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Conserved domains on  [gi|1046878794|ref|XP_017447069|]
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glycerol-3-phosphate acyltransferase 2, mitochondrial isoform X1 [Rattus norvegicus]

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; ...
176-387 9.01e-54

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: 185.08  E-value: 9.01e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794 176 FLNVQLHKGQMKMVHKAAQEGSPLVFLSTHKSLLDGFLLPFVLFSQGLGVLRVALDSRTCSPALRALLRKLGGLFLPPEA 255
Cdd:cd07993     1 FDGVQVNEGQLERLRKAAQEGHPVVLLPTHRSYLDFLLLSFILFSLGLPLPHIAAGENLNIPILGTLLRRLGAFFIRRSF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794 256 NlsldssEGILARAVVRATVEQLLTSGQPLLIFLEEAPGYPG-PRLSALGQAWlgLVVQAVQAGIVPDATLVPVATAYDL 334
Cdd:cd07993    81 G------KDPLYRAVLQEYVQELLKNGQPLEFFIEGTRSRTGkLLPPKLGLLS--VVVEAYLKGSVPDVLIVPVSISYDR 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1046878794 335 VPDAPCNMTHDLAPLGLWTGALAIFRRLcnCWGCNRRVCVRVHLAQPFSLQEY 387
Cdd:cd07993   153 VLEEELYAEELLGPPKPKESLSGLLGAS--KILRENFGRIRVDFGEPISLREY 203
ZF_RNaseIII_KREN_KREPB-like super family cl49632
C2H2 zinc finger and Ribonuclease III-like domain of RNA-editing catalytic complex (RECC) ...
470-527 2.03e-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: 2.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046878794 470 LLLKHQKGVVLSQLLGEFSWLTEETLLRGFDVGFSGQLRCLAQHTLSLLRAHVVLLRV 527
Cdd:cd23383   126 LLSFHRKGDFVRALIGELHWALIRREGIPPPPSDSARLRVLAQFVLRSLVAELIYLRL 183
 
Name Accession Description Interval E-value
LPLAT_DHAPAT-like cd07993
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: GPAT-like; ...
176-387 9.01e-54

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: 185.08  E-value: 9.01e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794 176 FLNVQLHKGQMKMVHKAAQEGSPLVFLSTHKSLLDGFLLPFVLFSQGLGVLRVALDSRTCSPALRALLRKLGGLFLPPEA 255
Cdd:cd07993     1 FDGVQVNEGQLERLRKAAQEGHPVVLLPTHRSYLDFLLLSFILFSLGLPLPHIAAGENLNIPILGTLLRRLGAFFIRRSF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794 256 NlsldssEGILARAVVRATVEQLLTSGQPLLIFLEEAPGYPG-PRLSALGQAWlgLVVQAVQAGIVPDATLVPVATAYDL 334
Cdd:cd07993    81 G------KDPLYRAVLQEYVQELLKNGQPLEFFIEGTRSRTGkLLPPKLGLLS--VVVEAYLKGSVPDVLIVPVSISYDR 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1046878794 335 VPDAPCNMTHDLAPLGLWTGALAIFRRLcnCWGCNRRVCVRVHLAQPFSLQEY 387
Cdd:cd07993   153 VLEEELYAEELLGPPKPKESLSGLLGAS--KILRENFGRIRVDFGEPISLREY 203
PlsB COG2937
Glycerol-3-phosphate O-acyltransferase [Lipid transport and metabolism]; Glycerol-3-phosphate ...
131-548 1.16e-19

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: 94.22  E-value: 1.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794 131 AAGEGQAPDLVKKEVQRILGHIQTTPRPFLLRLFSWALLWFLNRLFLNVQLHkgQMKMVHKAAQeGSPLVFLSTHKSLLD 210
Cdd:COG2937   140 AKSKGISEEKARKEARRYLREIAADFSYSAIRFLDRVLRWLWNRLYDGIRVD--NLERLRELAK-GHEIVYVPCHRSHMD 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794 211 GFLLPFVLFSQGLGVLRVA----LDsrtcSPALRALLRKLGGLFLPpeanlslDSSEGI-LARAVVRATVEQLLTSGQPL 285
Cdd:COG2937   217 YLLLSYVLYHNGLVPPHIAaginLN----FWPLGPILRRGGAFFIR-------RSFKGNkLYSAVFREYLAELFERGYSV 285
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794 286 LIFLEeapgypGPRlS---ALGQAWLGL---VVQAVQAGIVPDATLVPVATAYDLVPDAPcNMTHDLA-----PLGLWtG 354
Cdd:COG2937   286 EYFIE------GGR-SrtgRLLPPKTGMlsmTVQAFLRGARRPVVFVPVYIGYERVLEVG-SYAKELRggekkKESLG-G 356
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794 355 ALAIFRRLCNCWGcnrrvcvRVHL--AQPFSLQEYtinarscwgsrqtlehLLQpivlgecsVVPDTEKEQEWTPptsll 432
Cdd:COG2937   357 LLRALRKLRRRFG-------RVYVnfGEPISLSEY----------------LDQ--------HVPDWRESEDLRP----- 400
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794 433 lalkEEDQLLVRRLSRHVLSASVASSAVMSTAIMATLLLLKHQKGvvlsqllgefswLTEETLLRgfdvgfsgQLRCLaq 512
Cdd:COG2937   401 ----EWLRPAVDKLAFEIMVRINRAAAVNPVNLVALALLASPKRA------------LTEAELLA--------QLDLY-- 454
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1046878794 513 htLSLLRahvvllRVHQGDLVVVPRPGP--GLTHLARL 548
Cdd:COG2937   455 --LDLLR------NVPYSLSVTLPELTPeeLLEHLLSL 484
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
199-333 7.42e-10

