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Conserved domains on  [gi|1448298693|ref|XP_014624051|]
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uncharacterized protein LOC100788200 [Glycine max]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02847 super family cl27225
triacylglycerol lipase
 53-380 0e+00

triacylglycerol lipase


The actual alignment was detected with superfamily member PLN02847:

Pssm-ID: 178439 [Multi-domain]  Cd Length: 633  Bit Score: 521.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448298693  53 MATAAGAVALLYYTLNRKLQTHDVIDEDGEENGSDSPAdtplGIGCVSHRLIQAPATWLETISTLLETLRFTYSETLGKW 132
Cdd:PLN02847    6 MATAVGAAVLLYYVLSRRLAAEDGEDGGGGGDGSSGRS----GRRRIARRPAQAPATWLETITTLSETLRFTYSETLGKW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448298693 133 PIRDLAFGINFLLKRQGNYHVGSEFCGKDSVQLKGSEITAELKYLLNLLTLCWHFSKKPFPLFLEETGYTEENVLLREAK 212
Cdd:PLN02847   82 PIGDLAFGINYLMRRQGNLQVASVYAGSNCIELKGPEIIAELIVLLRLLTLCMLFSKKPFPVFLELAGFSQEDVLIQKPK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448298693 213 AGILKPTFTIIADHKMGCLLLLIRGTHNIKDTLTTVTGNVVPFHHIVVNLGGVSDLVLGYAHCGMVAAARWIAKLATPCL 292
Cdd:PLN02847  162 AGILKPAFTIIRDENSKCFLLLIRGTHSIKDTLTAATGAVVPFHHSVLHDGGVSNLVLGYAHCGMVAAARWIAKLSTPCL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448298693 293 LEALGHYPDYKVKIVGHSLGGGTAAILTYVLRERKDLPVTTCITFAPAACMTWELAESGDSFITSIINGADLVPTFSVAF 372
Cdd:PLN02847  242 LKALDEYPDFKIKIVGHSLGGGTAALLTYILREQKEFSSTTCVTFAPAACMTWDLAESGKHFITTIINGSDLVPTFSAAS 321


                  ....*...
gi 1448298693 373 VDDLCSEV 380
Cdd:PLN02847  322 VDDLRSEV 329
tify pfam06200
tify domain; This short possible domain is found in a variety of plant transcription factors ...
 24-50 4.50e-12

tify domain; This short possible domain is found in a variety of plant transcription factors that contain GATA domains as well as other motifs. Although previously known as the Zim domain this is now called the tify domain after its most conserved amino acids. TIFY proteins can be further classified into two groups depending on the presence (group I) or absence (group II) of a C2C2-GATA domain. Functional annotation of these proteins is still poor, but several screens revealed a link between TIFY proteins of group II and jasmonic acid-related stress response.


:

Pssm-ID: 461847  Cd Length: 33  Bit Score: 60.08  E-value: 4.50e-12
                          10        20
                  ....*....|....*....|....*..
gi 1448298693  24 AKAAQLTIFYDGQVVVFDDFPADKVQE 50
Cdd:pfam06200   1 PASAQLTIFYGGKVCVFDDVPAEKAQA 27
 
Name Accession Description Interval E-value
PLN02847 PLN02847
triacylglycerol lipase
 53-380 0e+00

triacylglycerol lipase


Pssm-ID: 178439 [Multi-domain]  Cd Length: 633  Bit Score: 521.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448298693  53 MATAAGAVALLYYTLNRKLQTHDVIDEDGEENGSDSPAdtplGIGCVSHRLIQAPATWLETISTLLETLRFTYSETLGKW 132
Cdd:PLN02847    6 MATAVGAAVLLYYVLSRRLAAEDGEDGGGGGDGSSGRS----GRRRIARRPAQAPATWLETITTLSETLRFTYSETLGKW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448298693 133 PIRDLAFGINFLLKRQGNYHVGSEFCGKDSVQLKGSEITAELKYLLNLLTLCWHFSKKPFPLFLEETGYTEENVLLREAK 212
Cdd:PLN02847   82 PIGDLAFGINYLMRRQGNLQVASVYAGSNCIELKGPEIIAELIVLLRLLTLCMLFSKKPFPVFLELAGFSQEDVLIQKPK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448298693 213 AGILKPTFTIIADHKMGCLLLLIRGTHNIKDTLTTVTGNVVPFHHIVVNLGGVSDLVLGYAHCGMVAAARWIAKLATPCL 292
Cdd:PLN02847  162 AGILKPAFTIIRDENSKCFLLLIRGTHSIKDTLTAATGAVVPFHHSVLHDGGVSNLVLGYAHCGMVAAARWIAKLSTPCL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448298693 293 LEALGHYPDYKVKIVGHSLGGGTAAILTYVLRERKDLPVTTCITFAPAACMTWELAESGDSFITSIINGADLVPTFSVAF 372
Cdd:PLN02847  242 LKALDEYPDFKIKIVGHSLGGGTAALLTYILREQKEFSSTTCVTFAPAACMTWDLAESGKHFITTIINGSDLVPTFSAAS 321


