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Conserved domains on  [gi|1333914110|ref|WP_103016262|]
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alpha/beta fold hydrolase [Salinibacter ruber]

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, ...
 40-322 1.05e-32

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: 120.88  E-value: 1.05e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110  40 DGVDLYVVEFGAAaapGDTVVVLHGGWGaeHSYLWPAIIP-LADRYHFVLYDQRGSLRSPAPDSTISLQRFVSDLEDLRR 118
Cdd:COG0596    10 DGVRLHYREAGPD---GPPVVLLHGLPG--SSYEWRPLIPaLAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110 119 ELGQERLTIFAHSMGSRLAYTYLRKHPEHVRRLALAGPLvptgsplgdkrkmrkvrkqfvqwakkrekaeiteegldrds 198
Cdd:COG0596    85 ALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEV----------------------------------------- 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110 199 lsdrektarwrigfaagniyhVERWHQMEGGRAFYNGDIAELINQNTPDSLRanqfETLRTSEVPVRVIIGDHDLAdFGL 278
Cdd:COG0596   124 ---------------------LAALAEPLRRPGLAPEALAALLRALARTDLR----ERLARITVPTLVIWGEKDPI-VPP 177

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1333914110 279 VSWPAVADTLENVEITTLEKAGHNAWIDRPGKFRDAIRRALHAS 322
Cdd:COG0596   178 ALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 40-322 1.05e-32

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: 120.88  E-value: 1.05e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110  40 DGVDLYVVEFGAAaapGDTVVVLHGGWGaeHSYLWPAIIP-LADRYHFVLYDQRGSLRSPAPDSTISLQRFVSDLEDLRR 118
Cdd:COG0596    10 DGVRLHYREAGPD---GPPVVLLHGLPG--SSYEWRPLIPaLAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110 119 ELGQERLTIFAHSMGSRLAYTYLRKHPEHVRRLALAGPLvptgsplgdkrkmrkvrkqfvqwakkrekaeiteegldrds 198
Cdd:COG0596    85 ALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEV----------------------------------------- 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110 199 lsdrektarwrigfaagniyhVERWHQMEGGRAFYNGDIAELINQNTPDSLRanqfETLRTSEVPVRVIIGDHDLAdFGL 278
Cdd:COG0596   124 ---------------------LAALAEPLRRPGLAPEALAALLRALARTDLR----ERLARITVPTLVIWGEKDPI-VPP 177

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1333914110 279 VSWPAVADTLENVEITTLEKAGHNAWIDRPGKFRDAIRRALHAS 322
Cdd:COG0596   178 ALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 57-308 8.36e-21

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 89.49  E-value: 8.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110  57 DTVVVLHGGwgAEHSYLWPAIIP--LADRYHFVLYDQRGSLRSPAP--DSTISLQRFVSDLEDLRRELGQERLTIFAHSM 132
Cdd:pfam00561   1 PPVLLLHGL--PGSSDLWRKLAPalARDGFRVIALDLRGFGKSSRPkaQDDYRTDDLAEDLEYILEALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110 133 GSRLAYTYLRKHPEHVRRLALAGPLVPTGSPLgdkRKMRKVRKQFVQWAKK-REKAEITEEGLDRDSLSDREKTaRWRIG 211
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGALDPPHELD---EADRFILALFPGFFDGfVADFAPNPLGRLVAKLLALLLL-RLRLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110 212 FA----AGNIYHVERWHQMEGGRaFYNGDIaELINQNTPDSLRANQfetlrtsEVPVRVIIGDHDLAdFGLVSWPAVADT 287
Cdd:pfam00561 155 KAlpllNKRFPSGDYALAKSLVT-GALLFI-ETWSTELRAKFLGRL-------DEPTLIIWGDQDPL-VPPQALEKLAQL 224

                         250       260
                  ....*....|....*....|.
gi 1333914110 288 LENVEITTLEKAGHNAWIDRP 308
Cdd:pfam00561 225 FPNARLVVIPDAGHFAFLEGP 245
PRK05855 PRK05855
SDR family oxidoreductase;
37-134 3.75e-10

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 60.76  E-value: 3.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110  37 EASDGVDLYVVEFGAAAAPgdTVVVLHGgWGAEHSyLWPAIIP-LADRYHFVLYDQRGSLRS--PAPDSTISLQRFVSDL 113
Cdd:PRK05855    8 VSSDGVRLAVYEWGDPDRP--TVVLVHG-YPDNHE-VWDGVAPlLADRFRVVAYDVRGAGRSsaPKRTAAYTLARLADDF 83

