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Conserved domains on  [gi|19921912|ref|NP_610496|]
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alkaline phosphatase 6 [Drosophila melanogaster]

Protein Classification

alkaline phosphatase( domain architecture ID 10638771)

alkaline phosphatase is a zinc and magnesium dependent non-specific phosphomonoesterase that catalyzes the hydrolysis of phosphate monoesters at basic pH values

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
alkPPc smart00098
Alkaline phosphatase homologues;
73-512 1.94e-154

Alkaline phosphatase homologues;


:

Pssm-ID: 214515 [Multi-domain]  Cd Length: 419  Bit Score: 446.88  E-value: 1.94e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912     73 KNVILFLGDGMSVHTVTATRNLLGDSA------EQVYFEGFPYTGLSKTYCVNRQVADSACTATAYLGGVKANYGTIGVN 146
Cdd:smart00098   1 KNVILFIGDGMGVSTITAARILKGQAGgklgeeTLLAFDQFPTGALSKTYNPDYQVTDSAATATAYLCGVKTYNGAIGVD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912    147 ANVSRyscdgaaneedRVLSIAHWAQAAGKDAGLVTTARVTHASPAGVYAHIADRNWENDWEVANRECDPEQTiDIARQL 226
Cdd:smart00098  81 AATGK-----------EVPSVLEWAKKAGKSTGLVTTTRITHATPAATYAHVASRKWYNDADIPAEALENGCG-DIARQL 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912    227 VEQPVgqqlKVILGGGRKNFIDATVNDEEGYPGKRTDGRHLIRSWldQKkeanVSAKYVWSRKGLSLVDLENTDYLLGLF 306
Cdd:smart00098 149 INNRI----DVLLGGGRSYFAPTGTADPEGQRGTRRDGRNLIEEW--KA----AGYQYVWDRTELLAVGANKVDPLLGLF 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912    307 ANDHLPYNGDRDRKrsqlaDPSLSELTEAAITVLSRNDKGFFLFVEGARIDMAHHDTFAKRSLEDTAEFARAVQKARELT 386
Cdd:smart00098 219 ADGDMPYEIDRDST-----EPSLAEMTEVAIRLLSKNERGFFLMVEGGRIDHAHHENDACGALHETVDFDQAIQAALEFA 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912    387 S-EDDTLIVVTADHAHVMSINGYPYRDQEITGLA-QLADDNLPYTiLSYANGPGYYSGYNRAEgRALLKEKLVADSDYQY 464
Cdd:smart00098 294 KkEDETLVIVTADHSHVGTFGGYSLRGNDIFGLApSLDADRKPYT-LAYKNGPGYVVKDSNGI-RPNVTKAEIGSPEYRA 371
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 19921912    465 PTLAPLDAETHGGDDVAVYASGPYAQYFSGNYEQSNIPALMARAAGIG 512
Cdd:smart00098 372 QTAVPLDSETHTGEDVAVFAYGPHAHLFRGVQEQTYIAHVMAYALCLG 419
 
Name Accession Description Interval E-value
alkPPc smart00098
Alkaline phosphatase homologues;
73-512 1.94e-154

Alkaline phosphatase homologues;


