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Conserved domains on  [gi|298231207|ref|NP_001177143|]
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inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1 isoform 6 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
His_Phos_2 pfam00328
Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so ...
 390-906 1.31e-84

Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches.The smaller branch 2 contains predominantly eukaryotic proteins. The catalytic functions in members include phytase, glucose-1-phosphatase and multiple inositol polyphosphate phosphatase. The in vivo roles of the mammalian acid phosphatases in branch 2 are not fully understood, although activity against lysophosphatidic acid and tyrosine-phosphorylated proteins has been demonstrated.


:

Pssm-ID: 395259 [Multi-domain]  Cd Length: 356  Bit Score: 281.22  E-value: 1.31e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207   390 ELRCVIAIIRHGDRTPKQKMKMEVKHPRFFALFekhggyktgklklkrpeqlqevlditrlllaelekepggeieektgk 469
Cdd:pfam00328    1 ELEQVQVVSRHGDRTPTQKFKKSYESLIFKILS----------------------------------------------- 33

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207   470 leqLKSVLEMYGHFSGINRKVQLTYyphgvkasnegqdpqretlapslllVLKWGGeLTPAGRVQAEELGRAFRCMYPGG 549
Cdd:pfam00328   34 ---LAGSLEGKLSFPGDYRYFKLQY-------------------------TLGWGG-LTPSGRVQAENLGRYFRQRYVGG 84

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207   550 qgdyagfpgcgLLRLHStFRHDLKIYASDEGRVQMTAAAFAKGLLALEGEltpilvqmvksanmnglldSDGDSLSSCQH 629
Cdd:pfam00328   85 -----------LLRDGY-NAKDIYIRASSEGRVIASAQAFAEGLFGPEGE-------------------DVDKDLLDDSN 133

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207   630 RVKARLHHILQQDAPFGPEDYDQLAPTRSTSllnsmtiiQNPVKVCDQVFALIENLTHQIRERMQdprsvdlQLYHSETL 709
Cdd:pfam00328  134 VAKVTIDEDKKALANNLTAGYCSCPAFEWPL--------QLLKQVDEALDYYLPVFLEPIAKRLE-------QLCPGETN 198

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207   710 ELMLQRWSKLERDFRQKSGRyDISKIPDIYDCvkYDVQHNgslglqgtAELLRLSKALADvvipqeYGISREEKLEIAVG 789
Cdd:pfam00328  199 LTADDVWALLFLCFFETNKA-DLSPFCDLFTE--EDALHN--------EYLLDLEEYYGL------AGIGNELKKTIGGP 261

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207   790 FCLPLLRKILLDLQRTHEdesvnklhplysrgvLSPGRHVRTRLYFTSESHVHSLLSVFrygGLLDETQDAQWQRALDYL 869
Cdd:pfam00328  262 LLNELLARLTNDLVCTQE---------------ATFPLDAKLYLYFTHDTTIYSLLSAL---GLFDDLPPLSSLRVLDGY 323

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 298231207   870 SAISELNYMTQIVIMLYEDNTqdplSEERFHVELHFS 906
Cdd:pfam00328  324 SASGEVPYGARLVFELYECSS----EKDSRYVRLLLN 356
PPIP5K2_N pfam18086
Diphosphoinositol pentakisphosphate kinase 2 N-terminal domain; This is the N-terminal domain ...
 55-144 7.63e-57

Diphosphoinositol pentakisphosphate kinase 2 N-terminal domain; This is the N-terminal domain found in the Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2 (PPIP5K2), EC:2.7.4.24. Structure analysis of human PPIP5K2 indicate that this region forms alpha-beta-alpha domain.PPIP5K2 is one of the mammalian PPIP5K isoforms responsible for synthesis of diphosphoinositol polyphosphates (inositol pyrophosphates; PP-InsPs), regulatory molecules that function at the interface of cell signaling and organizmic homeostasis.


