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Conserved domains on  [gi|1544845764|gb|RUJ33981|]
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alpha/beta fold hydrolase [Pseudomonas aeruginosa]

Protein Classification

COG4757 superfamily protein( domain architecture ID 1904597)

COG4757 superfamily protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG4757 super family cl44124
Predicted alpha/beta hydrolase [General function prediction only];
38-315 1.56e-32

Predicted alpha/beta hydrolase [General function prediction only];


The actual alignment was detected with superfamily member COG4757:

Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 122.30  E-value: 1.56e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764  38 VELVVTRLGQQAAGerrgPPVILLHGSFSNRRFWYSPralgLGPYLARAGFDVWLPEMRGHGLSIRNDGYR-DNRVADYA 116
Cdd:COG4757    18 YPLAARLFPPAGPP----RAVVLINPATGVPQRFYRP----FARYLAERGFAVLTYDYRGIGLSRPGSLRGfDAGYRDWG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764 117 RYDLPALASFIHEQ-CGQPAHWIGHSLGGVVLAAGLGGGyldqaRIASVALFGSQvsTAHWLFRLPMAGILARLLLRRVD 195
Cdd:COG4757    90 ELDLPAVLDALRARfPGLPLLLVGHSLGGQLLGLAPNAE-----RVDRLVTVASG--SGYWRDYPPRRRLKVLLFWHLLG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764 196 ALS--------GSRWRQGpEDEPVGLALEVLRWhGLFGRFGEPGNDWW--KGLAAVDVPLLAVAGAGDRQDPSWACRKLF 265
Cdd:COG4757   163 PLLtrllgyfpGRRLGFG-EDLPAGVARQWRRW-CRRPRYFFDDDGEDleAALAAVTAPVLAISFTDDELAPPAAVDRLL 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1544845764 266 EQFASSEREYLLLGREAGYAEDYGHIEMLiGKAAQLEVWPLVERWLRQRS 315
Cdd:COG4757   241 AYYPNAPVTRRRLAPADLGLKRIGHFGFF-RRRFAAALWPRVLDWLRAGA 289
 
Name Accession Description Interval E-value
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
38-315 1.56e-32

Predicted alpha/beta hydrolase [General function prediction only];


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 122.30  E-value: 1.56e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764  38 VELVVTRLGQQAAGerrgPPVILLHGSFSNRRFWYSPralgLGPYLARAGFDVWLPEMRGHGLSIRNDGYR-DNRVADYA 116
Cdd:COG4757    18 YPLAARLFPPAGPP----RAVVLINPATGVPQRFYRP----FARYLAERGFAVLTYDYRGIGLSRPGSLRGfDAGYRDWG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764 117 RYDLPALASFIHEQ-CGQPAHWIGHSLGGVVLAAGLGGGyldqaRIASVALFGSQvsTAHWLFRLPMAGILARLLLRRVD 195
Cdd:COG4757    90 ELDLPAVLDALRARfPGLPLLLVGHSLGGQLLGLAPNAE-----RVDRLVTVASG--SGYWRDYPPRRRLKVLLFWHLLG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764 196 ALS--------GSRWRQGpEDEPVGLALEVLRWhGLFGRFGEPGNDWW--KGLAAVDVPLLAVAGAGDRQDPSWACRKLF 265
Cdd:COG4757   163 PLLtrllgyfpGRRLGFG-EDLPAGVARQWRRW-CRRPRYFFDDDGEDleAALAAVTAPVLAISFTDDELAPPAAVDRLL 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1544845764 266 EQFASSEREYLLLGREAGYAEDYGHIEMLiGKAAQLEVWPLVERWLRQRS 315
Cdd:COG4757   241 AYYPNAPVTRRRLAPADLGLKRIGHFGFF-RRRFAAALWPRVLDWLRAGA 289
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
58-277 1.06e-12