Pssm-ID: 214515 [Multi-domain]  Cd Length: 419  Bit Score: 446.88  E-value: 1.94e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912     73 KNVILFLGDGMSVHTVTATRNLLGDSA------EQVYFEGFPYTGLSKTYCVNRQVADSACTATAYLGGVKANYGTIGVN 146
Cdd:smart00098   1 KNVILFIGDGMGVSTITAARILKGQAGgklgeeTLLAFDQFPTGALSKTYNPDYQVTDSAATATAYLCGVKTYNGAIGVD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912    147 ANVSRyscdgaaneedRVLSIAHWAQAAGKDAGLVTTARVTHASPAGVYAHIADRNWENDWEVANRECDPEQTiDIARQL 226
Cdd:smart00098  81 AATGK-----------EVPSVLEWAKKAGKSTGLVTTTRITHATPAATYAHVASRKWYNDADIPAEALENGCG-DIARQL 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912    227 VEQPVgqqlKVILGGGRKNFIDATVNDEEGYPGKRTDGRHLIRSWldQKkeanVSAKYVWSRKGLSLVDLENTDYLLGLF 306
Cdd:smart00098 149 INNRI----DVLLGGGRSYFAPTGTADPEGQRGTRRDGRNLIEEW--KA----AGYQYVWDRTELLAVGANKVDPLLGLF 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912    307 ANDHLPYNGDRDRKrsqlaDPSLSELTEAAITVLSRNDKGFFLFVEGARIDMAHHDTFAKRSLEDTAEFARAVQKARELT 386
Cdd:smart00098 219 ADGDMPYEIDRDST-----EPSLAEMTEVAIRLLSKNERGFFLMVEGGRIDHAHHENDACGALHETVDFDQAIQAALEFA 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912    387 S-EDDTLIVVTADHAHVMSINGYPYRDQEITGLA-QLADDNLPYTiLSYANGPGYYSGYNRAEgRALLKEKLVADSDYQY 464
Cdd:smart00098 294 KkEDETLVIVTADHSHVGTFGGYSLRGNDIFGLApSLDADRKPYT-LAYKNGPGYVVKDSNGI-RPNVTKAEIGSPEYRA 371
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 19921912    465 PTLAPLDAETHGGDDVAVYASGPYAQYFSGNYEQSNIPALMARAAGIG 512
Cdd:smart00098 372 QTAVPLDSETHTGEDVAVFAYGPHAHLFRGVQEQTYIAHVMAYALCLG 419
Alk_phosphatase pfam00245
Alkaline phosphatase;
72-511 4.64e-153

Alkaline phosphatase;


Pssm-ID: 395188  Cd Length: 418  Bit Score: 443.45  E-value: 4.64e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912    72 AKNVILFLGDGMSVHTVTATRNLLGD------SAEQVYFEGFPYTGLSKTYCVNRQVADSACTATAYLGGVKANYGTIGV 145
Cdd:pfam00245   1 AKNVIIFLGDGMGVSTVTAARILKGQkggkpgPETPLAFDRFPLVGLSKTYNVDKQVTDSAATATAYLCGVKTYNGAIGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912   146 NANvsryscdgaaneEDRVLSIAHWAQAAGKDAGLVTTARVTHASPAGVYAHIADRNWENDWEVANrECDPEQTIDIARQ 225
Cdd:pfam00245  81 DAA------------GKEVKSVLEAAKAAGKSTGLVTTTRIQHATPAGTYAHVVSRKWYSDAAMPA-SALQEGCKDIAEQ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912   226 LVEqpvGQQLKVILGGGRKNFIDATVNDEegypGKRTDGRHLIRSWLDQkkeanvSAKYVWSRKGLSLVDLEN-TDYLLG 304
Cdd:pfam00245 148 LIN---NMKIDVILGGGRKYFFPPEYPTD----GTRKDGRNLIEEWKHQ------GYQYVWNRKELLKNKDSNsVTYLLG 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912   305 LFANDHLPYNGDRDRKrsqlADPSLSELTEAAITVLSRNDKGFFLFVEGARIDMAHHDTFAKRSLEDTAEFARAVQKARE 384
Cdd:pfam00245 215 LFADGDMPYEIDRDEA----TDPSLKEMTEVAIRLLSKNPKGFFLMVEGGRIDHAHHDNDAYGALTETVDFDQAVKRALE 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912   385 LTS-EDDTLIVVTADHAHVMSINGYPYRDQEITGLAQ-LADDNLPYTILSYANGPGYYSGYNRAEGRALLKEKLVADSdY 462
Cdd:pfam00245 291 FAKkEKDTLVVVTADHSHVFSFGGYTTRGTSIWGLAPlLAAKRKPFTLILYGNGPGYKEEINGVRPNVTADESKGNDM-Y 369
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 19921912   463 QYPTLAPLDAETHGGDDVAVYASGPYAQYFSGNYEQSNIPALMARAAGI 511
Cdd:pfam00245 370 RTRSAVPWTSETHTGEDVAVFAYGPHAHLVHGLQEQTEIAHVMAKALCL 418
PhoA COG1785
Alkaline phosphatase [Inorganic ion transport and metabolism, General function prediction only] ...
57-513 4.95e-128