:

Pssm-ID: 465643  Cd Length: 90  Bit Score: 191.20  E-value: 7.63e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207    55 IIVGICAMTKKSKSKPMTQILERLCRFDYLTVVILGEDVILNEPVENWPSCHCLISFHSKGFPLDKAVAYSKLRNPFLIN 134
Cdd:pfam18086    1 IRIGVCAMDKKARSKPMREILNRLEEFGEFEIIIFGDKVILNEPVEEWPICDCLISFYSTGFPLEKAIEYAKLRKPFLIN 80

                           90
                   ....*....|
gi 298231207   135 DLAMQYYIQD 144
Cdd:pfam18086   81 DLEMQYLLLD 90
LysX super family cl43055
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 144-337 1.09e-05

Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis


The actual alignment was detected with superfamily member COG0189:

Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 48.78  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207  144 DRREVYRILQEEGIDLPRYAVLnRDPARPEEcnLIEGedqvevngavFPKPFVEKPVSaedhnvyiyypssaGGGSQRLF 223
Cdd:COG0189    96 DKLFTLQLLARAGIPVPPTLVT-RDPDDLRA--FLEE----------LGGPVVLKPLD--------------GSGGRGVF 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207  224 RkIGSRSSVYSPESSVRKTGS--YIYEEFMPT-DGTDVKVYTVGPDYAHAEARKSPALDGKVERDSEGKEIRYPvmLTAM 300
Cdd:COG0189   149 L-VEDEDALESILEALTELGSepVLVQEFIPEeDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVE--LTDE 225

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 298231207  301 EKLVARKVCVAFKQTVCGFDLLRANGHSFVCDVNGFS 337
Cdd:COG0189   226 ERELALRAAPALGLDFAGVDLIEDDDGPLVLEVNVTP 262
 
Name Accession Description Interval E-value
His_Phos_2 pfam00328
Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so ...
 390-906 1.31e-84

Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches.The smaller branch 2 contains predominantly eukaryotic proteins. The catalytic functions in members include phytase, glucose-1-phosphatase and multiple inositol polyphosphate phosphatase. The in vivo roles of the mammalian acid phosphatases in branch 2 are not fully understood, although activity against lysophosphatidic acid and tyrosine-phosphorylated proteins has been demonstrated.


Pssm-ID: 395259 [Multi-domain]  Cd Length: 356  Bit Score: 281.22  E-value: 1.31e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207   390 ELRCVIAIIRHGDRTPKQKMKMEVKHPRFFALFekhggyktgklklkrpeqlqevlditrlllaelekepggeieektgk 469
Cdd:pfam00328    1 ELEQVQVVSRHGDRTPTQKFKKSYESLIFKILS----------------------------------------------- 33

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207   470 leqLKSVLEMYGHFSGINRKVQLTYyphgvkasnegqdpqretlapslllVLKWGGeLTPAGRVQAEELGRAFRCMYPGG 549
Cdd:pfam00328   34 ---LAGSLEGKLSFPGDYRYFKLQY-------------------------TLGWGG-LTPSGRVQAENLGRYFRQRYVGG 84

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207   550 qgdyagfpgcgLLRLHStFRHDLKIYASDEGRVQMTAAAFAKGLLALEGEltpilvqmvksanmnglldSDGDSLSSCQH 629
Cdd:pfam00328   85 -----------LLRDGY-NAKDIYIRASSEGRVIASAQAFAEGLFGPEGE-------------------DVDKDLLDDSN 133

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207   630 RVKARLHHILQQDAPFGPEDYDQLAPTRSTSllnsmtiiQNPVKVCDQVFALIENLTHQIRERMQdprsvdlQLYHSETL 709
Cdd:pfam00328  134 VAKVTIDEDKKALANNLTAGYCSCPAFEWPL--------QLLKQVDEALDYYLPVFLEPIAKRLE-------QLCPGETN 198

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207   710 ELMLQRWSKLERDFRQKSGRyDISKIPDIYDCvkYDVQHNgslglqgtAELLRLSKALADvvipqeYGISREEKLEIAVG 789
Cdd:pfam00328  199 LTADDVWALLFLCFFETNKA-DLSPFCDLFTE--EDALHN--------EYLLDLEEYYGL------AGIGNELKKTIGGP 261

