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Conserved domains on  [gi|490261029|ref|WP_004158249|]
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alpha/beta fold hydrolase [Erwinia amylovora]

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, ...
 52-292 2.99e-53

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: 172.88  E-value: 2.99e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  52 TGYAQVNGIALFYGTVG-QGSPVIFLHGGLANSDYWGNQIPVIARTHQVIVVDSRGHGRSSRDSRPFGYDLMTDDVVALM 130
Cdd:COG0596    4 PRFVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029 131 DQLKIAKADIVGWSDGAIIGIDAAMRYPDRVGKVfayapntttagvrtdTANNPLFARYItrasgeyRRLSKTPQQYENF 210
Cdd:COG0596   84 DALGLERVVLVGHSMGGMVALELAARHPERVAGL---------------VLVDEVLAALA-------EPLRRPGLAPEAL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029 211 VGQIGemWQSQPDWSdDRLKKIHTPILIADGDHDESIIRSHLEHIAATIPQAGLLIMPDSSHFAFLQAPKEFNDALVNFL 290
Cdd:COG0596  142 AALLR--ALARTDLR-ERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFL 218


                 ..
gi 490261029 291 AR 292
Cdd:COG0596  219 AR 220
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 52-292 2.99e-53

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: 172.88  E-value: 2.99e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  52 TGYAQVNGIALFYGTVG-QGSPVIFLHGGLANSDYWGNQIPVIARTHQVIVVDSRGHGRSSRDSRPFGYDLMTDDVVALM 130
Cdd:COG0596    4 PRFVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029 131 DQLKIAKADIVGWSDGAIIGIDAAMRYPDRVGKVfayapntttagvrtdTANNPLFARYItrasgeyRRLSKTPQQYENF 210
Cdd:COG0596   84 DALGLERVVLVGHSMGGMVALELAARHPERVAGL---------------VLVDEVLAALA-------EPLRRPGLAPEAL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029 211 VGQIGemWQSQPDWSdDRLKKIHTPILIADGDHDESIIRSHLEHIAATIPQAGLLIMPDSSHFAFLQAPKEFNDALVNFL 290
Cdd:COG0596  142 AALLR--ALARTDLR-ERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFL 218


                 ..
gi 490261029 291 AR 292
Cdd:COG0596  219 AR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 72-279 8.70e-25

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: 99.50  E-value: 8.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029   72 PVIFLHGGLANSDYWGNQIPVIARTH-QVIVVDSRGHGRSSRDSRPFGYDLMT--DDVVALMDQLKIAKADIVGWSDGAI 148
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGfRVIALDLRGFGKSSRPKAQDDYRTDDlaEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  149 IGIDAAMRYPDRVGKVFAYAPNTTTAGVRTD---------------------TANNPLFARYITRASGEYRRLSKTPQQY 207
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGALDPPHELDEAdrfilalfpgffdgfvadfapNPLGRLVAKLLALLLLRLRLLKALPLLN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  208 ENFVGQ---IGEM-----WQSQPDWS-DDRLKKIH---TPILIADGDHDESIIRSHLEHIAATIPQAGLLIMPDSSHFAF 275
Cdd:pfam00561 162 KRFPSGdyaLAKSlvtgaLLFIETWStELRAKFLGrldEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFAF 241


                  ....
gi 490261029  276 LQAP 279
Cdd:pfam00561 242 LEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 54-292 3.73e-16

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 77.68  E-value: 3.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  54 YAQVNGIALFYGTVGQGS--PVIFLHGGLANSDYWGNQIPVIARTHQVIVVDSRGHGRSSRDSRPFGYDLMTDDVVALMD 131
Cdd:PRK14875 113 KARIGGRTVRYLRLGEGDgtPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDELAAAVLAFLD 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029 132 QLKIAKADIVGWSDGAIIGIDAAMRYPDRVGKVFAYAP-------NT------TTAGVRTDTAnnP----LFAR--YITR 192
Cdd:PRK14875 193 ALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAPaglgpeiNGdyidgfVAAESRRELK--PvlelLFADpaLVTR 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029 193 ASGE----YRRLSKTPQQYENFVGQI--GEMWQSQPdwsDDRLKKIHTPILIADGDHDESIIRSHLEHIAatiPQAGLLI 266
Cdd:PRK14875 271 QMVEdllkYKRLDGVDDALRALADALfaGGRQRVDL---RDRLASLAIPVLVIWGEQDRIIPAAHAQGLP---DGVAVHV 344

