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Conserved domains on  [gi|46255017|ref|NP_996889|]
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protein FAM83A isoform b [Homo sapiens]

Protein Classification

PLDc_FAM83A_N domain-containing protein( domain architecture ID 10173806)

PLDc_FAM83A_N domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLDc_FAM83A_N cd09181
N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence ...
24-298 0e+00

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: 537.48  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017  24 PARADFSDNESARLATDALLDGGSEAYWRVLSQEGEVDFLSSVEAQYIQAQAREPPCPPDTLGGAEAGPKGLDSSSLQSG 103
Cdd:cd09181   1 GHRLDLSHNESARLATDALLDGGLDEYHQVLRKEGEVDFLSSVEKQYIMENAREPSYGSDRTLSTSADQVGSSSPSLQSE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017 104 TYFPVASEGSEPALLHSWASAE-KPYLKEKSSATVYFQTVKHNNIRDLVRRCITRTSQVLVILMDVFTDVEIFCDILEAA 182
Cdd:cd09181  81 TYFPVASESSEPVLLHDWSSAEvKPYLKEKSSATVYFQTVKASNMRDLIRRCIRKTTQVLAIVMDVFTDVEIFCDLLEAA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017 183 NKRGVFVCVLLDQGGVKLFQEMCDKVQISDSHLKNISIRSVEGEIYCAKSGRKFAGQIREKFIISDWRFVLSGSYSFTWL 262
Cdd:cd09181 161 NKRNVFVYLLLDHGNLSLFQEMCEKLQINDSHFKNISVRSVEGDTYCAKSGRKFTGQIREKFIISDWREVLSGSYSFTWL 240
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 46255017 263 CGHVHRNILSKFTGQAVELFDEEFRHLYASSKPVMG 298
Cdd:cd09181 241 SGQVHRNLLVKFKGSAVELFDEEFRHLYASSKPVPG 276
 
Name Accession Description Interval E-value
PLDc_FAM83A_N cd09181
N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence ...
24-298 0e+00

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: 537.48  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017  24 PARADFSDNESARLATDALLDGGSEAYWRVLSQEGEVDFLSSVEAQYIQAQAREPPCPPDTLGGAEAGPKGLDSSSLQSG 103
Cdd:cd09181   1 GHRLDLSHNESARLATDALLDGGLDEYHQVLRKEGEVDFLSSVEKQYIMENAREPSYGSDRTLSTSADQVGSSSPSLQSE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017 104 TYFPVASEGSEPALLHSWASAE-KPYLKEKSSATVYFQTVKHNNIRDLVRRCITRTSQVLVILMDVFTDVEIFCDILEAA 182
Cdd:cd09181  81 TYFPVASESSEPVLLHDWSSAEvKPYLKEKSSATVYFQTVKASNMRDLIRRCIRKTTQVLAIVMDVFTDVEIFCDLLEAA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017 183 NKRGVFVCVLLDQGGVKLFQEMCDKVQISDSHLKNISIRSVEGEIYCAKSGRKFAGQIREKFIISDWRFVLSGSYSFTWL 262
Cdd:cd09181 161 NKRNVFVYLLLDHGNLSLFQEMCEKLQINDSHFKNISVRSVEGDTYCAKSGRKFTGQIREKFIISDWREVLSGSYSFTWL 240
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 46255017 263 CGHVHRNILSKFTGQAVELFDEEFRHLYASSKPVMG 298
Cdd:cd09181 241 SGQVHRNLLVKFKGSAVELFDEEFRHLYASSKPVPG 276
DUF1669 pfam07894
Protein of unknown function (DUF1669); This family is composed of sequences derived from ...
20-295 3.02e-149

Protein of unknown function (DUF1669); This family is composed of sequences derived from hypothetical eukaryotic proteins of unknown function. Some members of this family are annotated as being potential phospholipases but no literature was found to support this.


