FYRkLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSIA 294
Cdd:PLN02578 245 YKDKSNvddylvesitepaadpnagevYYR-LMSRFLFNQSRYTLDSLLSKLSCPLLLLWGDLDPWVGPAKAEKIKAFYP 323
                        330       340       350
                 ....*....|....*....|....*....|..
gi 821389629 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 821389629   71 KPSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGH---EGTTR--SSLDDLsidgqVKRIHQFVECLKLN--KKPF 142
Cdd:pfam12146   4 RAVVVLVHGLGEHSGRYAHLADALAAQgFAVYAYDHRGHgrsDGKRGhvPSFDDY-----VDDLDTFVDKIREEhpGLPL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629  143 HLIGTSMGGHVAGVYAAHYPSDVCSLSLVCPA-GLQYSTDNQFVQRLKELQESAAVEKIPLIPSTPEEMS---EMLQLC- 217
Cdd:pfam12146  79 FLLGHSMGGLIAALYALRYPDKVDGLILSAPAlKIKPYLAPPILKLLAKLLGKLFPRLRVPNNLLPDSLSrdpEVVAAYa 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629  218 --SYVRFRVPQQILQGLVDVRIphnnfyrklfleivseksrySLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSI-- 293
Cdd:pfam12146 159 adPLVHGGISARTLYELLDAGE--------------------RLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAgs 218
                         250
                  ....*....|....*....
gi 821389629  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 821389629   62 YSFRGRPGNKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGH----EGTTRSSLDDLSIDgqvkrihqfVECL-- 135
Cdd:TIGR02427   4 YRLDGAADGAPVLVFINSLGTDLRMWDPVLPALTPDFRVLRYDKRGHglsdAPEGPYSIEDLADD---------VLALld 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629  136 KLNKKPFHLIGTSMGGHVAGVYAAHYPSDVCSLSLVCPAGlQYSTDNQFVQRLkelqesAAVEKiplipstpEEMSEMLQ 215
Cdd:TIGR02427  75 HLGIERAVFCGLSLGGLIAQGLAARRPDRVRALVLSNTAA-KIGTPESWNARI------AAVRA--------EGLAALAD 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629  216 lCSYVRFRVPqqilqglvDVRIPHN---NFYRKLFLEivSEKSRYSLH----QNMD------KIKVPTQIIWGKQDQVLD 282
Cdd:TIGR02427 140 -AVLERWFTP--------GFREAHParlDLYRNMLVR--QPPDGYAGCcaaiRDADfrdrlgAIAVPTLCIAGDQDGSTP 208
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 821389629  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 821389629  47 GMQVRYVRHEDYQFCY----SFRGRPgNKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHEGTTRSSLDDLSID 122
Cdd:PLN02894  78 GSKVRWFRSASNEPRFintvTFDSKE-DAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTCKSTE 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 123 -GQVKRIHQFVECLKL-NKKPFHLIGTSMGGHVAGVYAAHYPSDVCSLSLVCPAGlqystdnqfvqrlkelqesaaveki 200
Cdd:PLN02894 157 eTEAWFIDSFEEWRKAkNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAG------------------------- 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 201 plIPSTPEEMSEMLqlcsyVRFR----------------VPQQILQGL-----------VDVRIPHNN------------ 241
Cdd:PLN02894 212 --FSSESDDKSEWL-----TKFRatwkgavlnhlwesnfTPQKIIRGLgpwgpnlvrryTTARFGAHStgdilseeeskl 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 242 ----FYRKLFLEIVSEK-----------SRYSLHQNMDKIKVPTQIIWGKQDQvLDVSGADMLAKSI-ANCQVELLENCG 305
Cdd:PLN02894 285 ltdyVYHTLAAKASGELclkyifsfgafARKPLLESASEWKVPTTFIYGRHDW-MNYEGAVEARKRMkVPCEIIRVPQGG 363

                 ....*...