                        250       260
                 ....*....|....*....|....*.
gi 490261029 267 MPDSSHFAFLQAPKEFNDALVNFLAR 292
Cdd:PRK14875 345 LPGAGHMPQMEAAADVNRLLAEFLGK 370
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 72-290 2.24e-14

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: 71.09  E-value: 2.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029   72 PVIFLHGGLANSDYWGNQIPVIARTHQVIVVDSRGHGRS--SRDSRPFGYDLMTDDVVA-LMDQLKIAKADIVGWSDGAI 148
Cdd:TIGR03695   4 VLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSqsPSDIERYDFEEAAQLLLAtLLDQLGIEPFFLVGYSMGGR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  149 IGIDAAMRYPDRV----------------------------GKVFAYAPnttTAGVRTDTANNPLFA---------RYIT 191
Cdd:TIGR03695  84 IALYYALQYPERVqglilesgspglqteeeraarrqndeqlAQRFEQEG---LEAFLDDWYQQPLFAsqknlppeqRQAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  192 RAsgeyRRLSKTPQqyenfvgQIGEMWQ-----SQPDWSdDRLKKIHTPILIADGDHDESIIRSHLEhIAATIPQAGLLI 266
Cdd:TIGR03695 161 RA----ERLANNPE-------GLAKMLRatglgKQPSLW-PKLQALKIPVLYLCGERDEKFVQIAKE-MQKLIPNLTLHI 227

                         250       260
                  ....*....|....*....|....
gi 490261029  267 MPDSSHFAFLQAPKEFNDALVNFL 290
Cdd:TIGR03695 228 IPNAGHNIHLENPEAFAKILLAFL 251
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 52-292 2.99e-53

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: 172.88  E-value: 2.99e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  52 TGYAQVNGIALFYGTVG-QGSPVIFLHGGLANSDYWGNQIPVIARTHQVIVVDSRGHGRSSRDSRPFGYDLMTDDVVALM 130
Cdd:COG0596    4 PRFVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029 131 DQLKIAKADIVGWSDGAIIGIDAAMRYPDRVGKVfayapntttagvrtdTANNPLFARYItrasgeyRRLSKTPQQYENF 210
Cdd:COG0596   84 DALGLERVVLVGHSMGGMVALELAARHPERVAGL---------------VLVDEVLAALA-------EPLRRPGLAPEAL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029 211 VGQIGemWQSQPDWSdDRLKKIHTPILIADGDHDESIIRSHLEHIAATIPQAGLLIMPDSSHFAFLQAPKEFNDALVNFL 290
Cdd:COG0596  142 AALLR--ALARTDLR-ERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFL 218


                 ..
gi 490261029 291 AR 292
Cdd:COG0596  219 AR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 72-279 8.70e-25

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: 99.50  E-value: 8.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029   72 PVIFLHGGLANSDYWGNQIPVIARTH-QVIVVDSRGHGRSSRDSRPFGYDLMT--DDVVALMDQLKIAKADIVGWSDGAI 148
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGfRVIALDLRGFGKSSRPKAQDDYRTDDlaEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  149 IGIDAAMRYPDRVGKVFAYAPNTTTAGVRTD---------------------TANNPLFARYITRASGEYRRLSKTPQQY 207
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGALDPPHELDEAdrfilalfpgffdgfvadfapNPLGRLVAKLLALLLLRLRLLKALPLLN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  208 ENFVGQ---IGEM-----WQSQPDWS-DDRLKKIH---TPILIADGDHDESIIRSHLEHIAATIPQAGLLIMPDSSHFAF 275
Cdd:pfam00561 162 KRFPSGdyaLAKSlvtgaLLFIETWStELRAKFLGrldEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFAF 241


