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Conserved domains on  [gi|1907137530|ref|XP_006499195|]
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glycerol-3-phosphate acyltransferase 2, mitochondrial isoform X2 [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; ...
 203-415 1.89e-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: 184.31  E-value: 1.89e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530 203 FLNVQLHKGQMKMVQKAVQEqGSPLVFLSTHKSLLDGFLLPFVLFSQGLGVVRVALDSRTCSPALRALLRKLGGLFLPPE 282
Cdd:cd07993     1 FDGVQVNEGQLERLRKAAQE-GHPVVLLPTHRSYLDFLLLSFILFSLGLPLPHIAAGENLNIPILGTLLRRLGAFFIRRS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530 283 VNlsldnsEGILARAVVRATVEELLTSGQPLLIFLEEPPGSPG-PRLSALGQAWlgVVIQAVQAGIISDATLVPVAIAYD 361
Cdd:cd07993    80 FG------KDPLYRAVLQEYVQELLKNGQPLEFFIEGTRSRTGkLLPPKLGLLS--VVVEAYLKGSVPDVLIVPVSISYD 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907137530 362 LVPDAPCNMNHDLAPLGLWTGALAvFRRLCNcWGCNRRVCVRVHLAQPFSLQEY 415
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) ...
 498-555 1.99e-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: 1.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907137530 498 LLLKHQKGVVLSQLLGEFSWLTEETLLRGFDVGFSGQLRCLAQHTLSLLRAHVVLLRV 555
Cdd:cd23383   126 LLSFHRKGDFVRALIGELHWALIRREGIPPPPSDSARLRVLAQFVLRSLVAELIYLRL 183
 
Name Accession Description Interval E-value
LPLAT_DHAPAT-like cd07993
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: GPAT-like; ...
 203-415 1.89e-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: 184.31  E-value: 1.89e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530 203 FLNVQLHKGQMKMVQKAVQEqGSPLVFLSTHKSLLDGFLLPFVLFSQGLGVVRVALDSRTCSPALRALLRKLGGLFLPPE 282
Cdd:cd07993     1 FDGVQVNEGQLERLRKAAQE-GHPVVLLPTHRSYLDFLLLSFILFSLGLPLPHIAAGENLNIPILGTLLRRLGAFFIRRS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530 283 VNlsldnsEGILARAVVRATVEELLTSGQPLLIFLEEPPGSPG-PRLSALGQAWlgVVIQAVQAGIISDATLVPVAIAYD 361
Cdd:cd07993    80 FG------KDPLYRAVLQEYVQELLKNGQPLEFFIEGTRSRTGkLLPPKLGLLS--VVVEAYLKGSVPDVLIVPVSISYD 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907137530 362 LVPDAPCNMNHDLAPLGLWTGALAvFRRLCNcWGCNRRVCVRVHLAQPFSLQEY 415
Cdd:cd07993   152 RVLEEELYAEELLGPPKPKESLSG-LLGASK-ILRENFGRIRVDFGEPISLREY 203
PlsB COG2937
Glycerol-3-phosphate O-acyltransferase [Lipid transport and metabolism]; Glycerol-3-phosphate ...
 158-576 2.01e-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: 90.37  E-value: 2.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530 158 AAGEGQAPELVKKEVQRILGHIQTTPRPFLLRLFSWALLWFLNRLFLNVQLHkgQMKMVQKAVQeqGSPLVFLSTHKSLL 237
Cdd:COG2937   140 AKSKGISEEKARKEARRYLREIAADFSYSAIRFLDRVLRWLWNRLYDGIRVD--NLERLRELAK--GHEIVYVPCHRSHM 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530 238 DGFLLPFVLFSQGLGVVRVA----LDsrtcSPALRALLRKLGGLFL-------PpevnlsldnsegiLARAVVRATVEEL 306
Cdd:COG2937   216 DYLLLSYVLYHNGLVPPHIAaginLN----FWPLGPILRRGGAFFIrrsfkgnK-------------LYSAVFREYLAEL 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530 307 LTSGQPLLIFLEeppG--SpgpRLSALGQAWLGV---VIQAVQAGIISDATLVPVAIAYDLVPDAPcNMNHDLA-----P 376
Cdd:COG2937   279 FERGYSVEYFIE---GgrS---RTGRLLPPKTGMlsmTVQAFLRGARRPVVFVPVYIGYERVLEVG-SYAKELRggekkK 351