Pssm-ID: 429723  Cd Length: 276  Bit Score: 421.97  E-value: 3.02e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017    20 QWVRPARADFSDNESARLATDALLDGGSEAYWRVLSQEGEVDFLSSVEAQYIQAQAREPPCPPDTLGGAEAGPKGLDSSS 99
Cdd:pfam07894   2 WRVSESKPEFLYSEEQRLALEALLEGGEEAYYEFLKEEGERDFLSSLELQYILENAQKPASEEYEPGEEEEGAGSDDGDS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017   100 lQSGTYFPVASEGSEPALLHSWAsaEKPYLKEKSSATVYFQT--VKHNNIRDLVRRCITRTSQVLVILMDVFTDVEIFCD 177
Cdd:pfam07894  82 -SSGTYWPMQSDTEVPALDLGWP--DEPSYKGVTRVTVYFQPpkEGSPHIKEVVRRLIQQAQKVIAIVMDVFTDVDIFCD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017   178 ILEAANKRGVFVCVLLDQGGVKLFQEMCDKVQISDSHLKNISIRSVEGEIYCAKSGRKFAGQIREKFIISDWRFVLSGSY 257
Cdd:pfam07894 159 LLEAASKRGVPVYILLDERNLKHFLEMCEKLQVNLQHLKNMRVRSVTGVTYYSRSGKKFTGQLKEKFMLVDGEKVLSGSY 238
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 46255017   258 SFTWLCGHVHRNILSKFTGQAVELFDEEFRHLYASSKP 295
Cdd:pfam07894 239 SFTWSSSRLHRNLVTVLTGQVVETFDREFRELYAQSKP 276
 
Name Accession Description Interval E-value
PLDc_FAM83A_N cd09181
N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence ...
24-298 0e+00

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: 537.48  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017  24 PARADFSDNESARLATDALLDGGSEAYWRVLSQEGEVDFLSSVEAQYIQAQAREPPCPPDTLGGAEAGPKGLDSSSLQSG 103
Cdd:cd09181   1 GHRLDLSHNESARLATDALLDGGLDEYHQVLRKEGEVDFLSSVEKQYIMENAREPSYGSDRTLSTSADQVGSSSPSLQSE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017 104 TYFPVASEGSEPALLHSWASAE-KPYLKEKSSATVYFQTVKHNNIRDLVRRCITRTSQVLVILMDVFTDVEIFCDILEAA 182
Cdd:cd09181  81 TYFPVASESSEPVLLHDWSSAEvKPYLKEKSSATVYFQTVKASNMRDLIRRCIRKTTQVLAIVMDVFTDVEIFCDLLEAA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017 183 NKRGVFVCVLLDQGGVKLFQEMCDKVQISDSHLKNISIRSVEGEIYCAKSGRKFAGQIREKFIISDWRFVLSGSYSFTWL 262
Cdd:cd09181 161 NKRNVFVYLLLDHGNLSLFQEMCEKLQINDSHFKNISVRSVEGDTYCAKSGRKFTGQIREKFIISDWREVLSGSYSFTWL 240
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 46255017 263 CGHVHRNILSKFTGQAVELFDEEFRHLYASSKPVMG 298
Cdd:cd09181 241 SGQVHRNLLVKFKGSAVELFDEEFRHLYASSKPVPG 276
PLDc_FAM83_N cd09119
N-terminal phospholipase D-like domain of proteins from the Family with sequence similarity 83; ...
24-293 3.29e-155

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: 436.81  E-value: 3.29e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017  24 PARADFSDNESARLATDALLDGGSEAYWRVLSQEGEVDFLSSVEAQYIQAQAREPPCPPDTLGgAEAGPKGLDSSSLQSG 103
Cdd:cd09119   1 ESYPEFFYSESARLALEALLEGGPEAYYRVLSTEREADFLSPEEIQYILSAARPYPEKPEAPG-AAAGTQLSLSSELSSG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017 104 TYFPVASEGSEPALLHSWAsaEKPYLKEKSSATVYFQTVK--HNNIRDLVRRCITRTSQVLVILMDVFTDVEIFCDILEA 181
Cdd:cd09119  80 TYFPVNSDVEPPDLDLGWP--ETDAYRGVTRATVHFQPPKegAPNIKDLVRRMIQQAQKVIAVVMDVFTDVDIFCDLLEA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017 182 ANKRGVFVCVLLDQGGVKLFQEMCDKVQISDSHLKNISIRSVEGEIYCAKSGRKFAGQIREKFIISDWRFVLSGSYSFTW 261
Cdd:cd09119 158 ANKRGVAVYILLDQGNVKHFLEMCDKLQLSDEHLKNMRVRSVGGKTYCSRSGKKFKGQMKEKFLLVDGDRVVSGSYSFTW 237
                       250       260       270
                ....*....|....*....|....*....|..
gi 46255017 262 LCGHVHRNILSKFTGQAVELFDEEFRHLYASS 293
Cdd:cd09119 238 SDAKLHRSMLSVLTGQVVESFDEEFRILYAQS 269
DUF1669 pfam07894
Protein of unknown function (DUF1669); This family is composed of sequences derived from ...
20-295 3.02e-149