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: 66.85  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764  58 VILLHGsfsnrRFWYSPRALGLGPYLARAGFDVWLPEMRGHGLSirnDGYRdNRVADYARY--DLPALASFIHEQ-CGQP 134
Cdd:pfam12146   7 VVLVHG-----LGEHSGRYAHLADALAAQGFAVYAYDHRGHGRS---DGKR-GHVPSFDDYvdDLDTFVDKIREEhPGLP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764 135 AHWIGHSLGG-VVLAAGLGGGYLDQARIASVALFGSQVSTAHWLFRLpMAGILARL-----LLRRVDALSGSRW----RQ 204
Cdd:pfam12146  78 LFLLGHSMGGlIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKL-LAKLLGKLfprlrVPNNLLPDSLSRDpevvAA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764 205 GPEDE------PVGLALEVLRwhglfgrfgePGNDWWKGLAAVDVPLLAVAGAGDR-QDPSwACRKLFEQFASSEREYLL 277
Cdd:pfam12146 157 YAADPlvhggiSARTLYELLD----------AGERLLRRAAAITVPLLLLHGGADRvVDPA-GSREFYERAGSTDKTLKL 225
PLN02872 PLN02872
triacylglycerol lipase
51-151 1.33e-09

triacylglycerol lipase


Pssm-ID: 215470 [Multi-domain]  Cd Length: 395  Bit Score: 58.72  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764  51 GERRGPPVILLHGSFSNRRFWY--SPRAlGLGPYLARAGFDVWLPEMRG----HG---LSIRNDGYRDNRVADYARYDLP 121
Cdd:PLN02872   70 GSQRGPPVLLQHGLFMAGDAWFlnSPEQ-SLGFILADHGFDVWVGNVRGtrwsYGhvtLSEKDKEFWDWSWQELALYDLA 148
                          90       100       110
                  ....*....|....*....|....*....|
gi 1544845764 122 ALASFIHEQCGQPAHWIGHSLGGVVLAAGL 151
Cdd:PLN02872  149 EMIHYVYSITNSKIFIVGHSQGTIMSLAAL 178
FIST smart00897
FIST N domain; The FIST N domain is a novel sensory domain, which is present in signal ...
116-230 9.66e-03

FIST N domain; The FIST N domain is a novel sensory domain, which is present in signal transduction proteins from Bacteria, Archaea and Eukarya. Chromosomal proximity of FIST-encoding genes to those coding for proteins involved in amino acid metabolism and transport suggest that FIST domains bind small ligands, such as amino acids.


Pssm-ID: 214894  Cd Length: 196  Bit Score: 36.91  E-value: 9.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764  116 ARYDLPALASFIHEQCGQPAHWIGHSLGGVVLAAGLGGgyLDQARIASVALFGSQVStahwlfRLPMAGILARLLLRRVD 195
Cdd:smart00897  11 PAYDAEALLAALRERFPGATPIVGCSTAGEITTGVVQE--FEDEPALSVMLFELPLV------SFDVFSLVDPLPDLVAG 82
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1544845764  196 ALSGSRWRQGPEDEPVGLALevlrWHGLFGRFGEP 230
Cdd:smart00897  83 LLLAALLAAIDPRNTFALLL----LDDLSSSNEEE 113
 
Name Accession Description Interval E-value
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
38-315 1.56e-32

Predicted alpha/beta hydrolase [General function prediction only];


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 122.30  E-value: 1.56e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764  38 VELVVTRLGQQAAGerrgPPVILLHGSFSNRRFWYSPralgLGPYLARAGFDVWLPEMRGHGLSIRNDGYR-DNRVADYA 116
Cdd:COG4757    18 YPLAARLFPPAGPP----RAVVLINPATGVPQRFYRP----FARYLAERGFAVLTYDYRGIGLSRPGSLRGfDAGYRDWG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764 117 RYDLPALASFIHEQ-CGQPAHWIGHSLGGVVLAAGLGGGyldqaRIASVALFGSQvsTAHWLFRLPMAGILARLLLRRVD 195
Cdd:COG4757    90 ELDLPAVLDALRARfPGLPLLLVGHSLGGQLLGLAPNAE-----RVDRLVTVASG--SGYWRDYPPRRRLKVLLFWHLLG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764 196 ALS--------GSRWRQGpEDEPVGLALEVLRWhGLFGRFGEPGNDWW--KGLAAVDVPLLAVAGAGDRQDPSWACRKLF 265
Cdd:COG4757   163 PLLtrllgyfpGRRLGFG-EDLPAGVARQWRRW-CRRPRYFFDDDGEDleAALAAVTAPVLAISFTDDELAPPAAVDRLL 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1544845764 266 EQFASSEREYLLLGREAGYAEDYGHIEMLiGKAAQLEVWPLVERWLRQRS 315
Cdd:COG4757   241 AYYPNAPVTRRRLAPADLGLKRIGHFGFF-RRRFAAALWPRVLDWLRAGA 289
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
50-313 1.55e-23