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: 57.37  E-value: 7.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794  199 LVFLSTHKSLLDGFLLPFVLFSQGLGVLRVALDSRTCSPALRALLRKLGGLFlppeanlsLDSSEGILARAVVRATVEqL 278
Cdd:smart00563   1 ALVVANHQSFLDPLVLSALLPRKLGRVRFVAKKELFYVPLLGWLLRLLGAIF--------IDRSNGRKARAALREAVE-L 71
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1046878794  279 LTSGQPLLIFLEEAPGYPGprlsALGQAWLGLVVQAVQAGivpdATLVPVATAYD 333
Cdd:smart00563  72 LKEGEWLLIFPEGTRSRPG----KLLPFKKGAARLALEAG----VPIVPVAIRGT 118
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
194-329 1.51e-06

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: 48.04  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794 194 QEGSPLVFLSTHKSLLDGFLLPFVLFSQGlGVLRVALDSRTCS-PALRALLRKLGGLFLppeanlsldSSEGILARAVVR 272
Cdd:pfam01553  11 PRGGPAIVVANHQSYLDVLLLSLALYKRG-RPLVFVAKKELFDiPLVGWLMRLLGCIFI---------DRKNRKDAAGTL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1046878794 273 ATVEQLLTSGQPLLIFLEeapgypGPRLSA--LGQAWLGLVVQAVQAGIvpdaTLVPVA 329
Cdd:pfam01553  81 EYLVELLREGKLVVIFPE------GTRSREgeLLPFKKGAFRLAIEAGV----PIVPVA 129
PTZ00374 PTZ00374
dihydroxyacetone phosphate acyltransferase; Provisional
131-394 6.46e-05

dihydroxyacetone phosphate acyltransferase; Provisional


Pssm-ID: 240389 [Multi-domain]  Cd Length: 1108  Bit Score: 46.79  E-value: 6.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794  131 AAGEGQAPDLVKKEVQRILGHIQTTPRPFLLRLFSWALLWFLNRLFLNVQLHKGQMKMVHKA-AQEGSPLVFLSTHKSLL 209
Cdd:PTZ00374   562 AKKEGASEKDVEARAKAILRTCGDNLNHVQCRLFGLMVRRILFRLYDRVSLNSGAFERLHRYvAMPRVAVVLLPLHRSYI 641
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794  210 DGFLLPFVLFSQGLGVLRV-ALDSRTCSPALRALLRKLGGLFLppeaNLSLDSSEgiLARAVVRATVEQLLTSGQPLLIF 288
Cdd:PTZ00374   642 DFIIMTYLLAVMGLPLPHVcAGDDFLRMGPIATLMRGSGAFFM----RRSFRDDP--LYAALFKEYVRHLVLRRRPLEFF 715
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794  289 LEEAPGYPGPRLSALgqawLGLV-------VQAVQAgiVPDATLVPVATAYDLVPDApcnMTHDLAPLGLW-----TGAL 356
Cdd:PTZ00374   716 IEGTRSRTGKTMAPK----LGLLkficdtfYEGQQE--LDDVLIIPVSLSYDELLET---TLYAKEQLGVSkpkenPGNL 786
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1046878794  357 AIFRRLCNcwgcNRRVCVRVHLAQPFSLQEYTINARSC 394
Cdd:PTZ00374   787 LRARSLLK----RRHGKIHVHIGEPVSLRSFKDHPLQC 820
ZF_RNaseIII_KREN_KREPB-like cd23383
C2H2 zinc finger and Ribonuclease III-like domain of RNA-editing catalytic complex (RECC) ...
470-527 2.03e-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: 2.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046878794 470 LLLKHQKGVVLSQLLGEFSWLTEETLLRGFDVGFSGQLRCLAQHTLSLLRAHVVLLRV 527
Cdd:cd23383   126 LLSFHRKGDFVRALIGELHWALIRREGIPPPPSDSARLRVLAQFVLRSLVAELIYLRL 183
 