Protein of unknown function (DUF1669); This family is composed of sequences derived from hypothetical eukaryotic proteins of unknown function. Some members of this family are annotated as being potential phospholipases but no literature was found to support this.


Pssm-ID: 429723  Cd Length: 276  Bit Score: 421.97  E-value: 3.02e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017    20 QWVRPARADFSDNESARLATDALLDGGSEAYWRVLSQEGEVDFLSSVEAQYIQAQAREPPCPPDTLGGAEAGPKGLDSSS 99
Cdd:pfam07894   2 WRVSESKPEFLYSEEQRLALEALLEGGEEAYYEFLKEEGERDFLSSLELQYILENAQKPASEEYEPGEEEEGAGSDDGDS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017   100 lQSGTYFPVASEGSEPALLHSWAsaEKPYLKEKSSATVYFQT--VKHNNIRDLVRRCITRTSQVLVILMDVFTDVEIFCD 177
Cdd:pfam07894  82 -SSGTYWPMQSDTEVPALDLGWP--DEPSYKGVTRVTVYFQPpkEGSPHIKEVVRRLIQQAQKVIAIVMDVFTDVDIFCD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017   178 ILEAANKRGVFVCVLLDQGGVKLFQEMCDKVQISDSHLKNISIRSVEGEIYCAKSGRKFAGQIREKFIISDWRFVLSGSY 257
Cdd:pfam07894 159 LLEAASKRGVPVYILLDERNLKHFLEMCEKLQVNLQHLKNMRVRSVTGVTYYSRSGKKFTGQLKEKFMLVDGEKVLSGSY 238
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 46255017   258 SFTWLCGHVHRNILSKFTGQAVELFDEEFRHLYASSKP 295
Cdd:pfam07894 239 SFTWSSSRLHRNLVTVLTGQVVETFDREFRELYAQSKP 276
PLDc_FAM83C_N cd09183
N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence ...
29-293 6.15e-93

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: 279.04  E-value: 6.15e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017  29 FSDNESARLATDALLDGGSEAYWRVLSQEGEVDFLSSVEAQYIQAQAREPPCPPDTLGGAEAGPKGLDSSS----LQSGT 104
Cdd:cd09183   6 LNHNETARLATDALLERGEKAYLQVLQEEKELPFLSTLDIDYITNSVAINGKANHAIVSELDGTNDIDEDSlpseLTSGT 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017 105 YFPVASEGSEPALLHSWASAEKPYLKEKSSATVYFQTVKHNNIRDLVRRCITRTSQVLVILMDVFTDVEIFCDILEAANK 184
Cdd:cd09183  86 YFPMMSDFDPPDLELGWPEIPLATKASPTEAQIFFQRDKANNIKDLIRSLISMAKTVIAIVMDLFTDVDILCDLMEASNK 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017 185 RGVFVCVLLDQGGVKLFQEMCDKVQISDSHLKNISIRSVEGEIYCAKSGRKFAGQIREKFIISDWRFVLSGSYSFTWLCG 264
Cdd:cd09183 166 RRVPVYLLLDEENLGHFLEMCEKLDLNKTSLPNMRIRSVCGDTYCTKSGKKFTGQVLEKFLLIDCEQVVAGSYSFTWLSS 245
                       250       260
                ....*....|....*....|....*....
gi 46255017 265 HVHRNILSKFTGQAVELFDEEFRHLYASS 293
Cdd:cd09183 246 QVHSNLVTHFRGNIVEEFDREFRCLYADS 274
PLDc_FAM83B_N cd09182
N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence ...
33-293 6.09e-62

