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Conserved domains on  [gi|1660651605|gb|TLL41822|]
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alpha/beta fold hydrolase [Acinetobacter baumannii]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PhaC super family cl43819
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];
33-360 5.68e-78

Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];


The actual alignment was detected with superfamily member COG3243:

Pssm-ID: 442475 [Multi-domain]  Cd Length: 545  Bit Score: 249.10  E-value: 5.68e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605  33 TPFEVIGEFNQTRVRYYA-ATEKSFREPLVFVAPLAINMAIYDLYPYRSLIKYFQNAGFDVYLVDWGRLGFKDRHLNFLS 111
Cdd:COG3243   178 TPGKVVYRNDLMELIQYApTTEKVHKTPLLIVPPWINKYYILDLQPGNSLVRYLVDQGFTVFLISWGNPDAEDRDLGLDD 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 112 FIEDFIPKAIELVRTHSGSDQVSLHGWSMAGIFVTLYTAH---NHPNYVKNLIVLGSPIDSYASGYIGKLyrtinntiar 188
Cdd:COG3243   258 YVEDGILAAVDAVREITGEDKVNLLGYCLGGTLLAIYAALlaaRGPDRVASLTLLATPLDFSEPGELGVF---------- 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 189 nkkLQERIYSGLpKRLIHT----PGILNSLGFKILDPkgwFDGHIQllKNLNNLQFVQE--HATLSSFLNNMIDYPGGIN 262
Cdd:COG3243   328 ---IDESQLADL-EALMAAkgylPGRLMAGAFSLLRP---NDLIWS--YYVNNYLLGENppPFDLLYWNADSTRLPGRMH 398
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 263 QDMLFNVWLQNPLIQGSIQLKDKKIELKNIDCSLLVGAGRSDQLVTADAAQPLSQLTSSQDVTFTLIPGGHLGLMSS--- 339
Cdd:COG3243   399 SQYLRDLYLENRLAKGELELGGRPVDLSDITVPVLVVAGEEDHIAPWRSVYALAQLVGGKDVTFVLAPGGHIGGIVNppg 478
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1660651605 340 -------------------QASAQEF----WPKLATWLSERSTK 360
Cdd:COG3243   479 kpkrsywtndrlpgdpdewLAGAEEHpgswWPDWADWLAERSGK 522
 
Name Accession Description Interval E-value
PhaC COG3243
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];
33-360 5.68e-78

Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];


Pssm-ID: 442475 [Multi-domain]  Cd Length: 545  Bit Score: 249.10  E-value: 5.68e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605  33 TPFEVIGEFNQTRVRYYA-ATEKSFREPLVFVAPLAINMAIYDLYPYRSLIKYFQNAGFDVYLVDWGRLGFKDRHLNFLS 111
Cdd:COG3243   178 TPGKVVYRNDLMELIQYApTTEKVHKTPLLIVPPWINKYYILDLQPGNSLVRYLVDQGFTVFLISWGNPDAEDRDLGLDD 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 112 FIEDFIPKAIELVRTHSGSDQVSLHGWSMAGIFVTLYTAH---NHPNYVKNLIVLGSPIDSYASGYIGKLyrtinntiar 188
Cdd:COG3243   258 YVEDGILAAVDAVREITGEDKVNLLGYCLGGTLLAIYAALlaaRGPDRVASLTLLATPLDFSEPGELGVF---------- 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 189 nkkLQERIYSGLpKRLIHT----PGILNSLGFKILDPkgwFDGHIQllKNLNNLQFVQE--HATLSSFLNNMIDYPGGIN 262
Cdd:COG3243   328 ---IDESQLADL-EALMAAkgylPGRLMAGAFSLLRP---NDLIWS--YYVNNYLLGENppPFDLLYWNADSTRLPGRMH 398
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 263 QDMLFNVWLQNPLIQGSIQLKDKKIELKNIDCSLLVGAGRSDQLVTADAAQPLSQLTSSQDVTFTLIPGGHLGLMSS--- 339
Cdd:COG3243   399 SQYLRDLYLENRLAKGELELGGRPVDLSDITVPVLVVAGEEDHIAPWRSVYALAQLVGGKDVTFVLAPGGHIGGIVNppg 478
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1660651605 340 -------------------QASAQEF----WPKLATWLSERSTK 360
Cdd:COG3243   479 kpkrsywtndrlpgdpdewLAGAEEHpgswWPDWADWLAERSGK 522
PHA_synth_III_C TIGR01836
poly(R)-hydroxyalkanoic acid synthase, class III, PhaC subunit; This model represents the PhaC ...
32-357 4.27e-50

