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Conserved domains on  [gi|1747199317|ref|NP_001361268|]
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cytosolic 5'-nucleotidase 3A isoform 6 [Homo sapiens]

Protein Classification

5'-nucleotidase( domain architecture ID 11576270)

5'-nucleotidase is a HAD (haloacid dehalogenase) family protein similar to cytosolic 5'-nucleotidases 3A and 3B, which are 7-methylguanosine phosphate-specific 5'-nucleotidases

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HAD_5NT cd07504
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to human cytosolic IIIA and IIIB; 5 ...
12-264 1.63e-175

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to human cytosolic IIIA and IIIB; 5'-nucleotidases dephosphorylate nucleoside 5prime-monophosphates. This family includes human 5'-nucleotidase, cytosolic IIIA (cN-IIIA, previously called cN-III; NT5C3A) the main pyrimidine 5'-nucleotidase in erythrocytes which dephosphorylates the pyrimidine nucleotides CMP, UMP, TMP, and the purine 7-methylguanosine monophosphate (m7GM), and possesses phosphotransferase activity. It also includes human 5'-nucleotidase, cytosolic IIIB (cN-IIIB; NT5C3B) which has a strong preference for m7GMP, dephosphorylates CMP and UMP and, with significantly lower efficiency, GMP and AMP, and can also act as a phosphotransferase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


:

Pssm-ID: 319807 [Multi-domain]  Cd Length: 273  Bit Score: 484.12  E-value: 1.63e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317  12 MIITDFDMTLSRFSYKGKRCPTCHNIIDNCKLVTDECRKKLLQLKEKYYAIEVDPVLTVEEKYPYMVEWYTKSHGLLVQQ 91
Cdd:cd07504    21 QIISDFDMTLSRFRYNGGRCPTCHNIFDNCKLLTEECRAKLVQLKEKYYPIEIDPHLTIEEKVPYMEEWWTKSHELLIEQ 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317  92 ALPKAKLKEIVAESDVMLKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVYHPNVKVVSNFMDFDETGVLKGFK 171
Cdd:cd07504   101 GFQKDAIDQIVAESDIALRDGYEEFFEKLQQHGIPVLIFSAGLGDIIEEVLRQAGVYHPNVKVVSNFMDFDDNGVLTGFK 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317 172 GELIHVFNKHDGALRNTEYFNQLKDNSNIILLGDSQGDLRMADGVANVEHILKIGYLNDRVDELLEKYMDSYDIVLVQDE 251
Cdd:cd07504   181 GPLIHVFNKNESALKNTDYFKQLKGRTNIILLGDSIGDLRMADGVPNVEHILKIGFLNDKVEELLEKYMDSYDIVLVNDE 260
                         250
                  ....*....|...
gi 1747199317 252 SLEVANSILQKIL 264
Cdd:cd07504   261 TLDVPNSILQKIL 273
 
Name Accession Description Interval E-value
HAD_5NT cd07504
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to human cytosolic IIIA and IIIB; 5 ...
12-264 1.63e-175