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530 377 LGLWtGALAVFRRLCNCWGcnrrvcvRVHL--AQPFSLQEYtinarscwdsrqtlehLLQpivlgecsVVPDTEKEQEWT 454
Cdd:COG2937   352 ESLG-GLLRALRKLRRRFG-------RVYVnfGEPISLSEY----------------LDQ--------HVPDWRESEDLR 399

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530 455 PptglllalkEEDQLLVRRLSRHVLSASVASSAVMSTAIMATLLLLKHQKGvvlsqllgefswLTEETLLRgfdvgfsgQ 534
Cdd:COG2937   400 P---------EWLRPAVDKLAFEIMVRINRAAAVNPVNLVALALLASPKRA------------LTEAELLA--------Q 450

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1907137530 535 LRCLaqhtLSLLRahvvllRVHQGDLVVVPRPGP--GLTHLARL 576
Cdd:COG2937   451 LDLY----LDLLR------NVPYSLSVTLPELTPeeLLEHLLSL 484
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 227-361 2.17e-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: 2.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530  227 LVFLSTHKSLLDGFLLPFVLFSQGLGVVRVALDSRTCSPALRALLRKLGGLFlppevnlsLDNSEGILARAVVRATVeEL 306
Cdd:smart00563   1 ALVVANHQSFLDPLVLSALLPRKLGRVRFVAKKELFYVPLLGWLLRLLGAIF--------IDRSNGRKARAALREAV-EL 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907137530  307 LTSGQPLLIFLEeppgspGPRLS--ALGQAWLGVVIQAVQAGiisdATLVPVAIAYD 361
Cdd:smart00563  72 LKEGEWLLIFPE------GTRSRpgKLLPFKKGAARLALEAG----VPIVPVAIRGT 118
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 223-358 3.25e-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: 3.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530 223 QGSPLVFLSTHKSLLDGFLLPFVLFSQGLGVVRVALDSRTCSPALRALLRKLGGLFLppevnlsldNSEGILARAVVRAT 302
Cdd:pfam01553  12 RGGPAIVVANHQSYLDVLLLSLALYKRGRPLVFVAKKELFDIPLVGWLMRLLGCIFI---------DRKNRKDAAGTLEY 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907137530 303 VEELLTSGQPLLIFLEeppgspGPRLSA--LGQAWLGVVIQAVQAGIisdaTLVPVAI 358
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) ...
 498-555 1.99e-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: 1.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907137530 498 LLLKHQKGVVLSQLLGEFSWLTEETLLRGFDVGFSGQLRCLAQHTLSLLRAHVVLLRV 555
Cdd:cd23383   126 LLSFHRKGDFVRALIGELHWALIRREGIPPPPSDSARLRVLAQFVLRSLVAELIYLRL 183
PTZ00374 PTZ00374
dihydroxyacetone phosphate acyltransferase; Provisional
 158-422 3.25e-04

dihydroxyacetone phosphate acyltransferase; Provisional


Pssm-ID: 240389 [Multi-domain]  Cd Length: 1108  Bit Score: 44.48  E-value: 3.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530  158 AAGEGQAPELVKKEVQRILGHIQTTPRPFLLRLFSWALLWFLNRLFLNVQLHKGQMKMVQKAVQEQGSPLVFLSTHKSLL 237
Cdd:PTZ00374   562 AKKEGASEKDVEARAKAILRTCGDNLNHVQCRLFGLMVRRILFRLYDRVSLNSGAFERLHRYVAMPRVAVVLLPLHRSYI 641

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530  238 DGFLLPFVLFSQGLGVVRV-ALDSRTCSPALRALLRKLGGLFLppevNLSLDNSEgiLARAVVRATVEELLTSGQPLLIF 316
Cdd:PTZ00374   642 DFIIMTYLLAVMGLPLPHVcAGDDFLRMGPIATLMRGSGAFFM----RRSFRDDP--LYAALFKEYVRHLVLRRRPLEFF 715

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530  317 LEEPPGSPG----PRLSALgQAWLGVVIQAVQAgiISDATLVPVAIAYDLVPDAPCNMNHDLA-------PLGLWTGALA 385
Cdd:PTZ00374   716 IEGTRSRTGktmaPKLGLL-KFICDTFYEGQQE--LDDVLIIPVSLSYDELLETTLYAKEQLGvskpkenPGNLLRARSL 792

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1907137530  386 VFRRLCNcwgcnrrvcVRVHLAQPFSLQEYTINARSC 422
Cdd:PTZ00374   793 LKRRHGK---------IHVHIGEPVSLRSFKDHPLQC 820
 
