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Conserved domains on  [gi|767939493|ref|XP_011512696|]
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protein FAM83B isoform X1 [Homo sapiens]

Protein Classification

phospholipase D-like domain-containing protein; phospholipase D family protein( domain architecture ID 10173813)

phospholipase D-like domain-containing protein may hydrolyze phospholipid phosphodiester bonds to yield phosphatidic acid and a free polar head group, and may also catalyze the transphosphatidylation of phospholipids to acceptor alcohols; phospholipase D family protein similar to Escherichia coli cardiolipin synthase C and Neisseria gonorrhoeae phospholipase D; hydrolyzes phospholipid phosphodiester bonds

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLDc_FAM83B_N cd09182
N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence ...
 17-283 0e+00

N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence similarity 83B; N-terminal phospholipase D (PLD)-like domain of the uncharacterized protein, Family with sequence similarity 83B (FAM83B). Since the N-terminal PLD-like domain of FAM83 proteins shows only trace similarity to the PLD catalytic domain and lacks the functionally important histidine residue, FAM83 proteins may share a similar three-dimensional fold with PLD enzymes, but are most unlikely to carry PLD activity. The N-terminus of FAM83B shows high homology to other FAM83 family members, indicating that FAM83B might have arisen early in vertebrate evolution by duplication of a gene in the FAM83 family.


:

Pssm-ID: 197279  Cd Length: 266  Bit Score: 559.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493   17 DNYIEPHYKEWYRVAIDILIEHGLEAYQEFLVQERVSDFLAEEEINYILKNVQKVAQSTAHGTDDSCDDTLSSGTYWPVE 96
Cdd:cd09182     1 DNYIQPHYKEWYRLAIDALIEGGLEAYQEFLRAERISDFLSEEEILYILENVEKPPQETDESEDKRTDDTASSGTYWPAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493   97 SDVEAPNLDLGWPYVMpGLLGGTHIDLLFHPPRAHLLTIKETIRKMIKEARKVIALVMDIFTDVDIFKEIVEASTRGVSV 176
Cdd:cd09182    81 SDVEAPNLDLGWPYVM-LEAGGTSIDLLFHPPRANTPTIKEVIRKQIQEARQVIAIAMDVFTDVDIFKEVVEASTRGVAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  177 YILLDESNFNHFLNMTEKQGCSVQRLRNIRVRTVKGQDYLSKTGAKFHGKMEQKFLLVDCQKVMYGSYSYMWSFEKAHLS 256
Cdd:cd09182   160 YILLDHSHFASFLTMTEKQGIQIQRLRNIRVRTVKGQDYQCKSGAKFHGAMEQKFLLVDCQKVLYGSYSYMWSFEKIHLS 239

                         250       260
                  ....*....|....*....|....*..
gi 767939493  257 MVQIITGQLVESFDEEFRTLYARSCVP 283
Cdd:cd09182   240 MVQVITGQLVESYDEEFRTLYARSAVP 266
 
Name Accession Description Interval E-value
PLDc_FAM83B_N cd09182
N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence ...
 17-283 0e+00

N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence similarity 83B; N-terminal phospholipase D (PLD)-like domain of the uncharacterized protein, Family with sequence similarity 83B (FAM83B). Since the N-terminal PLD-like domain of FAM83 proteins shows only trace similarity to the PLD catalytic domain and lacks the functionally important histidine residue, FAM83 proteins may share a similar three-dimensional fold with PLD enzymes, but are most unlikely to carry PLD activity. The N-terminus of FAM83B shows high homology to other FAM83 family members, indicating that FAM83B might have arisen early in vertebrate evolution by duplication of a gene in the FAM83 family.


Pssm-ID: 197279  Cd Length: 266  Bit Score: 559.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493   17 DNYIEPHYKEWYRVAIDILIEHGLEAYQEFLVQERVSDFLAEEEINYILKNVQKVAQSTAHGTDDSCDDTLSSGTYWPVE 96
Cdd:cd09182     1 DNYIQPHYKEWYRLAIDALIEGGLEAYQEFLRAERISDFLSEEEILYILENVEKPPQETDESEDKRTDDTASSGTYWPAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493   97 SDVEAPNLDLGWPYVMpGLLGGTHIDLLFHPPRAHLLTIKETIRKMIKEARKVIALVMDIFTDVDIFKEIVEASTRGVSV 176
Cdd:cd09182    81 SDVEAPNLDLGWPYVM-LEAGGTSIDLLFHPPRANTPTIKEVIRKQIQEARQVIAIAMDVFTDVDIFKEVVEASTRGVAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  177 YILLDESNFNHFLNMTEKQGCSVQRLRNIRVRTVKGQDYLSKTGAKFHGKMEQKFLLVDCQKVMYGSYSYMWSFEKAHLS 256
Cdd:cd09182   160 YILLDHSHFASFLTMTEKQGIQIQRLRNIRVRTVKGQDYQCKSGAKFHGAMEQKFLLVDCQKVLYGSYSYMWSFEKIHLS 239

                         250       260
                  ....*....|....*....|....*..
gi 767939493  257 MVQIITGQLVESFDEEFRTLYARSCVP 283
Cdd:cd09182   240 MVQVITGQLVESYDEEFRTLYARSAVP 266
FAM83 pfam07894
FAM83 A-H; The FAM83 family members include FAM83A-H. They are oncogenes that function as ...
 12-281 1.91e-147

FAM83 A-H; The FAM83 family members include FAM83A-H. They are oncogenes that function as intermediaries in EGFR/RAS signaling.


Pssm-ID: 462308  Cd Length: 276  Bit Score: 439.67  E-value: 1.91e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493    12 DECKSDNYIEPHYKEWYRVAIDILIEHGLEAYQEFLVQERVSDFLAEEEINYILKNVQKVA-----QSTAHGTDDSCDDT 86
Cdd:pfam07894    1 NWPVSESKPEFLYSEEQRLALEALLEGGEEAYYEFLKEEGEVDFLSSLEIQYILENAQKPAseeyePSEGEQGQGSGDGD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493    87 LSSGTYWPVESDVEAPNLDLGWPyVMPGLLGGTHIDLLFHPPRAHLLTIKETIRKMIKEARKVIALVMDIFTDVDIFKEI 166
Cdd:pfam07894   81 SSSGTYWPMQSDTEVPALDLGWP-DEPSYKGVTRVTVYFQPPKEGSPHIKEVVRRLIQQAQKVIAIVMDVFTDVDIFCDL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493   167 VEAST-RGVSVYILLDESNFNHFLNMTEKQGCSVQRLRNIRVRTVKGQDYLSKTGAKFHGKMEQKFLLVDCQKVMYGSYS 245
Cdd:pfam07894  160 LEAASkRGVPVYILLDEANLKHFLEMCEKLQVNLGHLKNMRVRSVTGDTYYSRSGKKFTGQLKEKFLLVDGEKVLTGSYS 239