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to human cytosolic IIIA and IIIB; 5'-nucleotidases dephosphorylate nucleoside 5prime-monophosphates. This family includes human 5'-nucleotidase, cytosolic IIIA (cN-IIIA, previously called cN-III; NT5C3A) the main pyrimidine 5'-nucleotidase in erythrocytes which dephosphorylates the pyrimidine nucleotides CMP, UMP, TMP, and the purine 7-methylguanosine monophosphate (m7GM), and possesses phosphotransferase activity. It also includes human 5'-nucleotidase, cytosolic IIIB (cN-IIIB; NT5C3B) which has a strong preference for m7GMP, dephosphorylates CMP and UMP and, with significantly lower efficiency, GMP and AMP, and can also act as a phosphotransferase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319807 [Multi-domain]  Cd Length: 273  Bit Score: 484.12  E-value: 1.63e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317  12 MIITDFDMTLSRFSYKGKRCPTCHNIIDNCKLVTDECRKKLLQLKEKYYAIEVDPVLTVEEKYPYMVEWYTKSHGLLVQQ 91
Cdd:cd07504    21 QIISDFDMTLSRFRYNGGRCPTCHNIFDNCKLLTEECRAKLVQLKEKYYPIEIDPHLTIEEKVPYMEEWWTKSHELLIEQ 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317  92 ALPKAKLKEIVAESDVMLKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVYHPNVKVVSNFMDFDETGVLKGFK 171
Cdd:cd07504   101 GFQKDAIDQIVAESDIALRDGYEEFFEKLQQHGIPVLIFSAGLGDIIEEVLRQAGVYHPNVKVVSNFMDFDDNGVLTGFK 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317 172 GELIHVFNKHDGALRNTEYFNQLKDNSNIILLGDSQGDLRMADGVANVEHILKIGYLNDRVDELLEKYMDSYDIVLVQDE 251
Cdd:cd07504   181 GPLIHVFNKNESALKNTDYFKQLKGRTNIILLGDSIGDLRMADGVPNVEHILKIGFLNDKVEELLEKYMDSYDIVLVNDE 260
                         250
                  ....*....|...
gi 1747199317 252 SLEVANSILQKIL 264
Cdd:cd07504   261 TLDVPNSILQKIL 273
HAD-SF-IE TIGR01544
haloacid dehalogenase superfamily, subfamily IE hydrolase, TIGR01544; This model represents a ...
13-263 2.04e-157

haloacid dehalogenase superfamily, subfamily IE hydrolase, TIGR01544; This model represents a small group of metazoan sequences. The sequences from mouse are annotated as Pyrimidine 5'-nucleotidases, aparrently in reference to HSPC233, the human homolog. However, no such annotation can currently be found for this gene. This group of sequences was found during searches for members of the haloacid dehalogenase (HAD) superfamily. All of the conserved catalytic motifs are found. The placement of the variable domain between motifs 1 and 2 indicates membership in subfamily I of the superfamily, but these sequences are sufficiently different from any of the branches (IA, TIGR01493, TIGR01509, TIGR01549; IB, TIGR01488; IC, TIGR01494; ID, TIGR01658; IF TIGR01545) of that subfamily as to constitute a separate branch to now be called IE. Considering that the closest identifiable hit outside of the noise range is to a phosphoserine phosphatase, this group may be considered to be most closely allied to subfamily IB.


Pssm-ID: 273683 [Multi-domain]  Cd Length: 283  Bit Score: 438.90  E-value: 2.04e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317  13 IITDFDMTLSRFSYK-GKRCPTCHNIIDNCKLVTDECRKKLLQLKEKYYAIEVDPVLTVEEKYPYMVEWYTKSHGLLVQQ 91
Cdd:TIGR01544  31 IISDFDYTLSRFRTEdGGRVPTSHGIFDACQSLPEEFKAKTDKLKHKYYPIEIDPHLTIEEKVPYMIEWWTKSHELTVGF 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317  92 ALPKAKLKEIVAESDVMLKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVYHPNVKVVSNFMDFDETGVLKGFK 171
Cdd:TIGR01544 111 PFDKSEIDQIVSKSTHALKDGTEEFFADLQRHGIPTLIFSAGIGNSVESVLRQANVLHPNVKVVSNFLQFDEDGLLDGFQ 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317 172 GELIHVFNK-HDGALRNTEYFNQLKDNSNIILLGDSQGDLRMADGVANVEHILKIGYLNDRVDELLEKYMDSYDIVLVQD 250
Cdd:TIGR01544 191 QPLIHTFNKnETVLNETTEYFDLVHTRDNIILLGDSIGDADMASGVPASSHILKIGYLNDHVDANLKKYMDTYDIVLVDD 270
                         250
                  ....*....|...
gi 1747199317 251 ESLEVANSILQKI 263
Cdd:TIGR01544 271 QTLDVARTILSLI 283
UMPH-1 pfam05822
Pyrimidine 5'-nucleotidase (UMPH-1); This family consists of several eukaryotic pyrimidine 5 ...
19-264 8.84e-151

Pyrimidine 5'-nucleotidase (UMPH-1); This family consists of several eukaryotic pyrimidine 5'-nucleotidase proteins. P5'N-1, also known as uridine monophosphate hydrolase-1 (UMPH-1), is a member of a large functional group of enzymes, characterized by the ability to dephosphorylate nucleic acids. P5'N-1 catalyzes the dephosphorylation of pyrimidine nucleoside monophosphates to the corresponding nucleosides. Deficiencies in this proteins function can lead to several different disorders in humans.