                  ....
gi 490261029  276 LQAP 279
Cdd:pfam00561 242 LEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 54-292 3.73e-16

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 77.68  E-value: 3.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  54 YAQVNGIALFYGTVGQGS--PVIFLHGGLANSDYWGNQIPVIARTHQVIVVDSRGHGRSSRDSRPFGYDLMTDDVVALMD 131
Cdd:PRK14875 113 KARIGGRTVRYLRLGEGDgtPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDELAAAVLAFLD 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029 132 QLKIAKADIVGWSDGAIIGIDAAMRYPDRVGKVFAYAP-------NT------TTAGVRTDTAnnP----LFAR--YITR 192
Cdd:PRK14875 193 ALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAPaglgpeiNGdyidgfVAAESRRELK--PvlelLFADpaLVTR 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029 193 ASGE----YRRLSKTPQQYENFVGQI--GEMWQSQPdwsDDRLKKIHTPILIADGDHDESIIRSHLEHIAatiPQAGLLI 266
Cdd:PRK14875 271 QMVEdllkYKRLDGVDDALRALADALfaGGRQRVDL---RDRLASLAIPVLVIWGEQDRIIPAAHAQGLP---DGVAVHV 344

                        250       260
                 ....*....|....*....|....*.
gi 490261029 267 MPDSSHFAFLQAPKEFNDALVNFLAR 292
Cdd:PRK14875 345 LPGAGHMPQMEAAADVNRLLAEFLGK 370
PRK10673 PRK10673
esterase;
71-291 4.81e-15

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 73.23  E-value: 4.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  71 SPVIFLHGGLANSDYWGnqipVIAR----THQVIVVDSRGHGRSSRDSRpFGYDLMTDDVVALMDQLKIAKADIVGWSDG 146
Cdd:PRK10673  17 SPIVLVHGLFGSLDNLG----VLARdlvnDHDIIQVDMRNHGLSPRDPV-MNYPAMAQDLLDTLDALQIEKATFIGHSMG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029 147 AIIGIDAAMRYPDRVGK------------------VFAYAPNTTTAGVRTDTANNPLFARYITR-----------ASGEY 197
Cdd:PRK10673  92 GKAVMALTALAPDRIDKlvaidiapvdyhvrrhdeIFAAINAVSEAGATTRQQAAAIMRQHLNEegviqfllksfVDGEW 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029 198 R-RLSKTPQQYENFVGqigemWQSQPDWsddrlkkiHTPILIADGDHDESIIRSHLEHIAATIPQAGLLIMPDSSHFAFL 276
Cdd:PRK10673 172 RfNVPVLWDQYPHIVG-----WEKIPAW--------PHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHA 238

                        250
                 ....*....|....*
gi 490261029 277 QAPKEFNDALVNFLA 291
Cdd:PRK10673 239 EKPDAVLRAIRRYLN 253
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
72-292 5.09e-15

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 72.34  E-value: 5.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  72 PVIFLHGGLANSDYWGNQIPVIART-HQVIVVDSRGHGRSSRDSRPF-GYDLMTDDVVALMDQLKIAKAD---IVGWSDG 146
Cdd:COG2267   30 TVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVdSFDDYVDDLRAALDALRARPGLpvvLLGHSMG 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029 147 AIIGIDAAMRYPDRVGKVFAYAPntttagvrtDTANNPLFARYitrasgeyrrlsktpqqyenfVGQIGEMWQSqpdwsd 226
Cdd:COG2267  110 GLIALLYAARYPDRVAGLVLLAP---------AYRADPLLGPS---------------------ARWLRALRLA------ 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490261029 227 DRLKKIHTPILIADGDHDESIIRSHLEHIAATI-PQAGLLIMPDSSHFAFLQAPKE-FNDALVNFLAR 292
Cdd:COG2267  154 EALARIDVPVLVLHGGADRVVPPEAARRLAARLsPDVELVLLPGARHELLNEPAREeVLAAILAWLER 221
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 72-290 2.24e-14