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207   790 FCLPLLRKILLDLQRTHEdesvnklhplysrgvLSPGRHVRTRLYFTSESHVHSLLSVFrygGLLDETQDAQWQRALDYL 869
Cdd:pfam00328  262 LLNELLARLTNDLVCTQE---------------ATFPLDAKLYLYFTHDTTIYSLLSAL---GLFDDLPPLSSLRVLDGY 323

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 298231207   870 SAISELNYMTQIVIMLYEDNTqdplSEERFHVELHFS 906
Cdd:pfam00328  324 SASGEVPYGARLVFELYECSS----EKDSRYVRLLLN 356
PPIP5K2_N pfam18086
Diphosphoinositol pentakisphosphate kinase 2 N-terminal domain; This is the N-terminal domain ...
 55-144 7.63e-57

Diphosphoinositol pentakisphosphate kinase 2 N-terminal domain; This is the N-terminal domain found in the Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2 (PPIP5K2), EC:2.7.4.24. Structure analysis of human PPIP5K2 indicate that this region forms alpha-beta-alpha domain.PPIP5K2 is one of the mammalian PPIP5K isoforms responsible for synthesis of diphosphoinositol polyphosphates (inositol pyrophosphates; PP-InsPs), regulatory molecules that function at the interface of cell signaling and organizmic homeostasis.


Pssm-ID: 465643  Cd Length: 90  Bit Score: 191.20  E-value: 7.63e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207    55 IIVGICAMTKKSKSKPMTQILERLCRFDYLTVVILGEDVILNEPVENWPSCHCLISFHSKGFPLDKAVAYSKLRNPFLIN 134
Cdd:pfam18086    1 IRIGVCAMDKKARSKPMREILNRLEEFGEFEIIIFGDKVILNEPVEEWPICDCLISFYSTGFPLEKAIEYAKLRKPFLIN 80

                           90
                   ....*....|
gi 298231207   135 DLAMQYYIQD 144
Cdd:pfam18086   81 DLEMQYLLLD 90
HP_HAP_like cd07061
Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His ...
 525-902 8.16e-22

Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His residue which is phosphorylated during the reaction; Catalytic domain of HAP (histidine acid phosphatases) and phytases (myo-inositol hexakisphosphate phosphohydrolases). The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. Functions in this subgroup include roles in metabolism, signaling, or regulation, for example Escherichia coli glucose-1-phosphatase functions to scavenge glucose from glucose-1-phosphate and the signaling molecules inositol 1,3,4,5,6-pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6) are in vivo substrates for eukaryotic multiple inositol polyphosphate phosphatase 1 (Minpp1). Phytases scavenge phosphate from extracellular sources and are added to animal feed while prostatic acid phosphatase (PAP) has been used for many years as a serum marker for prostate cancer. Recently PAP has been shown in mouse models to suppress pain by functioning as an ecto-5prime-nucleotidase. In vivo it dephosphorylates extracellular adenosine monophosphate (AMP) generating adenosine,and leading to the activation of A1-adenosine receptors in dorsal spinal cord.


Pssm-ID: 132717 [Multi-domain]  Cd Length: 242  Bit Score: 96.29  E-value: 8.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207  525 GELTPAGRVQAEELGRAFRCMYPGgqgdyagfpgcgLLRLHSTFRHDLKIYASDEGRVQMTAAAFAKGLLalegeltpil 604
Cdd:cd07061    17 GELTPFGRQQAFELGRYFRQRYGE------------LLLLHSYNRSDLYIRSSDSQRTLQSAQAFLAGLF---------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207  605 vqmvksanmnglldsdgdslsscqhrvkarlhhilqqdapfgPEDYDQLAPtrstsllnsmtiiqnpvkvcdqVFALIEN 684
Cdd:cd07061    75 ------------------------------------------PPDGWQPIA----------------------VHTIPEE 90