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: 199.29  E-value: 6.09e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017  33 ESARLATDALLDGGSEAYWRVLSQEGEVDFLSSVEAQYIQAQAREPPcppdtLGGAEAGPKGLDSSSlQSGTYFPVASEG 112
Cdd:cd09182  10 EWYRLAIDALIEGGLEAYQEFLRAERISDFLSEEEILYILENVEKPP-----QETDESEDKRTDDTA-SSGTYWPAESDV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017 113 SEPALLHSWasaekPYLKEKSSAT---VYFQTVKHN--NIRDLVRRCITRTSQVLVILMDVFTDVEIFCDILEAANkRGV 187
Cdd:cd09182  84 EAPNLDLGW-----PYVMLEAGGTsidLLFHPPRANtpTIKEVIRKQIQEARQVIAIAMDVFTDVDIFKEVVEAST-RGV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017 188 FVCVLLDQGGVKLFQEMCDKVQISDSHLKNISIRSVEGEIYCAKSGRKFAGQIREKFIISDWRFVLSGSYSFTWLCGHVH 267
Cdd:cd09182 158 AVYILLDHSHFASFLTMTEKQGIQIQRLRNIRVRTVKGQDYQCKSGAKFHGAMEQKFLLVDCQKVLYGSYSYMWSFEKIH 237
                       250       260
                ....*....|....*....|....*.
gi 46255017 268 RNILSKFTGQAVELFDEEFRHLYASS 293
Cdd:cd09182 238 LSMVQVITGQLVESYDEEFRTLYARS 263
PLDc_FAM83F_N cd09186
N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence ...
25-293 3.54e-58

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: 189.72  E-value: 3.54e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017  25 ARADFSDNESARLATDALLDGGSEAYWRVLSQEGEVDFLSSVEAQYIQAQAREPPCPPDTLGgAEAGPKGLDSSSLQSgT 104
Cdd:cd09186   2 AKAEFYYSEEQRAALEQLLRNGEGAYRERLKKERLKDFLSSQEIQALRETWQEYDSDSDTCC-SRSPHDTPEDSGVSL-A 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017 105 YFPVASEGSEPALLHSWASaeKPYLKEKSSATVYFQTVKHNN---IRDLVRRCITRTSQVLVILMDVFTDVEIFCDILEA 181
Cdd:cd09186  80 YWPTMSDTEVPPLDLGWTD--NGFYRGVSRVSLFTHPPKEENsphLKEVVRKMIQQAQKLIAVVMDLFTDLDIFQDIVDA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017 182 ANKRGVFVCVLLDQGGVKLFQEMCDKVQISDSHLKNISIRSVEGEIYCAKSGrKFAGQIREKFIISDWRFVLSGSYSFTW 261
Cdd:cd09186 158 ASKRRVPVYIILDENGVKHFLEMCSRLQLSDFHIRNIRVRSVTGSGFYMSFG-KIPGTLCSKFLMVDGEKVATGSYSFTW 236
                       250       260       270
                ....*....|....*....|....*....|..
gi 46255017 262 LCGHVHRNILSKFTGQAVELFDEEFRHLYASS 293
Cdd:cd09186 237 SSSRMDRNTLLVLTGQVVEFFDNEFRELYAIS 268
PLDc_FAM83G_N cd09187
N-terminal phospholipase D-like domain of the uncharacterized protein Family with sequence ...
25-293 1.93e-56