Name Accession Description Interval E-value
LPLAT_DHAPAT-like cd07993
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: GPAT-like; ...
176-387 9.01e-54

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: 185.08  E-value: 9.01e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794 176 FLNVQLHKGQMKMVHKAAQEGSPLVFLSTHKSLLDGFLLPFVLFSQGLGVLRVALDSRTCSPALRALLRKLGGLFLPPEA 255
Cdd:cd07993     1 FDGVQVNEGQLERLRKAAQEGHPVVLLPTHRSYLDFLLLSFILFSLGLPLPHIAAGENLNIPILGTLLRRLGAFFIRRSF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794 256 NlsldssEGILARAVVRATVEQLLTSGQPLLIFLEEAPGYPG-PRLSALGQAWlgLVVQAVQAGIVPDATLVPVATAYDL 334
Cdd:cd07993    81 G------KDPLYRAVLQEYVQELLKNGQPLEFFIEGTRSRTGkLLPPKLGLLS--VVVEAYLKGSVPDVLIVPVSISYDR 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1046878794 335 VPDAPCNMTHDLAPLGLWTGALAIFRRLcnCWGCNRRVCVRVHLAQPFSLQEY 387
Cdd:cd07993   153 VLEEELYAEELLGPPKPKESLSGLLGAS--KILRENFGRIRVDFGEPISLREY 203
PlsB COG2937
Glycerol-3-phosphate O-acyltransferase [Lipid transport and metabolism]; Glycerol-3-phosphate ...
131-548 1.16e-19

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: 94.22  E-value: 1.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794 131 AAGEGQAPDLVKKEVQRILGHIQTTPRPFLLRLFSWALLWFLNRLFLNVQLHkgQMKMVHKAAQeGSPLVFLSTHKSLLD 210
Cdd:COG2937   140 AKSKGISEEKARKEARRYLREIAADFSYSAIRFLDRVLRWLWNRLYDGIRVD--NLERLRELAK-GHEIVYVPCHRSHMD 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794 211 GFLLPFVLFSQGLGVLRVA----LDsrtcSPALRALLRKLGGLFLPpeanlslDSSEGI-LARAVVRATVEQLLTSGQPL 285
Cdd:COG2937   217 YLLLSYVLYHNGLVPPHIAaginLN----FWPLGPILRRGGAFFIR-------RSFKGNkLYSAVFREYLAELFERGYSV 285
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794 286 LIFLEeapgypGPRlS---ALGQAWLGL---VVQAVQAGIVPDATLVPVATAYDLVPDAPcNMTHDLA-----PLGLWtG 354
Cdd:COG2937   286 EYFIE------GGR-SrtgRLLPPKTGMlsmTVQAFLRGARRPVVFVPVYIGYERVLEVG-SYAKELRggekkKESLG-G 356
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794 355 ALAIFRRLCNCWGcnrrvcvRVHL--AQPFSLQEYtinarscwgsrqtlehLLQpivlgecsVVPDTEKEQEWTPptsll 432
Cdd:COG2937   357 LLRALRKLRRRFG-------RVYVnfGEPISLSEY----------------LDQ--------HVPDWRESEDLRP----- 400
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794 433 lalkEEDQLLVRRLSRHVLSASVASSAVMSTAIMATLLLLKHQKGvvlsqllgefswLTEETLLRgfdvgfsgQLRCLaq 512
Cdd:COG2937   401 ----EWLRPAVDKLAFEIMVRINRAAAVNPVNLVALALLASPKRA------------LTEAELLA--------QLDLY-- 454
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1046878794 513 htLSLLRahvvllRVHQGDLVVVPRPGP--GLTHLARL 548
Cdd:COG2937   455 --LDLLR------NVPYSLSVTLPELTPeeLLEHLLSL 484
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
199-333 7.42e-10

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: 57.37  E-value: 7.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794  199 LVFLSTHKSLLDGFLLPFVLFSQGLGVLRVALDSRTCSPALRALLRKLGGLFlppeanlsLDSSEGILARAVVRATVEqL 278
Cdd:smart00563   1 ALVVANHQSFLDPLVLSALLPRKLGRVRFVAKKELFYVPLLGWLLRLLGAIF--------IDRSNGRKARAALREAVE-L 71
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1046878794  279 LTSGQPLLIFLEEAPGYPGprlsALGQAWLGLVVQAVQAGivpdATLVPVATAYD 333
Cdd:smart00563  72 LKEGEWLLIFPEGTRSRPG----KLLPFKKGAARLALEAG----VPIVPVAIRGT 118
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
194-329 1.51e-06