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207  685 lthqirermqdprsvdlqlyhsETLELMLQRWSKLERDFRQKSGrydiskipdiydcvkydvqhngslglqgtaellrls 764
Cdd:cd07061    91 ----------------------EDDVSNLFDLCAYETVAKGYSA------------------------------------ 112

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207  765 kALADVVIPQEY-GISREEKLEIAVGFCLpllrkiLLDLQRTHEDESVNKLHPLYSRGVLSPGRHVRTRLYFTSESHVHS 843
Cdd:cd07061   113 -PFCDLFTEEEWvKLEYLNDLKFYYGYGP------GNPLARAQGSPLLNELLARLTNGPSGSQTFPLDRKLYLYFSHDTT 185

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 298231207  844 LLSVFRYGGLLDETQDAQWqralDYLSAISELNYMTQIVIMLYE--DNTQDPLSEERFHVE 902
Cdd:cd07061   186 ILPLLTALGLFDFAEPLPP----DFLRGFSESDYPPFAARLVFElwRCPGDGESYVRVLVN 242
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 144-337 1.09e-05

Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 48.78  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207  144 DRREVYRILQEEGIDLPRYAVLnRDPARPEEcnLIEGedqvevngavFPKPFVEKPVSaedhnvyiyypssaGGGSQRLF 223
Cdd:COG0189    96 DKLFTLQLLARAGIPVPPTLVT-RDPDDLRA--FLEE----------LGGPVVLKPLD--------------GSGGRGVF 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207  224 RkIGSRSSVYSPESSVRKTGS--YIYEEFMPT-DGTDVKVYTVGPDYAHAEARKSPALDGKVERDSEGKEIRYPvmLTAM 300
Cdd:COG0189   149 L-VEDEDALESILEALTELGSepVLVQEFIPEeDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVE--LTDE 225

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 298231207  301 EKLVARKVCVAFKQTVCGFDLLRANGHSFVCDVNGFS 337
Cdd:COG0189   226 ERELALRAAPALGLDFAGVDLIEDDDGPLVLEVNVTP 262
 
Name Accession Description Interval E-value
His_Phos_2 pfam00328
Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so ...
 390-906 1.31e-84

Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches.The smaller branch 2 contains predominantly eukaryotic proteins. The catalytic functions in members include phytase, glucose-1-phosphatase and multiple inositol polyphosphate phosphatase. The in vivo roles of the mammalian acid phosphatases in branch 2 are not fully understood, although activity against lysophosphatidic acid and tyrosine-phosphorylated proteins has been demonstrated.


Pssm-ID: 395259 [Multi-domain]  Cd Length: 356  Bit Score: 281.22  E-value: 1.31e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207   390 ELRCVIAIIRHGDRTPKQKMKMEVKHPRFFALFekhggyktgklklkrpeqlqevlditrlllaelekepggeieektgk 469
Cdd:pfam00328    1 ELEQVQVVSRHGDRTPTQKFKKSYESLIFKILS----------------------------------------------- 33

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207   470 leqLKSVLEMYGHFSGINRKVQLTYyphgvkasnegqdpqretlapslllVLKWGGeLTPAGRVQAEELGRAFRCMYPGG 549
Cdd:pfam00328   34 ---LAGSLEGKLSFPGDYRYFKLQY-------------------------TLGWGG-LTPSGRVQAENLGRYFRQRYVGG 84

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207   550 qgdyagfpgcgLLRLHStFRHDLKIYASDEGRVQMTAAAFAKGLLALEGEltpilvqmvksanmnglldSDGDSLSSCQH 629
Cdd:pfam00328   85 -----------LLRDGY-NAKDIYIRASSEGRVIASAQAFAEGLFGPEGE-------------------DVDKDLLDDSN 133

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207   630 RVKARLHHILQQDAPFGPEDYDQLAPTRSTSllnsmtiiQNPVKVCDQVFALIENLTHQIRERMQdprsvdlQLYHSETL 709
Cdd:pfam00328  134 VAKVTIDEDKKALANNLTAGYCSCPAFEWPL--------QLLKQVDEALDYYLPVFLEPIAKRLE-------QLCPGETN 198