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: 185.45  E-value: 1.93e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017  25 ARADFSDNESARLATDALLDGGSEAYWRVLSQEGEVDFLSSVEAQYI--QAQAREPPC---PPDTLGGAEAGPKGLDSSS 99
Cdd:cd09187   2 SKAEFFYSEEQRLALEALIARGRDAFYEVLKDENIRDFLSELELKRIlqRLEAYDPGSehqRPEGPGNLTPGSAEDEQDG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017 100 LQSGTYFPVASEGSEPALLHSWAsaEKPYLKEKSSATVYFQ--TVKHNNIRDLVRRCITRTSQVLVILMDVFTDVEIFCD 177
Cdd:cd09187  82 APSLEYWPDRSDRSIPQLDLGWP--EAIAYRGVTRATVYMQppVEGQAHIKEVVRKMIAQAQKVIAVVMDMFTDVDIFRD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017 178 ILEAANKRGVFVCVLLDQGGVKLFQEMCDKVQISDSHLKNISIRSVEGEIYCAKSGRKFAGQIREKFIISDWRFVLSGSY 257
Cdd:cd09187 160 LLDAGFKRKVPVYIILDETNVKYFLQMCERAQMHRGHLKNLRVRSCGGTEFFTRSATKFKGSLGQKFMFVDGDRAICGSY 239
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 46255017 258 SFTWLCGHVHRNILSKFTGQAVELFDEEFRHLYASS 293
Cdd:cd09187 240 SFTWSASRTDRNLITVLSGQVVETFDRQFQDLYLMS 275
PLDc_FAM83D_N cd09184
N-terminal phospholipase D-like domain of the protein, Family with sequence similarity 83D; ...
32-293 3.66e-56

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: 184.69  E-value: 3.66e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017  32 NESARLATDALLDGGSEAYWRVLSQEGEVDFLSSVEAQYIQAQAREPPCPPDTLGGAEAGPKG-LDSSSlqsGTYFPVAS 110
Cdd:cd09184   9 NEAHRLALEELVAGGPEAFRGFLKRERLPNFLSEDEVRAILRAAVVPKTISINGDDSELSQSAsLDCSS---VTYFPERS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017 111 EGSEPALLHSWASAEKPYLKEKSSATVYFQTVKHNNI---RDLVRRCITRTSQVLVILMDVFTDVEIFCDILEAANKRGV 187
Cdd:cd09184  86 DIEPPVLELGWPAFTTGSYRGVTRVEAHFQPSYGDCIygcKEAARRQIRSAREVIALVMDSFTDLDIFRDLREACRKRRV 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017 188 FVCVLLDQGGVKLFQEMCDKVQISDSHLKNISIRSVEGEIYCAKSGRKFAGQIREKFIISDWRFVLSGSYSFTWLCGHVH 267
Cdd:cd09184 166 PVYILLDQSSVSHFLQMCKNLGVHLEQEKLMRVRTITGNTYYTRSGAKIIGKVHEKFMLIDGIKVATGSYSFTWTDGKLN 245
                       250       260
                ....*....|....*....|....*.
gi 46255017 268 RNILSKFTGQAVELFDEEFRHLYASS 293
Cdd:cd09184 246 SSNLLILSGQVVEKFDLEFRILYAQS 271
PLDc_FAM83H_N cd09188
N-terminal phospholipase D-like domain of the uncharacterized protein, Family with sequence ...
33-293 2.05e-55

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: 182.36  E-value: 2.05e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017  33 ESARLATDALLDGGSEAYWRVLSQEGEVDFLSSVEAQYIQAQAREPPCPPDTLGGAEAGPKGLDSSSlqsGTYFPVASEG 112
Cdd:cd09188  10 EYYRLAIDALAEDGIEGYERFLAEEGVPDFLCPSEVEHIKSTLQTPQYAGQEPEYLPYGDIDQDGSS---GTYWPMNSDL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017 113 SEPALLHSWASAekpYLKEKSSATVYFQTVKHNN--IRDLVRRCITRTSQVLVILMDVFTDVEIFCDILEAANKRgVFVC 190
Cdd:cd09188  87 AAPELDLGWPMQ---FGFQGTEVTTLVQPPPPDNpsIKEEARRMIRSAQQVIAVVMDIFTDVDILSELLEAAARR-VPVY 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017 191 VLLDQGGVKLFQEMCDKVQISDSHLKNISIRSVEGEIYCAKSGRKFAGQIREKFIISDWRFVLSGSYSFTWLCGHVHRNI 270
Cdd:cd09188 163 ILLDEMNAQLFLDMAAKCRVNLNYVEFLRVRTVSGPTYFCRTGKSFKGHVKEKFLLVDCRVVLSGNYSFMWSFEKIHRSI 242
                       250       260
                ....*....|....*....|...
gi 46255017 271 LSKFTGQAVELFDEEFRHLYASS 293
Cdd:cd09188 243 AHIFQGELVASFDEEFRILFAQS 265
PLDc_Nuc_like cd09116
Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6, and similar ...
145-289 1.08e-07