poly(R)-hydroxyalkanoic acid synthase, class III, PhaC subunit; This model represents the PhaC subunit of a heterodimeric form of polyhydroxyalkanoic acid (PHA) synthase. Excepting the PhaC of Bacillus megaterium (which needs PhaR), all members require PhaE (TIGR01834) for activity and are designated class III. This enzyme builds ester polymers for carbon and energy storage that accumulate in inclusions, and both this enzyme and the depolymerase associate with the inclusions. Class III enzymes polymerize short-chain-length hydroxyalkanoates. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 130895  Cd Length: 350  Bit Score: 171.07  E-value: 4.27e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605  32 STPFEVIGEFNQTRV-RYYAATEKSFREPLVFVAPLAINMAIYDLYPYRSLIKYFQNAGFDVYLVDWGRLGFKDRHLNFL 110
Cdd:TIGR01836  36 VTPKEVVYREDKVVLyRYTPVKDNTHKTPLLIVYALVNRPYMLDLQEDRSLVRGLLERGQDVYLIDWGYPDRADRYLTLD 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 111 SFIEDFIPKAIELVRTHSGSDQVSLHGWSMAGIFVTLYTAHnHPNYVKNLIVLGSPIDSYASGYIGKLYrtinntiARNK 190
Cdd:TIGR01836 116 DYINGYIDKCVDYICRTSKLDQISLLGICQGGTFSLCYAAL-YPDKIKNLVTMVTPVDFETPGNMLSNW-------ARHV 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 191 KLQERI-YSGlpkrliHTPGILNSLGFKILDP-KGWFDGHIQLLKNLNNLQFVQEHATLSSFLNNMIDYPGGINQDMLFN 268
Cdd:TIGR01836 188 DIDLAVdTMG------NIPGELLNLTFLMLKPfSLGYQKYVNLVDILEDERKVENFLRMEKWIFDSPDQAGEAFRQFVKD 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 269 VWLQNPLIQGSIQLKDKKIELKNIDCSLLVGAGRSDQLVTADAAQPLSQLTSSQDVTFTLIPGGHLGLMSSQASAQEFWP 348
Cdd:TIGR01836 262 FYQQNGLINGEVEIGGRKVDLKNIKMPILNIYAERDHLVPPDASKALNDLVSSEDYTELSFPGGHIGIYVSGKAQKEVPP 341

                  ....*....
gi 1660651605 349 KLATWLSER 357
Cdd:TIGR01836 342 AIGKWLQAR 350
PRK07868 PRK07868
acyl-CoA synthetase; Validated
30-359 8.62e-17

acyl-CoA synthetase; Validated


Pssm-ID: 236121 [Multi-domain]  Cd Length: 994  Bit Score: 82.07  E-value: 8.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605  30 SQSTPFEVIGEFNQTRVRYY-----AATEKSFREPLVFVAPLAINMAIYDLYPYRSLIKYFQNAGFDVYLVDWGR----L 100
Cdd:PRK07868   35 SVPSPFQIVESVPMYRLRRYfppdnRPGQPPVGPPVLMVHPMMMSADMWDVTRDDGAVGILHRAGLDPWVIDFGSpdkvE 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 101 GFKDRHLnflsfiEDFI---PKAIELVRTHSGSDqVSLHGWSMAGIFVTLYTAHNHPNYVKNLIVLGSPIDSYASGYIGk 177
Cdd:PRK07868  115 GGMERNL------ADHVvalSEAIDTVKDVTGRD-VHLVGYSQGGMFCYQAAAYRRSKDIASIVTFGSPVDTLAALPMG- 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 178 LYRTINNTIArnKKLQERIYSGLPkrlihTPGILNSLGFKILDPKGWFDGHIQLLKNLNNLQFVQEHATLSSFLNN--MI 255
Cdd:PRK07868  187 IPAGLAAAAA--DFMADHVFNRLD-----IPGWMARTGFQMLDPVKTAKARVDFLRQLHDREALLPREQQRRFLESegWI 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 256 DYPGGINQDMLFNVWLQNPLIQGSIQLKDKKIELKNIDCSLLVGAGRSDqlvtaDAAQPLS-----QLTSSQDVTFTLIP 330
Cdd:PRK07868  260 AWSGPAISELLKQFIAHNRMMTGGFAINGQMVTLADITCPVLAFVGEVD-----DIGQPASvrgirRAAPNAEVYESLIR 334
                         330       340
                  ....*....|....*....|....*....
gi 1660651605 331 GGHLGLMSSQASAQEFWPKLATWLSERST 359
Cdd:PRK07868  335 AGHFGLVVGSRAAQQTWPTVADWVKWLEG 363
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
75-337 8.45e-12