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 767939493   246 YMWSFEKAHLSMVQIITGQLVESFDEEFRTLYARSC 281
Cdd:pfam07894  240 FTWSSSKLHRNLVTVLTGQVVESFDEEFRILYAQSK 275
PRK13912 PRK13912
nuclease NucT; Provisional
 136-277 6.21e-10

nuclease NucT; Provisional


Pssm-ID: 184389 [Multi-domain]  Cd Length: 177  Bit Score: 59.40  E-value: 6.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  136 KETIRKMIKEARKVIALVMDIFTDVDIFKEIVEASTRGVSVYILLDESNfNHflNMTEKQGCSVQRLRNIRVRTVKGqdy 215
Cdd:PRK13912   35 LNKLVSLISNARSSIKIAIYSFTHKDIAKALKSAAKRGVKISIIYDYES-NH--NNDQSTIGYLDKYPNIKVCLLKG--- 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767939493  216 LSKTGAKFHGKMEQKFLLVDCQKVMYGSYSymWSFekahlsmvqiitgqlvESFDEEFRTLY 277
Cdd:PRK13912  109 LKAKNGKYYGIMHQKVAIIDDKIVVLGSAN--WSK----------------NAFENNYEVLL 152
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 115-280 2.39e-04

Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and metabolism]; Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 441111 [Multi-domain]  Cd Length: 367  Bit Score: 44.55  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  115 LLGGTHIDLLFHPPRAhlltiKETIRKMIKEARKVIALVMDIFTD----VDIFKEIVEASTRGVSVYILLDE----SNFN 186
Cdd:COG1502    11 LVGGNRVTLLVDGDEA-----FAALLEAIEAARRSIDLEYYIFDDdevgRRLADALIAAARRGVKVRVLLDGigsrALNR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  187 HFLNMTEKQGCSVQRLRNIRVRTvkgqdylsktgAKFHGKMEQKFLLVDCQKVMYGSY----SYMWSFEKAHL---SMVq 259
Cdd:COG1502    86 DFLRRLRAAGVEVRLFNPVRLLF-----------RRLNGRNHRKIVVIDGRVAFVGGAnitdEYLGRDPGFGPwrdTHV- 153

                         170       180
                  ....*....|....*....|.
gi 767939493  260 IITGQLVESFDEEFRTLYARS 280
Cdd:COG1502   154 RIEGPAVADLQAVFAEDWNFA 174
 
Name Accession Description Interval E-value
PLDc_FAM83B_N cd09182
N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence ...
 17-283 0e+00

N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence similarity 83B; N-terminal phospholipase D (PLD)-like domain of the uncharacterized protein, Family with sequence similarity 83B (FAM83B). Since the N-terminal PLD-like domain of FAM83 proteins shows only trace similarity to the PLD catalytic domain and lacks the functionally important histidine residue, FAM83 proteins may share a similar three-dimensional fold with PLD enzymes, but are most unlikely to carry PLD activity. The N-terminus of FAM83B shows high homology to other FAM83 family members, indicating that FAM83B might have arisen early in vertebrate evolution by duplication of a gene in the FAM83 family.


Pssm-ID: 197279  Cd Length: 266  Bit Score: 559.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493   17 DNYIEPHYKEWYRVAIDILIEHGLEAYQEFLVQERVSDFLAEEEINYILKNVQKVAQSTAHGTDDSCDDTLSSGTYWPVE 96
Cdd:cd09182     1 DNYIQPHYKEWYRLAIDALIEGGLEAYQEFLRAERISDFLSEEEILYILENVEKPPQETDESEDKRTDDTASSGTYWPAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493   97 SDVEAPNLDLGWPYVMpGLLGGTHIDLLFHPPRAHLLTIKETIRKMIKEARKVIALVMDIFTDVDIFKEIVEASTRGVSV 176
Cdd:cd09182    81 SDVEAPNLDLGWPYVM-LEAGGTSIDLLFHPPRANTPTIKEVIRKQIQEARQVIAIAMDVFTDVDIFKEVVEASTRGVAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  177 YILLDESNFNHFLNMTEKQGCSVQRLRNIRVRTVKGQDYLSKTGAKFHGKMEQKFLLVDCQKVMYGSYSYMWSFEKAHLS 256
Cdd:cd09182   160 YILLDHSHFASFLTMTEKQGIQIQRLRNIRVRTVKGQDYQCKSGAKFHGAMEQKFLLVDCQKVLYGSYSYMWSFEKIHLS 239

                         250       260
                  ....*....|....*....|....*..
gi 767939493  257 MVQIITGQLVESFDEEFRTLYARSCVP 283
Cdd:cd09182   240 MVQVITGQLVESYDEEFRTLYARSAVP 266
PLDc_FAM83_N cd09119
N-terminal phospholipase D-like domain of proteins from the Family with sequence similarity 83; ...
 17-280 2.15e-152

N-terminal phospholipase D-like domain of proteins from the Family with sequence similarity 83; N-terminal phospholipase D (PLD)-like domain of vetebrate proteins from the Family with sequence similarity 83 (FAM83), which is comprised of 8 members, designated FAM83A through FAM83H. Since the N-terminal PLD-like domain of FAM83 proteins shows only trace similarity to the PLD catalytic domain and lacks the functionally important histidine residue, the FAM83 proteins may share a similar three-dimensional fold with PLD enzymes, but are unlikely to carry PLD activity. Members of the FAM83 are mostly uncharacterized proteins. FAM83A, also known as tumor antigen BJ-TSA-9, is a novel tumor-specific gene highly expressed in human lung adenocarcinoma. FAM83D, also known as spindle protein CHICA, is a cell-cycle-regulated spindle component which localizes to the mitotic spindle and is both upregulated and phosphorylated during mitosis. The gene encoding protein FAM83H is the first gene involved in the etiology of amelogenesis imperfecta (AI), that encodes a non-secreted protein due to the absence of a signal peptide. Defects in gene FAM83H cause autosomal dominant hypocalcified amelogenesis imperfecta (ADHCAI). FAM83B, FAM83C, FAM83F, and FAM83G are uncharacterized proteins present across vertebrates while FAM83E is an uncharacterized protein found only in mammals.