Name Accession Description Interval E-value
LPLAT_DHAPAT-like cd07993
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: GPAT-like; ...
 203-415 1.89e-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: 184.31  E-value: 1.89e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530 203 FLNVQLHKGQMKMVQKAVQEqGSPLVFLSTHKSLLDGFLLPFVLFSQGLGVVRVALDSRTCSPALRALLRKLGGLFLPPE 282
Cdd:cd07993     1 FDGVQVNEGQLERLRKAAQE-GHPVVLLPTHRSYLDFLLLSFILFSLGLPLPHIAAGENLNIPILGTLLRRLGAFFIRRS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530 283 VNlsldnsEGILARAVVRATVEELLTSGQPLLIFLEEPPGSPG-PRLSALGQAWlgVVIQAVQAGIISDATLVPVAIAYD 361
Cdd:cd07993    80 FG------KDPLYRAVLQEYVQELLKNGQPLEFFIEGTRSRTGkLLPPKLGLLS--VVVEAYLKGSVPDVLIVPVSISYD 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907137530 362 LVPDAPCNMNHDLAPLGLWTGALAvFRRLCNcWGCNRRVCVRVHLAQPFSLQEY 415
Cdd:cd07993   152 RVLEEELYAEELLGPPKPKESLSG-LLGASK-ILRENFGRIRVDFGEPISLREY 203
PlsB COG2937
Glycerol-3-phosphate O-acyltransferase [Lipid transport and metabolism]; Glycerol-3-phosphate ...
 158-576 2.01e-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: 90.37  E-value: 2.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530 158 AAGEGQAPELVKKEVQRILGHIQTTPRPFLLRLFSWALLWFLNRLFLNVQLHkgQMKMVQKAVQeqGSPLVFLSTHKSLL 237
Cdd:COG2937   140 AKSKGISEEKARKEARRYLREIAADFSYSAIRFLDRVLRWLWNRLYDGIRVD--NLERLRELAK--GHEIVYVPCHRSHM 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530 238 DGFLLPFVLFSQGLGVVRVA----LDsrtcSPALRALLRKLGGLFL-------PpevnlsldnsegiLARAVVRATVEEL 306
Cdd:COG2937   216 DYLLLSYVLYHNGLVPPHIAaginLN----FWPLGPILRRGGAFFIrrsfkgnK-------------LYSAVFREYLAEL 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530 307 LTSGQPLLIFLEeppG--SpgpRLSALGQAWLGV---VIQAVQAGIISDATLVPVAIAYDLVPDAPcNMNHDLA-----P 376
Cdd:COG2937   279 FERGYSVEYFIE---GgrS---RTGRLLPPKTGMlsmTVQAFLRGARRPVVFVPVYIGYERVLEVG-SYAKELRggekkK 351

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530 377 LGLWtGALAVFRRLCNCWGcnrrvcvRVHL--AQPFSLQEYtinarscwdsrqtlehLLQpivlgecsVVPDTEKEQEWT 454
Cdd:COG2937   352 ESLG-GLLRALRKLRRRFG-------RVYVnfGEPISLSEY----------------LDQ--------HVPDWRESEDLR 399

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530 455 PptglllalkEEDQLLVRRLSRHVLSASVASSAVMSTAIMATLLLLKHQKGvvlsqllgefswLTEETLLRgfdvgfsgQ 534
Cdd:COG2937   400 P---------EWLRPAVDKLAFEIMVRINRAAAVNPVNLVALALLASPKRA------------LTEAELLA--------Q 450