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: 64.45  E-value: 8.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605  75 LYPYRSLIKYFQNAGFDVYLVDWGRLGFKDRHLNFLSFIEDFIPKAIELVRTHSGSDQVSLHGWSMAGIFVTLYtAHNHP 154
Cdd:pfam00561  13 SDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGLIALAY-AAKYP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 155 NYVKNLIVLGSPIDSY----ASGYIGKLYRTINNTIARnkklqeriysglpkrlihtPGILNSLGFKILDPKGWFDGHIQ 230
Cdd:pfam00561  92 DRVKALVLLGALDPPHeldeADRFILALFPGFFDGFVA-------------------DFAPNPLGRLVAKLLALLLLRLR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 231 LLKNLNNLQfvqehatlSSFLNNMIDYPGGI--NQDMLFNVWLQNPLIQGSIQLKDKkielknidcSLLVgAGRSDQLVT 308
Cdd:pfam00561 153 LLKALPLLN--------KRFPSGDYALAKSLvtGALLFIETWSTELRAKFLGRLDEP---------TLII-WGDQDPLVP 214
                         250       260
                  ....*....|....*....|....*....
gi 1660651605 309 ADAAQPLSQLTSSQDVtFTLIPGGHLGLM 337
Cdd:pfam00561 215 PQALEKLAQLFPNARL-VVIPDAGHFAFL 242
 
Name Accession Description Interval E-value
PhaC COG3243
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];
33-360 5.68e-78

Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];


Pssm-ID: 442475 [Multi-domain]  Cd Length: 545  Bit Score: 249.10  E-value: 5.68e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605  33 TPFEVIGEFNQTRVRYYA-ATEKSFREPLVFVAPLAINMAIYDLYPYRSLIKYFQNAGFDVYLVDWGRLGFKDRHLNFLS 111
Cdd:COG3243   178 TPGKVVYRNDLMELIQYApTTEKVHKTPLLIVPPWINKYYILDLQPGNSLVRYLVDQGFTVFLISWGNPDAEDRDLGLDD 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 112 FIEDFIPKAIELVRTHSGSDQVSLHGWSMAGIFVTLYTAH---NHPNYVKNLIVLGSPIDSYASGYIGKLyrtinntiar 188
Cdd:COG3243   258 YVEDGILAAVDAVREITGEDKVNLLGYCLGGTLLAIYAALlaaRGPDRVASLTLLATPLDFSEPGELGVF---------- 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 189 nkkLQERIYSGLpKRLIHT----PGILNSLGFKILDPkgwFDGHIQllKNLNNLQFVQE--HATLSSFLNNMIDYPGGIN 262
Cdd:COG3243   328 ---IDESQLADL-EALMAAkgylPGRLMAGAFSLLRP---NDLIWS--YYVNNYLLGENppPFDLLYWNADSTRLPGRMH 398
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 263 QDMLFNVWLQNPLIQGSIQLKDKKIELKNIDCSLLVGAGRSDQLVTADAAQPLSQLTSSQDVTFTLIPGGHLGLMSS--- 339
Cdd:COG3243   399 SQYLRDLYLENRLAKGELELGGRPVDLSDITVPVLVVAGEEDHIAPWRSVYALAQLVGGKDVTFVLAPGGHIGGIVNppg 478
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1660651605 340 -------------------QASAQEF----WPKLATWLSERSTK 360
Cdd:COG3243   479 kpkrsywtndrlpgdpdewLAGAEEHpgswWPDWADWLAERSGK 522
PHA_synth_III_C TIGR01836
poly(R)-hydroxyalkanoic acid synthase, class III, PhaC subunit; This model represents the PhaC ...
32-357 4.27e-50