Pssm-ID: 197218  Cd Length: 269  Bit Score: 452.22  E-value: 2.15e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493   17 DNYIEPHYKEWYRVAIDILIEHGLEAYQEFLVQERVSDFLAEEEINYILKNVQKVAQST-----AHGTDDSCDDTLSSGT 91
Cdd:cd09119     1 ESYPEFFYSESARLALEALLEGGPEAYYRVLSTEREADFLSPEEIQYILSAARPYPEKPeapgaAAGTQLSLSSELSSGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493   92 YWPVESDVEAPNLDLGWPYVMpGLLGGTHIDLLFHPPRAHLLTIKETIRKMIKEARKVIALVMDIFTDVDIFKEIVEAS- 170
Cdd:cd09119    81 YFPVNSDVEPPDLDLGWPETD-AYRGVTRATVHFQPPKEGAPNIKDLVRRMIQQAQKVIAVVMDVFTDVDIFCDLLEAAn 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  171 TRGVSVYILLDESNFNHFLNMTEKQGCSVQRLRNIRVRTVKGQDYLSKTGAKFHGKMEQKFLLVDCQKVMYGSYSYMWSF 250
Cdd:cd09119   160 KRGVAVYILLDQGNVKHFLEMCDKLQLSDEHLKNMRVRSVGGKTYCSRSGKKFKGQMKEKFLLVDGDRVVSGSYSFTWSD 239

                         250       260       270
                  ....*....|....*....|....*....|
gi 767939493  251 EKAHLSMVQIITGQLVESFDEEFRTLYARS 280
Cdd:cd09119   240 AKLHRSMLSVLTGQVVESFDEEFRILYAQS 269
FAM83 pfam07894
FAM83 A-H; The FAM83 family members include FAM83A-H. They are oncogenes that function as ...
 12-281 1.91e-147

FAM83 A-H; The FAM83 family members include FAM83A-H. They are oncogenes that function as intermediaries in EGFR/RAS signaling.


Pssm-ID: 462308  Cd Length: 276  Bit Score: 439.67  E-value: 1.91e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493    12 DECKSDNYIEPHYKEWYRVAIDILIEHGLEAYQEFLVQERVSDFLAEEEINYILKNVQKVA-----QSTAHGTDDSCDDT 86
Cdd:pfam07894    1 NWPVSESKPEFLYSEEQRLALEALLEGGEEAYYEFLKEEGEVDFLSSLEIQYILENAQKPAseeyePSEGEQGQGSGDGD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493    87 LSSGTYWPVESDVEAPNLDLGWPyVMPGLLGGTHIDLLFHPPRAHLLTIKETIRKMIKEARKVIALVMDIFTDVDIFKEI 166
Cdd:pfam07894   81 SSSGTYWPMQSDTEVPALDLGWP-DEPSYKGVTRVTVYFQPPKEGSPHIKEVVRRLIQQAQKVIAIVMDVFTDVDIFCDL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493   167 VEAST-RGVSVYILLDESNFNHFLNMTEKQGCSVQRLRNIRVRTVKGQDYLSKTGAKFHGKMEQKFLLVDCQKVMYGSYS 245
Cdd:pfam07894  160 LEAASkRGVPVYILLDEANLKHFLEMCEKLQVNLGHLKNMRVRSVTGDTYYSRSGKKFTGQLKEKFLLVDGEKVLTGSYS 239

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 767939493   246 YMWSFEKAHLSMVQIITGQLVESFDEEFRTLYARSC 281
Cdd:pfam07894  240 FTWSSSKLHRNLVTVLTGQVVESFDEEFRILYAQSK 275
PLDc_FAM83H_N cd09188
N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence ...
 18-280 7.96e-95

N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence similarity 83H; N-terminal phospholipase D (PLD)-like domain of the protein, Family with sequence similarity 83H (FAM83H) on chromosome 8q24.3, which localizes in the intracellular environment and is associated with vesicles, can be regulated by kinases, and plays important roles during ameloblast differentiation and enamel matrix calcification. The gene encoding protein FAM83H is the first gene involved in the etiology of amelogenesis imperfecta (AI), that encodes a non-secreted protein due to the absence of a signal peptide. Defects in gene FAM83H cause autosomal dominant hypocalcified amelogenesis imperfecta (ADHCAI). Since the N-terminal PLD-like domain of FAM83H shows only trace similarity to the PLD catalytic domain and lacks the functionally important histidine residue, FAM83H may share a similar three-dimensional fold with PLD enzymes, but is most unlikely to carry PLD activity.


Pssm-ID: 197284  Cd Length: 265  Bit Score: 301.39  E-value: 7.96e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493   18 NYIEPHYKEWYRVAIDILIEHGLEAYQEFLVQERVSDFLAEEEINYILKNVQK---VAQSTAHGTDDSCDDTLSSGTYWP 94
Cdd:cd09188     2 NYLPPHYKEYYRLAIDALAEDGIEGYERFLAEEGVPDFLCPSEVEHIKSTLQTpqyAGQEPEYLPYGDIDQDGSSGTYWP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493   95 VESDVEAPNLDLGWPyvMPGLLGGTHIDLLFHPPRAHLLTIKETIRKMIKEARKVIALVMDIFTDVDIFKEIVEASTRGV 174
Cdd:cd09188    82 MNSDLAAPELDLGWP--MQFGFQGTEVTTLVQPPPPDNPSIKEEARRMIRSAQQVIAVVMDIFTDVDILSELLEAAARRV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  175 SVYILLDESNFNHFLNMTEKQGCSVQRLRNIRVRTVKGQDYLSKTGAKFHGKMEQKFLLVDCQKVMYGSYSYMWSFEKAH 254
Cdd:cd09188   160 PVYILLDEMNAQLFLDMAAKCRVNLNYVEFLRVRTVSGPTYFCRTGKSFKGHVKEKFLLVDCRVVLSGNYSFMWSFEKIH 239

                         250       260
                  ....*....|....*....|....*.
gi 767939493  255 LSMVQIITGQLVESFDEEFRTLYARS 280
Cdd:cd09188   240 RSIAHIFQGELVASFDEEFRILFAQS 265
PLDc_FAM83C_N cd09183
N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence ...
 24-280 1.13e-71

N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence similarity 83C; N-terminal phospholipase D (PLD)-like domain of the uncharacterized protein, Family with sequence similarity 83C (FAM83C). Since the N-terminal PLD-like domain of FAM83 proteins shows only trace similarity to the PLD catalytic domain and lacks the functionally important histidine residue, FAM83 proteins may share a similar three-dimensional fold with PLD enzymes, but are most unlikely to carry PLD activity. The N-terminus of FAM83C shows high homology to other FAM83 family members, indicating that FAM83C might have arisen early in vertebrate evolution by duplication of a gene in the FAM83 family.