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1907137530 535 LRCLaqhtLSLLRahvvllRVHQGDLVVVPRPGP--GLTHLARL 576
Cdd:COG2937   451 LDLY----LDLLR------NVPYSLSVTLPELTPeeLLEHLLSL 484
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 227-361 2.17e-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: 2.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530  227 LVFLSTHKSLLDGFLLPFVLFSQGLGVVRVALDSRTCSPALRALLRKLGGLFlppevnlsLDNSEGILARAVVRATVeEL 306
Cdd:smart00563   1 ALVVANHQSFLDPLVLSALLPRKLGRVRFVAKKELFYVPLLGWLLRLLGAIF--------IDRSNGRKARAALREAV-EL 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907137530  307 LTSGQPLLIFLEeppgspGPRLS--ALGQAWLGVVIQAVQAGiisdATLVPVAIAYD 361
Cdd:smart00563  72 LKEGEWLLIFPE------GTRSRpgKLLPFKKGAARLALEAG----VPIVPVAIRGT 118
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 223-358 3.25e-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: 3.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530 223 QGSPLVFLSTHKSLLDGFLLPFVLFSQGLGVVRVALDSRTCSPALRALLRKLGGLFLppevnlsldNSEGILARAVVRAT 302
Cdd:pfam01553  12 RGGPAIVVANHQSYLDVLLLSLALYKRGRPLVFVAKKELFDIPLVGWLMRLLGCIFI---------DRKNRKDAAGTLEY 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907137530 303 VEELLTSGQPLLIFLEeppgspGPRLSA--LGQAWLGVVIQAVQAGIisdaTLVPVAI 358
Cdd:pfam01553  83 LVELLREGKLVVIFPE------GTRSREgeLLPFKKGAFRLAIEAGV----PIVPVAI 130
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 185-360 1.77e-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: 1.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530 185 PFLLRLFSWALLWFLNRLFLNVQLHKgqMKMVQKAVQEQGSPLVFLSTHKSLLDGFLLPFVLFSQglgvVR-VALDSRTC 263
Cdd:COG0204     5 FLLLRRFRYRLVRLWARLLLRLLGVR--VRVEGLENLPADGPVLIVANHQSWLDILLLLAALPRP----VRfVAKKELFK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530 264 SPALRALLRKLGGLFlppevnlsLDNSEGILARAVVRATVeELLTSGQPLLIFLEeppG--SPGPRLSAL--GQAWLgvv 339
Cdd:COG0204    79 IPLLGWLLRALGAIP--------VDRSKRRAALRALRQAV-EALKAGESLVIFPE---GtrSPDGRLLPFktGAARL--- 143

                         170       180
                  ....*....|....*....|.
gi 1907137530 340 iqAVQAGiisdATLVPVAIAY 360
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) ...
 498-555 1.99e-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: 1.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907137530 498 LLLKHQKGVVLSQLLGEFSWLTEETLLRGFDVGFSGQLRCLAQHTLSLLRAHVVLLRV 555
Cdd:cd23383   126 LLSFHRKGDFVRALIGELHWALIRREGIPPPPSDSARLRVLAQFVLRSLVAELIYLRL 183
PTZ00374 PTZ00374
dihydroxyacetone phosphate acyltransferase; Provisional
 158-422 3.25e-04

dihydroxyacetone phosphate acyltransferase; Provisional


Pssm-ID: 240389 [Multi-domain]  Cd Length: 1108  Bit Score: 44.48  E-value: 3.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530  158 AAGEGQAPELVKKEVQRILGHIQTTPRPFLLRLFSWALLWFLNRLFLNVQLHKGQMKMVQKAVQEQGSPLVFLSTHKSLL 237
Cdd:PTZ00374   562 AKKEGASEKDVEARAKAILRTCGDNLNHVQCRLFGLMVRRILFRLYDRVSLNSGAFERLHRYVAMPRVAVVLLPLHRSYI 641

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530  238 DGFLLPFVLFSQGLGVVRV-ALDSRTCSPALRALLRKLGGLFLppevNLSLDNSEgiLARAVVRATVEELLTSGQPLLIF 316
Cdd:PTZ00374   642 DFIIMTYLLAVMGLPLPHVcAGDDFLRMGPIATLMRGSGAFFM----RRSFRDDP--LYAALFKEYVRHLVLRRRPLEFF 715

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530  317 LEEPPGSPG----PRLSALgQAWLGVVIQAVQAgiISDATLVPVAIAYDLVPDAPCNMNHDLA-------PLGLWTGALA 385
Cdd:PTZ00374   716 IEGTRSRTGktmaPKLGLL-KFICDTFYEGQQE--LDDVLIIPVSLSYDELLETTLYAKEQLGvskpkenPGNLLRARSL 792

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1907137530  386 VFRRLCNcwgcnrrvcVRVHLAQPFSLQEYTINARSC 422
Cdd:PTZ00374   793 LKRRHGK---------IHVHIGEPVSLRSFKDHPLQC 820
LPLAT_AGPAT-like cd07989
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; ...
 226-360 4.42e-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: 4.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137530 226 PLVFLSTHKSLLDGFLLPFVLFSQGLGVVRVALDSRtcsPALRALLRKLGGLFlppevnlsLDNSEGILARAVVRAtVEE 305
Cdd:cd07989    25 PVIIVANHQSYLDPLVLGAALPRPIRFVAKKELFKI---PFLGWLLRLLGAIP--------IDRGNGRSAREALRE-AIE 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907137530 306 LLTSGQPLLIFLEeppG--SPGPRLSALGqawLGVVIQAVQAGiisdATLVPVAIAY 360
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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