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Conserved domains on  [gi|1337351040|ref|WP_103243841|]
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MULTISPECIES: alkaline phosphatase family protein [Aeromonas]

Protein Classification

alkaline phosphatase family protein( domain architecture ID 11445914)

alkaline phosphatase family protein catalyzes the hydrolysis of phosphate monoesters or diesters, similar to ectonucleotide pyrophosphatases/phosphodiesterases (ENPPs), which hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates

CATH:  3.40.720.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
2-209 4.23e-39

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


:

Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 140.27  E-value: 4.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040   2 QHKVIVVLVDGLAAEV--AHCMGYLCGMveAERGLY-TTLSAALPSLSRPLYECILTGVPPVASGITHNGVTRLSQHDAI 78
Cdd:COG1524    23 AKKVVLILVDGLRADLleRAHAPNLAAL--AARGVYaRPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDPELGRVV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040  79 FHLARAAGKRTAAAA-------------------YHWVSelYNQSPWLAARDRFTHDEQLPiqhgcfYWDDAYPDSHLLM 139
Cdd:COG1524   101 NSLSWVEDGFGSNSLlpvptiferaraaglttaaVFWPS--FEGSGLIDAARPYPYDGRKP------LLGNPAADRWIAA 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1337351040 140 DGEWLRSQYDPDFLLIHPMGVDDAGHQFGLDSRQYRNQARRMDSLLADLLPQW----LAEGYQVVITSDHGMNN 209
Cdd:COG1524   173 AALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALkargLYEGTLVIVTADHGMVD 246
YejM super family cl34548
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
172-258 1.20e-04

Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG3083:

Pssm-ID: 442317 [Multi-domain]  Cd Length: 603  Bit Score: 43.36  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040 172 RQYRNQARRMDSLLADLLPQWLAEGYQ----VVITSDHGM------NNDLSHGGTLPEERT-VPLwlfgdafIERWPDGV 240
Cdd:COG3083   427 NRYRNAVHYVDSQIGRVLDTLEQRGLLentiVIITADHGEefnengQNYWGHNSNFSRYQLqVPL-------VIHWPGTP 499
                          90       100
                  ....*....|....*....|....*
gi 1337351040 241 AIAQTQLC-------ALMADLLGVS 258
Cdd:COG3083   500 PQVISKLTshldivpTLMQRLLGVQ 524
 
Name Accession Description Interval E-value
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
2-209 4.23e-39

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 140.27  E-value: 4.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040   2 QHKVIVVLVDGLAAEV--AHCMGYLCGMveAERGLY-TTLSAALPSLSRPLYECILTGVPPVASGITHNGVTRLSQHDAI 78
Cdd:COG1524    23 AKKVVLILVDGLRADLleRAHAPNLAAL--AARGVYaRPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDPELGRVV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040  79 FHLARAAGKRTAAAA-------------------YHWVSelYNQSPWLAARDRFTHDEQLPiqhgcfYWDDAYPDSHLLM 139
Cdd:COG1524   101 NSLSWVEDGFGSNSLlpvptiferaraaglttaaVFWPS--FEGSGLIDAARPYPYDGRKP------LLGNPAADRWIAA 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1337351040 140 DGEWLRSQYDPDFLLIHPMGVDDAGHQFGLDSRQYRNQARRMDSLLADLLPQW----LAEGYQVVITSDHGMNN 209
Cdd:COG1524   173 AALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALkargLYEGTLVIVTADHGMVD 246
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
3-256 3.43e-15

Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.


Pssm-ID: 293742 [Multi-domain]  Cd Length: 267  Bit Score: 73.39  E-value: 3.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040   3 HKVIVVLVDGLAAEVAHCMGYLCGMVE-AERGLYTT-LSAALPSLSRPLYECILTGVPPVASGITHNGVtrlsqhdaIFH 80
Cdd:cd16018     1 PPLIVISIDGFRWDYLDRAGLTPNLKRlAEEGVRAKyVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYF--------YDP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040  81 LARAAGKRTAAAAYHWvselYNQSP--WLAAR--------------DRFTHDEQLPIQHGCFYW---DDAYPDSHLLMDG 141
Cdd:cd16018    73 KTNEEFSDSDWVWDPW----WIGGEpiWVTAEkaglktasyfwpgsEVAIIGYNPTPIPLGGYWqpyNDSFPFEERVDTI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040 142 EWLRSQYDPDFLLIHPMGVDDAGHQFGLDSRQYRNQARRMDSLLADLL----PQWLAEGYQVVITSDHGMNNDLSHGG-- 215
Cdd:cd16018   149 LEWLDLERPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIealkERGLLDDTNIIVVSDHGMTDVGTHGYdn 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1337351040 216 TLPEERTVpLWLFGDAFIErwpdGVAIA---QTQLCALMADLLG 256
Cdd:cd16018   229 ELPDMRAI-FIARGPAFKK----GKKLGpfrNVDIYPLMCNLLG 267
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
5-243 8.23e-15

Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 73.22  E-value: 8.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040   5 VIVVLVDGLAAEVAHCMGYLCGMVE-AERGLY-TTLSAALPSLSRPLYECILTGVPPVASGITHNGV-TRLSQHDAIFHL 81
Cdd:pfam01663   1 LLVISLDGFRADYLDRFELTPNLAAlAKEGVSaPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFyDPKTGEYLVFVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040  82 ARaagkrtaaaayHWVSELYNQSPWL--AARDRFT----------HDEQLPIQHGCFYWDDAYPDSHLLMD-------GE 142
Cdd:pfam01663  81 SD-----------PEDPRWWQGEPIWdtAAKAGVRaaalfwpgseVDYSTYYGTPPRYLKDDYNNSVPFEDrvdtavlQT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040 143 WL------RSQYDPDFLLIHPMGVDDAGHQFGLDSRQYRNQARRMDSLLADLL----PQWLAEGYQVVITSDHGMnndls 212
Cdd:pfam01663 150 WLdlpfadVAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLealdERGLFEDTNVIVVSDHGM----- 224
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1337351040 213 hgGTLPEERTVPL-WLFGDAFIERWPDGVAIA 243
Cdd:pfam01663 225 --TPVSDDKVIFLnDYLREKGLLHLVDGGPVV 254
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
172-258 1.20e-04

Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];


Pssm-ID: 442317 [Multi-domain]  Cd Length: 603  Bit Score: 43.36  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040 172 RQYRNQARRMDSLLADLLPQWLAEGYQ----VVITSDHGM------NNDLSHGGTLPEERT-VPLwlfgdafIERWPDGV 240
Cdd:COG3083   427 NRYRNAVHYVDSQIGRVLDTLEQRGLLentiVIITADHGEefnengQNYWGHNSNFSRYQLqVPL-------VIHWPGTP 499
                          90       100
                  ....*....|....*....|....*
gi 1337351040 241 AIAQTQLC-------ALMADLLGVS 258
Cdd:COG3083   500 PQVISKLTshldivpTLMQRLLGVQ 524
 
Name Accession Description Interval E-value
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
2-209 4.23e-39

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 140.27  E-value: 4.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040   2 QHKVIVVLVDGLAAEV--AHCMGYLCGMveAERGLY-TTLSAALPSLSRPLYECILTGVPPVASGITHNGVTRLSQHDAI 78
Cdd:COG1524    23 AKKVVLILVDGLRADLleRAHAPNLAAL--AARGVYaRPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDPELGRVV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040  79 FHLARAAGKRTAAAA-------------------YHWVSelYNQSPWLAARDRFTHDEQLPiqhgcfYWDDAYPDSHLLM 139
Cdd:COG1524   101 NSLSWVEDGFGSNSLlpvptiferaraaglttaaVFWPS--FEGSGLIDAARPYPYDGRKP------LLGNPAADRWIAA 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1337351040 140 DGEWLRSQYDPDFLLIHPMGVDDAGHQFGLDSRQYRNQARRMDSLLADLLPQW----LAEGYQVVITSDHGMNN 209
Cdd:COG1524   173 AALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALkargLYEGTLVIVTADHGMVD 246
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
3-256 3.43e-15

Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.


Pssm-ID: 293742 [Multi-domain]  Cd Length: 267  Bit Score: 73.39  E-value: 3.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040   3 HKVIVVLVDGLAAEVAHCMGYLCGMVE-AERGLYTT-LSAALPSLSRPLYECILTGVPPVASGITHNGVtrlsqhdaIFH 80
Cdd:cd16018     1 PPLIVISIDGFRWDYLDRAGLTPNLKRlAEEGVRAKyVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYF--------YDP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040  81 LARAAGKRTAAAAYHWvselYNQSP--WLAAR--------------DRFTHDEQLPIQHGCFYW---DDAYPDSHLLMDG 141
Cdd:cd16018    73 KTNEEFSDSDWVWDPW----WIGGEpiWVTAEkaglktasyfwpgsEVAIIGYNPTPIPLGGYWqpyNDSFPFEERVDTI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040 142 EWLRSQYDPDFLLIHPMGVDDAGHQFGLDSRQYRNQARRMDSLLADLL----PQWLAEGYQVVITSDHGMNNDLSHGG-- 215
Cdd:cd16018   149 LEWLDLERPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIealkERGLLDDTNIIVVSDHGMTDVGTHGYdn 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1337351040 216 TLPEERTVpLWLFGDAFIErwpdGVAIA---QTQLCALMADLLG 256
Cdd:cd16018   229 ELPDMRAI-FIARGPAFKK----GKKLGpfrNVDIYPLMCNLLG 267
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
5-243 8.23e-15

Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 73.22  E-value: 8.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040   5 VIVVLVDGLAAEVAHCMGYLCGMVE-AERGLY-TTLSAALPSLSRPLYECILTGVPPVASGITHNGV-TRLSQHDAIFHL 81
Cdd:pfam01663   1 LLVISLDGFRADYLDRFELTPNLAAlAKEGVSaPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFyDPKTGEYLVFVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040  82 ARaagkrtaaaayHWVSELYNQSPWL--AARDRFT----------HDEQLPIQHGCFYWDDAYPDSHLLMD-------GE 142
Cdd:pfam01663  81 SD-----------PEDPRWWQGEPIWdtAAKAGVRaaalfwpgseVDYSTYYGTPPRYLKDDYNNSVPFEDrvdtavlQT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040 143 WL------RSQYDPDFLLIHPMGVDDAGHQFGLDSRQYRNQARRMDSLLADLL----PQWLAEGYQVVITSDHGMnndls 212
Cdd:pfam01663 150 WLdlpfadVAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLealdERGLFEDTNVIVVSDHGM----- 224
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1337351040 213 hgGTLPEERTVPL-WLFGDAFIERWPDGVAIA 243
Cdd:pfam01663 225 --TPVSDDKVIFLnDYLREKGLLHLVDGGPVV 254
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
152-267 6.83e-13

GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293744  Cd Length: 294  Bit Score: 67.23  E-value: 6.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040 152 FLLIHPMGVDDAGHQFGLDSRQYRNQARRMDSLLADLLPqwLAEGYQV------VITSDHGMNNDLSHGGTLPEERTVPL 225
Cdd:cd16020   159 VFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYP--LIEEYFNdgrtayIFTSDHGMTDWGSHGDGSPDETETPF 236
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1337351040 226 WLFGDAFI----ERWPDGVA-----------IAQTQLCALMADLLGVshdkpaAPPL 267
Cdd:cd16020   237 IAWGAGIKhptpGRGPSFSAnwgglrlprhdLDQADLAPLMSALLGL------PPPV 287
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
4-258 1.34e-12

GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293748 [Multi-domain]  Cd Length: 274  Bit Score: 66.05  E-value: 1.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040   4 KVIVVLVDGLAAEVAHC----MGYLCGMVEAERGLYTTLSAALPSLSRPLYECILTGVPP--------VASGITH--NGV 69
Cdd:cd16024     6 KLVFMVIDALRADFVFGpdsnMPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPsfldvvlnFASSLLEedNWL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040  70 TRLSQHDaifhlaraagkrtaaaayhWVSELYNQSPWLaaR---DRFTHDEQlpiqHGCFYWDDAYP-DS----HL---L 138
Cdd:cd16024    86 SQLKAAG-------------------KKIVFYGDDTWL--KlfpGSFTRSDG----TTSFFVSDFTEvDNnvtrHLdseL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040 139 MDGEWlrsqydpDFLLIHPMGVDDAGHQFGLDSRQYRNQARRMDSLLADLLPQWLAEGYQ----VVITSDHGMNNDLSHG 214
Cdd:cd16024   141 SRDDW-------DVLILHYLGLDHIGHLEGPKSPLMPPKLKEMDDVIKRIYESLEEQSSNnptlLVVCGDHGMTDAGNHG 213
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1337351040 215 GTLPEERTVPLWLFGDAF-IERWPDGVA------IAQTQLCALMADLLGVS 258
Cdd:cd16024   214 GSSPGETSVPLLFISPKFsSKPSNADGElsyyetVQQVDLAPTLALLLGLP 264
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
126-221 1.05e-11

GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293743 [Multi-domain]  Cd Length: 292  Bit Score: 63.92  E-value: 1.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040 126 FYWDDAYPDSHLLMDGEWLRSQYDPDFLLIHPMGVDDAGHQFGLDSRQ-YRNQARRMDSLLADLLPQwLAEGYQVVITSD 204
Cdd:cd16019   129 MHDVDPIFYNHINDNLDENIYYDNWDFIILHFLGLDHLGHKHNTTSSPeLEKKLDQMDNLIRDIYDR-MDNDTLLVVVSD 207
                          90
                  ....*....|....*..
gi 1337351040 205 HGMNNDLSHGGTLPEER 221
Cdd:cd16019   208 HGMNNDGNHGGSSTEET 224
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
144-228 1.22e-08

GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293747  Cd Length: 289  Bit Score: 54.87  E-value: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040 144 LRSQYDPDFLLIHPMGVDDAGHQFGLDSRQYRNQARRMDSLLADLLpQWLAEGYQVVITSDHGMNNDLSHGGTLPEERTV 223
Cdd:cd16023   154 LQSEDDWDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDII-ERLDDDTLLLVFGDHGMTETGDHGGDSDEEVDA 232