Pssm-ID: 197280  Cd Length: 274  Bit Score: 238.98  E-value: 1.13e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493   24 YKEWYRVAIDILIEHGLEAYQEFLVQERVSDFLAEEEINYILKNVQKVAQS----------TAHGTDDSCDDTLSSGTYW 93
Cdd:cd09183     8 HNETARLATDALLERGEKAYLQVLQEEKELPFLSTLDIDYITNSVAINGKAnhaivseldgTNDIDEDSLPSELTSGTYF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493   94 PVESDVEAPNLDLGWPYV-MPGLLGGTHIDLLFHPPRAHllTIKETIRKMIKEARKVIALVMDIFTDVDIFKEIVEAST- 171
Cdd:cd09183    88 PMMSDFDPPDLELGWPEIpLATKASPTEAQIFFQRDKAN--NIKDLIRSLISMAKTVIAIVMDLFTDVDILCDLMEASNk 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  172 RGVSVYILLDESNFNHFLNMTEKQGCSVQRLRNIRVRTVKGQDYLSKTGAKFHGKMEQKFLLVDCQKVMYGSYSYMWSFE 251
Cdd:cd09183   166 RRVPVYLLLDEENLGHFLEMCEKLDLNKTSLPNMRIRSVCGDTYCTKSGKKFTGQVLEKFLLIDCEQVVAGSYSFTWLSS 245

                         250       260
                  ....*....|....*....|....*....
gi 767939493  252 KAHLSMVQIITGQLVESFDEEFRTLYARS 280
Cdd:cd09183   246 QVHSNLVTHFRGNIVEEFDREFRCLYADS 274
PLDc_FAM83D_N cd09184
N-terminal phospholipase D-like domain of the protein, Family with sequence similarity 83D; ...
 24-280 3.27e-70

N-terminal phospholipase D-like domain of the protein, Family with sequence similarity 83D; N-terminal phospholipase D (PLD)-like domain of the protein Family with sequence similarity 83D (FAM83D), also known as spindle protein CHICA. CHICA is a cell-cycle-regulated spindle component, which localizes to the mitotic spindle and is both upregulated and phosphorylated during mitosis. CHICA is required to localize the chromokinesin Kid to the mitotic spindle and serves as a novel interaction partner of Kid, which is required for the generation of polar ejection forces and chromosome congression. Since the N-terminal PLD-like domain of FAM83D shows only trace similarity to the PLD catalytic domain and lacks the functionally important histidine residue, FAM83D may share a similar three-dimensional fold with PLD enzymes, but is unlikely to carry PLD activity.


Pssm-ID: 197281  Cd Length: 271  Bit Score: 234.76  E-value: 3.27e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493   24 YKEWYRVAIDILIEHGLEAYQEFLVQERVSDFLAEEEINYILK--NVQKVAQSTAHGTDDSCDDTL--SSGTYWPVESDV 99
Cdd:cd09184     8 YNEAHRLALEELVAGGPEAFRGFLKRERLPNFLSEDEVRAILRaaVVPKTISINGDDSELSQSASLdcSSVTYFPERSDI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  100 EAPNLDLGWPYVMPGLL-GGTHIDLLFHPPRAH-LLTIKETIRKMIKEARKVIALVMDIFTDVDIFKEIVEAST-RGVSV 176
Cdd:cd09184    88 EPPVLELGWPAFTTGSYrGVTRVEAHFQPSYGDcIYGCKEAARRQIRSAREVIALVMDSFTDLDIFRDLREACRkRRVPV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  177 YILLDESNFNHFLNMTEKQGCSVQRLRNIRVRTVKGQDYLSKTGAKFHGKMEQKFLLVDCQKVMYGSYSYMWSFEKAHLS 256
Cdd:cd09184   168 YILLDQSSVSHFLQMCKNLGVHLEQEKLMRVRTITGNTYYTRSGAKIIGKVHEKFMLIDGIKVATGSYSFTWTDGKLNSS 247

                         250       260
                  ....*....|....*....|....
gi 767939493  257 MVQIITGQLVESFDEEFRTLYARS 280
Cdd:cd09184   248 NLLILSGQVVEKFDLEFRILYAQS 271
PLDc_FAM83F_N cd09186
N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence ...
 23-280 6.91e-65

N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence similarity 83F; N-terminal phospholipase D (PLD)-like domain of the uncharacterized protein, Family with sequence similarity 83F (FAM83F). Since the N-terminal PLD-like domain of FAM83 proteins shows only trace similarity to the PLD catalytic domain and lacks the functionally important histidine residue, FAM83 proteins may share a similar three-dimensional fold with PLD enzymes, but are most unlikely to carry PLD activity. The N-terminus of FAM83F shows high homology to other FAM83 family members, indicating that FAM83F might have arisen early in vertebrate evolution by duplication of a gene in the FAM83 family.


Pssm-ID: 197282  Cd Length: 268  Bit Score: 219.77  E-value: 6.91e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493   23 HYKEWYRVAIDILIEHGLEAYQEFLVQERVSDFLAEEEINYILKNVQK----VAQSTAHGTDDSCDDTLSSGTYWPVESD 98
Cdd:cd09186     7 YYSEEQRAALEQLLRNGEGAYRERLKKERLKDFLSSQEIQALRETWQEydsdSDTCCSRSPHDTPEDSGVSLAYWPTMSD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493   99 VEAPNLDLGWP----YvmpglLGGTHIDLLFHPPRAHLLT-IKETIRKMIKEARKVIALVMDIFTDVDIFKEIVEA-STR 172
Cdd:cd09186    87 TEVPPLDLGWTdngfY-----RGVSRVSLFTHPPKEENSPhLKEVVRKMIQQAQKLIAVVMDLFTDLDIFQDIVDAaSKR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  173 GVSVYILLDESNFNHFLNMTEKQGCSVQRLRNIRVRTVKGQDYLSKTGaKFHGKMEQKFLLVDCQKVMYGSYSYMWSFEK 252
Cdd:cd09186   162 RVPVYIILDENGVKHFLEMCSRLQLSDFHIRNIRVRSVTGSGFYMSFG-KIPGTLCSKFLMVDGEKVATGSYSFTWSSSR 240