Alkaline phosphatase [Inorganic ion transport and metabolism, General function prediction only]; Alkaline phosphatase is part of the Pathway/BioSystem: Folate biosynthesis


Pssm-ID: 441391 [Multi-domain]  Cd Length: 401  Bit Score: 378.80  E-value: 4.95e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912  57 LLSKLAEQESATTNKAKNVILFLGDGMSVHTVTATRNLLGD--SAEQVYFEGFPYTGLSKTYCVNRQVADSACTATAYLG 134
Cdd:COG1785  14 AAAAAAVAAAAAAKKAKNVILFIGDGMGLSQITAARIYKGGpgEDGRLAFDQFPVTGLVTTYSADSLVTDSAAAATALAT 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912 135 GVKANYGTIGVNANvsryscdgaaneEDRVLSIAHWAQAAGKDAGLVTTARVTHASPAGVYAHIADRNWENDwevanrec 214
Cdd:COG1785  94 GVKTYNGAIGVDPD------------GKPLETILELAKAAGKATGIVTTARITHATPAAFYAHVPSRNNYDE-------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912 215 dpeqtidIARQLVEQPVgqqlKVILGGGRKNFidatvnDEEGYPGKRTDGRHLIRSWldqkKEANvsAKYVWSRKGLSLV 294
Cdd:COG1785 154 -------IAEQLLDSGV----DVILGGGRRYF------LPKGTGGKRKDGRDLIEEA----KAKG--YTVVTTKEELAAL 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912 295 DlENTDYLLGLFANDHLPYngDRDRKRSQLADPSLSELTEAAITVLSRNDKGFFLFVEGARIDMAHHDTFAKRSLEDTAE 374
Cdd:COG1785 211 D-AGGGKLLGLFADSHMPY--EIDRDNDFPDEPSLAEMTKKAIDVLSKNPKGFFLMVEGGRIDWAGHANDAAGAIEETLA 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912 375 FARAVQKARELTSED-DTLIVVTADHAHV-MSINGYPYrdQEITGLAQLADDNLPYTILSYAngpgyYSGYNRAegrall 452
Cdd:COG1785 288 FDKAVGVALDFAKKNpDTLVIVTADHETGgLTLGGPIL--DLVKNYKALDADGVKNGLGDLT-----YGKNQRA------ 354
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19921912 453 keklvadsdyqyptLAPLDAETHGGDDVAVYASGPYAQYFSGNYEQSNIPALMARAAGIGP 513
Cdd:COG1785 355 --------------GVGWTSGGHTGEDVPVYAYGPGAELFSGTIDNTDIFKKMAKALGLKL 401
ALP cd16012
Alkaline Phosphatase; Alkaline phosphatases are non-specific membrane-bound ...
73-510 4.97e-116

Alkaline Phosphatase; Alkaline phosphatases are non-specific membrane-bound phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Mammalian alkaline phosphatase is divided into four isozymes depending upon the site of tissue expression. They are Intestinal ALP, Placental ALP, Germ cell ALP and tissue nonspecific alkaline phosphatase or liver/bone/kidney (L/B/K) ALP.