                  ....*...
gi 1448298693 373 VDDLCSEV 380
Cdd:PLN02847  322 VDDLRSEV 329
Lipase_3 pfam01764
Lipase (class 3);
233-369 7.90e-33

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 120.06  E-value: 7.90e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448298693 233 LLIRGTHNIKDTLTTVTGNVVPFHHIVVNLGgvsdlvlgYAHCGMVAAARWIAKLATPCLLEALGHYPDYKVKIVGHSLG 312
Cdd:pfam01764   2 VAFRGTNSILDWLTDFDFSLTPFKDFFLGGG--------KVHSGFLSAYTSVREQVLAELKRLLEKYPDYSIVVTGHSLG 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1448298693 313 GGTAAILTYVLRERKDLPV--TTCITFAPAACMTWELAESGDS----FITSIINGADLVPTFS 369
Cdd:pfam01764  74 GALASLAALDLVENGLRLSsrVTVVTFGQPRVGNLEFAKLHDSqgpkFSYRVVHQRDIVPRLP 136
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 225-369 6.33e-32

Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 120.66  E-value: 6.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448298693 225 DHKMGCLLLLIRGTHNIKDTLTTVTGNVVPFHHIVVNLGgvsdlvlgYAHCGMVAAARWIAKLATPCLLEALGHYPDYKV 304
Cdd:cd00519    59 DHDRKTIVIAFRGTVSLADWLTDLDFSPVPLDPPLCSGG--------KVHSGFYSAYKSLYNQVLPELKSALKQYPDYKI 130

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1448298693 305 KIVGHSLGGGTAAILTYVLRERKDLPVTTCITFAPAACMTWELAE---SGDSFITSIINGADLVPTFS 369
Cdd:cd00519   131 IVTGHSLGGALASLLALDLRLRGPGSDVTVYTFGQPRVGNAAFAEyleSTKGRVYRVVHGNDIVPRLP 198
tify pfam06200
tify domain; This short possible domain is found in a variety of plant transcription factors ...
 24-50 4.50e-12

tify domain; This short possible domain is found in a variety of plant transcription factors that contain GATA domains as well as other motifs. Although previously known as the Zim domain this is now called the tify domain after its most conserved amino acids. TIFY proteins can be further classified into two groups depending on the presence (group I) or absence (group II) of a C2C2-GATA domain. Functional annotation of these proteins is still poor, but several screens revealed a link between TIFY proteins of group II and jasmonic acid-related stress response.


Pssm-ID: 461847  Cd Length: 33  Bit Score: 60.08  E-value: 4.50e-12
                          10        20
                  ....*....|....*....|....*..
gi 1448298693  24 AKAAQLTIFYDGQVVVFDDFPADKVQE 50
Cdd:pfam06200   1 PASAQLTIFYGGKVCVFDDVPAEKAQA 27
TIFY smart00979
This short possible domain is found in a variety of plant transcription factors that contain ...
 26-58 3.60e-08

This short possible domain is found in a variety of plant transcription factors that contain GATA domains as well as other motifs; Although previously known as the Zim domain this is now called the tify domain after its most conserved amino acids. TIFY proteins can be further classified into two groups depending on the presence (group I) or absence (group II) of a C2C2-GATA domain. Functional annotation of these proteins is still poor, but several screens revealed a link between TIFY proteins of group II and jasmonic acid-related stress response.


