NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|569000921|ref|XP_006524645|]
View 

omega-hydroxyceramide transacylase isoform X1 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Patatin_and_cPLA2 super family cl11396
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 2-296 4.34e-159

Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates. This family also includes the catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms.


The actual alignment was detected with superfamily member cd07219:

Pssm-ID: 416256  Cd Length: 382  Bit Score: 457.43  E-value: 4.34e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921   2 GLAEVKKFFLGPLSPSCKMVQMMRQFLYDVLPEDSYKFATGKLHVSLTRVTDGENVVVSEYRSKEELIEALYCSCFVPVY 81
Cdd:cd07219   77 GVAEVRKSFLGPLSPSCKMVQMMRQFLYRVLPEDSYKVATGKLHVSLTRVTDGENVVVSEFTSKEELIEALYCSCFVPVY 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921  82 CGFIPPTYRGERYIDGGFTSMQPCSFWTDSITISTFSSQQDICPRDCPTIFHDFRMFNFSFQFSLENITRMTHALFPPDL 161
Cdd:cd07219  157 CGLIPPTYRGVRYIDGGFTGMQPCSFWTDSITISTFSGQQDICPRDCPAIFHDFRIFNCSFQFSLENIARMTHALFPPDL 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921 162 VILQEYYYRGYNDAVSYLRRLNAAYLDSPSKRVIFPRVEVYCQievALGHEPPPPSLQNLPALRRSPADSSQTHAQGSPK 241
Cdd:cd07219  237 MVLHDYYYRGYQDTVLYLRRLNAVYLNSPSKRVIFPRVEVYCQ---ALGKECPQRSQPSLQDGQASLEESWQPHLARAPK 313

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 569000921 242 KDRKDSHSS-AAPSVQTPESGCKESVESPVSLRVSISKQPSVSPLSPAQPVPVMRP 296
Cdd:cd07219  314 GDGRGLHDPpLSPPLAAPESTAEWVVESPVSSPASPLESSPSLPGSLTDLSPASLP 369
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
 211-497 6.03e-07

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 52.38  E-value: 6.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921 211 HEPPP-PSLQNLPALRRSPADSSQTHAQGSPKKDRKDSHSSAAPSVQTPESgckesvespvsLRVSISKQPSVSPLSPAQ 289
Cdd:PTZ00449 567 HKPSKiPTLSKKPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPEL-----------LDIPKSPKRPESPKSPKR 635

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921 290 PVPVMRPTGP-RDSCPINVQTPNPERGVKGALDSATERGMKDALASATDEQSTTTLPPVLLPAADSRGSKTGSSVPIGSP 368
Cdd:PTZ00449 636 PPPPQRPSSPeRPEGPKIIKSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPF 715

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921 369 ESPRLLlrssqgatasratlglpplspstppagPPVEDLGPERP-TATGSPALSQLTGS--AAPGTGKKAPHKPLLVEGP 445
Cdd:PTZ00449 716 TTPRPL---------------------------PPKLPRDEEFPfEPIGDPDAEQPDDIefFTPPEEERTFFHETPADTP 768

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 569000921 446 GEDSNTakTMFKRKQKTNATREcfhRNAQSKKPASKLKSAPCPL-NFPVLPKR 497
Cdd:PTZ00449 769 LPDILA--EEFKEEDIHAETGE---PDEAMKRPDSPSEHEDKPPgDHPSLPKK 816
 
Name Accession Description Interval E-value
Pat_PNPLA1 cd07219
Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin ...
 2-296 4.34e-159

Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin domain, initially discovered in potato tubers. Some members of PNPLA1 subfamily do not have the lipase consensus sequence Gly-X-Ser-X-Gly which is essential for hydrolase activity. This family includes PNPLA1 from Homo sapiens and Gallus gallus. Currently, there is no literature available on the physiological role, structure, or enzymatic activity of PNPLA1. It is expressed in various human tissues in low mRNA levels.