                         250       260
                  ....*....|....*....|....*...
gi 767939493  253 AHLSMVQIITGQLVESFDEEFRTLYARS 280
Cdd:cd09186   241 MDRNTLLVLTGQVVEFFDNEFRELYAIS 268
PLDc_FAM83G_N cd09187
N-terminal phospholipase D-like domain of the uncharacterized protein Family with sequence ...
 24-280 6.48e-63

N-terminal phospholipase D-like domain of the uncharacterized protein Family with sequence similarity 83G; N-terminal phospholipase D (PLD)-like domain of the uncharacterized protein, Family with sequence similarity 83G (FAM83G). Since the N-terminal PLD-like domain of FAM83 proteins shows only trace similarity to the PLD catalytic domain and lacks the functionally important histidine residue, FAM83 proteins may share a similar three-dimensional fold with PLD enzymes, but are most unlikely to carry PLD activity. The N-terminus of FAM83G shows high homology to other FAM83 family members, indicating that FAM83G might have arisen early in vertebrate evolution by duplication of a gene in the FAM83 family.


Pssm-ID: 197283  Cd Length: 275  Bit Score: 214.72  E-value: 6.48e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493   24 YKEWYRVAIDILIEHGLEAYQEFLVQERVSDFLAEEEINYILKNVQKVAQSTAH--------GTDDSCD---DTLSSGTY 92
Cdd:cd09187     8 YSEEQRLALEALIARGRDAFYEVLKDENIRDFLSELELKRILQRLEAYDPGSEHqrpegpgnLTPGSAEdeqDGAPSLEY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493   93 WPVESDVEAPNLDLGWPYVMpGLLGGTHIDLLFHPPRAHLLTIKETIRKMIKEARKVIALVMDIFTDVDIFKEIVEAS-T 171
Cdd:cd09187    88 WPDRSDRSIPQLDLGWPEAI-AYRGVTRATVYMQPPVEGQAHIKEVVRKMIAQAQKVIAVVMDMFTDVDIFRDLLDAGfK 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  172 RGVSVYILLDESNFNHFLNMTEKQGCSVQRLRNIRVRTVKGQDYLSKTGAKFHGKMEQKFLLVDCQKVMYGSYSYMWSFE 251
Cdd:cd09187   167 RKVPVYIILDETNVKYFLQMCERAQMHRGHLKNLRVRSCGGTEFFTRSATKFKGSLGQKFMFVDGDRAICGSYSFTWSAS 246

                         250       260
                  ....*....|....*....|....*....
gi 767939493  252 KAHLSMVQIITGQLVESFDEEFRTLYARS 280
Cdd:cd09187   247 RTDRNLITVLSGQVVETFDRQFQDLYLMS 275
PLDc_FAM83A_N cd09181
N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence ...
 24-280 3.49e-62

N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence similarity 83A; N-terminal phospholipase D (PLD)-like domain of the uncharacterized protein, Family with sequence similarity 83A (FAM83A), also known as tumor antigen BJ-TSA-9. FAM83A or BJ-TSA-9 is a novel tumor-specific gene highly expressed in human lung adenocarcinoma. Due to this specific expression pattern, it may serve as a biomarker for lung cancer, especially in the early detection of micrometastasis for lung adenocarcinoma patients. Since the N-terminal PLD-like domain of FAM83 proteins shows only trace similarity to the PLD catalytic domain and lacks the functionally important histidine residue, FAM83 proteins may share a similar three-dimensional fold with PLD enzymes, but are most unlikely to carry PLD activity.


Pssm-ID: 197278  Cd Length: 276  Bit Score: 212.76  E-value: 3.49e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493   24 YKEWYRVAIDILIEHGLEAYQEFLVQERVSDFLAEEEINYILKNVQK--VAQSTAHGTD----DSCDDTLSSGTYWPVES 97
Cdd:cd09181     8 HNESARLATDALLDGGLDEYHQVLRKEGEVDFLSSVEKQYIMENAREpsYGSDRTLSTSadqvGSSSPSLQSETYFPVAS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493   98 DVEAPNLDLGWPY--VMPGLLGGTHIDLLFHPPRAHllTIKETIRKMIKEARKVIALVMDIFTDVDIFKEIVEAST-RGV 174
Cdd:cd09181    88 ESSEPVLLHDWSSaeVKPYLKEKSSATVYFQTVKAS--NMRDLIRRCIRKTTQVLAIVMDVFTDVEIFCDLLEAANkRNV 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  175 SVYILLDESNFNHFLNMTEKQGCSVQRLRNIRVRTVKGQDYLSKTGAKFHGKMEQKFLLVDCQKVMYGSYSYMWSFEKAH 254
Cdd:cd09181   166 FVYLLLDHGNLSLFQEMCEKLQINDSHFKNISVRSVEGDTYCAKSGRKFTGQIREKFIISDWREVLSGSYSFTWLSGQVH 245

                         250       260
                  ....*....|....*....|....*.
gi 767939493  255 LSMVQIITGQLVESFDEEFRTLYARS 280
Cdd:cd09181   246 RNLLVKFKGSAVELFDEEFRHLYASS 271
PLDc_Nuc_like cd09116
Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6, and similar ...
 125-276 1.73e-19

Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6, and similar proteins; Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6 (PLD6, EC 3.1.4.4), and similar proteins. Nuc is an endonuclease from Salmonella typhimurium and the smallest known member of the PLD superfamily. It cleaves both single- and double-stranded DNA. PLD6 selectively hydrolyzes the terminal phosphodiester bond of phosphatidylcholine (PC), with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. PLD6 also catalyzes the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Both Nuc and PLD6 belong to the phospholipase D (PLD) superfamily. They contain a short conserved sequence motif, the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), which is essential for catalysis. PLDs utilize a two-step mechanism to cleave phosphodiester bonds: Upon substrate binding, the bond is first attacked by a histidine residue from one HKD motif to form a covalent phosphohistidine intermediate, which is then hydrolyzed by water with the aid of a second histidine residue from the other HKD motif in the opposite subunit. This subfamily also includes some uncharacterized hypothetical proteins, which have two HKD motifs in a single polypeptide chain.