Pssm-ID: 198047  Cd Length: 36  Bit Score: 48.80  E-value: 3.60e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1448298693   26 AAQLTIFYDGQVVVFDDFPADKVQETkMATAAG 58
Cdd:smart00979   5 SQQLTIFYGGSVCVFDDVPPEKAQEI-MSLAGN 36
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
235-367 1.31e-04

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 43.20  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448298693 235 IRGTHNIKDTLTTVTGNVVPFHHivvnlggvsDLVLGYAHCG---MVAAARwiaklatPCLLEAL-GHYPDYKVKIVGHS 310
Cdd:COG3675    33 FRGTESLTDWLTNLNAAQVPYPF---------AKTGGKVHRGfyrALQSLR-------ELLEDALrPLSPGKRLYVTGHS 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1448298693 311 LGGGTAAILTYVLRERKDLPVTTCITFAPAACMTWELAES-----GDSFitSIINGADLVPT 367
Cdd:COG3675    97 LGGALATLAAADLERNYIFPVRGLYTFGQPRVGDRSFAKYynlhvPNSY--RIVNNNDIVPL 156
 
Name Accession Description Interval E-value
PLN02847 PLN02847
triacylglycerol lipase
 53-380 0e+00

triacylglycerol lipase


Pssm-ID: 178439 [Multi-domain]  Cd Length: 633  Bit Score: 521.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448298693  53 MATAAGAVALLYYTLNRKLQTHDVIDEDGEENGSDSPAdtplGIGCVSHRLIQAPATWLETISTLLETLRFTYSETLGKW 132
Cdd:PLN02847    6 MATAVGAAVLLYYVLSRRLAAEDGEDGGGGGDGSSGRS----GRRRIARRPAQAPATWLETITTLSETLRFTYSETLGKW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448298693 133 PIRDLAFGINFLLKRQGNYHVGSEFCGKDSVQLKGSEITAELKYLLNLLTLCWHFSKKPFPLFLEETGYTEENVLLREAK 212
Cdd:PLN02847   82 PIGDLAFGINYLMRRQGNLQVASVYAGSNCIELKGPEIIAELIVLLRLLTLCMLFSKKPFPVFLELAGFSQEDVLIQKPK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448298693 213 AGILKPTFTIIADHKMGCLLLLIRGTHNIKDTLTTVTGNVVPFHHIVVNLGGVSDLVLGYAHCGMVAAARWIAKLATPCL 292
Cdd:PLN02847  162 AGILKPAFTIIRDENSKCFLLLIRGTHSIKDTLTAATGAVVPFHHSVLHDGGVSNLVLGYAHCGMVAAARWIAKLSTPCL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448298693 293 LEALGHYPDYKVKIVGHSLGGGTAAILTYVLRERKDLPVTTCITFAPAACMTWELAESGDSFITSIINGADLVPTFSVAF 372
Cdd:PLN02847  242 LKALDEYPDFKIKIVGHSLGGGTAALLTYILREQKEFSSTTCVTFAPAACMTWDLAESGKHFITTIINGSDLVPTFSAAS 321


                  ....*...
gi 1448298693 373 VDDLCSEV 380
Cdd:PLN02847  322 VDDLRSEV 329
Lipase_3 pfam01764
Lipase (class 3);
233-369 7.90e-33

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 120.06  E-value: 7.90e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448298693 233 LLIRGTHNIKDTLTTVTGNVVPFHHIVVNLGgvsdlvlgYAHCGMVAAARWIAKLATPCLLEALGHYPDYKVKIVGHSLG 312
Cdd:pfam01764   2 VAFRGTNSILDWLTDFDFSLTPFKDFFLGGG--------KVHSGFLSAYTSVREQVLAELKRLLEKYPDYSIVVTGHSLG 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1448298693 313 GGTAAILTYVLRERKDLPV--TTCITFAPAACMTWELAESGDS----FITSIINGADLVPTFS 369
Cdd:pfam01764  74 GALASLAALDLVENGLRLSsrVTVVTFGQPRVGNLEFAKLHDSqgpkFSYRVVHQRDIVPRLP 136
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 225-369 6.33e-32

Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 120.66  E-value: 6.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448298693 225 DHKMGCLLLLIRGTHNIKDTLTTVTGNVVPFHHIVVNLGgvsdlvlgYAHCGMVAAARWIAKLATPCLLEALGHYPDYKV 304
Cdd:cd00519    59 DHDRKTIVIAFRGTVSLADWLTDLDFSPVPLDPPLCSGG--------KVHSGFYSAYKSLYNQVLPELKSALKQYPDYKI 130