                          90       100
                  ....*....|....*....|..
gi 1333914110 114 EDLRRELGQER-LTIFAHSMGS 134
Cdd:PRK05855   84 AAVIDAVSPDRpVHLLAHDWGS 105
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 40-322 1.05e-32

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: 120.88  E-value: 1.05e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110  40 DGVDLYVVEFGAAaapGDTVVVLHGGWGaeHSYLWPAIIP-LADRYHFVLYDQRGSLRSPAPDSTISLQRFVSDLEDLRR 118
Cdd:COG0596    10 DGVRLHYREAGPD---GPPVVLLHGLPG--SSYEWRPLIPaLAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110 119 ELGQERLTIFAHSMGSRLAYTYLRKHPEHVRRLALAGPLvptgsplgdkrkmrkvrkqfvqwakkrekaeiteegldrds 198
Cdd:COG0596    85 ALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEV----------------------------------------- 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110 199 lsdrektarwrigfaagniyhVERWHQMEGGRAFYNGDIAELINQNTPDSLRanqfETLRTSEVPVRVIIGDHDLAdFGL 278
Cdd:COG0596   124 ---------------------LAALAEPLRRPGLAPEALAALLRALARTDLR----ERLARITVPTLVIWGEKDPI-VPP 177

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1333914110 279 VSWPAVADTLENVEITTLEKAGHNAWIDRPGKFRDAIRRALHAS 322
Cdd:COG0596   178 ALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
34-156 3.90e-21

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 89.68  E-value: 3.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110  34 WYLEASDGVDLYVVEFGAAAAPGDTVVVLHGGWgaEHSYLWPAIIP-LADR-YHFVLYDQRGSLRSPAPDSTI-SLQRFV 110
Cdd:COG2267     6 VTLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLG--EHSGRYAELAEaLAAAgYAVLAFDLRGHGRSDGPRGHVdSFDDYV 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1333914110 111 SDLEDLRRELGQE---RLTIFAHSMGSRLAYTYLRKHPEHVRRLALAGP 156
Cdd:COG2267    84 DDLRAALDALRARpglPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAP 132
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 57-308 8.36e-21

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 89.49  E-value: 8.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110  57 DTVVVLHGGwgAEHSYLWPAIIP--LADRYHFVLYDQRGSLRSPAP--DSTISLQRFVSDLEDLRRELGQERLTIFAHSM 132
Cdd:pfam00561   1 PPVLLLHGL--PGSSDLWRKLAPalARDGFRVIALDLRGFGKSSRPkaQDDYRTDDLAEDLEYILEALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110 133 GSRLAYTYLRKHPEHVRRLALAGPLVPTGSPLgdkRKMRKVRKQFVQWAKK-REKAEITEEGLDRDSLSDREKTaRWRIG 211
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGALDPPHELD---EADRFILALFPGFFDGfVADFAPNPLGRLVAKLLALLLL-RLRLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110 212 FA----AGNIYHVERWHQMEGGRaFYNGDIaELINQNTPDSLRANQfetlrtsEVPVRVIIGDHDLAdFGLVSWPAVADT 287
Cdd:pfam00561 155 KAlpllNKRFPSGDYALAKSLVT-GALLFI-ETWSTELRAKFLGRL-------DEPTLIIWGDQDPL-VPPQALEKLAQL 224

                         250       260
                  ....*....|....*....|.
gi 1333914110 288 LENVEITTLEKAGHNAWIDRP 308
Cdd:pfam00561 225 FPNARLVVIPDAGHFAFLEGP 245
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 58-182 7.56e-15

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: 72.63  E-value: 7.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110  58 TVVVLHGGwgAEHS--YLwpaiiPLADR-----YHFVLYDQRGSLRSPAPDSTI-SLQRFVSDL----EDLRRELGQERL 125
Cdd:pfam12146   6 VVVLVHGL--GEHSgrYA-----HLADAlaaqgFAVYAYDHRGHGRSDGKRGHVpSFDDYVDDLdtfvDKIREEHPGLPL 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1333914110 126 TIFAHSMGSRLAYTYLRKHPEHVRRLALAGPLV--PTGSPLGDKRKMRKVRKQFVQWAK 182
Cdd:pfam12146  79 FLLGHSMGGLIAALYALRYPDKVDGLILSAPALkiKPYLAPPILKLLAKLLGKLFPRLR 137
PRK05855 PRK05855
SDR family oxidoreductase;
37-134 3.75e-10