                  ....*
gi 1337351040 224 PLWLF 228
Cdd:cd16023   233 ALFAY 237
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
5-255 2.47e-08

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: 53.19  E-value: 2.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040   5 VIVVLVDGLAAEVAHCMGYLCGMV-----EAERGLYTTLSAALP-SLSRPLYECILTGVPPVASGITHNGVTRLSQHDAI 78
Cdd:cd00016     3 VVLIVLDGLGADDLGKAGNPAPTTpnlkrLASEGATFNFRSVSPpTSSAPNHAALLTGAYPTLHGYTGNGSADPELPSRA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040  79 FHLAraagkrtaaaaYHWVS--ELYNQspwlaARDRFthdeqlpiqhGCFYWDDAypdshllmdGEWLrSQYDPDFLLIH 156
Cdd:cd00016    83 AGKD-----------EDGPTipELLKQ-----AGYRT----------GVIGLLKA---------IDET-SKEKPFVLFLH 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040 157 PMGVDDAGHQFGLDSRQYRNQARRMDS----LLADLLPQWLAEGYQVVITSDHGMnNDLSHGGTLPE---------ERTV 223
Cdd:cd00016   127 FDGPDGPGHAYGPNTPEYYDAVEEIDErigkVLDALKKAGDADDTVIIVTADHGG-IDKGHGGDPKAdgkadkshtGMRV 205
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1337351040 224 PLWLFGDAFIERWPDGVAIAQTQLCALMADLL 255
Cdd:cd00016   206 PFIAYGPGVKKGGVKHELISQYDIAPTLADLL 237
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
172-258 1.20e-04

Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];


Pssm-ID: 442317 [Multi-domain]  Cd Length: 603  Bit Score: 43.36  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040 172 RQYRNQARRMDSLLADLLPQWLAEGYQ----VVITSDHGM------NNDLSHGGTLPEERT-VPLwlfgdafIERWPDGV 240
Cdd:COG3083   427 NRYRNAVHYVDSQIGRVLDTLEQRGLLentiVIITADHGEefnengQNYWGHNSNFSRYQLqVPL-------VIHWPGTP 499
                          90       100
                  ....*....|....*....|....*
gi 1337351040 241 AIAQTQLC-------ALMADLLGVS 258
Cdd:COG3083   500 PQVISKLTshldivpTLMQRLLGVQ 524
Sulfatase pfam00884
Sulfatase;
5-239 8.45e-04

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 40.10  E-value: 8.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040   5 VIVVLVDGLAAEVAHCMGYLCGMV-----EAERGLYTT---LSAALPSLSRPlyeCILTGVPPVASGITHNGVTRLSQH- 75
Cdd:pfam00884   3 VVLVLGESLRAPDLGLYGYPRPTTpfldrLAEEGLLFSnfySGGTLTAPSRF---ALLTGLPPHNFGSYVSTPVGLPRTe 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040  76 DAIFHLARAAGKRTAAAAYHWVSELYNQSP----------WLAARDRFTHDEQLPiqhgcFYWDDAYPDSHLLMDG--EW 143
Cdd:pfam00884  80 PSLPDLLKRAGYNTGAIGKWHLGWYNNQSPcnlgfdkffgRNTGSDLYADPPDVP-----YNCSGGGVSDEALLDEalEF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337351040 144 LRSQYDPDFLLIHPMGVDDAGH---------QFGLDSRQYRNQARR--------MDSLLADLLPQWLAEGYQ----VVIT 202
Cdd:pfam00884 155 LDNNDKPFFLVLHTLGSHGPPYypdrypekyATFKPSSCSEEQLLNsydntllyTDDAIGRVLDKLEENGLLdntlVVYT 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1337351040 203 SDHG-----MNNDL--SHGGTLPEERT-VPLwlfgdaFIeRWPDG 239
Cdd:pfam00884 235 SDHGeslgeGGGYLhgGKYDNAPEGGYrVPL------LI-WSPGG 272
PPM cd16009
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ...
163-216 7.08e-03

Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase superfamily members that interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribose 1-phosphate (ribose 1-phosphate). This reaction bridges glucose metabolism and RNA biosynthesis. PPM is a Mn(2+)-dependent enzyme and protein phosphorylation activates the enzyme.


Pssm-ID: 293733  Cd Length: 382  Bit Score: 37.43  E-value: 7.08e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1337351040 163 AGHQfgLDSRQYRNQARRMDSLLADLLPQwLAEGYQVVITSDHGmnNDLSHGGT 216
Cdd:cd16009   285 YGHR--RDPEGYAEALEEFDRRLPELLAK-LKEDDLLIITADHG--NDPTIGGT 333
 
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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