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 96.61  E-value: 1.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764  50 AGERRGPPVILLHGSFSNRRFWYSpralgLGPYLARAGFDVWLPEMRGHGLSIRNDGYRDnRVADYARyDLPALASFIHE 129
Cdd:COG2267    23 PAGSPRGTVVLVHGLGEHSGRYAE-----LAEALAAAGYAVLAFDLRGHGRSDGPRGHVD-SFDDYVD-DLRAALDALRA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764 130 QCGQPAHWIGHSLGGVVLAAGLGGGyldQARIASVALFGSqvstahWLFRLPMAGILARLLlrrvdalsgsrwrqgpede 209
Cdd:COG2267    96 RPGLPVVLLGHSMGGLIALLYAARY---PDRVAGLVLLAP------AYRADPLLGPSARWL------------------- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764 210 pvgLALEVlrwhglfgrfgepgndwWKGLAAVDVPLLAVAGAGDRQDPSWACRKLFEQFaSSEREYLLLgreagyaEDYG 289
Cdd:COG2267   148 ---RALRL-----------------AEALARIDVPVLVLHGGADRVVPPEAARRLAARL-SPDVELVLL-------PGAR 199
                         250       260
                  ....*....|....*....|....
gi 1544845764 290 HieMLIGKAAQLEVWPLVERWLRQ 313
Cdd:COG2267   200 H--ELLNEPAREEVLAAILAWLER 221
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
55-276 4.03e-16

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: 76.19  E-value: 4.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764  55 GPPVILLHGSFSNRRFWyspraLGLGPYLArAGFDVWLPEMRGHGLSIRNDGyrDNRVADYARydlpALASFIHEQCGQP 134
Cdd:COG0596    23 GPPVVLLHGLPGSSYEW-----RPLIPALA-AGYRVIAPDLRGHGRSDKPAG--GYTLDDLAD----DLAALLDALGLER 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764 135 AHWIGHSLGG-VVLAAGLgggyLDQARIASVALFGSQVstAHWLFRLPMAGILARLLLRRVDALSGSrwrqgpedepvgl 213
Cdd:COG0596    91 VVLVGHSMGGmVALELAA----RHPERVAGLVLVDEVL--AALAEPLRRPGLAPEALAALLRALART------------- 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1544845764 214 alevlrwhglfgrfgepgnDWWKGLAAVDVPLLAVAGAGDRQDPSWACRKLFEQFASSEREYL 276
Cdd:COG0596   152 -------------------DLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVL 195
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
58-277 1.06e-12