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: 71.09  E-value: 2.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029   72 PVIFLHGGLANSDYWGNQIPVIARTHQVIVVDSRGHGRS--SRDSRPFGYDLMTDDVVA-LMDQLKIAKADIVGWSDGAI 148
Cdd:TIGR03695   4 VLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSqsPSDIERYDFEEAAQLLLAtLLDQLGIEPFFLVGYSMGGR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  149 IGIDAAMRYPDRV----------------------------GKVFAYAPnttTAGVRTDTANNPLFA---------RYIT 191
Cdd:TIGR03695  84 IALYYALQYPERVqglilesgspglqteeeraarrqndeqlAQRFEQEG---LEAFLDDWYQQPLFAsqknlppeqRQAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  192 RAsgeyRRLSKTPQqyenfvgQIGEMWQ-----SQPDWSdDRLKKIHTPILIADGDHDESIIRSHLEhIAATIPQAGLLI 266
Cdd:TIGR03695 161 RA----ERLANNPE-------GLAKMLRatglgKQPSLW-PKLQALKIPVLYLCGERDEKFVQIAKE-MQKLIPNLTLHI 227

                         250       260
                  ....*....|....*....|....
gi 490261029  267 MPDSSHFAFLQAPKEFNDALVNFL 290
Cdd:TIGR03695 228 IPNAGHNIHLENPEAFAKILLAFL 251
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
73-292 3.75e-13

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 67.35  E-value: 3.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  73 VIFLHGGlansdyWGNQIPVIARTHQ--------VIVVDSRGHGRSSRDsrpFGYDlMTDDVVALMDQLK---IAKAD-- 139
Cdd:COG1506   26 VVYVHGG------PGSRDDSFLPLAQalasrgyaVLAPDYRGYGESAGD---WGGD-EVDDVLAAIDYLAarpYVDPDri 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029 140 -IVGWSDGAIIGIDAAMRYPDRVGKVFAYAPNTTtagvrtdtannplFARYITRASGEYRRLSKTPQQYENfvgqigEMW 218
Cdd:COG1506   96 gIYGHSYGGYMALLAAARHPDRFKAAVALAGVSD-------------LRSYYGTTREYTERLMGGPWEDPE------AYA 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490261029 219 QSQPdwsDDRLKKIHTPILIADGDHDESIIRSHLEHIAATIPQAG----LLIMPDSSHFAFLQAPKEFNDALVNFLAR 292
Cdd:COG1506  157 ARSP---LAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAGkpveLLVYPGEGHGFSGAGAPDYLERILDFLDR 231
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 68-289 8.23e-13

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: 66.76  E-value: 8.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029   68 GQGSP-VIFLHGGLANSDYWGNQIPVIARTHQVIVVDSRGHGRsSRDSRPFGYDLMTDDVVALMDqlkiAKADIVGWSDG 146
Cdd:TIGR01738   1 GQGNVhLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGR-SRGFGPLSLADMAEAIAAQAP----DPAIWLGWSLG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  147 AIIGIDAAMRYPDRVGKV----------------FAYAPNTTTAGVRTDTANnplFARYITR-----------ASGEYRR 199
Cdd:TIGR01738  76 GLVALHIAATHPDRVRALvtvasspcfsaredwpEGIKPDVLTGFQQQLSDD---YQRTIERflalqtlgtptARQDARA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  200 LSK------TPqqyENFVGQIGEMWQSQPDWSDDrLKKIHTPILIADGDHDESIIRSHLEHIAATIPQAGLLIMPDSSHF 273
Cdd:TIGR01738 153 LKQtllarpTP---NVQVLQAGLEILATVDLRQP-LQNISVPFLRLYGYLDGLVPAKVVPMLDKLAPHSELYIFAKAAHA 228

                         250
                  ....*....|....*.
gi 490261029  274 AFLQAPKEFNDALVNF 289
Cdd:TIGR01738 229 PFLSHAEAFCALLVAF 244
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
73-292 1.32e-12