Pssm-ID: 293736  Cd Length: 283  Bit Score: 343.64  E-value: 4.97e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912  73 KNVILFLGDGMSVHTVTATR----NLLGDSAEQVYFEGFPYTGLSKTYCVNRQVADSACTATAYLGGVKANYGTIGVNAN 148
Cdd:cd16012   1 KNVILFIGDGMGLAQVTAARiykgGKLGGKGTLLLMEDFPVVGLVKTYSADSLVTDSAAAATALATGVKTNNGAIGVDPD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912 149 VSRyscdgaaneedRVLSIAHWAQAAGKDAGLVTTARVTHASPAGVYAHIADRNWENdwevanrecdpeqtiDIARQLVE 228
Cdd:cd16012  81 GGK-----------PLETILEAAKEAGKATGIVTTTRITHATPAAFYAHVPSRDWED---------------DIAEQLLE 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912 229 QPVgqqlKVILGGGRKNFidatvndeegypgkrtdgrhlirswldqkkeanvsakyvwsrkglslvdlentdYLLGLFAN 308
Cdd:cd16012 135 SGI----DVILGGGRKYF------------------------------------------------------KLLGLFAD 156
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912 309 DHLPYNGDRDRKRsqlaDPSLSELTEAAITVLSRNDKGFFLFVEGARIDMAHHDTFAKRSLEDTAEFARAVQKARELTSE 388
Cdd:cd16012 157 SHLPYEIDRDETD----EPSLAEMTEKAIEVLSKNPKGFFLMVEGGRIDWAGHANDAARAIEETLAFDKAVKVALDFAKK 232
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912 389 D-DTLIVVTADHAHvmsingypyrdqeitglaqladdnlpytilsyangpgyysgynraegrallkeklvadsdyqyptl 467
Cdd:cd16012 233 DgDTLVIVTADHET------------------------------------------------------------------ 246
                       410       420       430       440
                ....*....|....*....|....*....|....*....|...
gi 19921912 468 apldaeTHGGDDVAVYASGPYAQYFSGNYEQSNIPALMARAAG 510
Cdd:cd16012 247 ------GHTGEDVPVFAYGPGAELFGGVYDNTDIFHKIAEALG 283
PRK10518 PRK10518
alkaline phosphatase; Provisional
62-511 1.51e-50

alkaline phosphatase; Provisional


Pssm-ID: 236706 [Multi-domain]  Cd Length: 476  Bit Score: 179.91  E-value: 1.51e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912   62 AEQESATTNKAKNVILFLGDGMSVHTVTATRNLLGDSAEqvYFEG---FPYTGLSKTYCVNRQ------VADSACTATAY 132
Cdd:PRK10518  59 ALRDSLSNKPAKNVILLIGDGMGDSEITAARNYAEGAGG--FFKGidaLPLTGQYTHYALNKKtgkpdyVTDSAASATAW 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912  133 LGGVKANYGTIGVNANvsryscdgaANEEDRVLSIAhwaQAAGKDAGLVTTARVTHASPAGVYAHiadrnwendweVANR 212
Cdd:PRK10518 137 STGVKTYNGALGVDIH---------GKDHPTLLELA---KAAGKATGNVSTAELQDATPAALVAH-----------VTSR 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912  213 EC-DPEQTID--------------IARQLVEQpvgqQLKVILGGGRKNFIDATVNDEegYPGKrtdgrhlirSWLDQKKE 277
Cdd:PRK10518 194 KCyGPEETSEkcpgnalenggrgsITEQLLNT----RADVTLGGGAKTFAETATAGE--WKGK---------TLREQAKA 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912  278 ANvsakYVWSR--KGLSLVDLENTDY-LLGLFANDHLP---------YNGDRDRK------RSQLAD--PSLSELTEAAI 337
Cdd:PRK10518 259 RG----YQLVEdaDSLNAVTEANQDKpLLGLFADGNMPvrwlgpkatYHGNLDKPpvtctpNPQRTAdvPTLAQMTDKAI 334
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912  338 TVLSRNDKGFFLFVEGARIDMAHHDTFAKRSLEDTAEFARAVQKARELTSED-DTLIVVTADHAHVMSINGypyRDQEIT 416
Cdd:PRK10518 335 DLLKKNEKGFFLQVEGASIDKQDHAANPCGQIGETVDLDEAVQKALEFARKDgNTLVIVTADHAHSSQIIA---PDAKAP 411
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912  417 GLAQL--ADDNLPYTIlSYANgpgyysgynraegrallkeklvadsdyqyptlAPLDAETHGGDDVAVYASGPYAQYFSG 494
Cdd:PRK10518 412 GLTQAlnTKDGAVMVV-SYGN--------------------------------SEEDSQEHTGTQLRIAAYGPHAANVVG 458
                        490
                 ....*....|....*..
gi 19921912  495 NYEQSNIPALMARAAGI 511
Cdd:PRK10518 459 LTDQTDLFYTMKDALGL 475
 
Name Accession Description Interval E-value
alkPPc smart00098
Alkaline phosphatase homologues;
73-512 1.94e-154

Alkaline phosphatase homologues;