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: 66.85  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764  58 VILLHGsfsnrRFWYSPRALGLGPYLARAGFDVWLPEMRGHGLSirnDGYRdNRVADYARY--DLPALASFIHEQ-CGQP 134
Cdd:pfam12146   7 VVLVHG-----LGEHSGRYAHLADALAAQGFAVYAYDHRGHGRS---DGKR-GHVPSFDDYvdDLDTFVDKIREEhPGLP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764 135 AHWIGHSLGG-VVLAAGLGGGYLDQARIASVALFGSQVSTAHWLFRLpMAGILARL-----LLRRVDALSGSRW----RQ 204
Cdd:pfam12146  78 LFLLGHSMGGlIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKL-LAKLLGKLfprlrVPNNLLPDSLSRDpevvAA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764 205 GPEDE------PVGLALEVLRwhglfgrfgePGNDWWKGLAAVDVPLLAVAGAGDR-QDPSwACRKLFEQFASSEREYLL 277
Cdd:pfam12146 157 YAADPlvhggiSARTLYELLD----------AGERLLRRAAAITVPLLLLHGGADRvVDPA-GSREFYERAGSTDKTLKL 225
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
56-176 3.74e-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: 65.22  E-value: 3.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764  56 PPVILLHGSFSNRRFWYspralGLGPYLARAGFDVWLPEMRGHGLS---IRNDGYRDNRVADYARYdlpalasfIHEQCG 132
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWR-----KLAPALARDGFRVIALDLRGFGKSsrpKAQDDYRTDDLAEDLEY--------ILEALG 67
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1544845764 133 Q-PAHWIGHSLGGVVLAAglgggYLDQA--RIASVALFGSQVSTAHW 176
Cdd:pfam00561  68 LeKVNLVGHSMGGLIALA-----YAAKYpdRVKALVLLGALDPPHEL 109
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
49-313 5.55e-10

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 59.16  E-value: 5.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764  49 AAGERRGPPVILLHGsFSNRRFWYSPRAlglgPYLARAGFDVWLPEMRGHGLS---IRNDGyrdnrvaDYARYDLPALAS 125
Cdd:COG1073    31 AGASKKYPAVVVAHG-NGGVKEQRALYA----QRLAELGFNVLAFDYRGYGESegePREEG-------SPERRDARAAVD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764 126 FIHEQCGQPAHWI---GHSLGG--VVLAAGlgggylDQARIASVALfgsqVStahwlfrlpMAGILARLLLRRVDALSGS 200
Cdd:COG1073    99 YLRTLPGVDPERIgllGISLGGgyALNAAA------TDPRVKAVIL----DS---------PFTSLEDLAAQRAKEARGA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764 201 RWrqgpedePVGLALEVLRWHGLFGRFGEPGNDwwkgLAAVDVPLLAVAGAGDRQDPSWACRKLFEQfASSEREYLLLgr 280
Cdd:COG1073   160 YL-------PGVPYLPNVRLASLLNDEFDPLAK----IEKISRPLLFIHGEKDEAVPFYMSEDLYEA-AAEPKELLIV-- 225
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1544845764 281 eagyaEDYGHIEMLIGKAAqlEVWPLVERWLRQ 313
Cdd:COG1073   226 -----PGAGHVDLYDRPEE--EYFDKLAEFFKK 251
PLN02872 PLN02872
triacylglycerol lipase
51-151 1.33e-09

triacylglycerol lipase


Pssm-ID: 215470 [Multi-domain]  Cd Length: 395  Bit Score: 58.72  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764  51 GERRGPPVILLHGSFSNRRFWY--SPRAlGLGPYLARAGFDVWLPEMRG----HG---LSIRNDGYRDNRVADYARYDLP 121
Cdd:PLN02872   70 GSQRGPPVLLQHGLFMAGDAWFlnSPEQ-SLGFILADHGFDVWVGNVRGtrwsYGhvtLSEKDKEFWDWSWQELALYDLA 148
                          90       100       110
                  ....*....|....*....|....*....|
gi 1544845764 122 ALASFIHEQCGQPAHWIGHSLGGVVLAAGL 151
Cdd:PLN02872  149 EMIHYVYSITNSKIFIVGHSQGTIMSLAAL 178
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
57-169 2.09e-09

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 54.45  E-value: 2.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764  57 PVILLHGSFSNRRFWYspralGLGPYLARAGFDVWLPEMRGHGLSIrndgyrdnrvADYARYDLPALASFIHEQCGQPAH 136
Cdd:COG1075     7 PVVLVHGLGGSAASWA-----PLAPRLRAAGYPVYALNYPSTNGSI----------EDSAEQLAAFVDAVLAATGAEKVD 71
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1544845764 137 WIGHSLGGVV---LAAGLGGgyldQARIASVALFGS 169
Cdd:COG1075    72 LVGHSMGGLVaryYLKRLGG----AAKVARVVTLGT 103
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
50-316 3.46e-08