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 60.76  E-value: 3.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110  37 EASDGVDLYVVEFGAAAAPgdTVVVLHGgWGAEHSyLWPAIIP-LADRYHFVLYDQRGSLRS--PAPDSTISLQRFVSDL 113
Cdd:PRK05855    8 VSSDGVRLAVYEWGDPDRP--TVVLVHG-YPDNHE-VWDGVAPlLADRFRVVAYDVRGAGRSsaPKRTAAYTLARLADDF 83

                          90       100
                  ....*....|....*....|..
gi 1333914110 114 EDLRRELGQER-LTIFAHSMGS 134
Cdd:PRK05855   84 AAVIDAVSPDRpVHLLAHDWGS 105
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 28-156 1.75e-09

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 58.38  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110  28 PDGAE-DWYLEASDGVD-LYVVEF-GAAAAPgdTVVVLHGgWGAEHSYLWPAIIPLADRYHFVLYDQRGSLRSPAPDSTI 104
Cdd:PLN02894   76 PPGSKvRWFRSASNEPRfINTVTFdSKEDAP--TLVMVHG-YGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTC 152

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333914110 105 SLQR-----FVSDLEDLRRELGQERLTIFAHSMGSRLAYTYLRKHPEHVRRLALAGP 156
Cdd:PLN02894  153 KSTEeteawFIDSFEEWRKAKNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGP 209
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 56-186 3.03e-07

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 51.15  E-value: 3.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110  56 GDTVVVLHGGwgAEHSYLWPAIIP-LADRYHFVLYDQRGSLRSPAPDSTISLQRFVSDLEDLRRELGQERLTIFAHSMGS 134
Cdd:PRK03592   27 GDPIVFLHGN--PTSSYLWRNIIPhLAGLGRCLAPDLIGMGASDKPDIDYTFADHARYLDAWFDALGLDDVVLVGHDWGS 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333914110 135 RLAYTYLRKHPEHVRRLALAGPLV-PTGS---PLGDKRKMRKVRKQFVQWAKKREK 186
Cdd:PRK03592  105 ALGFDWAARHPDRVRGIAFMEAIVrPMTWddfPPAVRELFQALRSPGEGEEMVLEE 160
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 52-156 6.45e-06

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 44.44  E-value: 6.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110  52 AAAPGDTVVVLHGGWGaeHSYLWPAIIPLADRYHFVLYdqRGSLRSPAPDSTISLQRFVSDLEDLRRELGQERLTIFAHS 131
Cdd:COG1075     1 YAATRYPVVLVHGLGG--SAASWAPLAPRLRAAGYPVY--ALNYPSTNGSIEDSAEQLAAFVDAVLAATGAEKVDLVGHS 76

                          90       100
                  ....*....|....*....|....*...
gi 1333914110 132 MGSRLAYTYLRKH--PEHVRRL-ALAGP 156
Cdd:COG1075    77 MGGLVARYYLKRLggAAKVARVvTLGTP 104
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 44-173 2.15e-05

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 45.95  E-value: 2.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110  44 LYV-VEFGAAAAPGDTVVVLHGGWGAehSYLW-----PAIIPLA-DRYHFVLYDQRGSLRSPAP-DSTISLQRFVSDLEd 115
Cdd:PLN03087  188 LFVhVQQPKDNKAKEDVLFIHGFISS--SAFWtetlfPNFSDAAkSTYRLFAVDLLGFGRSPKPaDSLYTLREHLEMIE- 264

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333914110 116 lRRELGQERLTIF---AHSMGSRLAYTYLRKHPEHVRRLALAGP---LVPTGSPlGDKRKMRKV 173
Cdd:PLN03087  265 -RSVLERYKVKSFhivAHSLGCILALALAVKHPGAVKSLTLLAPpyyPVPKGVQ-ATQYVMRKV 326
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 45-156 2.59e-05

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 45.64  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110  45 YVVEFGAAAAPgdTVVVLHGGWGAEHSYlwPAIIP-LADRYHFVLYDQRGSLRS--PAPDSTI--SLQRFVSDLEDLRRE 119
Cdd:PLN03084  118 FCVESGSNNNP--PVLLIHGFPSQAYSY--RKVLPvLSKNYHAIAFDWLGFGFSdkPQPGYGFnyTLDEYVSSLESLIDE 193