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 66.12  E-value: 1.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  73 VIFLHGGLANS---DYWGNQIpvIARTHQVIVVDSRGHGRSSRDSRPFGYDLMTDDVVALMDQLKiAKAD---IVGWSDG 146
Cdd:COG1647   18 VLLLHGFTGSPaemRPLAEAL--AKAGYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILK-AGYDkviVIGLSMG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029 147 AIIGIDAAMRYPDrVGKVFAYAPNtttagVRTDTANNPL------FARYITRASGEYRRLSKTPQQYENF-VGQIGEMWQ 219
Cdd:COG1647   95 GLLALLLAARYPD-VAGLVLLSPA-----LKIDDPSAPLlpllkyLARSLRGIGSDIEDPEVAEYAYDRTpLRALAELQR 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490261029 220 SQpDWSDDRLKKIHTPILIADGDHDESIIRSHLEHIAATIPQAG--LLIMPDSSHFAFL-QAPKEFNDALVNFLAR 292
Cdd:COG1647  169 LI-REVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDkeLVWLEDSGHVITLdKDREEVAEEILDFLER 243
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 73-285 1.20e-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: 62.88  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029   73 VIFLHGGLANSDYWgnqIPVIARTHQVIVVDSRGHGRSSRDSRPFGydlMTDDVVALMDQLKIAK-ADIVGWSDGAIIGI 151
Cdd:pfam12697   1 VVLVHGAGLSAAPL---AALLAAGVAVLAPDLPGHGSSSPPPLDLA---DLADLAALLDELGAARpVVLVGHSLGGAVAL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  152 DAAMRYPDRvgkVFAYAPNTTTAGVRTDTANNPLFARYITRASG---------EYRRLSKTPQQYENFVGQIGEMWQSQP 222
Cdd:pfam12697  75 AAAAAALVV---GVLVAPLAAPPGLLAALLALLARLGAALAAPAwlaaeslarGFLDDLPADAEWAAALARLAALLAALA 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490261029  223 DWSDDRLKKIHTPILI-ADGDHdesIIRSHLEHIAATIPQAGLLIMPDSSHFAFLQaPKEFNDA 285
Cdd:pfam12697 152 LLPLAAWRDLPVPVLVlAEEDR---LVPELAQRLLAALAGARLVVLPGAGHLPLDD-PEEVAEA 211
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 54-161 4.42e-10

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 59.24  E-value: 4.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  54 YAQVNGIALFYGTVGQGSPVIFLHGGLANSDYWGNQIPVIARTHQVIVVDSRGHGRSSRDSRPFGYDLMTDDVVALMDQL 133
Cdd:PRK03592  11 RVEVLGSRMAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKPDIDYTFADHARYLDAWFDAL 90

                         90       100
                 ....*....|....*....|....*...
gi 490261029 134 KIAKADIVGWSDGAIIGIDAAMRYPDRV 161
Cdd:PRK03592  91 GLDDVVLVGHDWGSALGFDWAARHPDRV 118
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 43-161 2.38e-09

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 57.06  E-value: 2.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  43 TPAPDASLKTGYAQVNGIALFYGTVG-QGSPVIFLHGGLANSDYWGNQIPVIARTHQVIVVDSRGHGRSSR-DSRPFG-- 118
Cdd:PLN02824   1 TVKPEPQVETRTWRWKGYNIRYQRAGtSGPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKpNPRSAPpn 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 490261029 119 ----YDLMTDDVVALMDQLKIAKADIVGWSDGAIIGIDAAMRYPDRV 161
Cdd:PLN02824  81 sfytFETWGEQLNDFCSDVVGDPAFVICNSVGGVVGLQAAVDAPELV 127
PLN02578 PLN02578
hydrolase
 68-164 5.31e-09

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 56.39  E-value: 5.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  68 GQGSPVIFLHGGLANSDYWGNQIPVIARTHQVIVVDSRGHGRSSRDSRPFGYDLMTDDVVALMDQLKIAKADIVGWSDGA 147
Cdd:PLN02578  84 GEGLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMVWRDQVADFVKEVVKEPAVLVGNSLGG 163

                         90
                 ....*....|....*..
gi 490261029 148 IIGIDAAMRYPDRVGKV 164
Cdd:PLN02578 164 FTALSTAVGYPELVAGV 180
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 65-292 1.29e-07