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 53.41  E-value: 3.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764  50 AGERRGppVILLHGSFSNRRFWYSpralgLGPYLARAGFDVWLPEMRGHGLSIRND---GYRDNRvaDYARYDLPALAsf 126
Cdd:COG1647    12 EGGRKG--VLLLHGFTGSPAEMRP-----LAEALAKAGYTVYAPRLPGHGTSPEDLlktTWEDWL--EDVEEAYEILK-- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764 127 iheQCGQPAHWIGHSLGGvVLAAGLgggYLDQARIASVALFGSQVSTAHWLFRL-PMAGILARLL-LRRVDALSGSRWRQ 204
Cdd:COG1647    81 ---AGYDKVIVIGLSMGG-LLALLL---AARYPDVAGLVLLSPALKIDDPSAPLlPLLKYLARSLrGIGSDIEDPEVAEY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764 205 GPEDEPVGLALEVLRwhgLFgrfgepgNDWWKGLAAVDVPLLAVAGAGDRQDPSWACRKLFEQFASSEREYLLLgreagy 284
Cdd:COG1647   154 AYDRTPLRALAELQR---LI-------REVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWL------ 217
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1544845764 285 aEDYGHIeMLIGKAAQlEVWPLVERWLRQRSP 316
Cdd:COG1647   218 -EDSGHV-ITLDKDRE-EVAEEILDFLERLAA 246
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
50-313 1.30e-06

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 48.86  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764  50 AGERRGPPVILLHGSFSNRRFWYSPRAlglgPYLARAGFDVWLPEMRGHGLSIRNDGYRDnrvadyaRYDLPALASFIHE 129
Cdd:COG1506    18 ADGKKYPVVVYVHGGPGSRDDSFLPLA----QALASRGYAVLAPDYRGYGESAGDWGGDE-------VDDVLAAIDYLAA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764 130 QCG---QPAHWIGHSLGGVVLAAGLGggyLDQARIASVAlfgSQVSTAHWLFRLPMAGILARlllrrvdalsgsRWRQGP 206
Cdd:COG1506    87 RPYvdpDRIGIYGHSYGGYMALLAAA---RHPDRFKAAV---ALAGVSDLRSYYGTTREYTE------------RLMGGP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764 207 EDEPVGLALEVLRWHglfgrfgepgndwwkgLAAVDVPLLAVAGAGDRQDPSWACRKLFEQFASSEREYLLLgreagYAE 286
Cdd:COG1506   149 WEDPEAYAARSPLAY----------------ADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELL-----VYP 207
                         250       260
                  ....*....|....*....|....*..
gi 1544845764 287 DYGHiemLIGKAAQLEVWPLVERWLRQ 313
Cdd:COG1506   208 GEGH---GFSGAGAPDYLERILDFLDR 231
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
58-264 1.03e-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: 45.93  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764  58 VILLHGsfsnrrFWYSPRALglgPYLARAGFDVWLPEMRGHGLSIRndgyrdnrvADYARYDLPALASFIHE-QCGQPAH 136
Cdd:pfam12697   1 VVLVHG------AGLSAAPL---AALLAAGVAVLAPDLPGHGSSSP---------PPLDLADLADLAALLDElGAARPVV 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764 137 WIGHSLGGVVLAAGLGGGYLDQARIASVALFGSQVSTAHWLFRLPMAGILARLLLRRvdALSGSRWRQGPEDEPVGLALE 216
Cdd:pfam12697  63 LVGHSLGGAVALAAAAAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAA--ESLARGFLDDLPADAEWAAAL 140
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1544845764 217 VLRWHGLFGRFGEPGNDWWKGLAAVdvpllAVAGAGDRQDPSWACRKL 264
Cdd:pfam12697 141 ARLAALLAALALLPLAAWRDLPVPV-----LVLAEEDRLVPELAQRLL 183
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
43-283 2.48e-05