Pssm-ID: 214515 [Multi-domain]  Cd Length: 419  Bit Score: 446.88  E-value: 1.94e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912     73 KNVILFLGDGMSVHTVTATRNLLGDSA------EQVYFEGFPYTGLSKTYCVNRQVADSACTATAYLGGVKANYGTIGVN 146
Cdd:smart00098   1 KNVILFIGDGMGVSTITAARILKGQAGgklgeeTLLAFDQFPTGALSKTYNPDYQVTDSAATATAYLCGVKTYNGAIGVD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912    147 ANVSRyscdgaaneedRVLSIAHWAQAAGKDAGLVTTARVTHASPAGVYAHIADRNWENDWEVANRECDPEQTiDIARQL 226
Cdd:smart00098  81 AATGK-----------EVPSVLEWAKKAGKSTGLVTTTRITHATPAATYAHVASRKWYNDADIPAEALENGCG-DIARQL 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912    227 VEQPVgqqlKVILGGGRKNFIDATVNDEEGYPGKRTDGRHLIRSWldQKkeanVSAKYVWSRKGLSLVDLENTDYLLGLF 306
Cdd:smart00098 149 INNRI----DVLLGGGRSYFAPTGTADPEGQRGTRRDGRNLIEEW--KA----AGYQYVWDRTELLAVGANKVDPLLGLF 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912    307 ANDHLPYNGDRDRKrsqlaDPSLSELTEAAITVLSRNDKGFFLFVEGARIDMAHHDTFAKRSLEDTAEFARAVQKARELT 386
Cdd:smart00098 219 ADGDMPYEIDRDST-----EPSLAEMTEVAIRLLSKNERGFFLMVEGGRIDHAHHENDACGALHETVDFDQAIQAALEFA 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912    387 S-EDDTLIVVTADHAHVMSINGYPYRDQEITGLA-QLADDNLPYTiLSYANGPGYYSGYNRAEgRALLKEKLVADSDYQY 464
Cdd:smart00098 294 KkEDETLVIVTADHSHVGTFGGYSLRGNDIFGLApSLDADRKPYT-LAYKNGPGYVVKDSNGI-RPNVTKAEIGSPEYRA 371
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 19921912    465 PTLAPLDAETHGGDDVAVYASGPYAQYFSGNYEQSNIPALMARAAGIG 512
Cdd:smart00098 372 QTAVPLDSETHTGEDVAVFAYGPHAHLFRGVQEQTYIAHVMAYALCLG 419
Alk_phosphatase pfam00245
Alkaline phosphatase;
72-511 4.64e-153

Alkaline phosphatase;


Pssm-ID: 395188  Cd Length: 418  Bit Score: 443.45  E-value: 4.64e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912    72 AKNVILFLGDGMSVHTVTATRNLLGD------SAEQVYFEGFPYTGLSKTYCVNRQVADSACTATAYLGGVKANYGTIGV 145
Cdd:pfam00245   1 AKNVIIFLGDGMGVSTVTAARILKGQkggkpgPETPLAFDRFPLVGLSKTYNVDKQVTDSAATATAYLCGVKTYNGAIGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912   146 NANvsryscdgaaneEDRVLSIAHWAQAAGKDAGLVTTARVTHASPAGVYAHIADRNWENDWEVANrECDPEQTIDIARQ 225
Cdd:pfam00245  81 DAA------------GKEVKSVLEAAKAAGKSTGLVTTTRIQHATPAGTYAHVVSRKWYSDAAMPA-SALQEGCKDIAEQ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912   226 LVEqpvGQQLKVILGGGRKNFIDATVNDEegypGKRTDGRHLIRSWLDQkkeanvSAKYVWSRKGLSLVDLEN-TDYLLG 304
Cdd:pfam00245 148 LIN---NMKIDVILGGGRKYFFPPEYPTD----GTRKDGRNLIEEWKHQ------GYQYVWNRKELLKNKDSNsVTYLLG 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912   305 LFANDHLPYNGDRDRKrsqlADPSLSELTEAAITVLSRNDKGFFLFVEGARIDMAHHDTFAKRSLEDTAEFARAVQKARE 384
Cdd:pfam00245 215 LFADGDMPYEIDRDEA----TDPSLKEMTEVAIRLLSKNPKGFFLMVEGGRIDHAHHDNDAYGALTETVDFDQAVKRALE 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912   385 LTS-EDDTLIVVTADHAHVMSINGYPYRDQEITGLAQ-LADDNLPYTILSYANGPGYYSGYNRAEGRALLKEKLVADSdY 462
Cdd:pfam00245 291 FAKkEKDTLVVVTADHSHVFSFGGYTTRGTSIWGLAPlLAAKRKPFTLILYGNGPGYKEEINGVRPNVTADESKGNDM-Y 369
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 19921912   463 QYPTLAPLDAETHGGDDVAVYASGPYAQYFSGNYEQSNIPALMARAAGI 511
Cdd:pfam00245 370 RTRSAVPWTSETHTGEDVAVFAYGPHAHLVHGLQEQTEIAHVMAKALCL 418
PhoA COG1785
Alkaline phosphatase [Inorganic ion transport and metabolism, General function prediction only] ...
57-513 4.95e-128