2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 52.94  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029   65 GTVGQGSPVIFLHGGLANSDYWGNQIPVIARTHQVIVVDSRGHGRS--------SRDSRPFGYDLMTDDVVALMDQLKIA 136
Cdd:PLN02980 1366 GQNAEGSVVLFLHGFLGTGEDWIPIMKAISGSARCISIDLPGHGGSkiqnhakeTQTEPTLSVELVADLLYKLIEHITPG 1445

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  137 KADIVGWSDGAIIGIDAAMRYPDRV-GKVFAyapnTTTAGVRTDTANNPLFARYITRA----------------SGE-YR 198
Cdd:PLN02980 1446 KVTLVGYSMGARIALYMALRFSDKIeGAVII----SGSPGLKDEVARKIRSAKDDSRArmlidhgleiflenwySGElWK 1521

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  199 RLSKTPQ---------QYENfVGQIGEMW------QSQPDWSDdrLKKIHTPILIADGDHDESI------IRSHLEHIAA 257
Cdd:PLN02980 1522 SLRNHPHfnkivasrlLHKD-VPSLAKLLsdlsigRQPSLWED--LKQCDTPLLLVVGEKDVKFkqiaqkMYREIGKSKE 1598

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 490261029  258 TIPQAG-----LLIMPDSSHFAFLQAPKEFNDALVNFLAR 292
Cdd:PLN02980 1599 SGNDKGkeiieIVEIPNCGHAVHLENPLPVIRALRKFLTR 1638
PRK05855 PRK05855
SDR family oxidoreductase;
70-133 1.62e-05

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 46.13  E-value: 1.62e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490261029  70 GSPVIFLHGGLANSDYWGNQIPVIARTHQVIVVDSRGHGRSS--RDSRPFGYDLMTDDVVALMDQL 133
Cdd:PRK05855  25 RPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSapKRTAAYTLARLADDFAAVIDAV 90
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 72-172 6.36e-05

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 44.10  E-value: 6.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  72 PVIFLHGGLANSDYWGNQIPVIARTHQVIVVDSRGHGRSSRDSRPFGYDLMTDDVV----ALMDQLKIAKADIVGWSDGA 147
Cdd:PLN03084 129 PVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDKPQPGYGFNYTLDEYVssleSLIDELKSDKVSLVVQGYFS 208

                         90       100
                 ....*....|....*....|....*
gi 490261029 148 IIGIDAAMRYPDRVGKVFAYAPNTT 172
Cdd:PLN03084 209 PPVVKYASAHPDKIKKLILLNPPLT 233
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
64-184 3.82e-04

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 41.38  E-value: 3.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  64 YGTVGQGSPV-IFLHGGLANSDYWGNQIPV-------IARtHQ-----VIVVDSRGHGRSSRDSRPFG--YDLMTDDVVA 128
Cdd:COG2382  105 YDNPGKKYPVlYLLDGGGGDEQDWFDQGRLptildnlIAA-GKippmiVVMPDGGDGGDRGTEGPGNDafERFLAEELIP 183

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490261029 129 LMDQLKIAKAD-----IVGWSDGAIIGIDAAMRYPDRVGKVFAYAPNTTTAGVRTDTANNP 184
Cdd:COG2382  184 FVEKNYRVSADpehraIAGLSMGGLAALYAALRHPDLFGYVGSFSGSFWWPPGDADRGGWA 244
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
62-292 7.58e-04

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 40.39  E-value: 7.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  62 LFYGTVGQGS-PVIFLHGGLANSDYWGNQIPVIARTHQVIVVDSRGHGRSSrdsrpfGYDLMT-DDVVALMDQLKIAKAD 139
Cdd:PRK10349   4 IWWQTKGQGNvHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSR------GFGALSlADMAEAVLQQAPDKAI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029 140 IVGWSDGAIIGIDAAMRYPDRVGKVFAYAPNTTTA------GVRTDtannpLFARYITRASGEYRRL-----------SK 202
Cdd:PRK10349  78 WLGWSLGGLVASQIALTHPERVQALVTVASSPCFSardewpGIKPD-----VLAGFQQQLSDDFQRTverflalqtmgTE 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029 203 TPQQYENFVGQIgEMWQSQPDWS------------DDR--LKKIHTPILIADGDHDESIIRSHLEHIAATIPQAGLLIMP 268
Cdd:PRK10349 153 TARQDARALKKT-VLALPMPEVDvlnggleilktvDLRqpLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFA 231