Pssm-ID: 310424 [Multi-domain]  Cd Length: 246  Bit Score: 420.61  E-value: 8.84e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317  19 MTLSRFSYKGKRCPTCHNIIDNCKLVTDECRKKLLQLKEKYYAIEVDPVLTVEEKYPYMVEWYTKSHGLLVQQALPKAKL 98
Cdd:pfam05822   1 MTLSKFRVNGERCPSSHGIFDNCKSIPEECRKKLRELYHKYYPIEIDPHMPIEEKVPYMVEWWTKSHALLIGQGLQKEAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317  99 KEIVAESDVMLKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVYHPNVKVVSNFMDFDETGVLKGFKGELIHVF 178
Cdd:pfam05822  81 AEVVAESDIMLRDGTHEFFDDLQQLNVPVLIFSAGLGDVLEEVLRQANVMHPNVKVVSNFMDFDDDGVLNGFKGPLIHTF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317 179 NKHDGALRNTEYFNQLKDNSNIILLGDSQGDLRMADGVANVEHILKIGYLNDRVDELLEKYMDSYDIVLVQDESLEVANS 258
Cdd:pfam05822 161 NKNETVLDGTEYFDQLHTRDNIILLGDSLGDLGMADGVPSVEHILKIGFLNDKVEENLDKYMDAFDIVLVDDQTMDVPNA 240

                  ....*.
gi 1747199317 259 ILQKIL 264
Cdd:pfam05822 241 ILEMIL 246
 
Name Accession Description Interval E-value
HAD_5NT cd07504
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to human cytosolic IIIA and IIIB; 5 ...
12-264 1.63e-175

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to human cytosolic IIIA and IIIB; 5'-nucleotidases dephosphorylate nucleoside 5prime-monophosphates. This family includes human 5'-nucleotidase, cytosolic IIIA (cN-IIIA, previously called cN-III; NT5C3A) the main pyrimidine 5'-nucleotidase in erythrocytes which dephosphorylates the pyrimidine nucleotides CMP, UMP, TMP, and the purine 7-methylguanosine monophosphate (m7GM), and possesses phosphotransferase activity. It also includes human 5'-nucleotidase, cytosolic IIIB (cN-IIIB; NT5C3B) which has a strong preference for m7GMP, dephosphorylates CMP and UMP and, with significantly lower efficiency, GMP and AMP, and can also act as a phosphotransferase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319807 [Multi-domain]  Cd Length: 273  Bit Score: 484.12  E-value: 1.63e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317  12 MIITDFDMTLSRFSYKGKRCPTCHNIIDNCKLVTDECRKKLLQLKEKYYAIEVDPVLTVEEKYPYMVEWYTKSHGLLVQQ 91
Cdd:cd07504    21 QIISDFDMTLSRFRYNGGRCPTCHNIFDNCKLLTEECRAKLVQLKEKYYPIEIDPHLTIEEKVPYMEEWWTKSHELLIEQ 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317  92 ALPKAKLKEIVAESDVMLKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVYHPNVKVVSNFMDFDETGVLKGFK 171
Cdd:cd07504   101 GFQKDAIDQIVAESDIALRDGYEEFFEKLQQHGIPVLIFSAGLGDIIEEVLRQAGVYHPNVKVVSNFMDFDDNGVLTGFK 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317 172 GELIHVFNKHDGALRNTEYFNQLKDNSNIILLGDSQGDLRMADGVANVEHILKIGYLNDRVDELLEKYMDSYDIVLVQDE 251
Cdd:cd07504   181 GPLIHVFNKNESALKNTDYFKQLKGRTNIILLGDSIGDLRMADGVPNVEHILKIGFLNDKVEELLEKYMDSYDIVLVNDE 260
                         250
                  ....*....|...
gi 1747199317 252 SLEVANSILQKIL 264
Cdd:cd07504   261 TLDVPNSILQKIL 273
HAD-SF-IE TIGR01544
haloacid dehalogenase superfamily, subfamily IE hydrolase, TIGR01544; This model represents a ...
13-263 2.04e-157