Alkaline phosphatase [Inorganic ion transport and metabolism, General function prediction only]; Alkaline phosphatase is part of the Pathway/BioSystem: Folate biosynthesis


Pssm-ID: 441391 [Multi-domain]  Cd Length: 401  Bit Score: 378.80  E-value: 4.95e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912  57 LLSKLAEQESATTNKAKNVILFLGDGMSVHTVTATRNLLGD--SAEQVYFEGFPYTGLSKTYCVNRQVADSACTATAYLG 134
Cdd:COG1785  14 AAAAAAVAAAAAAKKAKNVILFIGDGMGLSQITAARIYKGGpgEDGRLAFDQFPVTGLVTTYSADSLVTDSAAAATALAT 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912 135 GVKANYGTIGVNANvsryscdgaaneEDRVLSIAHWAQAAGKDAGLVTTARVTHASPAGVYAHIADRNWENDwevanrec 214
Cdd:COG1785  94 GVKTYNGAIGVDPD------------GKPLETILELAKAAGKATGIVTTARITHATPAAFYAHVPSRNNYDE-------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912 215 dpeqtidIARQLVEQPVgqqlKVILGGGRKNFidatvnDEEGYPGKRTDGRHLIRSWldqkKEANvsAKYVWSRKGLSLV 294
Cdd:COG1785 154 -------IAEQLLDSGV----DVILGGGRRYF------LPKGTGGKRKDGRDLIEEA----KAKG--YTVVTTKEELAAL 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912 295 DlENTDYLLGLFANDHLPYngDRDRKRSQLADPSLSELTEAAITVLSRNDKGFFLFVEGARIDMAHHDTFAKRSLEDTAE 374
Cdd:COG1785 211 D-AGGGKLLGLFADSHMPY--EIDRDNDFPDEPSLAEMTKKAIDVLSKNPKGFFLMVEGGRIDWAGHANDAAGAIEETLA 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912 375 FARAVQKARELTSED-DTLIVVTADHAHV-MSINGYPYrdQEITGLAQLADDNLPYTILSYAngpgyYSGYNRAegrall 452
Cdd:COG1785 288 FDKAVGVALDFAKKNpDTLVIVTADHETGgLTLGGPIL--DLVKNYKALDADGVKNGLGDLT-----YGKNQRA------ 354
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19921912 453 keklvadsdyqyptLAPLDAETHGGDDVAVYASGPYAQYFSGNYEQSNIPALMARAAGIGP 513
Cdd:COG1785 355 --------------GVGWTSGGHTGEDVPVYAYGPGAELFSGTIDNTDIFKKMAKALGLKL 401
ALP cd16012
Alkaline Phosphatase; Alkaline phosphatases are non-specific membrane-bound ...
73-510 4.97e-116

Alkaline Phosphatase; Alkaline phosphatases are non-specific membrane-bound phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Mammalian alkaline phosphatase is divided into four isozymes depending upon the site of tissue expression. They are Intestinal ALP, Placental ALP, Germ cell ALP and tissue nonspecific alkaline phosphatase or liver/bone/kidney (L/B/K) ALP.