                        250       260
                 ....*....|....*....|....
gi 490261029 269 DSSHFAFLQAPKEFNDALVNFLAR 292
Cdd:PRK10349 232 KAAHAPFISHPAEFCHLLVALKQR 255
PRK08775 PRK08775
homoserine O-succinyltransferase;
70-168 9.50e-04

homoserine O-succinyltransferase;


Pssm-ID: 181553 [Multi-domain]  Cd Length: 343  Bit Score: 40.16  E-value: 9.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  70 GSPVIFLHGGLA-----------NSDYWGNQIPVIART-----HQVIVVDSRGhGRSSRDSRPFGYDlMTDDVVALMDQL 133
Cdd:PRK08775  57 GAPVVFVAGGISahrhvaatatfPEKGWWEGLVGSGRAldparFRLLAFDFIG-ADGSLDVPIDTAD-QADAIALLLDAL 134

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 490261029 134 KIAKAD-IVGWSDGAIIGIDAAMRYPDRVGKVFAYA 168
Cdd:PRK08775 135 GIARLHaFVGYSYGALVGLQFASRHPARVRTLVVVS 170
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 103-244 3.23e-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: 38.35  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  103 DSRGHGRSS-RDSRPFGYDLMTDDVVALMDQLK----IAKADIVGWSDGAIIGIDAAMRYPDRV-GKVFAyAPNTttaGV 176
Cdd:pfam12146  38 DHRGHGRSDgKRGHVPSFDDYVDDLDTFVDKIReehpGLPLFLLGHSMGGLIAALYALRYPDKVdGLILS-APAL---KI 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  177 RTDTAN----------NPLFARYITRASGEYRRLSKTPQQ---YEN--------FVGQIGEMWQSQpDWSDDRLKKIHTP 235
Cdd:pfam12146 114 KPYLAPpilkllakllGKLFPRLRVPNNLLPDSLSRDPEVvaaYAAdplvhggiSARTLYELLDAG-ERLLRRAAAITVP 192


                  ....*....
gi 490261029  236 ILIADGDHD 244
Cdd:pfam12146 193 LLLLHGGAD 201
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 72-169 3.36e-03

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 36.35  E-value: 3.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  72 PVIFLHGGLANSDYWGNQIPVIART-HQVIVVDSRGHGRSSRDSrpfGYDLMtDDVVALMDQLKIAKADIVGWSDGaiiG 150
Cdd:COG1075    7 PVVLVHGLGGSAASWAPLAPRLRAAgYPVYALNYPSTNGSIEDS---AEQLA-AFVDAVLAATGAEKVDLVGHSMG---G 79

                         90       100
                 ....*....|....*....|....*.
gi 490261029 151 IDAamRY-------PDRVGKVFAYAP 169
Cdd:COG1075   80 LVA--RYylkrlggAAKVARVVTLGT 103
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 70-166 4.94e-03

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 38.03  E-value: 4.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261029  70 GSPVIFLHGGLANSDYWGNQIPVIA-RTHQVIVVDSRGHGRSSRDSR--PFGYDLMTDDVVALMDQLKIAKADIVGWSDG 146
Cdd:PRK00870  46 GPPVLLLHGEPSWSYLYRKMIPILAaAGHRVIAPDLIGFGRSDKPTRreDYTYARHVEWMRSWFEQLDLTDVTLVCQDWG 125

                         90       100
                 ....*....|....*....|
gi 490261029 147 AIIGIDAAMRYPDRVGKVFA 166
Cdd:PRK00870 126 GLIGLRLAAEHPDRFARLVV 145
 
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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