NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|24111379|gb|AAN46813|]
View 

At1g15070/F9L1_1 [Arabidopsis thaliana]

Protein Classification

alpha/beta fold hydrolase domain-containing protein( domain architecture ID 1002311)

alpha/beta fold hydrolase domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PhaC super family cl43819
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];
328-552 4.89e-21

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: 96.95  E-value: 4.89e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379 328 DWDFDHYLEEDVPAAIEYVRAQSKPKdgKLFAIGHSMGGILLYAMLSRCAFEGREPsVAAVATLASSVDYTTSNsALKLL 407
Cdd:COG3243 252 DLGLDDYVEDGILAAVDAVREITGED--KVNLLGYCLGGTLLAIYAALLAARGPDR-VASLTLLATPLDFSEPG-ELGVF 327

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379 408 I--PLANPAEAL--SVPVVPlGALLAAAFpLSTRP------PYV--------------LSWLNDlisSTDM---MHPEML 460
Cdd:COG3243 328 IdeSQLADLEALmaAKGYLP-GRLMAGAF-SLLRPndliwsYYVnnyllgenpppfdlLYWNAD---STRLpgrMHSQYL 402

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379 461 EKLVLNNfctipaklliqlttAFREGGLR--DRsgkfyyKDHLPRTSVPVLALAGDRDLICPPAAVEDTVKLFPENLVTY 538
Cdd:COG3243 403 RDLYLEN--------------RLAKGELElgGR------PVDLSDITVPVLVVAGEEDHIAPWRSVYALAQLVGGKDVTF 462

                       250       260
                ....*....|....*....|...
gi 24111379 539 KL---------LGEPDGPHYAHY 552
Cdd:COG3243 463 VLapgghiggiVNPPGKPKRSYW 485
PldB super family cl34450
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
78-164 2.67e-03

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


The actual alignment was detected with superfamily member COG2267:

Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 39.60  E-value: 2.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379  78 DWRLALWRYLPPPQAPTrnhPLLLLSGVGTNAIGYDlspgcSFARHMSGQGFETWILEVRGAGLSTR----VSDLKDVEE 153
Cdd:COG2267  13 GLRLRGRRWRPAGSPRG---TVVLVHGLGEHSGRYA-----ELAEALAAAGYAVLAFDLRGHGRSDGprghVDSFDDYVD 84

                        90
                ....*....|.
gi 24111379 154 SAHELSNQIES 164
Cdd:COG2267  85 DLRAALDALRA 95
 
Name Accession Description Interval E-value
PhaC COG3243
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];
328-552 4.89e-21

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


Pssm-ID: 442475 [Multi-domain]  Cd Length: 545  Bit Score: 96.95  E-value: 4.89e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379 328 DWDFDHYLEEDVPAAIEYVRAQSKPKdgKLFAIGHSMGGILLYAMLSRCAFEGREPsVAAVATLASSVDYTTSNsALKLL 407
Cdd:COG3243 252 DLGLDDYVEDGILAAVDAVREITGED--KVNLLGYCLGGTLLAIYAALLAARGPDR-VASLTLLATPLDFSEPG-ELGVF 327

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379 408 I--PLANPAEAL--SVPVVPlGALLAAAFpLSTRP------PYV--------------LSWLNDlisSTDM---MHPEML 460
Cdd:COG3243 328 IdeSQLADLEALmaAKGYLP-GRLMAGAF-SLLRPndliwsYYVnnyllgenpppfdlLYWNAD---STRLpgrMHSQYL 402

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379 461 EKLVLNNfctipaklliqlttAFREGGLR--DRsgkfyyKDHLPRTSVPVLALAGDRDLICPPAAVEDTVKLFPENLVTY 538
Cdd:COG3243 403 RDLYLEN--------------RLAKGELElgGR------PVDLSDITVPVLVVAGEEDHIAPWRSVYALAQLVGGKDVTF 462