Pssm-ID: 293736  Cd Length: 283  Bit Score: 343.64  E-value: 4.97e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912  73 KNVILFLGDGMSVHTVTATR----NLLGDSAEQVYFEGFPYTGLSKTYCVNRQVADSACTATAYLGGVKANYGTIGVNAN 148
Cdd:cd16012   1 KNVILFIGDGMGLAQVTAARiykgGKLGGKGTLLLMEDFPVVGLVKTYSADSLVTDSAAAATALATGVKTNNGAIGVDPD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912 149 VSRyscdgaaneedRVLSIAHWAQAAGKDAGLVTTARVTHASPAGVYAHIADRNWENdwevanrecdpeqtiDIARQLVE 228
Cdd:cd16012  81 GGK-----------PLETILEAAKEAGKATGIVTTTRITHATPAAFYAHVPSRDWED---------------DIAEQLLE 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912 229 QPVgqqlKVILGGGRKNFidatvndeegypgkrtdgrhlirswldqkkeanvsakyvwsrkglslvdlentdYLLGLFAN 308
Cdd:cd16012 135 SGI----DVILGGGRKYF------------------------------------------------------KLLGLFAD 156
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912 309 DHLPYNGDRDRKRsqlaDPSLSELTEAAITVLSRNDKGFFLFVEGARIDMAHHDTFAKRSLEDTAEFARAVQKARELTSE 388
Cdd:cd16012 157 SHLPYEIDRDETD----EPSLAEMTEKAIEVLSKNPKGFFLMVEGGRIDWAGHANDAARAIEETLAFDKAVKVALDFAKK 232
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912 389 D-DTLIVVTADHAHvmsingypyrdqeitglaqladdnlpytilsyangpgyysgynraegrallkeklvadsdyqyptl 467
Cdd:cd16012 233 DgDTLVIVTADHET------------------------------------------------------------------ 246
                       410       420       430       440
                ....*....|....*....|....*....|....*....|...
gi 19921912 468 apldaeTHGGDDVAVYASGPYAQYFSGNYEQSNIPALMARAAG 510
Cdd:cd16012 247 ------GHTGEDVPVFAYGPGAELFGGVYDNTDIFHKIAEALG 283
PRK10518 PRK10518
alkaline phosphatase; Provisional
62-511 1.51e-50

alkaline phosphatase; Provisional


Pssm-ID: 236706 [Multi-domain]  Cd Length: 476  Bit Score: 179.91  E-value: 1.51e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912   62 AEQESATTNKAKNVILFLGDGMSVHTVTATRNLLGDSAEqvYFEG---FPYTGLSKTYCVNRQ------VADSACTATAY 132
Cdd:PRK10518  59 ALRDSLSNKPAKNVILLIGDGMGDSEITAARNYAEGAGG--FFKGidaLPLTGQYTHYALNKKtgkpdyVTDSAASATAW 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912  133 LGGVKANYGTIGVNANvsryscdgaANEEDRVLSIAhwaQAAGKDAGLVTTARVTHASPAGVYAHiadrnwendweVANR 212
Cdd:PRK10518 137 STGVKTYNGALGVDIH---------GKDHPTLLELA---KAAGKATGNVSTAELQDATPAALVAH-----------VTSR 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912  213 EC-DPEQTID--------------IARQLVEQpvgqQLKVILGGGRKNFIDATVNDEegYPGKrtdgrhlirSWLDQKKE 277
Cdd:PRK10518 194 KCyGPEETSEkcpgnalenggrgsITEQLLNT----RADVTLGGGAKTFAETATAGE--WKGK---------TLREQAKA 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912  278 ANvsakYVWSR--KGLSLVDLENTDY-LLGLFANDHLP---------YNGDRDRK------RSQLAD--PSLSELTEAAI 337
Cdd:PRK10518 259 RG----YQLVEdaDSLNAVTEANQDKpLLGLFADGNMPvrwlgpkatYHGNLDKPpvtctpNPQRTAdvPTLAQMTDKAI 334
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912  338 TVLSRNDKGFFLFVEGARIDMAHHDTFAKRSLEDTAEFARAVQKARELTSED-DTLIVVTADHAHVMSINGypyRDQEIT 416
Cdd:PRK10518 335 DLLKKNEKGFFLQVEGASIDKQDHAANPCGQIGETVDLDEAVQKALEFARKDgNTLVIVTADHAHSSQIIA---PDAKAP 411
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912  417 GLAQL--ADDNLPYTIlSYANgpgyysgynraegrallkeklvadsdyqyptlAPLDAETHGGDDVAVYASGPYAQYFSG 494
Cdd:PRK10518 412 GLTQAlnTKDGAVMVV-SYGN--------------------------------SEEDSQEHTGTQLRIAAYGPHAANVVG 458
                        490
                 ....*....|....*..
gi 19921912  495 NYEQSNIPALMARAAGI 511
Cdd:PRK10518 459 LTDQTDLFYTMKDALGL 475
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
296-442 7.50e-06