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1448298693 305 KIVGHSLGGGTAAILTYVLRERKDLPVTTCITFAPAACMTWELAE---SGDSFITSIINGADLVPTFS 369
Cdd:cd00519   131 IVTGHSLGGALASLLALDLRLRGPGSDVTVYTFGQPRVGNAAFAEyleSTKGRVYRVVHGNDIVPRLP 198
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 275-369 4.10e-25

Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 99.88  E-value: 4.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448298693 275 CGMVAAARWIAKLATPCLLEALGHYPDYKVKIVGHSLGGGTAAILTYVLRERKDLPVTTCITFAPAACMTWELA-----E 349
Cdd:cd00741     1 KGFYKAARSLANLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLDLRGRGLGRLVRVYTFGPPRVGNAAFAedrldP 80

                          90       100
                  ....*....|....*....|
gi 1448298693 350 SGDSFITSIINGADLVPTFS 369
Cdd:cd00741    81 SDALFVDRIVNDNDIVPRLP 100
Lipase3_N pfam03893
Lipase 3 N-terminal region; N terminal region to pfam01764, found on a subset of Lipase 3 ...
 99-173 1.59e-13

Lipase 3 N-terminal region; N terminal region to pfam01764, found on a subset of Lipase 3 containing proteins.


Pssm-ID: 427574  Cd Length: 75  Bit Score: 65.20  E-value: 1.59e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1448298693  99 VSHRLIQAPATWLETISTLLETLRFTYSETLGKWPIRDLAFginFLLKRQGNYHVGSEFCGKdsvqLKGSEITAE 173
Cdd:pfam03893   2 LSCLSCLACARWAWKTSTLSRECSYTYSEDFNFWPQYAAAE---YEPVPRGARVGLAVYCGK----LRCPEVEPA 69
tify pfam06200
tify domain; This short possible domain is found in a variety of plant transcription factors ...
 24-50 4.50e-12

tify domain; This short possible domain is found in a variety of plant transcription factors that contain GATA domains as well as other motifs. Although previously known as the Zim domain this is now called the tify domain after its most conserved amino acids. TIFY proteins can be further classified into two groups depending on the presence (group I) or absence (group II) of a C2C2-GATA domain. Functional annotation of these proteins is still poor, but several screens revealed a link between TIFY proteins of group II and jasmonic acid-related stress response.


Pssm-ID: 461847  Cd Length: 33  Bit Score: 60.08  E-value: 4.50e-12
                          10        20
                  ....*....|....*....|....*..
gi 1448298693  24 AKAAQLTIFYDGQVVVFDDFPADKVQE 50
Cdd:pfam06200   1 PASAQLTIFYGGKVCVFDDVPAEKAQA 27
TIFY smart00979
This short possible domain is found in a variety of plant transcription factors that contain ...
 26-58 3.60e-08

This short possible domain is found in a variety of plant transcription factors that contain GATA domains as well as other motifs; Although previously known as the Zim domain this is now called the tify domain after its most conserved amino acids. TIFY proteins can be further classified into two groups depending on the presence (group I) or absence (group II) of a C2C2-GATA domain. Functional annotation of these proteins is still poor, but several screens revealed a link between TIFY proteins of group II and jasmonic acid-related stress response.


Pssm-ID: 198047  Cd Length: 36  Bit Score: 48.80  E-value: 3.60e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1448298693   26 AAQLTIFYDGQVVVFDDFPADKVQETkMATAAG 58
Cdd:smart00979   5 SQQLTIFYGGSVCVFDDVPPEKAQEI-MSLAGN 36
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
235-367 1.31e-04

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 43.20  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448298693 235 IRGTHNIKDTLTTVTGNVVPFHHivvnlggvsDLVLGYAHCG---MVAAARwiaklatPCLLEAL-GHYPDYKVKIVGHS 310
Cdd:COG3675    33 FRGTESLTDWLTNLNAAQVPYPF---------AKTGGKVHRGfyrALQSLR-------ELLEDALrPLSPGKRLYVTGHS 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1448298693 311 LGGGTAAILTYVLRERKDLPVTTCITFAPAACMTWELAES-----GDSFitSIINGADLVPT 367
Cdd:COG3675    97 LGGALATLAAADLERNYIFPVRGLYTFGQPRVGDRSFAKYynlhvPNSY--RIVNNNDIVPL 156
 
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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