Pssm-ID: 132858  Cd Length: 382  Bit Score: 457.43  E-value: 4.34e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921   2 GLAEVKKFFLGPLSPSCKMVQMMRQFLYDVLPEDSYKFATGKLHVSLTRVTDGENVVVSEYRSKEELIEALYCSCFVPVY 81
Cdd:cd07219   77 GVAEVRKSFLGPLSPSCKMVQMMRQFLYRVLPEDSYKVATGKLHVSLTRVTDGENVVVSEFTSKEELIEALYCSCFVPVY 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921  82 CGFIPPTYRGERYIDGGFTSMQPCSFWTDSITISTFSSQQDICPRDCPTIFHDFRMFNFSFQFSLENITRMTHALFPPDL 161
Cdd:cd07219  157 CGLIPPTYRGVRYIDGGFTGMQPCSFWTDSITISTFSGQQDICPRDCPAIFHDFRIFNCSFQFSLENIARMTHALFPPDL 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921 162 VILQEYYYRGYNDAVSYLRRLNAAYLDSPSKRVIFPRVEVYCQievALGHEPPPPSLQNLPALRRSPADSSQTHAQGSPK 241
Cdd:cd07219  237 MVLHDYYYRGYQDTVLYLRRLNAVYLNSPSKRVIFPRVEVYCQ---ALGKECPQRSQPSLQDGQASLEESWQPHLARAPK 313

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 569000921 242 KDRKDSHSS-AAPSVQTPESGCKESVESPVSLRVSISKQPSVSPLSPAQPVPVMRP 296
Cdd:cd07219  314 GDGRGLHDPpLSPPLAAPESTAEWVVESPVSSPASPLESSPSLPGSLTDLSPASLP 369
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 211-497 6.03e-07

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 52.38  E-value: 6.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921 211 HEPPP-PSLQNLPALRRSPADSSQTHAQGSPKKDRKDSHSSAAPSVQTPESgckesvespvsLRVSISKQPSVSPLSPAQ 289
Cdd:PTZ00449 567 HKPSKiPTLSKKPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPEL-----------LDIPKSPKRPESPKSPKR 635

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921 290 PVPVMRPTGP-RDSCPINVQTPNPERGVKGALDSATERGMKDALASATDEQSTTTLPPVLLPAADSRGSKTGSSVPIGSP 368
Cdd:PTZ00449 636 PPPPQRPSSPeRPEGPKIIKSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPF 715

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921 369 ESPRLLlrssqgatasratlglpplspstppagPPVEDLGPERP-TATGSPALSQLTGS--AAPGTGKKAPHKPLLVEGP 445
Cdd:PTZ00449 716 TTPRPL---------------------------PPKLPRDEEFPfEPIGDPDAEQPDDIefFTPPEEERTFFHETPADTP 768

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 569000921 446 GEDSNTakTMFKRKQKTNATREcfhRNAQSKKPASKLKSAPCPL-NFPVLPKR 497
Cdd:PTZ00449 769 LPDILA--EEFKEEDIHAETGE---PDEAMKRPDSPSEHEDKPPgDHPSLPKK 816
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 9-104 1.76e-06

Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein but it also has the enzymatic activity of lipid acyl hydrolase, catalysing the cleavage of fatty acids from membrane lipids. Members of this family have been found also in vertebrates.


Pssm-ID: 396341  Cd Length: 190  Bit Score: 48.76  E-value: 1.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921    9 FFLGPLSPSCKMVQMMRQFLYDVLPEDSYKFA---------TGKLHVSLTRVTDGENVVVSEYRSKEELIEALYCSCFVP 79
Cdd:pfam01734  83 IGEGGLFDGDALRELLRKLLGDLTLEELAARLslllvvalrALLTVISTALGTRARILLPDDLDDDEDLADAVLASSALP 162

                          90       100
                  ....*....|....*....|....*
gi 569000921   80 VYcgFIPPTYRGERYIDGGFTSMQP 104
Cdd:pfam01734 163 GV--FPPVRLDGELYVDGGLVDNVP 185
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 24-181 4.62e-06

Predicted acylesterase/phospholipase RssA, containd patatin domain [General function prediction only];


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 48.36  E-value: 4.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921  24 MRQFLYDVLPEDSYKFATGKLHVSLTRVTDGENVVVSEyrskEELIEALYCSCFVPvycGFIPP-TYRGERYIDGGFTSM 102
Cdd:COG1752   99 LRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDS----GPLADAVRASAAIP---GVFPPvEIDGRLYVDGGVVNN 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921 103 QPCS----FWTDSITISTFSSQqdicPRDCPTIfhdFRMFNFSFQFSLENITRMTHALFPPDLVI--------------L 164
Cdd:COG1752  172 LPVDparaLGADRVIAVDLNPP----LRKLPSL---LDILGRALEIMFNSILRRELALEPADILIepdlsgislldfsrA 244

                        170
                 ....*....|....*..
gi 569000921 165 QEYYYRGYNDAVSYLRR 181
Cdd:COG1752  245 EELIEAGYEAARRALDE 261
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
213-373 2.48e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.71  E-value: 2.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921 213 PPPPSLQNLPAlRRSPADSSQTHAQGSPKKDRKDSHSSAAPSVQTPESGCKESVESPVSlRVSISKQPSVSPLSPAQPVP 292
Cdd:PRK12323 414 AAARAVAAAPA-RRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRP-VAAAAAAAPARAAPAAAPAP 491

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921 293 VMRPTGPRDSCPINVQTPNPERGVKGALDSATERGMKDALASATDEQSTTTLPPVLLPAAdsrgSKTGSSVPIGSPESPR 372
Cdd:PRK12323 492 ADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAP----RAAAATEPVVAPRPPR 567


                 .
gi 569000921 373 L 373
Cdd:PRK12323 568 A 568
 
Name Accession Description Interval E-value
Pat_PNPLA1 cd07219
Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin ...
 2-296 4.34e-159

Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin domain, initially discovered in potato tubers. Some members of PNPLA1 subfamily do not have the lipase consensus sequence Gly-X-Ser-X-Gly which is essential for hydrolase activity. This family includes PNPLA1 from Homo sapiens and Gallus gallus. Currently, there is no literature available on the physiological role, structure, or enzymatic activity of PNPLA1. It is expressed in various human tissues in low mRNA levels.


Pssm-ID: 132858  Cd Length: 382  Bit Score: 457.43  E-value: 4.34e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921   2 GLAEVKKFFLGPLSPSCKMVQMMRQFLYDVLPEDSYKFATGKLHVSLTRVTDGENVVVSEYRSKEELIEALYCSCFVPVY 81
Cdd:cd07219   77 GVAEVRKSFLGPLSPSCKMVQMMRQFLYRVLPEDSYKVATGKLHVSLTRVTDGENVVVSEFTSKEELIEALYCSCFVPVY 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921  82 CGFIPPTYRGERYIDGGFTSMQPCSFWTDSITISTFSSQQDICPRDCPTIFHDFRMFNFSFQFSLENITRMTHALFPPDL 161
Cdd:cd07219  157 CGLIPPTYRGVRYIDGGFTGMQPCSFWTDSITISTFSGQQDICPRDCPAIFHDFRIFNCSFQFSLENIARMTHALFPPDL 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921 162 VILQEYYYRGYNDAVSYLRRLNAAYLDSPSKRVIFPRVEVYCQievALGHEPPPPSLQNLPALRRSPADSSQTHAQGSPK 241
Cdd:cd07219  237 MVLHDYYYRGYQDTVLYLRRLNAVYLNSPSKRVIFPRVEVYCQ---ALGKECPQRSQPSLQDGQASLEESWQPHLARAPK 313

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 569000921 242 KDRKDSHSS-AAPSVQTPESGCKESVESPVSLRVSISKQPSVSPLSPAQPVPVMRP 296
Cdd:cd07219  314 GDGRGLHDPpLSPPLAAPESTAEWVVESPVSSPASPLESSPSLPGSLTDLSPASLP 369
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
 4-181 5.41e-99

Patatin-like phospholipase domain containing protein family; Members of this family share a patain domain, initially discovered in potato tubers. PNPLA protein members show non-specific hydrolase activity with a variety of substrates such as triacylglycerol, phospholipids, and retinylesters. It contains the lipase consensus sequence (Gly-X-Ser-X-Gly). Nomenclature of PNPLA family could be misleading as some of the mammalian members of this family show hydrolase, but no phospholipase activity.


Pssm-ID: 132843 [Multi-domain]  Cd Length: 243  Bit Score: 298.88  E-value: 5.41e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921   4 AEVKKFFLGPLSPSCKMVQMMRQFLYDVLPEDSYKFATGKLHVSLTRVTDGENVVVSEYRSKEELIEALYCSCFVPVYCG 83
Cdd:cd07204   66 SEARRRSLGPLHPSFNLLKILRQGLEKILPDDAHELASGRLHISLTRVSDGENVLVSEFDSKEELIQALVCSCFIPFYCG 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921  84 FIPPTYRGERYIDGGFTSMQPCSFWTDSITISTFSSQQDICPRDCPTIFHDFRMFNFSFQFSLENITRMTHALFPPDLVI 163
Cdd:cd07204  146 LIPPKFRGVRYIDGGLSDNLPILDDENTITVSPFSGESDICPQDKSSNLLEVNIANTSIQLSLENLYRLNRALFPPSLEI 225

                        170
                 ....*....|....*...
gi 569000921 164 LQEYYYRGYNDAVSYLRR 181
Cdd:cd07204  226 LSRMCQQGYLDALRFLER 243
Pat_PNPLA2 cd07220
Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis ...
 5-181 4.99e-73

Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis of stored triacylglecerols and is also known as adipose triglyceride lipase (ATGL). Members of this family share a patain domain, initially discovered in potato tubers. ATGL is expressed in white and brown adipose tissue in high mRNA levels. Mutations in PNPLA2 encoding adipose triglyceride lipase (ATGL) leads to neutral lipid storage disease (NLSD) which is characterized by the accumulation of triglycerides in multiple tissues. ATGL mutations are also commonly associated with severe forms of skeletal- and cardio-myopathy. This family includes patatin-like proteins: TTS-2.2 (transport-secretion protein 2.2), PNPLA2 (Patatin-like phospholipase domain-containing protein 2), and iPLA2-zeta (Calcium-independent phospholipase A2) from Homo sapiens.


Pssm-ID: 132859  Cd Length: 249  Bit Score: 232.33  E-value: 4.99e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921   5 EVKKFFLGPLSPSCKMVQMMRQFLYDVLPEDSYKFATGKLHVSLTRVTDGENVVVSEYRSKEELIEALYCSCFVPVYCGF 84
Cdd:cd07220   72 EARKRFLGPLHPSFNLVKILRDGLLRTLPENAHELASGRLGISLTRVSDGENVLVSDFNSKEELIQALVCSCFIPVYCGL 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921  85 IPPTYRGERYIDGGFTSMQPCSFWTDSITISTFSSQQDICPRDCPTIFHDFRMFNFSFQFSLENITRMTHALFPPDLVIL 164
Cdd:cd07220  152 IPPTLRGVRYVDGGISDNLPQYELKNTITVSPFSGESDICPRDSSTNFHELRFTNTSIQFNLRNLYRLSKALFPPEPQVL 231

                        170
                 ....*....|....*..
gi 569000921 165 QEYYYRGYNDAVSYLRR 181
Cdd:cd07220  232 AEMCKQGYRDALRFLKE 248
Pat_iPLA2 cd07218
Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent ...
 3-184 5.21e-65

Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent phospholipase A2; otherwise known as Group IVA-1 PLA2. It contains the lipase consensus sequence (Gly-X-Ser-X-Gly);mutagenesis experiments confirm the role of this serine as a nucleophile. Some members of this group show triacylglycerol lipase activity (EC 3:1:1:3). Members include iPLA-1, iPLA-2, and iPLA-3 from Aedes aegypti and show acylglycerol transacylase/lipase activity. Also includes putative iPLA2-eta from Pediculus humanus corporis which shows patatin-like phospholipase activity.


Pssm-ID: 132857  Cd Length: 245  Bit Score: 211.05  E-value: 5.21e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921   3 LAEVKKFFLGPLSPSCKMVQMMRQFLYDVLPEDSYKFATGKLHVSLTRVTDGENVVVSEYRSKEELIEALYCSCFVPVYC 82
Cdd:cd07218   64 VREARRHSLGPFSPSFNIQTCLLEGLQKFLPDDAHERVSGRLHISLTRVSDGKNVIVSEFESREELLQALLCSCFIPVFS 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921  83 GFIPPTYRGERYIDGGFTSMQPcSFWTDSITISTFSSQQDICPRDCPTIFHDFRMFNFSFQFSLENITRMTHALFPPDLV 162
Cdd:cd07218  144 GLLPPKFRGVRYMDGGFSDNLP-TLDENTITVSPFCGESDICPRDNSSQLFHINWANTSIELSRQNIYRLVRILFPPRPE 222

                        170       180
                 ....*....|....*....|..
gi 569000921 163 ILQEYYYRGYNDAVSYLRRLNA 184
Cdd:cd07218  223 VLSSLCQQGFDDALRFLHRNNL 244
Pat_PNPLA3 cd07221
Patatin-like phospholipase domain containing protein 3; PNPLA3 is a triacylglycerol lipase ...
 11-179 6.07e-54

Patatin-like phospholipase domain containing protein 3; PNPLA3 is a triacylglycerol lipase that mediates triacylglycerol hydrolysis in adipocytes and is an indicator of the nutritional state. PNPLA3 is also known as adiponutrin (ADPN) or iPLA2-epsilon. Human adiponutrins are bound to the cell membrane of adipocytes and show transacylase, TG hydrolase, and PLA2 activity. This family includes patatin-like proteins: ADPN (adiponutrin) from mammals, PNPLA3 (Patatin-like phospholipase domain-containing protein 3), and iPLA2-epsilon (Calcium-independent phospholipase A2) from Homo sapiens.


Pssm-ID: 132860  Cd Length: 252  Bit Score: 182.67  E-value: 6.07e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921  11 LGPLSPSCKMVQMMRQFLYDVLPEDSYKFATGKLHVSLTRVTDGENVVVSEYRSKEELIEALYCSCFVPVYCGFIPPTYR 90
Cdd:cd07221   74 IGILHPSFNLSKHLRDGLQRHLPDNVHQLISGKMCISLTRVSDGENVLVSDFHSKDEVVDALVCSCFIPFFSGLIPPSFR 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921  91 GERYIDGGFTSMQPCSFWTDSITISTFSSQQDICPRDCPTIFHDFRMFNFSFQFSLENITRMTHALFPPDLVILQEYYYR 170
Cdd:cd07221  154 GVRYVDGGVSDNVPFFDAKTTITVSPFYGEYDICPKVKSTNFLHVDFTKLSLRLCTENLYLLTRALFPPDVKVLGEICLR 233


                 ....*....
gi 569000921 171 GYNDAVSYL 179
Cdd:cd07221  234 GYLDAFRFL 242
Pat_PNPLA4 cd07222
Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene ...
 5-183 1.70e-53

Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene sequence-2), shows both lipase and transacylation activities. GS2 lipase is expressed in various tissues, predominantly in muscle and adipocytes tissue. It is also expressed in keratinocytes and shows retinyl ester hydrolase, acylglycerol, TG hydrolase, and PLA2 activity. This family includes patatin-like proteins: GS2 from mammals, PNPLA4 (Patatin-like phospholipase domain-containing protein 4), and iPLA2-eta (Calcium-independent phospholipase A2) from Homo sapiens.


Pssm-ID: 132861 [Multi-domain]  Cd Length: 246  Bit Score: 180.99  E-value: 1.70e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921   5 EVKKFFLGPLSPSCKMVQMMRQFLYDVLPEDSYKFATGKLHVSLTRVTDGENVVVSEYRSKEELIEALYCSCFVPVYCGF 84
Cdd:cd07222   68 EVRKQRFGAMTPGYDFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCYVPVYAGL 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921  85 IPPTYRGERYIDGGFTSMQPCSFWTDSITISTFSSQQDICPRDCPTIFHDFRMFNFSFQFSLENITRMTHALFPPDLVIL 164
Cdd:cd07222  148 KPVEYKGQKWIDGGFTNSLPVLPVGRTITVSPFSGRADICPQDKGQLDLYVRFANQDIMLSLANLVRLNQALFPPNRRKL 227

                        170
                 ....*....|....*....
gi 569000921 165 QEYYYRGYNDAVSYLRRLN 183
Cdd:cd07222  228 ESYYQMGFDDAVRFLKKEN 246
Pat_PNPLA5-mammals cd07223
Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), ...
 6-181 1.79e-41

Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), plays a role in regulation of adipocyte differentiation. PNPLA5 is expressed in brain tissue in high mRNA levels and low levels in liver tissue. There is no concrete evidence in support of the enzymatic activity of GS2L. This family includes patatin-like proteins: GS2L (GS2-like) and PNPLA5 (Patatin-like phospholipase domain-containing protein 5) reported exclusively in mammals.


Pssm-ID: 132862  Cd Length: 405  Bit Score: 153.53  E-value: 1.79e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921   6 VKKFFLGPLSPSCKMVQMMRQFLYDVLPEDSYKFATGKLHVSLTRVTDGENVVVSEYRSKEELIEALYCSCFVPVYCGFI 85
Cdd:cd07223   78 LERLSLGIFHPAYAPIEHIRQQLQESLPPNIHILASQRLGISMTRWPDGRNFIVTDFATRDELIQALICTLYFPFYCGII 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921  86 PPTYRGERYIDGGFTSMQPCSFWTDSITISTFSSQQDICPRDCPTIFHDFRMFNFSFQFSLENITRMTHALFPPDLVILQ 165
Cdd:cd07223  158 PPEFRGERYIDGALSNNLPFSDCPSTITVSPFHGTVDICPQSTSANLHELNAFNASFQISTRNFFLGLKCLIPPKPEVVA 237

                        170
                 ....*....|....*.
gi 569000921 166 EYYYRGYNDAVSYLRR 181
Cdd:cd07223  238 DNCRQGYLDALRFLER 253
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 1-115 1.37e-35

Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes PNPLA (1-9), TGL (3-5), ExoU-like, and SDP1-like subfamilies. There are some additional hypothetical proteins included in this family.


Pssm-ID: 132837 [Multi-domain]  Cd Length: 172  Bit Score: 130.54  E-value: 1.37e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921   1 MGLAEVKKFFLGPLSPSCKMVQMMRQFLYDVLPEDSYKFATGKLHVSLTRVTDGENVVVSEyRSKEELIEALYCSCFVPV 80
Cdd:cd07198   58 RLSREVRLRFDGAFPPTGRLLGILRQPLLSALPDDAHEDASGKLFISLTRLTDGENVLVSD-TSKGELWSAVRASSSIPG 136

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 569000921  81 YCGFIPPTYRGERYIDGGFTSMQPCSFWTDSITIS 115
Cdd:cd07198  137 YFGPVPLSFRGRRYGDGGLSNNLPVAELGNTINVS 171
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 14-116 3.93e-21

Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates. This family also includes the catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms.


Pssm-ID: 132836 [Multi-domain]  Cd Length: 155  Bit Score: 89.78  E-value: 3.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921  14 LSPSCKMVQMMRQFLYDVLpedsykfaTGKLHVSLTRVTDGENVVVSEYRSKEELIEALYCSCFVPVYCGFIPP------ 87
Cdd:cd01819   46 YPPSSSLDNKPRQSLEEAL--------SGKLWVSFTPVTAGENVLVSRFVSKEELIRALFASGSWPSYFGLIPPaelyts 117

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 569000921  88 ----TYRGERYIDGGFTSMQPCS-----FWTDSITIST 116
Cdd:cd01819  118 ksnlKEKGVRLVDGGVSNNLPAPvllrpGRGVTLTISP 155
Pat_like cd07224
Patatin-like phospholipase; Patatin-like phospholipase. This family consists of various ...
 23-181 4.30e-20

Patatin-like phospholipase; Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of lipid acyl hydrolase, catalysing the cleavage of fatty acids from membrane lipids. Members of this family have been found also in vertebrates.


Pssm-ID: 132863  Cd Length: 233  Bit Score: 89.32  E-value: 4.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921  23 MMRQFLYDVLPEDSYKF-ATGKLHVSLTR---VTDGENVvvSEYRSKEELIEALYCSCFVPVYCGFIPPT-YRGERYIDG 97
Cdd:cd07224   78 VLRDELDKTLPDDAHERcNRGRIRVAVTQlfpVPRGLLV--SSFDSKSDLIDALLASCNIPGYLAPWPATmFRGKLCVDG 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921  98 GFTSMQPCSFWTD-SITISTFSSQ------QDICPRDCPTIFHDFR-MFNFsfqfslenitrmthALFPPDLVILQEYYY 169
Cdd:cd07224  156 GFALFIPPTTAADrTVRVCPFPASrssikgQNLDNDDTEDVPYSRRqLLNW--------------ALEPADDAMLLELFN 221

                        170
                 ....*....|..
gi 569000921 170 RGYNDAVSYLRR 181
Cdd:cd07224  222 EGYKDANEWAKE 233
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 211-497 6.03e-07

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 52.38  E-value: 6.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921 211 HEPPP-PSLQNLPALRRSPADSSQTHAQGSPKKDRKDSHSSAAPSVQTPESgckesvespvsLRVSISKQPSVSPLSPAQ 289
Cdd:PTZ00449 567 HKPSKiPTLSKKPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPEL-----------LDIPKSPKRPESPKSPKR 635

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921 290 PVPVMRPTGP-RDSCPINVQTPNPERGVKGALDSATERGMKDALASATDEQSTTTLPPVLLPAADSRGSKTGSSVPIGSP 368
Cdd:PTZ00449 636 PPPPQRPSSPeRPEGPKIIKSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPF 715

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921 369 ESPRLLlrssqgatasratlglpplspstppagPPVEDLGPERP-TATGSPALSQLTGS--AAPGTGKKAPHKPLLVEGP 445
Cdd:PTZ00449 716 TTPRPL---------------------------PPKLPRDEEFPfEPIGDPDAEQPDDIefFTPPEEERTFFHETPADTP 768

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 569000921 446 GEDSNTakTMFKRKQKTNATREcfhRNAQSKKPASKLKSAPCPL-NFPVLPKR 497
Cdd:PTZ00449 769 LPDILA--EEFKEEDIHAETGE---PDEAMKRPDSPSEHEDKPPgDHPSLPKK 816
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 9-104 1.76e-06

Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein but it also has the enzymatic activity of lipid acyl hydrolase, catalysing the cleavage of fatty acids from membrane lipids. Members of this family have been found also in vertebrates.


Pssm-ID: 396341  Cd Length: 190  Bit Score: 48.76  E-value: 1.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921    9 FFLGPLSPSCKMVQMMRQFLYDVLPEDSYKFA---------TGKLHVSLTRVTDGENVVVSEYRSKEELIEALYCSCFVP 79
Cdd:pfam01734  83 IGEGGLFDGDALRELLRKLLGDLTLEELAARLslllvvalrALLTVISTALGTRARILLPDDLDDDEDLADAVLASSALP 162

                          90       100
                  ....*....|....*....|....*
gi 569000921   80 VYcgFIPPTYRGERYIDGGFTSMQP 104
Cdd:pfam01734 163 GV--FPPVRLDGELYVDGGLVDNVP 185
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 24-181 4.62e-06

Predicted acylesterase/phospholipase RssA, containd patatin domain [General function prediction only];


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 48.36  E-value: 4.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921  24 MRQFLYDVLPEDSYKFATGKLHVSLTRVTDGENVVVSEyrskEELIEALYCSCFVPvycGFIPP-TYRGERYIDGGFTSM 102
Cdd:COG1752   99 LRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDS----GPLADAVRASAAIP---GVFPPvEIDGRLYVDGGVVNN 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921 103 QPCS----FWTDSITISTFSSQqdicPRDCPTIfhdFRMFNFSFQFSLENITRMTHALFPPDLVI--------------L 164
Cdd:COG1752  172 LPVDparaLGADRVIAVDLNPP----LRKLPSL---LDILGRALEIMFNSILRRELALEPADILIepdlsgislldfsrA 244

                        170
                 ....*....|....*..
gi 569000921 165 QEYYYRGYNDAVSYLRR 181
Cdd:COG1752  245 EELIEAGYEAARRALDE 261
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 23-101 2.91e-05

Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase similar to Z1214 protein of Escherichia coli. This family predominantly consists of bacterial patatin glycoproteins and some representatives from eukaryotes and archaea. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates.


Pssm-ID: 132848 [Multi-domain]  Cd Length: 215  Bit Score: 45.36  E-value: 2.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921  23 MMRQFLYDVLPEDS---YKFATGKLHVSLTRVTDGENVVVSEyRSKEELIEALYCSCFVPVycGFIPPTYRGERYIDGGF 99
Cdd:cd07209   67 FLRGLLDRALDFDTlrlLAILFAGLVIVAVNVLTGEPVYFDD-IPDGILPEHLLASAALPP--FFPPVEIDGRYYWDGGV 143


                 ..
gi 569000921 100 TS 101
Cdd:cd07209  144 VD 145
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
213-373 2.48e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.71  E-value: 2.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921 213 PPPPSLQNLPAlRRSPADSSQTHAQGSPKKDRKDSHSSAAPSVQTPESGCKESVESPVSlRVSISKQPSVSPLSPAQPVP 292
Cdd:PRK12323 414 AAARAVAAAPA-RRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRP-VAAAAAAAPARAAPAAAPAP 491

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921 293 VMRPTGPRDSCPINVQTPNPERGVKGALDSATERGMKDALASATDEQSTTTLPPVLLPAAdsrgSKTGSSVPIGSPESPR 372
Cdd:PRK12323 492 ADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAP----RAAAATEPVVAPRPPR 567


                 .
gi 569000921 373 L 373
Cdd:PRK12323 568 A 568
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 212-466 3.14e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 3.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921  212 EPPPPSLQNLPALRRSPADSSQTHAQGSPKKDRKDSHSSAAPSVQTPESGCKESVESPVSLRVSISKQPSVSPLSPAQPV 291
Cdd:PHA03307  114 PDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921  292 PVMRPTGPRDSCP----INVQTPNPERGVKGALDSATERGMKDALASATDEQSTTTLP----PVLLPAADSRGSKTGSSV 363
Cdd:PHA03307  194 PPSTPPAAASPRPprrsSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPenecPLPRPAPITLPTRIWEAS 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921  364 PiGSPESPRLLLRSSQGATASR--ATLGLPPLSPSTPPAGPPVEDLGPERPTATGSPaLSQLTGSAAPGTGKKAPHKPLL 441
Cdd:PHA03307  274 G-WNGPSSRPGPASSSSSPRERspSPSPSSPGSGPAPSSPRASSSSSSSRESSSSST-SSSSESSRGAAVSPGPSPSRSP 351

                         250       260
                  ....*....|....*....|....*
gi 569000921  442 VEGPGEDSNTAKTMFKRKQKTNATR 466
Cdd:PHA03307  352 SPSRPPPPADPSSPRKRPRPSRAPS 376
FRQ pfam09421
Frequency clock protein; The frequency clock protein, is the central component of the ...
 211-310 1.63e-03

Frequency clock protein; The frequency clock protein, is the central component of the frq-based circadian negative feedback loop, regulates various aspects of the circadian clock in Neurospora crassa. This protein has been shown to interact with itself via a coiled-coil.


Pssm-ID: 401394  Cd Length: 982  Bit Score: 41.31  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921  211 HEPPPPSLQNLPALRRSPADSSQTHAQGSPKKDR-KDSHSSAAPSVQTPESGCKesvespvslrvSISKQPSVSPLSPAQ 289
Cdd:pfam09421 347 HQPPNPPTGHPEPSREARILPQEQQSGHSGKKSRsKDNGSASNSNGDQTESGGN-----------GAVSGSGTNTSPPDP 415

                          90       100
                  ....*....|....*....|.
gi 569000921  290 PVPVMRPTGPRDSCPINVQTP 310
Cdd:pfam09421 416 PPPEQRPTRPLDLDPDRVQVP 436
PHA03247 PHA03247
large tegument protein UL36; Provisional
 214-454 1.99e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921  214 PPPSLQNLPALRRSPADSSQTHAQGSPKKDRKDSHSSAAPSVQTPESGCKESVESPVSLRVSISKQPSVSPlSPAQPVPV 293
Cdd:PHA03247 2575 PRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPT-VPPPERPR 2653

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921  294 MRPTGPRDSCPINVQTPNPERGVKGALDSATERGMKDALASATD-----------------EQSTTTLPPVLLPAADSRG 356
Cdd:PHA03247 2654 DDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSladpppppptpepaphaLVSATPLPPGPAAARQASP 2733

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000921  357 SKTGSSVPIGSPESPrlllrssqGATASRATLGLPPLSPSTPPAGPPVEDLGPERPTATGSPALSQLTGSAAPGTGKKAP 436
Cdd:PHA03247 2734 ALPAAPAPPAVPAGP--------ATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPA 2805

                         250
                  ....*....|....*...
gi 569000921  437 HKPLLVEGPGEDSNTAKT 454
Cdd:PHA03247 2806 DPPAAVLAPAAALPPAAS 2823
 
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