                       250       260
                ....*....|....*....|...
gi 24111379 539 KL---------LGEPDGPHYAHY 552
Cdd:COG3243 463 VLapgghiggiVNPPGKPKRSYW 485
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 330-545 1.93e-10

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


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 61.08  E-value: 1.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379   330 DFDHYLEeDVPAAIEYVRAQSKPKdgKLFAIGHSMGGI--LLYAMLSRCAFEGrepsvaavatlassvdyttsnsalklL 407
Cdd:pfam12146  54 SFDDYVD-DLDTFVDKIREEHPGL--PLFLLGHSMGGLiaALYALRYPDKVDG--------------------------L 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379   408 IpLANPAEALSVPVVPLGALLAAAFPLSTRPPYVLSWLNDLISSTDmmHPEMLEKLVLNNFCT--IPAKLLIQLTTAFRE 485
Cdd:pfam12146 105 I-LSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVPNNLLPDSLSR--DPEVVAAYAADPLVHggISARTLYELLDAGER 181

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24111379   486 ggLRDRSGKFyykdhlprtSVPVLALAGDRDLICPPAAVEDTVKLFPENLVTYK--------LLGEPD 545
Cdd:pfam12146 182 --LLRRAAAI---------TVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKlypglyheLLNEPD 238
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
78-164 2.67e-03

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 39.60  E-value: 2.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379  78 DWRLALWRYLPPPQAPTrnhPLLLLSGVGTNAIGYDlspgcSFARHMSGQGFETWILEVRGAGLSTR----VSDLKDVEE 153
Cdd:COG2267  13 GLRLRGRRWRPAGSPRG---TVVLVHGLGEHSGRYA-----ELAEALAAAGYAVLAFDLRGHGRSDGprghVDSFDDYVD 84

                        90
                ....*....|.
gi 24111379 154 SAHELSNQIES 164
Cdd:COG2267  85 DLRAALDALRA 95
 
Name Accession Description Interval E-value
PhaC COG3243
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];
328-552 4.89e-21

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


Pssm-ID: 442475 [Multi-domain]  Cd Length: 545  Bit Score: 96.95  E-value: 4.89e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379 328 DWDFDHYLEEDVPAAIEYVRAQSKPKdgKLFAIGHSMGGILLYAMLSRCAFEGREPsVAAVATLASSVDYTTSNsALKLL 407
Cdd:COG3243 252 DLGLDDYVEDGILAAVDAVREITGED--KVNLLGYCLGGTLLAIYAALLAARGPDR-VASLTLLATPLDFSEPG-ELGVF 327

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379 408 I--PLANPAEAL--SVPVVPlGALLAAAFpLSTRP------PYV--------------LSWLNDlisSTDM---MHPEML 460
Cdd:COG3243 328 IdeSQLADLEALmaAKGYLP-GRLMAGAF-SLLRPndliwsYYVnnyllgenpppfdlLYWNAD---STRLpgrMHSQYL 402

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379 461 EKLVLNNfctipaklliqlttAFREGGLR--DRsgkfyyKDHLPRTSVPVLALAGDRDLICPPAAVEDTVKLFPENLVTY 538
Cdd:COG3243 403 RDLYLEN--------------RLAKGELElgGR------PVDLSDITVPVLVVAGEEDHIAPWRSVYALAQLVGGKDVTF 462

                       250       260
                ....*....|....*....|...
gi 24111379 539 KL---------LGEPDGPHYAHY 552
Cdd:COG3243 463 VLapgghiggiVNPPGKPKRSYW 485
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 330-545 1.93e-10