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207   710 ELMLQRWSKLERDFRQKSGRyDISKIPDIYDCvkYDVQHNgslglqgtAELLRLSKALADvvipqeYGISREEKLEIAVG 789
Cdd:pfam00328  199 LTADDVWALLFLCFFETNKA-DLSPFCDLFTE--EDALHN--------EYLLDLEEYYGL------AGIGNELKKTIGGP 261

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207   790 FCLPLLRKILLDLQRTHEdesvnklhplysrgvLSPGRHVRTRLYFTSESHVHSLLSVFrygGLLDETQDAQWQRALDYL 869
Cdd:pfam00328  262 LLNELLARLTNDLVCTQE---------------ATFPLDAKLYLYFTHDTTIYSLLSAL---GLFDDLPPLSSLRVLDGY 323

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 298231207   870 SAISELNYMTQIVIMLYEDNTqdplSEERFHVELHFS 906
Cdd:pfam00328  324 SASGEVPYGARLVFELYECSS----EKDSRYVRLLLN 356
PPIP5K2_N pfam18086
Diphosphoinositol pentakisphosphate kinase 2 N-terminal domain; This is the N-terminal domain ...
 55-144 7.63e-57

Diphosphoinositol pentakisphosphate kinase 2 N-terminal domain; This is the N-terminal domain found in the Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2 (PPIP5K2), EC:2.7.4.24. Structure analysis of human PPIP5K2 indicate that this region forms alpha-beta-alpha domain.PPIP5K2 is one of the mammalian PPIP5K isoforms responsible for synthesis of diphosphoinositol polyphosphates (inositol pyrophosphates; PP-InsPs), regulatory molecules that function at the interface of cell signaling and organizmic homeostasis.


Pssm-ID: 465643  Cd Length: 90  Bit Score: 191.20  E-value: 7.63e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207    55 IIVGICAMTKKSKSKPMTQILERLCRFDYLTVVILGEDVILNEPVENWPSCHCLISFHSKGFPLDKAVAYSKLRNPFLIN 134
Cdd:pfam18086    1 IRIGVCAMDKKARSKPMREILNRLEEFGEFEIIIFGDKVILNEPVEEWPICDCLISFYSTGFPLEKAIEYAKLRKPFLIN 80

                           90
                   ....*....|
gi 298231207   135 DLAMQYYIQD 144
Cdd:pfam18086   81 DLEMQYLLLD 90
HP_HAP_like cd07061
Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His ...
 525-902 8.16e-22

Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His residue which is phosphorylated during the reaction; Catalytic domain of HAP (histidine acid phosphatases) and phytases (myo-inositol hexakisphosphate phosphohydrolases). The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. Functions in this subgroup include roles in metabolism, signaling, or regulation, for example Escherichia coli glucose-1-phosphatase functions to scavenge glucose from glucose-1-phosphate and the signaling molecules inositol 1,3,4,5,6-pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6) are in vivo substrates for eukaryotic multiple inositol polyphosphate phosphatase 1 (Minpp1). Phytases scavenge phosphate from extracellular sources and are added to animal feed while prostatic acid phosphatase (PAP) has been used for many years as a serum marker for prostate cancer. Recently PAP has been shown in mouse models to suppress pain by functioning as an ecto-5prime-nucleotidase. In vivo it dephosphorylates extracellular adenosine monophosphate (AMP) generating adenosine,and leading to the activation of A1-adenosine receptors in dorsal spinal cord.