Pssm-ID: 197215 [Multi-domain]  Cd Length: 138  Bit Score: 85.81  E-value: 1.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  125 FHPprAHLLTIKETIRKMIKEARKVIALVMDIFTDVDIFKEIVEASTRGVSVYILLDESNFNHFLNMTEkqgCSVQRLRN 204
Cdd:cd09116     2 FLP--RPQDNLERLIVALIANAKSSIDVAMYALTDPEIAEALKRAAKRGVRVRIILDKDSLADNLSITL---LALLSNLG 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767939493  205 IRVRTVKGQdylsktgakfhGKMEQKFLLVDCQKVMYGSYSYMWSFEKAHLSMVQIITG-QLVESFDEEFRTL 276
Cdd:cd09116    77 IPVRTDSGS-----------KLMHHKFIIIDGKIVITGSANWTKSGFHRNDENLLIIDDpKLAASFEEEFNRL 138
PLDc_Nuc cd09170
Catalytic domain of EDTA-resistant nuclease Nuc from Salmonella typhimurium and similar ...
 139-279 7.79e-11

Catalytic domain of EDTA-resistant nuclease Nuc from Salmonella typhimurium and similar proteins; Catalytic domain of an EDTA-resistant nuclease Nuc from Salmonella typhimurium and similar proteins. Nuc is an endonuclease cleaving both single- and double-stranded DNA. It is the smallest known member of the phospholipase D (PLD, EC 3.1.4.4) superfamily that includes a diverse group of proteins with various catalytic functions. Most members of this superfamily have two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) in a single polypeptide chain and both are required for catalytic activity. However, Nuc only has one copy of the HKD motif per subunit but form a functionally active homodimer (it is most likely also active in solution as a multimeric protein), which has a single active site at the dimer interface containing the HKD motifs from both subunits. Due to the lack of a distinct domain for DNA binding, Nuc cuts DNA non-specifically. It utilizes a two-step mechanism to cleave phosphodiester bonds: Upon substrate binding, the bond is first attacked by a histidine residue from one HKD motif to form a covalent phosphohistidine intermediate, which is then hydrolyzed by water with the aid of a second histidine residue from the other HKD motif in the opposite subunit.


Pssm-ID: 197267 [Multi-domain]  Cd Length: 142  Bit Score: 60.99  E-value: 7.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  139 IRKMIKEARKVIALVMDIFTDVDIFKEIVEASTRGVSVYILLDESNFNhflnmteKQGCSVQRLRN--IRVRTVKGqdyl 216
Cdd:cd09170    16 ILDVIDSARRSIDVAAYSFTSPPIARALIAAKKRGVDVRVVLDKSQAG-------GKYSALNYLANagIPVRIDDN---- 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767939493  217 sktgakfHGKMEQKFLLVDCQKVMYGSYSYMWSFEKAHLSMVQIITG--QLVESFDEEFRTLYAR 279
Cdd:cd09170    85 -------YAIMHNKVMVIDGKTVITGSFNFTASAEKRNAENLLVIRNppELAQQYLQEWQRRWAQ 142
PLDc_vPLD6_like cd09171
Catalytic domain of vertebrate phospholipase D6 and similar proteins; Catalytic domain of ...
 124-276 1.70e-10

Catalytic domain of vertebrate phospholipase D6 and similar proteins; Catalytic domain of vertebrate phospholipase D6 (PLD6, EC 3.1.4.4), a homolog of the EDTA-resistant nuclease Nuc from Salmonella typhimurium, and similar proteins. PLD6 can selectively hydrolyze the terminal phosphodiester bond of phosphatidylcholine (PC) with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. It also catalyzes the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. PLD6 belongs to the phospholipase D (PLD) superfamily. Its monomer contains a short conserved sequence motif, H-x-K-x(4)-D (where x represents any amino acid residue), termed the HKD motif, which is essential in catalysis. PLD6 is more closely related to the nuclease Nuc than to other vertebrate phospholipases, which have two copies of the HKD motif in a single polypeptide chain. Like Nuc, PLD6 may utilize a two-step mechanism to cleave phosphodiester bonds: Upon substrate binding, the bond is first attacked by a histidine residue from the HKD motif of one subunit to form a covalent phosphohistidine intermediate, which is then hydrolyzed by water with the aid of a second histidine residue from the other HKD motif in the opposite subunit.


Pssm-ID: 197268 [Multi-domain]  Cd Length: 136  Bit Score: 59.93  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  124 LFHPPRAHLLTIKETIRKmikeARKVIALVMDIFTDVDIFKEIVEASTRGVSVYILLDEsnfnhflNMTEKQGCSVQRLR 203
Cdd:cd09171     2 LFFPGETSLSKLLRYLLS----ARKSLDVCVFTITCDDLADAILDLHRRGVRVRIITDD-------DQMEDKGSDIGKLR 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767939493  204 N--IRVRTvkgqDYLSktgakFHgkMEQKFLLVDCQKVMYGSYSymWS---FEKAHLSMVQIITGQLVESFDEEFRTL 276
Cdd:cd09171    71 KagIPVRT----DLSS-----GH--MHHKFAVIDGKILITGSFN--WTrqaVTGNQENVLITNDPKLVKPFTEEFEKL 135
PLDc_Nuc_like_unchar2 cd09174
Putative catalytic domain of uncharacterized hypothetical proteins closely related to Nuc, , ...
 135-276 2.93e-10

Putative catalytic domain of uncharacterized hypothetical proteins closely related to Nuc, , an endonuclease from Salmonella typhimurium; Putative catalytic domain of uncharacterized hypothetical proteins, which show high sequence homology to the endonuclease from Salmonella typhimurium and vertebrate phospholipase D6. Nuc and PLD6 belong to the phospholipase D (PLD) superfamily. They contain a short conserved sequence motif, the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), which characterizes the PLD superfamily and is essential for catalysis. Nuc and PLD6 utilize a two-step mechanism to cleave phosphodiester bonds: Upon substrate binding, the bond is first attacked by a histidine residue from one HKD motif to form a covalent phosphohistidine intermediate, which is then hydrolyzed by water with the aid of a second histidine residue from the other HKD motif in the opposite subunit. However, proteins in this subfamily have two HKD motifs in a single polypeptide chain.