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: 48.04  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794 194 QEGSPLVFLSTHKSLLDGFLLPFVLFSQGlGVLRVALDSRTCS-PALRALLRKLGGLFLppeanlsldSSEGILARAVVR 272
Cdd:pfam01553  11 PRGGPAIVVANHQSYLDVLLLSLALYKRG-RPLVFVAKKELFDiPLVGWLMRLLGCIFI---------DRKNRKDAAGTL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1046878794 273 ATVEQLLTSGQPLLIFLEeapgypGPRLSA--LGQAWLGLVVQAVQAGIvpdaTLVPVA 329
Cdd:pfam01553  81 EYLVELLREGKLVVIFPE------GTRSREgeLLPFKKGAFRLAIEAGV----PIVPVA 129
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
158-332 7.80e-06

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: 47.70  E-value: 7.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794 158 PFLLRLFSWALLWFLNRLFLNVQLHKGQMKMVHKAAQEGsPLVFLSTHKSLLDGFLLPFVLFSQglgvLR-VALDSRTCS 236
Cdd:COG0204     5 FLLLRRFRYRLVRLWARLLLRLLGVRVRVEGLENLPADG-PVLIVANHQSWLDILLLLAALPRP----VRfVAKKELFKI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794 237 PALRALLRKLGGLFlppeanlsLDSSEGILARAVVRATVEqLLTSGQPLLIFLEeapG--YPGPRLSAL--GQAWLglvv 312
Cdd:COG0204    80 PLLGWLLRALGAIP--------VDRSKRRAALRALRQAVE-ALKAGESLVIFPE---GtrSPDGRLLPFktGAARL---- 143
                         170       180
                  ....*....|....*....|
gi 1046878794 313 qAVQAGiVPdatLVPVATAY 332
Cdd:COG0204   144 -ALEAG-VP---IVPVAIDG 158
PTZ00374 PTZ00374
dihydroxyacetone phosphate acyltransferase; Provisional
131-394 6.46e-05

dihydroxyacetone phosphate acyltransferase; Provisional


Pssm-ID: 240389 [Multi-domain]  Cd Length: 1108  Bit Score: 46.79  E-value: 6.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794  131 AAGEGQAPDLVKKEVQRILGHIQTTPRPFLLRLFSWALLWFLNRLFLNVQLHKGQMKMVHKA-AQEGSPLVFLSTHKSLL 209
Cdd:PTZ00374   562 AKKEGASEKDVEARAKAILRTCGDNLNHVQCRLFGLMVRRILFRLYDRVSLNSGAFERLHRYvAMPRVAVVLLPLHRSYI 641
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794  210 DGFLLPFVLFSQGLGVLRV-ALDSRTCSPALRALLRKLGGLFLppeaNLSLDSSEgiLARAVVRATVEQLLTSGQPLLIF 288
Cdd:PTZ00374   642 DFIIMTYLLAVMGLPLPHVcAGDDFLRMGPIATLMRGSGAFFM----RRSFRDDP--LYAALFKEYVRHLVLRRRPLEFF 715
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046878794  289 LEEAPGYPGPRLSALgqawLGLV-------VQAVQAgiVPDATLVPVATAYDLVPDApcnMTHDLAPLGLW-----TGAL 356
Cdd:PTZ00374   716 IEGTRSRTGKTMAPK----LGLLkficdtfYEGQQE--LDDVLIIPVSLSYDELLET---TLYAKEQLGVSkpkenPGNL 786
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1046878794  357 AIFRRLCNcwgcNRRVCVRVHLAQPFSLQEYTINARSC 394
Cdd:PTZ00374   787 LRARSLLK----RRHGKIHVHIGEPVSLRSFKDHPLQC 820
ZF_RNaseIII_KREN_KREPB-like cd23383
C2H2 zinc finger and Ribonuclease III-like domain of RNA-editing catalytic complex (RECC) ...
470-527 2.03e-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: 2.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046878794 470 LLLKHQKGVVLSQLLGEFSWLTEETLLRGFDVGFSGQLRCLAQHTLSLLRAHVVLLRV 527
Cdd:cd23383   126 LLSFHRKGDFVRALIGELHWALIRREGIPPPPSDSARLRVLAQFVLRSLVAELIYLRL 183
PRK04974 PRK04974
glycerol-3-phosphate 1-O-acyltransferase PlsB;
160-223 1.28e-03

glycerol-3-phosphate 1-O-acyltransferase PlsB;


Pssm-ID: 235325 [Multi-domain]  Cd Length: 818  Bit Score: 42.53  E-value: 1.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046878794 160 LLRLFSWALLWFLNRLFLNVQLHkgQMKMVHKAAQEGSPLVFLSTHKSLLDGFLLPFVLFSQGL 223
Cdd:PRK04974  267 AIRLADRFLTWLWNRLYQGINVH--NAERVRQLAQDGHEIVYVPCHRSHMDYLLLSYVLYHQGL 328
 
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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