Pssm-ID: 132717 [Multi-domain]  Cd Length: 242  Bit Score: 96.29  E-value: 8.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207  525 GELTPAGRVQAEELGRAFRCMYPGgqgdyagfpgcgLLRLHSTFRHDLKIYASDEGRVQMTAAAFAKGLLalegeltpil 604
Cdd:cd07061    17 GELTPFGRQQAFELGRYFRQRYGE------------LLLLHSYNRSDLYIRSSDSQRTLQSAQAFLAGLF---------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207  605 vqmvksanmnglldsdgdslsscqhrvkarlhhilqqdapfgPEDYDQLAPtrstsllnsmtiiqnpvkvcdqVFALIEN 684
Cdd:cd07061    75 ------------------------------------------PPDGWQPIA----------------------VHTIPEE 90

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207  685 lthqirermqdprsvdlqlyhsETLELMLQRWSKLERDFRQKSGrydiskipdiydcvkydvqhngslglqgtaellrls 764
Cdd:cd07061    91 ----------------------EDDVSNLFDLCAYETVAKGYSA------------------------------------ 112

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207  765 kALADVVIPQEY-GISREEKLEIAVGFCLpllrkiLLDLQRTHEDESVNKLHPLYSRGVLSPGRHVRTRLYFTSESHVHS 843
Cdd:cd07061   113 -PFCDLFTEEEWvKLEYLNDLKFYYGYGP------GNPLARAQGSPLLNELLARLTNGPSGSQTFPLDRKLYLYFSHDTT 185

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 298231207  844 LLSVFRYGGLLDETQDAQWqralDYLSAISELNYMTQIVIMLYE--DNTQDPLSEERFHVE 902
Cdd:cd07061   186 ILPLLTALGLFDFAEPLPP----DFLRGFSESDYPPFAARLVFElwRCPGDGESYVRVLVN 242
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 523-593 1.17e-08

Histidine phosphatase domain found in a functionally diverse set of proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This set of proteins includes cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, histidine acid phosphatases, phytases, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system; phytases scavenge phosphate from extracellular sources. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG. Clinical applications include the use of prostatic acid phosphatase (PAP) as a serum marker for prostate cancer. Agricultural applications include the addition of phytases to animal feed.


Pssm-ID: 132716 [Multi-domain]  Cd Length: 153  Bit Score: 55.50  E-value: 1.17e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 298231207  523 WGGELTPAGRVQAEELGRAFRCMYPggqgdyagfpgcgllrlhstfrHDLKIYASDEGRVQMTAAAFAKGL 593
Cdd:cd07040    22 GDGPLTEKGRQQARELGKALRERYI----------------------KFDRIYSSPLKRAIQTAEIILEGL 70
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 144-337 1.09e-05

Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 48.78  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207  144 DRREVYRILQEEGIDLPRYAVLnRDPARPEEcnLIEGedqvevngavFPKPFVEKPVSaedhnvyiyypssaGGGSQRLF 223
Cdd:COG0189    96 DKLFTLQLLARAGIPVPPTLVT-RDPDDLRA--FLEE----------LGGPVVLKPLD--------------GSGGRGVF 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298231207  224 RkIGSRSSVYSPESSVRKTGS--YIYEEFMPT-DGTDVKVYTVGPDYAHAEARKSPALDGKVERDSEGKEIRYPvmLTAM 300
Cdd:COG0189   149 L-VEDEDALESILEALTELGSepVLVQEFIPEeDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVE--LTDE 225

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 298231207  301 EKLVARKVCVAFKQTVCGFDLLRANGHSFVCDVNGFS 337
Cdd:COG0189   226 ERELALRAAPALGLDFAGVDLIEDDDGPLVLEVNVTP 262
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 526-604 3.49e-03

Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Subgroup of the catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This subgroup contains cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example, F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG.


Pssm-ID: 132718 [Multi-domain]  Cd Length: 153  Bit Score: 39.61  E-value: 3.49e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 298231207  526 ELTPAGRVQAEELGRAfrcmypggqgdyagfpgcgLLRLHSTFRHdlkIYASDEGRVQMTAAAFAKGLLALEGELTPIL 604
Cdd:cd07067    25 PLTEKGREQARALGKR-------------------LKELGIKFDR---IYSSPLKRAIQTAEIILEELPGLPVEVDPRL 81
 
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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