Pssm-ID: 197271 [Multi-domain]  Cd Length: 136  Bit Score: 59.25  E-value: 2.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  135 IKETIRKMIKEARKVIALVMDIFTDVDIFKEIVEASTRGVSVYILLDESNFNhflnmteKQGCSVQRLRNIRVRTVKGqd 214
Cdd:cd09174     8 IENRIIEEIKKAKFSIWIAVAWFTNKDIFNALKNKKKEGVNIQIIINDDDIN-------KKDVLILDEDSFEIYKLPG-- 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767939493  215 ylskTGAKFHGKMEQKFLLVDCQKVMYGSYSYMWSFEKAHLSMVQIITGQLVESFDEEFRTL 276
Cdd:cd09174    79 ----NGSRYGNLMHNKFCVIDFKTVITGSYNWTKNAEYNFENIIITDDRELAEQFAKEFIKL 136
PRK13912 PRK13912
nuclease NucT; Provisional
 136-277 6.21e-10

nuclease NucT; Provisional


Pssm-ID: 184389 [Multi-domain]  Cd Length: 177  Bit Score: 59.40  E-value: 6.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  136 KETIRKMIKEARKVIALVMDIFTDVDIFKEIVEASTRGVSVYILLDESNfNHflNMTEKQGCSVQRLRNIRVRTVKGqdy 215
Cdd:PRK13912   35 LNKLVSLISNARSSIKIAIYSFTHKDIAKALKSAAKRGVKISIIYDYES-NH--NNDQSTIGYLDKYPNIKVCLLKG--- 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767939493  216 LSKTGAKFHGKMEQKFLLVDCQKVMYGSYSymWSFekahlsmvqiitgqlvESFDEEFRTLY 277
Cdd:PRK13912  109 LKAKNGKYYGIMHQKVAIIDDKIVVLGSAN--WSK----------------NAFENNYEVLL 152
PLDc_2 pfam13091
PLD-like domain;
139-276 8.31e-10

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 57.69  E-value: 8.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493   139 IRKMIKEARKVIALVMDIF-TDVDIFKEIVEASTRGVSVYILLDESNFNHFLnMTEKQGCSVQRLRNIRVRTVKGQdyls 217
Cdd:pfam13091    1 LIDLINSAKKSIDIATYYFvPDREIIDALIAAAKRGVDVRIILDSNKDDAGG-PKKASLKELRSLLRAGVEIREYQ---- 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493   218 ktgaKFHGKMEQKFLLVDCQKVMYGSYSY-MWSFEKAHLSMVQIITGQLVESFDEEFRTL 276
Cdd:pfam13091   76 ----SFLRSMHAKFYIIDGKTVIVGSANLtRRALRLNLENNVVIKDPELAQELEKEFDRL 131
PLDc_vPLD3_4_5_like_1 cd09106
Putative catalytic domain, repeat 1, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 124-248 5.15e-08

Putative catalytic domain, repeat 1, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral envelope proteins K4 and p37, and similar proteins; Putative catalytic domain, repeat 1, of vertebrate phospholipases D, PLD3, PLD4, and PLD5 (EC 3.1.4.4), viral envelope proteins (vaccinia virus proteins K4 and p37), and similar proteins. Most family members contain two copies of the HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue), and have been classified into the phospholipase D (PLD) superfamily. Proteins in this subfamily are associated with Golgi membranes, altering their lipid content by the conversion of phospholipids into phosphatidic acid, which is thought to be involved in the regulation of lipid movement. ADP ribosylation factor (ARF), a small guanosine triphosphate binding protein, might be required activity. The vaccinia virus p37 protein, encoded by the F13L gene, is also associated with Golgi membranes and is required for the envelopment and spread of the extracellular enveloped virus (EEV). The vaccinia virus protein K4, encoded by the HindIII K4L gene, remains to be characterized. Sequence analysis indicates that the vaccinia virus proteins K4 and p37 might have evolved from one or more captured eukaryotic genes involved in cellular lipid metabolism. Up to date, no catalytic activity of PLD3 has been shown. Furthermore, due to the lack of functional important histidine and lysine residues in the HKD motif, mammalian PLD5 has been characterized as an inactive PLD. The poxvirus p37 proteins may also lack PLD enzymatic activity, since they contain only one partially conserved HKD motif (N-x-K-x(4)-D).


Pssm-ID: 197205 [Multi-domain]  Cd Length: 153  Bit Score: 53.02  E-value: 5.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  124 LFHPPRAHLLTIKETIRKMIKEARKVIALVM--------DIFTDV------DIFKEIVEASTRGVSVYILLDESNfnhfL 189
Cdd:cd09106     9 LTFLSSSSHLSTFEAWMELISSAKKSIDIASfywnlrgtDTNPDSsaqegeDIFNALLEAAKRGVKIRILQDKPS----K 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767939493  190 NMTEKQGCSVQRLRNIRVRTVkgqDYLSKTGAkfhGKMEQKFLLVDCQKVMYGSYSYMW 248
Cdd:cd09106    85 DKPDEDDLELAALGGAEVRSL---DFTKLIGG---GVLHTKFWIVDGKHFYLGSANLDW 137
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 137-252 4.87e-07

Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D (PLD) superfamily proteins. The PLD superfamily is composed of a large and diverse group of proteins including plant, mammalian and bacterial PLDs, bacterial cardiolipin (CL) synthases, bacterial phosphatidylserine synthases (PSS), eukaryotic phosphatidylglycerophosphate (PGP) synthase, eukaryotic tyrosyl-DNA phosphodiesterase 1 (Tdp1), and some bacterial endonucleases (Nuc and BfiI), among others. PLD enzymes hydrolyze phospholipid phosphodiester bonds to yield phosphatidic acid and a free polar head group. They can also catalyze the transphosphatidylation of phospholipids to acceptor alcohols. The majority of members in this superfamily contain a short conserved sequence motif (H-x-K-x(4)-D, where x represents any amino acid residue), called the HKD signature motif. There are varying expanded forms of this motif in different family members. Some members contain variant HKD motifs. Most PLD enzymes are monomeric proteins with two HKD motif-containing domains. Two HKD motifs from two domains form a single active site. Some PLD enzymes have only one copy of the HKD motif per subunit but form a functionally active dimer, which has a single active site at the dimer interface containing the two HKD motifs from both subunits. Different PLD enzymes may have evolved through domain fusion of a common catalytic core with separate substrate recognition domains. Despite their various catalytic functions and a very broad range of substrate specificities, the diverse group of PLD enzymes can bind to a phosphodiester moiety. Most of them are active as bi-lobed monomers or dimers, and may possess similar core structures for catalytic activity. They are generally thought to utilize a common two-step ping-pong catalytic mechanism, involving an enzyme-substrate intermediate, to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group.