gi 821389629 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 821389629   72 PSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHEGTTrsSLDDLSIDGQVKRIHQFVEclklnkKPFHLIGTSMGG 151
Cdd:TIGR01738   5 VHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSR--GFGPLSLADMAEAIAAQAP------DPAIWLGWSLGG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629  152 HVAGVYAAHYPSDVCSLSLVC-----------PAGLQYSTDNQFVQRLK-ELQESaaVEKIPLIPS--TPEEMSEMLQLC 217
Cdd:TIGR01738  77 LVALHIAATHPDRVRALVTVAsspcfsaredwPEGIKPDVLTGFQQQLSdDYQRT--IERFLALQTlgTPTARQDARALK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629  218 SYVRFR-VPQ-QILQGLVDVriphnnfyrklfleivseKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSIAN 295
Cdd:TIGR01738 155 QTLLARpTPNvQVLQAGLEI------------------LATVDLRQPLQNISVPFLRLYGYLDGLVPAKVVPMLDKLAPH 216
                         250       260
                  ....*....|....*....|....*...
gi 821389629  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 821389629  68 PGNKPSILMLHGFSAHKD-MWLSVVKFLPKN-LHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKPFHLI 145
Cdd:COG1506   20 GKKYPVVVYVHGGPGSRDdSFLPLAQALASRgYAVLAPDYRGY-GESAGDWGGDEVDDVLAAIDYLAARPYVDPDRIGIY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 146 GTSMGGHVAGVYAAHYPSDVCSLSLVCPA---GLQYSTDNQFVQRLKElqesaavekiplipsTPEEMSEMLQlcsyvrf 222
Cdd:COG1506   99 GHSYGGYMALLAAARHPDRFKAAVALAGVsdlRSYYGTTREYTERLMG---------------GPWEDPEAYA------- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 223 rvpqqilqglvdvriphnnfyrklfleivseksRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSI--ANCQVEL 300
Cdd:COG1506  157 ---------------------------------ARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALkkAGKPVEL 203
                        250       260
                 ....*....|....*....|....*..
gi 821389629 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 821389629  70 NKPSILMLHGFSAHKDMWLSVVKFLPKNlHLVCVDMPGHeGTTRssldDLSIDGQVKRIHQFVECLK-LNKKPFHLIGTS 148
Cdd:PRK11126   1 GLPWLVFLHGLLGSGQDWQPVGEALPDY-PRLYIDLPGH-GGSA----AISVDGFADVSRLLSQTLQsYNILPYWLVGYS 74
                         90
                 ....*....|..
gi 821389629 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 821389629  62 YSFRGRPGNKPSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGH---EGTTRSSLDDLSIDgqvkrIHQFVEclKL 137
Cdd:COG1073   28 YLPAGASKKYPAVVVAHGNGGVKEQRALYAQRLAELgFNVLAFDYRGYgesEGEPREEGSPERRD-----ARAAVD--YL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 138 NKKPFH------LIGTSMGGHVAGVYAAHYPsDVCSLSLVCPAglqystdNQFVQRLKELQESAAVEKIPLIPSTPeems 211
Cdd:COG1073  101 RTLPGVdperigLLGISLGGGYALNAAATDP-RVKAVILDSPF-------TSLEDLAAQRAKEARGAYLPGVPYLP---- 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 212 emlqlcsyvrfrvpqqilqglvdvRIPHNNFYRKLFleivseksrYSLHQnMDKIKVPTQIIWGKQDQVldVS---GADM 288
Cdd:COG1073  169 ------------------------NVRLASLLNDEF---------DPLAK-IEKISRPLLFIHGEKDEA--VPfymSEDL 212
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 821389629 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 821389629  67 RPGNKPsILMLHGFSAHKDMWLSVVKFLPKNLHLVC-VDMPGHEGTTRSSLDDLsiDGQVKRIHQfveclKLNKKPFHLI 145
Cdd:COG1075    2 AATRYP-VVLVHGLGGSAASWAPLAPRLRAAGYPVYaLNYPSTNGSIEDSAEQL--AAFVDAVLA-----ATGAEKVDLV 73
                         90
                 ....*....|....*.
gi 821389629 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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