poly(R)-hydroxyalkanoic acid synthase, class III, PhaC subunit; This model represents the PhaC subunit of a heterodimeric form of polyhydroxyalkanoic acid (PHA) synthase. Excepting the PhaC of Bacillus megaterium (which needs PhaR), all members require PhaE (TIGR01834) for activity and are designated class III. This enzyme builds ester polymers for carbon and energy storage that accumulate in inclusions, and both this enzyme and the depolymerase associate with the inclusions. Class III enzymes polymerize short-chain-length hydroxyalkanoates. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 130895  Cd Length: 350  Bit Score: 171.07  E-value: 4.27e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605  32 STPFEVIGEFNQTRV-RYYAATEKSFREPLVFVAPLAINMAIYDLYPYRSLIKYFQNAGFDVYLVDWGRLGFKDRHLNFL 110
Cdd:TIGR01836  36 VTPKEVVYREDKVVLyRYTPVKDNTHKTPLLIVYALVNRPYMLDLQEDRSLVRGLLERGQDVYLIDWGYPDRADRYLTLD 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 111 SFIEDFIPKAIELVRTHSGSDQVSLHGWSMAGIFVTLYTAHnHPNYVKNLIVLGSPIDSYASGYIGKLYrtinntiARNK 190
Cdd:TIGR01836 116 DYINGYIDKCVDYICRTSKLDQISLLGICQGGTFSLCYAAL-YPDKIKNLVTMVTPVDFETPGNMLSNW-------ARHV 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 191 KLQERI-YSGlpkrliHTPGILNSLGFKILDP-KGWFDGHIQLLKNLNNLQFVQEHATLSSFLNNMIDYPGGINQDMLFN 268
Cdd:TIGR01836 188 DIDLAVdTMG------NIPGELLNLTFLMLKPfSLGYQKYVNLVDILEDERKVENFLRMEKWIFDSPDQAGEAFRQFVKD 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 269 VWLQNPLIQGSIQLKDKKIELKNIDCSLLVGAGRSDQLVTADAAQPLSQLTSSQDVTFTLIPGGHLGLMSSQASAQEFWP 348
Cdd:TIGR01836 262 FYQQNGLINGEVEIGGRKVDLKNIKMPILNIYAERDHLVPPDASKALNDLVSSEDYTELSFPGGHIGIYVSGKAQKEVPP 341

                  ....*....
gi 1660651605 349 KLATWLSER 357
Cdd:TIGR01836 342 AIGKWLQAR 350
PRK07868 PRK07868
acyl-CoA synthetase; Validated
30-359 8.62e-17

acyl-CoA synthetase; Validated


Pssm-ID: 236121 [Multi-domain]  Cd Length: 994  Bit Score: 82.07  E-value: 8.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605  30 SQSTPFEVIGEFNQTRVRYY-----AATEKSFREPLVFVAPLAINMAIYDLYPYRSLIKYFQNAGFDVYLVDWGR----L 100
Cdd:PRK07868   35 SVPSPFQIVESVPMYRLRRYfppdnRPGQPPVGPPVLMVHPMMMSADMWDVTRDDGAVGILHRAGLDPWVIDFGSpdkvE 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 101 GFKDRHLnflsfiEDFI---PKAIELVRTHSGSDqVSLHGWSMAGIFVTLYTAHNHPNYVKNLIVLGSPIDSYASGYIGk 177
Cdd:PRK07868  115 GGMERNL------ADHVvalSEAIDTVKDVTGRD-VHLVGYSQGGMFCYQAAAYRRSKDIASIVTFGSPVDTLAALPMG- 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 178 LYRTINNTIArnKKLQERIYSGLPkrlihTPGILNSLGFKILDPKGWFDGHIQLLKNLNNLQFVQEHATLSSFLNN--MI 255
Cdd:PRK07868  187 IPAGLAAAAA--DFMADHVFNRLD-----IPGWMARTGFQMLDPVKTAKARVDFLRQLHDREALLPREQQRRFLESegWI 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 256 DYPGGINQDMLFNVWLQNPLIQGSIQLKDKKIELKNIDCSLLVGAGRSDqlvtaDAAQPLS-----QLTSSQDVTFTLIP 330
Cdd:PRK07868  260 AWSGPAISELLKQFIAHNRMMTGGFAINGQMVTLADITCPVLAFVGEVD-----DIGQPASvrgirRAAPNAEVYESLIR 334
                         330       340
                  ....*....|....*....|....*....
gi 1660651605 331 GGHLGLMSSQASAQEFWPKLATWLSERST 359
Cdd:PRK07868  335 AGHFGLVVGSRAAQQTWPTVADWVKWLEG 363
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
75-337 8.45e-12