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


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 61.08  E-value: 1.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379   330 DFDHYLEeDVPAAIEYVRAQSKPKdgKLFAIGHSMGGI--LLYAMLSRCAFEGrepsvaavatlassvdyttsnsalklL 407
Cdd:pfam12146  54 SFDDYVD-DLDTFVDKIREEHPGL--PLFLLGHSMGGLiaALYALRYPDKVDG--------------------------L 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379   408 IpLANPAEALSVPVVPLGALLAAAFPLSTRPPYVLSWLNDLISSTDmmHPEMLEKLVLNNFCT--IPAKLLIQLTTAFRE 485
Cdd:pfam12146 105 I-LSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVPNNLLPDSLSR--DPEVVAAYAADPLVHggISARTLYELLDAGER 181

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24111379   486 ggLRDRSGKFyykdhlprtSVPVLALAGDRDLICPPAAVEDTVKLFPENLVTYK--------LLGEPD 545
Cdd:pfam12146 182 --LLRRAAAI---------TVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKlypglyheLLNEPD 238
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
337-577 4.36e-10

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 60.34  E-value: 4.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379 337 EDVPAAIEYVRAQSKpkdgKLFAIGHSMGGIL-LYAMLsrcafegREPSVAAVATLASSVDYTTSnsalklliplanpae 415
Cdd:COG1647  70 EDVEEAYEILKAGYD----KVIVIGLSMGGLLaLLLAA-------RYPDVAGLVLLSPALKIDDP--------------- 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379 416 alSVPVVPLGALLAAAFPLSTRppyvlswlndlisstDMMHPEMLEKlvlnNFCTIPAKLLIQLTTAFRegglrdrsgkf 495
Cdd:COG1647 124 --SAPLLPLLKYLARSLRGIGS---------------DIEDPEVAEY----AYDRTPLRALAELQRLIR----------- 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379 496 YYKDHLPRTSVPVLALAGDRDLICPPAAVEDTVKLFPENLVTYKLLgePDGPHYAHYDlvggrLAVEQVYPCITEFLSHH 575
Cdd:COG1647 172 EVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWL--EDSGHVITLD-----KDREEVAEEILDFLERL 244


                ..
gi 24111379 576 DS 577
Cdd:COG1647 245 AA 246
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
327-572 1.50e-09

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 58.47  E-value: 1.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379 327 YDWDFDHYLEeDVPAAIEYVRAQSkpkDGKLFAIGHSMGGILLYAMLSRcafegREPSVAAVAtlassvdyttsnsalkl 406
Cdd:COG2267  75 HVDSFDDYVD-DLRAALDALRARP---GLPVVLLGHSMGGLIALLYAAR-----YPDRVAGLV----------------- 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379 407 liplanpaealsvpvvplgallaaafplstrppyvlswlndLISSTDMMHPEmleklvlnnfCTIPAKLLIQLTTAfreg 486
Cdd:COG2267 129 -----------------------------------------LLAPAYRADPL----------LGPSARWLRALRLA---- 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379 487 glrdrsgkfyykDHLPRTSVPVLALAGDRDLICPPAAVEDTVKLFPENlVTYKLLgePDGPHYAHYDLVGgrlavEQVYP 566
Cdd:COG2267 154 ------------EALARIDVPVLVLHGGADRVVPPEAARRLAARLSPD-VELVLL--PGARHELLNEPAR-----EEVLA 213


                ....*.
gi 24111379 567 CITEFL 572
Cdd:COG2267 214 AILAWL 219
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 329-553 5.92e-08

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: 54.05  E-value: 5.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379   329 WDFDHYLEEDVPAAIEYVRAQSKpkDGKLFAIGHSMGGILLYAMLSRcaFEGREPSVAAVATLASSVDYTTSNSALKLLI 408
Cdd:pfam00561  45 KAQDDYRTDDLAEDLEYILEALG--LEKVNLVGHSMGGLIALAYAAK--YPDRVKALVLLGALDPPHELDEADRFILALF 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379   409 PLANPAEALSVPVVPLGALLA---AAFPLSTRPPYVLSWLNDLISSTDMMHPEMLEKLVLNNFCTIPAKLLIQLTTAFRE 485
Cdd:pfam00561 121 PGFFDGFVADFAPNPLGRLVAkllALLLLRLRLLKALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDE 200