Pssm-ID: 197200 [Multi-domain]  Cd Length: 119  Bit Score: 49.44  E-value: 4.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  137 ETIRKMIKEARKVIALVMDIF---TDVDIFKEIVEASTRGVSVYILLDESNFNHFLNMTekQGCSVQRLRNIRVRTVkgq 213
Cdd:cd00138     1 EALLELLKNAKESIFIATPNFsfnSADRLLKALLAAAERGVDVRLIIDKPPNAAGSLSA--ALLEALLRAGVNVRSY--- 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767939493  214 dylsKTGAKFHGKMEQKFLLVDCQKVMYGSYSYMWSFEK 252
Cdd:cd00138    76 ----VTPPHFFERLHAKVVVIDGEVAYVGSANLSTASAA 110
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 115-280 2.39e-04

Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and metabolism]; Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 441111 [Multi-domain]  Cd Length: 367  Bit Score: 44.55  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  115 LLGGTHIDLLFHPPRAhlltiKETIRKMIKEARKVIALVMDIFTD----VDIFKEIVEASTRGVSVYILLDE----SNFN 186
Cdd:COG1502    11 LVGGNRVTLLVDGDEA-----FAALLEAIEAARRSIDLEYYIFDDdevgRRLADALIAAARRGVKVRVLLDGigsrALNR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  187 HFLNMTEKQGCSVQRLRNIRVRTvkgqdylsktgAKFHGKMEQKFLLVDCQKVMYGSY----SYMWSFEKAHL---SMVq 259
Cdd:COG1502    86 DFLRRLRAAGVEVRLFNPVRLLF-----------RRLNGRNHRKIVVIDGRVAFVGGAnitdEYLGRDPGFGPwrdTHV- 153

                         170       180
                  ....*....|....*....|.
gi 767939493  260 IITGQLVESFDEEFRTLYARS 280
Cdd:COG1502   154 RIEGPAVADLQAVFAEDWNFA 174
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 113-280 2.52e-04

Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and metabolism]; Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 441111 [Multi-domain]  Cd Length: 367  Bit Score: 44.55  E-value: 2.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  113 PGLLGGTHIDLLFHPPRAHLLTIKETIRKMIKEARKVIALVM-DIFTDVDIFKEIVEASTRGVSVYILLDESNfNHFLnm 191
Cdd:COG1502   182 PEPAGDVRVQVVPSGPDSPRETIERALLAAIASARRRIYIETpYFVPDRSLLRALIAAARRGVDVRILLPAKS-DHPL-- 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  192 teKQGCS---VQRLRNIRVRTVKGQDylsktgakfhGKMEQKFLLVDCQKVMYGSY-----SYMWSFEkahlSMVQIITG 263
Cdd:COG1502   259 --VHWASrsyYEELLEAGVRIYEYEP----------GFLHAKVMVVDDEWALVGSAnldprSLRLNFE----VNLVIYDP 322

                         170
                  ....*....|....*..
gi 767939493  264 QLVESFDEEFRTLYARS 280
Cdd:COG1502   323 EFAAQLRARFEEDLAHS 339
PLDc_unchar1_1 cd09127
Putative catalytic domain, repeat 1, of uncharacterized phospholipase D-like proteins; ...
 143-243 4.89e-04

Putative catalytic domain, repeat 1, of uncharacterized phospholipase D-like proteins; Putative catalytic domain, repeat 1, of uncharacterized phospholipase D (PLD, EC 3.1.4.4)-like proteins. PLD enzymes hydrolyze phospholipid phosphodiester bonds to yield phosphatidic acid and a free polar head group. They can also catalyze transphosphatidylation of phospholipids to acceptor alcohols. Members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the PLD superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer.


Pssm-ID: 197225 [Multi-domain]  Cd Length: 141  Bit Score: 41.48  E-value: 4.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  143 IKEARKVIALVMDIFTDVDIFKEIVEASTRGVSVYILLDESNfNHFLNMTEKQgcsVQRLR--NIRVRTVKGQDYLSKTg 220
Cdd:cd09127    17 IASAKRSILLKMYEFTDPALEKALAAAAKRGVRVRVLLEGGP-VGGISRAEKL---LDYLNeaGVEVRWTNGTARYRYT- 91

                          90       100
                  ....*....|....*....|...
gi 767939493  221 akfHgkmeQKFLLVDCQKVMYGS 243
Cdd:cd09127    92 ---H----AKYIVVDDERALVLT 107
PLDc_unchar2_2 cd09130
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
 135-227 2.25e-03

Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; Putative catalytic domain, repeat 2, of uncharacterized phospholipase D (PLD, EC 3.1.4.4)-like proteins. PLD enzymes hydrolyze phospholipid phosphodiester bonds to yield phosphatidic acid and a free polar head group. They can also catalyze transphosphatidylation of phospholipids to acceptor alcohols. Members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the PLD superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer.


Pssm-ID: 197228 [Multi-domain]  Cd Length: 157  Bit Score: 39.92  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939493  135 IKETIRKMIKEARK--VIALVMDIFTDVDIFKEIVEASTRGVSVYILLDeSNFNHFLNmtEKQGC----SVQRLR----- 203
Cdd:cd09130     6 IGEALLKEINSARAgdKIWIGMFYLADRDVIKALIDAANRGVDVRLILD-PNKDAFGR--EKNGIpnrpVAAELMkktkg 82

                          90       100
                  ....*....|....*....|....
gi 767939493  204 NIRVRtvkgqdYLSKTGAKFHGKM 227
Cdd:cd09130    83 KIQIR------WYNTGGEQFHTKL 100
PLDc_like_TrmB_middle cd09124
Middle phospholipase D-like domain of the transcriptional regulator TrmB and similar proteins; ...
 134-183 6.73e-03

Middle phospholipase D-like domain of the transcriptional regulator TrmB and similar proteins; Middle phospholipase D (PLD)-like domain of the transcriptional regulator TrmB and similar proteins. TrmB acts as a bifunctional sugar-sensing transcriptional regulator which controls two operons encoding maltose/trehalose and maltodextrin ABC transporters of Pyrococcus fruiosus. It functions as a dimer. Full length TrmB includes an N-terminal DNA-binding domain, a C-terminal sugar-binding domain and middle region that has been named as a PLD-like domain. The middle domain displays homology to PLD enzymes, which contain one or two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) per chain. The HKD motif characterizes the PLD superfamily. Due to the lack of key residues related to PLD activity in the PLD-like domain, members of this subfamily are unlikely to carry PLD activity.


Pssm-ID: 197223 [Multi-domain]  Cd Length: 126  Bit Score: 37.69  E-value: 6.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767939493  134 TIKETIRKMIKEARKVIALVMDIFtDVDIFKE-IVEASTRGVSVYILLDES 183
Cdd:cd09124    10 NILAKIREMINSAKEEIYISLPSE-ELEELLEeLEKAAERGVKVVIIIFGD 59
 
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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