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: 64.45  E-value: 8.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605  75 LYPYRSLIKYFQNAGFDVYLVDWGRLGFKDRHLNFLSFIEDFIPKAIELVRTHSGSDQVSLHGWSMAGIFVTLYtAHNHP 154
Cdd:pfam00561  13 SDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGLIALAY-AAKYP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 155 NYVKNLIVLGSPIDSY----ASGYIGKLYRTINNTIARnkklqeriysglpkrlihtPGILNSLGFKILDPKGWFDGHIQ 230
Cdd:pfam00561  92 DRVKALVLLGALDPPHeldeADRFILALFPGFFDGFVA-------------------DFAPNPLGRLVAKLLALLLLRLR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605 231 LLKNLNNLQfvqehatlSSFLNNMIDYPGGI--NQDMLFNVWLQNPLIQGSIQLKDKkielknidcSLLVgAGRSDQLVT 308
Cdd:pfam00561 153 LLKALPLLN--------KRFPSGDYALAKSLvtGALLFIETWSTELRAKFLGRLDEP---------TLII-WGDQDPLVP 214
                         250       260
                  ....*....|....*....|....*....
gi 1660651605 309 ADAAQPLSQLTSSQDVtFTLIPGGHLGLM 337
Cdd:pfam00561 215 PQALEKLAQLFPNARL-VVIPDAGHFAFL 242
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
78-165 4.40e-08

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 53.08  E-value: 4.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605  78 YRSLIKYFQNAGFDVYLVDW---GRLGFKDRHLN-FLSFIEDfIPKAIELVRTHSGsDQVSLHGWSMAGIFVTLYtAHNH 153
Cdd:COG2267    44 YAELAEALAAAGYAVLAFDLrghGRSDGPRGHVDsFDDYVDD-LRAALDALRARPG-LPVVLLGHSMGGLIALLY-AARY 120
                          90
                  ....*....|..
gi 1660651605 154 PNYVKNLIVLGS 165
Cdd:COG2267   121 PDRVAGLVLLAP 132
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
40-171 3.04e-06

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: 47.69  E-value: 3.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605  40 EFNQTRVRYYAATEKsfREPLVFVAPLAINMAIYdlypyRSLIKYFQnAGFDVYLVDW---GRLGFKDRHLNFLSFIEDf 116
Cdd:COG0596     8 TVDGVRLHYREAGPD--GPPVVLLHGLPGSSYEW-----RPLIPALA-AGYRVIAPDLrghGRSDKPAGGYTLDDLADD- 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1660651605 117 ipkaIELVRTHSGSDQVSLHGWSMAGIfVTLYTAHNHPNYVKNLIVLGSPIDSYA 171
Cdd:COG0596    79 ----LAALLDALGLERVVLVGHSMGGM-VALELAARHPERVAGLVLVDEVLAALA 128
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
78-168 9.45e-05

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 43.08  E-value: 9.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605  78 YRSLIKYFQNAGFDVYLVDWGRLGFKDRHLNFlSFIEDFIpKAIELVRTHSGSD--QVSLHGWSMAGiFVTLYTAHNHPN 155
Cdd:COG1506    40 FLPLAQALASRGYAVLAPDYRGYGESAGDWGG-DEVDDVL-AAIDYLAARPYVDpdRIGIYGHSYGG-YMALLAAARHPD 116
                          90
                  ....*....|...
gi 1660651605 156 YVKNLIVLGSPID 168
Cdd:COG1506   117 RFKAAVALAGVSD 129
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
81-208 1.21e-03

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 39.89  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660651605  81 LIKYFQNAGFDVYLVDW-------GRLGFKDrhlNFLSFIEDFIpKAIELVRTHSGSDQVSLHGWSMAGIFVTLYtAHNH 153
Cdd:pfam12146  23 LADALAAQGFAVYAYDHrghgrsdGKRGHVP---SFDDYVDDLD-TFVDKIREEHPGLPLFLLGHSMGGLIAALY-ALRY 97
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1660651605 154 PNYVKNLIvLGSP---IDSYASGYIGKLYRTINNTIARNKKLQERIysgLPKRLIHTP 208
Cdd:pfam12146  98 PDKVDGLI-LSAPalkIKPYLAPPILKLLAKLLGKLFPRLRVPNNL---LPDSLSRDP 151
 
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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