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: 50.37  E-value: 1.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017 145 NNIRDLVRRCITRTSQVLVILMDVFTDVEIFcDILEAANKRGVFVCVLLDQGGVKLFQEMCDKvqisdSHLKNISIRsve 224
Cdd:cd09116   8 DNLERLIVALIANAKSSIDVAMYALTDPEIA-EALKRAAKRGVRVRIILDKDSLADNLSITLL-----ALLSNLGIP--- 78
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46255017 225 geiYCAKSGRKFAGQireKFIISDWRFVLSGSYSFTWLCGHVHRNILSKFTG-QAVELFDEEFRHL 289
Cdd:cd09116  79 ---VRTDSGSKLMHH---KFIIIDGKIVITGSANWTKSGFHRNDENLLIIDDpKLAASFEEEFNRL 138
PLDc_Nuc_like_unchar2 cd09174
Putative catalytic domain of uncharacterized hypothetical proteins closely related to Nuc, , ...
137-289 4.40e-05

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: 42.69  E-value: 4.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017 137 VYFqtvkhNNIRDLVRRCITRTSQVLVILMDVFTDVEIFcDILEAANKRGVFVCVLLDQGGVKlfqemCDKVQI-SDSHL 215
Cdd:cd09174   3 VLF-----DDIENRIIEEIKKAKFSIWIAVAWFTNKDIF-NALKNKKKEGVNIQIIINDDDIN-----KKDVLIlDEDSF 71
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46255017 216 knisirsvegEIY-CAKSGRKFAGQIREKFIISDWRFVLSGSYSFTWLCGHVHRNILSKFTGQAVELFDEEFRHL 289
Cdd:cd09174  72 ----------EIYkLPGNGSRYGNLMHNKFCVIDFKTVITGSYNWTKNAEYNFENIIITDDRELAEQFAKEFIKL 136
PLDc_Nuc_like_unchar1_1 cd09172
Putative catalytic domain, repeat 1, of uncharacterized hypothetical proteins similar to Nuc, ...
147-265 1.96e-04

Putative catalytic domain, repeat 1, of uncharacterized hypothetical proteins similar to Nuc, an endonuclease from Salmonella typhimurium; Putative catalytic domain, repeat 1, 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: 197269 [Multi-domain]  Cd Length: 144  Bit Score: 41.19  E-value: 1.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017 147 IRDLVRRCITRTSQVLVILMDvFTDVEIFcDILEAANKRGVFVCVLLDQGGVKlfqemcdkvqiSDSHLKNISIRSVEGE 226
Cdd:cd09172  11 LLAFLDEARSAGSSIRLAIYE-LDDPEII-DALKAAKDRGVRVRIILDDSSVT-----------GDPTEESAAATLSKGP 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 46255017 227 IycAKSGRKFAGQI-REKFIISD----WRFVLSGSYSFTW--LCGH 265
Cdd:cd09172  78 G--ALVKRRHSSGLmHNKFLVVDrkdgPNRVLTGSTNFTTsgLYGQ 121
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
162-261 8.13e-03

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: 35.96  E-value: 8.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255017 162 LVILMDVF---TDVEIFCDILEAANkRGVFVCVLLDQGGVKLFQEMCDKVQisDSHLKNISIRSVegeiycaKSGRKFAG 238
Cdd:cd00138  14 IFIATPNFsfnSADRLLKALLAAAE-RGVDVRLIIDKPPNAAGSLSAALLE--ALLRAGVNVRSY-------VTPPHFFE 83
                        90       100
                ....*....|....*....|...
gi 46255017 239 QIREKFIISDWRFVLSGSYSFTW 261
Cdd:cd00138  84 RLHAKVVVIDGEVAYVGSANLST 106
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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