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 47.54  E-value: 7.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912 296 LENTDYLLGLFAN--------------DHLPYNGDRDRKRSQLADPSLSELTEAAITVLSRNDKG--FFLFVEgarIDMA 359
Cdd:cd16148  83 LRKAGYYTAAVSSnphlfggpgfdrgfDTFEDFRGQEGDPGEEGDERAERVTDRALEWLDRNADDdpFFLFLH---YFDP 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912 360 HHD-------TFAkrsleDtAEFARAVQKARELTSEDDTLIVVTADHA------HVMSINGYPYRD-------------- 412
Cdd:cd16148 160 HEPylydaevRYV-----D-EQIGRLLDKLKELGLLEDTLVIVTSDHGeefgehGLYWGHGSNLYDeqlhvpliirwpgk 233
                       170       180       190
                ....*....|....*....|....*....|....*
gi 19921912 413 ---QEITGLAQLADdnLPYTILSYANG--PGYYSG 442
Cdd:cd16148 234 epgKRVDALVSHID--IAPTLLDLLGVepPDYSDG 266
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
342-409 8.59e-04

alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.


Pssm-ID: 293732 [Multi-domain]  Cd Length: 237  Bit Score: 40.87  E-value: 8.59e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19921912 342 RNDKGFFLFVEGARIDMAHHDTFAKR-----SLED-TAEFARAVQKARELTSEDDTLIVVTADHAHVMSINGYP 409
Cdd:cd00016 116 SKEKPFVLFLHFDGPDGPGHAYGPNTpeyydAVEEiDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGD 189
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
307-511 1.89e-03

c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 40.50  E-value: 1.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912 307 ANDHLPYNGDRDRKRSQLADpslSELTEAAITVLSRNDKGFFLFVEGArIDMAHHD-----TFAKRSLEDT-AEFARAVQ 380
Cdd:COG1524 148 AARPYPYDGRKPLLGNPAAD---RWIAAAALELLREGRPDLLLVYLPD-LDYAGHRygpdsPEYRAALREVdAALGRLLD 223
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912 381 KARELTSEDDTLIVVTADHAHVMSINGYPYRDQEITGLAQLADDNLPYTilsYANGPgyysgyNRAEGRALLKEK----- 455
Cdd:COG1524 224 ALKARGLYEGTLVIVTADHGMVDVPPDIDLNRLRLAGLLAVRAGESAHL---YLKDG------ADAEVRALLGLParvlt 294
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19921912 456 ----------------LVADSDYQYPTLAPLDAeTHGGD-----DVAVYASGPyaqYFSGNYEQSNIPALMARAAGI 511
Cdd:COG1524 295 reelaaghfgphrigdLVLVAKPGWALDAPLKG-SHGGLpdeemRVPLLASGP---GFRPGVRNVDVAPTIARLLGL 367
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
368-434 4.38e-03

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 39.51  E-value: 4.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921912 368 SLEDtAEFARAVQKARELTSEDDTLIVVTADH-----AHVMSINGYP-YRD-----------------QEITGLAQLADd 424
Cdd:cd16033 224 TLID-DAIGRILDALEELGLADDTLVIFTSDHgdalgAHRLWDKGPFmYEEtyripliikwpgviaagQVVDEFVSLLD- 301
                        90
                ....*....|
gi 19921912 425 nLPYTILSYA 434
Cdd:cd16033 302 -LAPTILDLA 310
 
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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