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 45.48  E-value: 2.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764  43 TRLGQQAAGERRGPPVILLHGSFSNRRFwYSPralgLGPYLARAGFDVWLPEMRGH---GLSIRNDGYRDNRVADYARY- 118
Cdd:COG4188    50 ATAPADAPAGGPFPLVVLSHGLGGSREG-YAY----LAEHLASHGYVVAAPDHPGSnaaDLSAALDGLADALDPEELWEr 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764 119 --DLPALASFIHEQCGQPAHW-----------IGHSLGGVVlAAGLGGGYLDQARIASVAlfgsQVSTAHWLFRLPMAGI 185
Cdd:COG4188   125 plDLSFVLDQLLALNKSDPPLagrldldrigvIGHSLGGYT-ALALAGARLDFAALRQYC----GKNPDLQCRALDLPRL 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764 186 LARLLLRRVDALsgsrwrqgpedepVGLALevlrwhGLFGRFGEpgndwwKGLAAVDVPLLAVAGAGDRQDPSWACRKLF 265
Cdd:COG4188   200 AYDLRDPRIKAV-------------VALAP------GGSGLFGE------EGLAAITIPVLLVAGSADDVTPAPDEQIRP 254
                         250
                  ....*....|....*...
gi 1544845764 266 EQFASSEREYLLLGREAG 283
Cdd:COG4188   255 FDLLPGADKYLLTLEGAT 272
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
50-152 3.74e-04

Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 41.67  E-value: 3.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764  50 AGERRGPPVILLH---GSfSNRrfWYsprALGLGPYLARAGFDVWLPEMRGHGLSI-RNDG-YRDNRVADYArydlpALA 124
Cdd:COG0429    56 PPAPSKPLVVLLHgleGS-SDS--HY---ARGLARALYARGWDVVRLNFRGCGGEPnLLPRlYHSGDTEDLV-----WVL 124
                          90       100
                  ....*....|....*....|....*....
gi 1544845764 125 SFIHEQCGQPAHW-IGHSLGGVVLAAGLG 152
Cdd:COG0429   125 AHLRARYPYAPLYaVGFSLGGNLLLKYLG 153
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
50-169 8.27e-04

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 40.70  E-value: 8.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764  50 AGERRGPPVILLHGSFSNRRFWyspraLGLGPYLArAGFDVWLPEMRGHGLSirndgyrdnrVADYARYDLPALA----S 125
Cdd:PRK14875  126 LGEGDGTPVVLIHGFGGDLNNW-----LFNHAALA-AGRPVIALDLPGHGAS----------SKAVGAGSLDELAaavlA 189
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1544845764 126 FIHEQCGQPAHWIGHSLGGVVLAAGLGGGyldQARIASVALFGS 169
Cdd:PRK14875  190 FLDALGIERAHLVGHSMGGAVALRLAARA---PQRVASLTLIAP 230
FIST smart00897
FIST N domain; The FIST N domain is a novel sensory domain, which is present in signal ...
116-230 9.66e-03

FIST N domain; The FIST N domain is a novel sensory domain, which is present in signal transduction proteins from Bacteria, Archaea and Eukarya. Chromosomal proximity of FIST-encoding genes to those coding for proteins involved in amino acid metabolism and transport suggest that FIST domains bind small ligands, such as amino acids.


Pssm-ID: 214894  Cd Length: 196  Bit Score: 36.91  E-value: 9.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1544845764  116 ARYDLPALASFIHEQCGQPAHWIGHSLGGVVLAAGLGGgyLDQARIASVALFGSQVStahwlfRLPMAGILARLLLRRVD 195
Cdd:smart00897  11 PAYDAEALLAALRERFPGATPIVGCSTAGEITTGVVQE--FEDEPALSVMLFELPLV------SFDVFSLVDPLPDLVAG 82
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1544845764  196 ALSGSRWRQGPEDEPVGLALevlrWHGLFGRFGEP 230
Cdd:smart00897  83 LLLAALLAAIDPRNTFALLL----LDDLSSSNEEE 113
 
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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