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24111379   486 gglrdrsgkfyykdhlprtsvPVLALAGDRDLICPPAAVEDTVKLFPENlvtyKLLGEPDGPHYAHYD 553
Cdd:pfam00561 201 ---------------------PTLIIWGDQDPLVPPQALEKLAQLFPNA----RLVVIPDAGHFAFLE 243
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 456-575 2.03e-07

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: 51.93  E-value: 2.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379 456 HPEMLEKLVLNNfctipaKLLIQLTTAFREGGLRDRS--------GKFYYKDHLPRTSVPVLALAGDRDLICPPAAVEDT 527
Cdd:COG0596 110 HPERVAGLVLVD------EVLAALAEPLRRPGLAPEAlaallralARTDLRERLARITVPTLVIWGEKDPIVPPALARRL 183

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 24111379 528 VKLFPEnlVTYKLLgePDGPHYAHYDlvggrlAVEQVYPCITEFLSHH 575
Cdd:COG0596 184 AELLPN--AELVVL--PGAGHFPPLE------QPEAFAAALRDFLARL 221
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
274-389 2.39e-05

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 45.73  E-value: 2.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379 274 NSGLVNQVRDLAQRLVNLfddGQRSVSPpliDLQERLtATIEDFQKQLDLIVKYDWDFdhyLEEDVPAAIEYVRAQSKPK 353
Cdd:COG0412  38 IFGLNPHIRDVARRLAAA---GYVVLAP---DLYGRG-GPGDDPDEARALMGALDPEL---LAADLRAALDWLKAQPEVD 107

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 24111379 354 DGKLFAIGHSMGG--ILLYAmlsrcafeGREPSVAAVA 389
Cdd:COG0412 108 AGRVGVVGFCFGGglALLAA--------ARGPDLAAAV 137
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
330-399 5.39e-04

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 41.93  E-value: 5.39e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24111379 330 DFDHYLEEDVPAAIEYVRAQSKPKDGKLFAIGHSMGGIL-LYAMlsrcafeGREPS-VAAVATLASSVDYTT 399
Cdd:COG1506  68 DWGGDEVDDVLAAIDYLAARPYVDPDRIGIYGHSYGGYMaLLAA-------ARHPDrFKAAVALAGVSDLRS 132
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 337-393 8.16e-04

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 39.04  E-value: 8.16e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24111379 337 EDVPAAIEYVRAQSKpkDGKLFAIGHSMGGILLYAMLSRcafEGREPSVAAVATLAS 393
Cdd:COG1075  52 EQLAAFVDAVLAATG--AEKVDLVGHSMGGLVARYYLKR---LGGAAKVARVVTLGT 103
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
78-164 2.67e-03

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 39.60  E-value: 2.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111379  78 DWRLALWRYLPPPQAPTrnhPLLLLSGVGTNAIGYDlspgcSFARHMSGQGFETWILEVRGAGLSTR----VSDLKDVEE 153
Cdd:COG2267  13 GLRLRGRRWRPAGSPRG---TVVLVHGLGEHSGRYA-----ELAEALAAAGYAVLAFDLRGHGRSDGprghVDSFDDYVD 84

                        90
                ....*....|.
gi 24111379 154 SAHELSNQIES 164
Cdd:COG2267  85 DLRAALDALRA 95
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
72-144 8.15e-03

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


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 38.33  E-value: 8.15e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24111379  72 VSVPNTD-WRLALWRYLPPPQAPtrnHPLLLLSGVGTNAIGYDlspgcSFARHMSGQGFETWILEVRGAGLSTR 144
Cdd:COG4757  10 VTITAADgYPLAARLFPPAGPPR---AVVLINPATGVPQRFYR-----PFARYLAERGFAVLTYDYRGIGLSRP 75
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH