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Conserved domains on  [gi|568916231|ref|XP_006499197|]
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glycerol-3-phosphate acyltransferase 2, mitochondrial isoform X3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LPLAT_DHAPAT-like cd07993
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: GPAT-like; ...
 176-388 1.96e-53

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: GPAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as dihydroxyacetone phosphate acyltransferase (DHAPAT, also known as 1 glycerol-3-phosphate O-acyltransferase 1) and similar proteins.


:

Pssm-ID: 153255 [Multi-domain]  Cd Length: 205  Bit Score: 183.93  E-value: 1.96e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231 176 FLNVQLHKGQMKMVQKAVQEqGSPLVFLSTHKSLLDGFLLPFVLFSQGLGVVRVALDSRTCSPALRALLRKLGGLFLPPE 255
Cdd:cd07993    1 FDGVQVNEGQLERLRKAAQE-GHPVVLLPTHRSYLDFLLLSFILFSLGLPLPHIAAGENLNIPILGTLLRRLGAFFIRRS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231 256 VNlsldnsEGILARAVVRATVEELLTSGQPLLIFLEEPPGSPG-PRLSALGQAWlgVVIQAVQAGIISDATLVPVAIAYD 334
Cdd:cd07993   80 FG------KDPLYRAVLQEYVQELLKNGQPLEFFIEGTRSRTGkLLPPKLGLLS--VVVEAYLKGSVPDVLIVPVSISYD 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568916231 335 LVPDAPCNMNHDLAPLGLWTGALAvFRRLCNcWGCNRRVCVRVHLAQPFSLQEY 388
Cdd:cd07993  152 RVLEEELYAEELLGPPKPKESLSG-LLGASK-ILRENFGRIRVDFGEPISLREY 203
ZF_RNaseIII_KREN_KREPB-like super family cl49632
C2H2 zinc finger and Ribonuclease III-like domain of RNA-editing catalytic complex (RECC) ...
 471-528 1.90e-04

C2H2 zinc finger and Ribonuclease III-like domain of RNA-editing catalytic complex (RECC) proteins KREN1-3, KREPB4-KREPB10, and related proteins; KREN1-3 (KREPB1-3) and KREPB4-KREPB10 are components of the RNA-editing catalytic complex (RECC) involved in U-insertion/deletion mRNA editing during kinetoplast RNA processing. The mitochondrial DNA of Trypanosomatids, known as the kinetoplast DNA (kDNA or mtDNA), consists of a network of dozens of maxicircles and thousands of minicircles concatenated together. Maxicircles are equivalent to other eukaryotic mitochondrial DNAs, while minicircles encode guide RNAs (gRNAs) involved in U-insertion/deletion editing processes exclusive of Trypanosomatids that produce the maturation of the maxicircle-encoded transcripts. Although most gRNAs are encoded by minicircles, varying numbers of maxicircle-encoded gRNAs have been identified in kinetoplastid species. Trypanosoma brucei maxicircles encode 9S and 12S rRNAs, two gRNAs, two ribosomal proteins and 16 subunits of respiratory complexes. 12 of the 18 maxicircle genes are present as cryptogenes whose transcripts require U-insertion/deletion editing, mediated by gRNAs, to restore a protein-coding capacity. The RECC core complex comprises a U-insertion subcomplex (KRET2 TUTase, KREPA1 zinc-finger protein, and KREL2 RNA ligase), a U-deletion subcomplex (KREX2 exonuclease, KREPA2 zinc-finger protein, and KREL1 RNA ligase), and six structural and/or RNA-binding proteins (KREPA3, KREPA4, KREPA5, KREPA6, KREPB4, and KREPB5). This core complex interacts with one of three RNase III family endonucleases (KREN1, KREN2, and KREN3) that may partner with one or more partner protein(s) with divergent RNase III domains, such as KREN1/KREPB8, KREN2/KREPB7, KREN3/KREPB6. KREPB4-KREPB10 have divergent RNase III domains. RECC interacts with two other complexes, the RNA-editing helicase 2 complex (REH2C) and the RNA-editing substrate-binding complex (RESC) to form an assembly (editosome/holoenzyme) that carries out U-insertion/deletion mRNA editing.


The actual alignment was detected with superfamily member cd23383:

Pssm-ID: 483972  Cd Length: 195  Bit Score: 43.10  E-value: 1.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568916231 471 LLLKHQKGVVLSQLLGEFSWLTEETLLRGFDVGFSGQLRCLAQHTLSLLRAHVVLLRV 528
Cdd:cd23383  126 LLSFHRKGDFVRALIGELHWALIRREGIPPPPSDSARLRVLAQFVLRSLVAELIYLRL 183
 
Name Accession Description Interval E-value
LPLAT_DHAPAT-like cd07993
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: GPAT-like; ...
 176-388 1.96e-53

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: GPAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as dihydroxyacetone phosphate acyltransferase (DHAPAT, also known as 1 glycerol-3-phosphate O-acyltransferase 1) and similar proteins.


Pssm-ID: 153255 [Multi-domain]  Cd Length: 205  Bit Score: 183.93  E-value: 1.96e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231 176 FLNVQLHKGQMKMVQKAVQEqGSPLVFLSTHKSLLDGFLLPFVLFSQGLGVVRVALDSRTCSPALRALLRKLGGLFLPPE 255
Cdd:cd07993    1 FDGVQVNEGQLERLRKAAQE-GHPVVLLPTHRSYLDFLLLSFILFSLGLPLPHIAAGENLNIPILGTLLRRLGAFFIRRS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231 256 VNlsldnsEGILARAVVRATVEELLTSGQPLLIFLEEPPGSPG-PRLSALGQAWlgVVIQAVQAGIISDATLVPVAIAYD 334
Cdd:cd07993   80 FG------KDPLYRAVLQEYVQELLKNGQPLEFFIEGTRSRTGkLLPPKLGLLS--VVVEAYLKGSVPDVLIVPVSISYD 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568916231 335 LVPDAPCNMNHDLAPLGLWTGALAvFRRLCNcWGCNRRVCVRVHLAQPFSLQEY 388
Cdd:cd07993  152 RVLEEELYAEELLGPPKPKESLSG-LLGASK-ILRENFGRIRVDFGEPISLREY 203
PlsB COG2937
Glycerol-3-phosphate O-acyltransferase [Lipid transport and metabolism]; Glycerol-3-phosphate ...
 131-549 2.81e-18

Glycerol-3-phosphate O-acyltransferase [Lipid transport and metabolism]; Glycerol-3-phosphate O-acyltransferase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 442180 [Multi-domain]  Cd Length: 707  Bit Score: 89.60  E-value: 2.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231 131 AAGEGQAPELVKKEVQRILGHIQTTPRPFLLRLFSWALLWFLNRLFLNVQLHkgQMKMVQKAVQeqGSPLVFLSTHKSLL 210
Cdd:COG2937  140 AKSKGISEEKARKEARRYLREIAADFSYSAIRFLDRVLRWLWNRLYDGIRVD--NLERLRELAK--GHEIVYVPCHRSHM 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231 211 DGFLLPFVLFSQGLGVVRVA----LDsrtcSPALRALLRKLGGLFL-------PpevnlsldnsegiLARAVVRATVEEL 279
Cdd:COG2937  216 DYLLLSYVLYHNGLVPPHIAaginLN----FWPLGPILRRGGAFFIrrsfkgnK-------------LYSAVFREYLAEL 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231 280 LTSGQPLLIFLEeppG--SpgpRLSALGQAWLGV---VIQAVQAGIISDATLVPVAIAYDLVPDAPcNMNHDLA-----P 349
Cdd:COG2937  279 FERGYSVEYFIE---GgrS---RTGRLLPPKTGMlsmTVQAFLRGARRPVVFVPVYIGYERVLEVG-SYAKELRggekkK 351

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231 350 LGLWtGALAVFRRLCNCWGcnrrvcvRVHL--AQPFSLQEYtinarscwdsrqtlehLLQpivlgecsVVPDTEKEQEWT 427
Cdd:COG2937  352 ESLG-GLLRALRKLRRRFG-------RVYVnfGEPISLSEY----------------LDQ--------HVPDWRESEDLR 399

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231 428 PptglllalkEEDQLLVRRLSRHVLSASVASSAVMSTAIMATLLLLKHQKGvvlsqllgefswLTEETLLRgfdvgfsgQ 507
Cdd:COG2937  400 P---------EWLRPAVDKLAFEIMVRINRAAAVNPVNLVALALLASPKRA------------LTEAELLA--------Q 450

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 568916231 508 LRCLaqhtLSLLRahvvllRVHQGDLVVVPRPGP--GLTHLARL 549
Cdd:COG2937  451 LDLY----LDLLR------NVPYSLSVTLPELTPeeLLEHLLSL 484
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 200-334 2.12e-11

Phosphate acyltransferases; Function in phospholipid biosynthesis and have either glycerolphosphate, 1-acylglycerolphosphate, or 2-acylglycerolphosphoethanolamine acyltransferase activities. Tafazzin, the product of the gene mutated in patients with Barth syndrome, is a member of this family.


Pssm-ID: 214724 [Multi-domain]  Cd Length: 118  Bit Score: 61.60  E-value: 2.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231   200 LVFLSTHKSLLDGFLLPFVLFSQGLGVVRVALDSRTCSPALRALLRKLGGLFlppevnlsLDNSEGILARAVVRATVeEL 279
Cdd:smart00563   1 ALVVANHQSFLDPLVLSALLPRKLGRVRFVAKKELFYVPLLGWLLRLLGAIF--------IDRSNGRKARAALREAV-EL 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568916231   280 LTSGQPLLIFLEeppgspGPRLS--ALGQAWLGVVIQAVQAGiisdATLVPVAIAYD 334
Cdd:smart00563  72 LKEGEWLLIFPE------GTRSRpgKLLPFKKGAARLALEAG----VPIVPVAIRGT 118
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 196-331 3.22e-08

Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis and other proteins of unknown function. This family also includes tafazzin, the Barth syndrome gene.


Pssm-ID: 366704 [Multi-domain]  Cd Length: 131  Bit Score: 53.05  E-value: 3.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231  196 QGSPLVFLSTHKSLLDGFLLPFVLFSQGLGVVRVALDSRTCSPALRALLRKLGGLFLppevnlsldNSEGILARAVVRAT 275
Cdd:pfam01553  12 RGGPAIVVANHQSYLDVLLLSLALYKRGRPLVFVAKKELFDIPLVGWLMRLLGCIFI---------DRKNRKDAAGTLEY 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568916231  276 VEELLTSGQPLLIFLEeppgspGPRLSA--LGQAWLGVVIQAVQAGIisdaTLVPVAI 331
Cdd:pfam01553  83 LVELLREGKLVVIFPE------GTRSREgeLLPFKKGAFRLAIEAGV----PIVPVAI 130
ZF_RNaseIII_KREN_KREPB-like cd23383
C2H2 zinc finger and Ribonuclease III-like domain of RNA-editing catalytic complex (RECC) ...
 471-528 1.90e-04

C2H2 zinc finger and Ribonuclease III-like domain of RNA-editing catalytic complex (RECC) proteins KREN1-3, KREPB4-KREPB10, and related proteins; KREN1-3 (KREPB1-3) and KREPB4-KREPB10 are components of the RNA-editing catalytic complex (RECC) involved in U-insertion/deletion mRNA editing during kinetoplast RNA processing. The mitochondrial DNA of Trypanosomatids, known as the kinetoplast DNA (kDNA or mtDNA), consists of a network of dozens of maxicircles and thousands of minicircles concatenated together. Maxicircles are equivalent to other eukaryotic mitochondrial DNAs, while minicircles encode guide RNAs (gRNAs) involved in U-insertion/deletion editing processes exclusive of Trypanosomatids that produce the maturation of the maxicircle-encoded transcripts. Although most gRNAs are encoded by minicircles, varying numbers of maxicircle-encoded gRNAs have been identified in kinetoplastid species. Trypanosoma brucei maxicircles encode 9S and 12S rRNAs, two gRNAs, two ribosomal proteins and 16 subunits of respiratory complexes. 12 of the 18 maxicircle genes are present as cryptogenes whose transcripts require U-insertion/deletion editing, mediated by gRNAs, to restore a protein-coding capacity. The RECC core complex comprises a U-insertion subcomplex (KRET2 TUTase, KREPA1 zinc-finger protein, and KREL2 RNA ligase), a U-deletion subcomplex (KREX2 exonuclease, KREPA2 zinc-finger protein, and KREL1 RNA ligase), and six structural and/or RNA-binding proteins (KREPA3, KREPA4, KREPA5, KREPA6, KREPB4, and KREPB5). This core complex interacts with one of three RNase III family endonucleases (KREN1, KREN2, and KREN3) that may partner with one or more partner protein(s) with divergent RNase III domains, such as KREN1/KREPB8, KREN2/KREPB7, KREN3/KREPB6. KREPB4-KREPB10 have divergent RNase III domains. RECC interacts with two other complexes, the RNA-editing helicase 2 complex (REH2C) and the RNA-editing substrate-binding complex (RESC) to form an assembly (editosome/holoenzyme) that carries out U-insertion/deletion mRNA editing.


Pssm-ID: 469560  Cd Length: 195  Bit Score: 43.10  E-value: 1.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568916231 471 LLLKHQKGVVLSQLLGEFSWLTEETLLRGFDVGFSGQLRCLAQHTLSLLRAHVVLLRV 528
Cdd:cd23383  126 LLSFHRKGDFVRALIGELHWALIRREGIPPPPSDSARLRVLAQFVLRSLVAELIYLRL 183
PTZ00374 PTZ00374
dihydroxyacetone phosphate acyltransferase; Provisional
 131-395 3.20e-04

dihydroxyacetone phosphate acyltransferase; Provisional


Pssm-ID: 240389 [Multi-domain]  Cd Length: 1108  Bit Score: 44.48  E-value: 3.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231  131 AAGEGQAPELVKKEVQRILGHIQTTPRPFLLRLFSWALLWFLNRLFLNVQLHKGQMKMVQKAVQEQGSPLVFLSTHKSLL 210
Cdd:PTZ00374  562 AKKEGASEKDVEARAKAILRTCGDNLNHVQCRLFGLMVRRILFRLYDRVSLNSGAFERLHRYVAMPRVAVVLLPLHRSYI 641

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231  211 DGFLLPFVLFSQGLGVVRV-ALDSRTCSPALRALLRKLGGLFLppevNLSLDNSEgiLARAVVRATVEELLTSGQPLLIF 289
Cdd:PTZ00374  642 DFIIMTYLLAVMGLPLPHVcAGDDFLRMGPIATLMRGSGAFFM----RRSFRDDP--LYAALFKEYVRHLVLRRRPLEFF 715

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231  290 LEEPPGSPG----PRLSALgQAWLGVVIQAVQAgiISDATLVPVAIAYDLVPDAPCNMNHDLA-------PLGLWTGALA 358
Cdd:PTZ00374  716 IEGTRSRTGktmaPKLGLL-KFICDTFYEGQQE--LDDVLIIPVSLSYDELLETTLYAKEQLGvskpkenPGNLLRARSL 792

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 568916231  359 VFRRLCNcwgcnrrvcVRVHLAQPFSLQEYTINARSC 395
Cdd:PTZ00374  793 LKRRHGK---------IHVHIGEPVSLRSFKDHPLQC 820
 
Name Accession Description Interval E-value
LPLAT_DHAPAT-like cd07993
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: GPAT-like; ...
 176-388 1.96e-53

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: GPAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as dihydroxyacetone phosphate acyltransferase (DHAPAT, also known as 1 glycerol-3-phosphate O-acyltransferase 1) and similar proteins.


Pssm-ID: 153255 [Multi-domain]  Cd Length: 205  Bit Score: 183.93  E-value: 1.96e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231 176 FLNVQLHKGQMKMVQKAVQEqGSPLVFLSTHKSLLDGFLLPFVLFSQGLGVVRVALDSRTCSPALRALLRKLGGLFLPPE 255
Cdd:cd07993    1 FDGVQVNEGQLERLRKAAQE-GHPVVLLPTHRSYLDFLLLSFILFSLGLPLPHIAAGENLNIPILGTLLRRLGAFFIRRS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231 256 VNlsldnsEGILARAVVRATVEELLTSGQPLLIFLEEPPGSPG-PRLSALGQAWlgVVIQAVQAGIISDATLVPVAIAYD 334
Cdd:cd07993   80 FG------KDPLYRAVLQEYVQELLKNGQPLEFFIEGTRSRTGkLLPPKLGLLS--VVVEAYLKGSVPDVLIVPVSISYD 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568916231 335 LVPDAPCNMNHDLAPLGLWTGALAvFRRLCNcWGCNRRVCVRVHLAQPFSLQEY 388
Cdd:cd07993  152 RVLEEELYAEELLGPPKPKESLSG-LLGASK-ILRENFGRIRVDFGEPISLREY 203
PlsB COG2937
Glycerol-3-phosphate O-acyltransferase [Lipid transport and metabolism]; Glycerol-3-phosphate ...
 131-549 2.81e-18

Glycerol-3-phosphate O-acyltransferase [Lipid transport and metabolism]; Glycerol-3-phosphate O-acyltransferase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 442180 [Multi-domain]  Cd Length: 707  Bit Score: 89.60  E-value: 2.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231 131 AAGEGQAPELVKKEVQRILGHIQTTPRPFLLRLFSWALLWFLNRLFLNVQLHkgQMKMVQKAVQeqGSPLVFLSTHKSLL 210
Cdd:COG2937  140 AKSKGISEEKARKEARRYLREIAADFSYSAIRFLDRVLRWLWNRLYDGIRVD--NLERLRELAK--GHEIVYVPCHRSHM 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231 211 DGFLLPFVLFSQGLGVVRVA----LDsrtcSPALRALLRKLGGLFL-------PpevnlsldnsegiLARAVVRATVEEL 279
Cdd:COG2937  216 DYLLLSYVLYHNGLVPPHIAaginLN----FWPLGPILRRGGAFFIrrsfkgnK-------------LYSAVFREYLAEL 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231 280 LTSGQPLLIFLEeppG--SpgpRLSALGQAWLGV---VIQAVQAGIISDATLVPVAIAYDLVPDAPcNMNHDLA-----P 349
Cdd:COG2937  279 FERGYSVEYFIE---GgrS---RTGRLLPPKTGMlsmTVQAFLRGARRPVVFVPVYIGYERVLEVG-SYAKELRggekkK 351

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231 350 LGLWtGALAVFRRLCNCWGcnrrvcvRVHL--AQPFSLQEYtinarscwdsrqtlehLLQpivlgecsVVPDTEKEQEWT 427
Cdd:COG2937  352 ESLG-GLLRALRKLRRRFG-------RVYVnfGEPISLSEY----------------LDQ--------HVPDWRESEDLR 399

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231 428 PptglllalkEEDQLLVRRLSRHVLSASVASSAVMSTAIMATLLLLKHQKGvvlsqllgefswLTEETLLRgfdvgfsgQ 507
Cdd:COG2937  400 P---------EWLRPAVDKLAFEIMVRINRAAAVNPVNLVALALLASPKRA------------LTEAELLA--------Q 450

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 568916231 508 LRCLaqhtLSLLRahvvllRVHQGDLVVVPRPGP--GLTHLARL 549
Cdd:COG2937  451 LDLY----LDLLR------NVPYSLSVTLPELTPeeLLEHLLSL 484
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 200-334 2.12e-11

Phosphate acyltransferases; Function in phospholipid biosynthesis and have either glycerolphosphate, 1-acylglycerolphosphate, or 2-acylglycerolphosphoethanolamine acyltransferase activities. Tafazzin, the product of the gene mutated in patients with Barth syndrome, is a member of this family.


Pssm-ID: 214724 [Multi-domain]  Cd Length: 118  Bit Score: 61.60  E-value: 2.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231   200 LVFLSTHKSLLDGFLLPFVLFSQGLGVVRVALDSRTCSPALRALLRKLGGLFlppevnlsLDNSEGILARAVVRATVeEL 279
Cdd:smart00563   1 ALVVANHQSFLDPLVLSALLPRKLGRVRFVAKKELFYVPLLGWLLRLLGAIF--------IDRSNGRKARAALREAV-EL 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568916231   280 LTSGQPLLIFLEeppgspGPRLS--ALGQAWLGVVIQAVQAGiisdATLVPVAIAYD 334
Cdd:smart00563  72 LKEGEWLLIFPE------GTRSRpgKLLPFKKGAARLALEAG----VPIVPVAIRGT 118
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 196-331 3.22e-08

Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis and other proteins of unknown function. This family also includes tafazzin, the Barth syndrome gene.


Pssm-ID: 366704 [Multi-domain]  Cd Length: 131  Bit Score: 53.05  E-value: 3.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231  196 QGSPLVFLSTHKSLLDGFLLPFVLFSQGLGVVRVALDSRTCSPALRALLRKLGGLFLppevnlsldNSEGILARAVVRAT 275
Cdd:pfam01553  12 RGGPAIVVANHQSYLDVLLLSLALYKRGRPLVFVAKKELFDIPLVGWLMRLLGCIFI---------DRKNRKDAAGTLEY 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568916231  276 VEELLTSGQPLLIFLEeppgspGPRLSA--LGQAWLGVVIQAVQAGIisdaTLVPVAI 331
Cdd:pfam01553  83 LVELLREGKLVVIFPE------GTRSREgeLLPFKKGAFRLAIEAGV----PIVPVAI 130
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 158-333 1.78e-07

1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; 1-acyl-sn-glycerol-3-phosphate acyltransferase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 439974 [Multi-domain]  Cd Length: 215  Bit Score: 52.70  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231 158 PFLLRLFSWALLWFLNRLFLNVQLHKgqMKMVQKAVQEQGSPLVFLSTHKSLLDGFLLPFVLFSQglgvVR-VALDSRTC 236
Cdd:COG0204    5 FLLLRRFRYRLVRLWARLLLRLLGVR--VRVEGLENLPADGPVLIVANHQSWLDILLLLAALPRP----VRfVAKKELFK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231 237 SPALRALLRKLGGLFlppevnlsLDNSEGILARAVVRATVeELLTSGQPLLIFLEeppG--SPGPRLSAL--GQAWLgvv 312
Cdd:COG0204   79 IPLLGWLLRALGAIP--------VDRSKRRAALRALRQAV-EALKAGESLVIFPE---GtrSPDGRLLPFktGAARL--- 143

                        170       180
                 ....*....|....*....|.
gi 568916231 313 iqAVQAGiisdATLVPVAIAY 333
Cdd:COG0204  144 --ALEAG----VPIVPVAIDG 158
ZF_RNaseIII_KREN_KREPB-like cd23383
C2H2 zinc finger and Ribonuclease III-like domain of RNA-editing catalytic complex (RECC) ...
 471-528 1.90e-04

C2H2 zinc finger and Ribonuclease III-like domain of RNA-editing catalytic complex (RECC) proteins KREN1-3, KREPB4-KREPB10, and related proteins; KREN1-3 (KREPB1-3) and KREPB4-KREPB10 are components of the RNA-editing catalytic complex (RECC) involved in U-insertion/deletion mRNA editing during kinetoplast RNA processing. The mitochondrial DNA of Trypanosomatids, known as the kinetoplast DNA (kDNA or mtDNA), consists of a network of dozens of maxicircles and thousands of minicircles concatenated together. Maxicircles are equivalent to other eukaryotic mitochondrial DNAs, while minicircles encode guide RNAs (gRNAs) involved in U-insertion/deletion editing processes exclusive of Trypanosomatids that produce the maturation of the maxicircle-encoded transcripts. Although most gRNAs are encoded by minicircles, varying numbers of maxicircle-encoded gRNAs have been identified in kinetoplastid species. Trypanosoma brucei maxicircles encode 9S and 12S rRNAs, two gRNAs, two ribosomal proteins and 16 subunits of respiratory complexes. 12 of the 18 maxicircle genes are present as cryptogenes whose transcripts require U-insertion/deletion editing, mediated by gRNAs, to restore a protein-coding capacity. The RECC core complex comprises a U-insertion subcomplex (KRET2 TUTase, KREPA1 zinc-finger protein, and KREL2 RNA ligase), a U-deletion subcomplex (KREX2 exonuclease, KREPA2 zinc-finger protein, and KREL1 RNA ligase), and six structural and/or RNA-binding proteins (KREPA3, KREPA4, KREPA5, KREPA6, KREPB4, and KREPB5). This core complex interacts with one of three RNase III family endonucleases (KREN1, KREN2, and KREN3) that may partner with one or more partner protein(s) with divergent RNase III domains, such as KREN1/KREPB8, KREN2/KREPB7, KREN3/KREPB6. KREPB4-KREPB10 have divergent RNase III domains. RECC interacts with two other complexes, the RNA-editing helicase 2 complex (REH2C) and the RNA-editing substrate-binding complex (RESC) to form an assembly (editosome/holoenzyme) that carries out U-insertion/deletion mRNA editing.


Pssm-ID: 469560  Cd Length: 195  Bit Score: 43.10  E-value: 1.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568916231 471 LLLKHQKGVVLSQLLGEFSWLTEETLLRGFDVGFSGQLRCLAQHTLSLLRAHVVLLRV 528
Cdd:cd23383  126 LLSFHRKGDFVRALIGELHWALIRREGIPPPPSDSARLRVLAQFVLRSLVAELIYLRL 183
PTZ00374 PTZ00374
dihydroxyacetone phosphate acyltransferase; Provisional
 131-395 3.20e-04

dihydroxyacetone phosphate acyltransferase; Provisional


Pssm-ID: 240389 [Multi-domain]  Cd Length: 1108  Bit Score: 44.48  E-value: 3.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231  131 AAGEGQAPELVKKEVQRILGHIQTTPRPFLLRLFSWALLWFLNRLFLNVQLHKGQMKMVQKAVQEQGSPLVFLSTHKSLL 210
Cdd:PTZ00374  562 AKKEGASEKDVEARAKAILRTCGDNLNHVQCRLFGLMVRRILFRLYDRVSLNSGAFERLHRYVAMPRVAVVLLPLHRSYI 641

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231  211 DGFLLPFVLFSQGLGVVRV-ALDSRTCSPALRALLRKLGGLFLppevNLSLDNSEgiLARAVVRATVEELLTSGQPLLIF 289
Cdd:PTZ00374  642 DFIIMTYLLAVMGLPLPHVcAGDDFLRMGPIATLMRGSGAFFM----RRSFRDDP--LYAALFKEYVRHLVLRRRPLEFF 715

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231  290 LEEPPGSPG----PRLSALgQAWLGVVIQAVQAgiISDATLVPVAIAYDLVPDAPCNMNHDLA-------PLGLWTGALA 358
Cdd:PTZ00374  716 IEGTRSRTGktmaPKLGLL-KFICDTFYEGQQE--LDDVLIIPVSLSYDELLETTLYAKEQLGvskpkenPGNLLRARSL 792

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 568916231  359 VFRRLCNcwgcnrrvcVRVHLAQPFSLQEYTINARSC 395
Cdd:PTZ00374  793 LKRRHGK---------IHVHIGEPVSLRSFKDHPLQC 820
LPLAT_AGPAT-like cd07989
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; ...
 199-333 4.33e-04

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), Tafazzin (product of Barth syndrome gene), and similar proteins.


Pssm-ID: 153251 [Multi-domain]  Cd Length: 184  Bit Score: 41.87  E-value: 4.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916231 199 PLVFLSTHKSLLDGFLLPFVLFSQGLGVVRVALDSRtcsPALRALLRKLGGLFlppevnlsLDNSEGILARAVVRAtVEE 278
Cdd:cd07989   25 PVIIVANHQSYLDPLVLGAALPRPIRFVAKKELFKI---PFLGWLLRLLGAIP--------IDRGNGRSAREALRE-AIE 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568916231 279 LLTSGQPLLIFLEeppG--SPGPRLSALGqawLGVVIQAVQAGiisdATLVPVAIAY 333
Cdd:cd07989   93 ALKEGESVVIFPE---GtrSRDGELLPFK---SGAFRLAKEAG----VPIVPVAISG 139
 
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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