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1333914110 120 LGQERLTIFAHSMGSRLAYTYLRKHPEHVRRLALAGP 156
Cdd:PLN03084  194 LKSDKVSLVVQGYFSPPVVKYASAHPDKIKKLILLNP 230
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 59-215 4.57e-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: 44.00  E-value: 4.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110  59 VVVLHGGWgAEHSYLWPAiipLADRYHFVLYDQRGSLRSPAPDSTISlqrFVSDLEDLRRELGQ-ERLTIFAHSMGSRLA 137
Cdd:pfam12697   1 VVLVHGAG-LSAAPLAAL---LAAGVAVLAPDLPGHGSSSPPPLDLA---DLADLAALLDELGAaRPVVLVGHSLGGAVA 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333914110 138 YTYLrkHPEHVRRLALAGPLVPTGSplgdkrkMRKVRKQFVQWAKKREKAE-ITEEGLDRDSLSDREKTARWRIGFAAG 215
Cdd:pfam12697  74 LAAA--AAALVVGVLVAPLAAPPGL-------LAALLALLARLGAALAAPAwLAAESLARGFLDDLPADAEWAAALARL 143
YpfH COG0400
Predicted esterase [General function prediction only];
50-174 1.81e-04

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 41.82  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110  50 GAAAAPgdTVVVLHGGWGAEHSylwpaIIPLA-----DRYHFVL--------------YDQRGSLRSPAPD----STISL 106
Cdd:COG0400     1 GGPAAP--LVVLLHGYGGDEED-----LLPLApelalPGAAVLAprapvpegpggrawFDLSFLEGREDEEglaaAAEAL 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333914110 107 QRFVSDLEDlRRELGQERLTIFAHSMGSRLAYTYLRKHPEHVRRL-ALAGPLVPTGSPLGDKRKMRKVR 174
Cdd:COG0400    74 AAFIDELEA-RYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVvALSGYLPGEEALPAPEAALAGTP 141
COG4782 COG4782
Esterase/lipase superfamily enzyme [General function prediction only];
113-156 4.53e-04

Esterase/lipase superfamily enzyme [General function prediction only];


Pssm-ID: 443812  Cd Length: 357  Bit Score: 41.48  E-value: 4.53e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1333914110 113 LEDLRRELGQERLTIFAHSMGSRLAYtylrkhpEHVRRLALAGP 156
Cdd:COG4782   188 LRDLARDPGAERIHIVAHSMGNWLTM-------EALRQLAIRGR 224
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 40-156 9.44e-04

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 40.70  E-value: 9.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110  40 DGVDLYVVEFGAAAapGDTVVVLHGgWGAEHSYLWPAIIPLADRYHFVLYDQRGSLRSPAPDSTISLQRFVSDLEDLRRE 119
Cdd:PRK14875  117 GGRTVRYLRLGEGD--GTPVVLIHG-FGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDELAAAVLAFLDA 193

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1333914110 120 LGQERLTIFAHSMGSRLAYTYLRKHPEHVRRLALAGP 156
Cdd:PRK14875  194 LGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 54-272 2.54e-03

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 39.18  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110  54 APGDTVVVLHG--GWgaehSYLWPAIIP-LADRYHFVLY-DQRGSLRS--PAPDSTISLQRFVSDLEDLRRELGQERLTI 127
Cdd:PRK00870   44 ADGPPVLLLHGepSW----SYLYRKMIPiLAAAGHRVIApDLIGFGRSdkPTRREDYTYARHVEWMRSWFEQLDLTDVTL 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333914110 128 FAHSMGSRLAYTYLRKHPEHVRRLALAGplvpTGSPLGDKR--KMRKVRKQFVQWAKKREKAEITEEGLDRDsLSDREkt 205
Cdd:PRK00870  120 VCQDWGGLIGLRLAAEHPDRFARLVVAN----TGLPTGDGPmpDAFWAWRAFSQYSPVLPVGRLVNGGTVRD-LSDAV-- 192

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333914110 206 arwRIGFAAGniYHVERWhqMEGGRAFyngdiAELInQNTPD--SLRANQ--FETLRTSEVPVRVIIGDHD 272
Cdd:PRK00870  193 ---RAAYDAP--FPDESY--KAGARAF-----PLLV-PTSPDdpAVAANRaaWAVLERWDKPFLTAFSDSD 250
 
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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