haloacid dehalogenase superfamily, subfamily IE hydrolase, TIGR01544; This model represents a small group of metazoan sequences. The sequences from mouse are annotated as Pyrimidine 5'-nucleotidases, aparrently in reference to HSPC233, the human homolog. However, no such annotation can currently be found for this gene. This group of sequences was found during searches for members of the haloacid dehalogenase (HAD) superfamily. All of the conserved catalytic motifs are found. The placement of the variable domain between motifs 1 and 2 indicates membership in subfamily I of the superfamily, but these sequences are sufficiently different from any of the branches (IA, TIGR01493, TIGR01509, TIGR01549; IB, TIGR01488; IC, TIGR01494; ID, TIGR01658; IF TIGR01545) of that subfamily as to constitute a separate branch to now be called IE. Considering that the closest identifiable hit outside of the noise range is to a phosphoserine phosphatase, this group may be considered to be most closely allied to subfamily IB.


Pssm-ID: 273683 [Multi-domain]  Cd Length: 283  Bit Score: 438.90  E-value: 2.04e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317  13 IITDFDMTLSRFSYK-GKRCPTCHNIIDNCKLVTDECRKKLLQLKEKYYAIEVDPVLTVEEKYPYMVEWYTKSHGLLVQQ 91
Cdd:TIGR01544  31 IISDFDYTLSRFRTEdGGRVPTSHGIFDACQSLPEEFKAKTDKLKHKYYPIEIDPHLTIEEKVPYMIEWWTKSHELTVGF 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317  92 ALPKAKLKEIVAESDVMLKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVYHPNVKVVSNFMDFDETGVLKGFK 171
Cdd:TIGR01544 111 PFDKSEIDQIVSKSTHALKDGTEEFFADLQRHGIPTLIFSAGIGNSVESVLRQANVLHPNVKVVSNFLQFDEDGLLDGFQ 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317 172 GELIHVFNK-HDGALRNTEYFNQLKDNSNIILLGDSQGDLRMADGVANVEHILKIGYLNDRVDELLEKYMDSYDIVLVQD 250
Cdd:TIGR01544 191 QPLIHTFNKnETVLNETTEYFDLVHTRDNIILLGDSIGDADMASGVPASSHILKIGYLNDHVDANLKKYMDTYDIVLVDD 270
                         250
                  ....*....|...
gi 1747199317 251 ESLEVANSILQKI 263
Cdd:TIGR01544 271 QTLDVARTILSLI 283
UMPH-1 pfam05822
Pyrimidine 5'-nucleotidase (UMPH-1); This family consists of several eukaryotic pyrimidine 5 ...
19-264 8.84e-151

Pyrimidine 5'-nucleotidase (UMPH-1); This family consists of several eukaryotic pyrimidine 5'-nucleotidase proteins. P5'N-1, also known as uridine monophosphate hydrolase-1 (UMPH-1), is a member of a large functional group of enzymes, characterized by the ability to dephosphorylate nucleic acids. P5'N-1 catalyzes the dephosphorylation of pyrimidine nucleoside monophosphates to the corresponding nucleosides. Deficiencies in this proteins function can lead to several different disorders in humans.


Pssm-ID: 310424 [Multi-domain]  Cd Length: 246  Bit Score: 420.61  E-value: 8.84e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317  19 MTLSRFSYKGKRCPTCHNIIDNCKLVTDECRKKLLQLKEKYYAIEVDPVLTVEEKYPYMVEWYTKSHGLLVQQALPKAKL 98
Cdd:pfam05822   1 MTLSKFRVNGERCPSSHGIFDNCKSIPEECRKKLRELYHKYYPIEIDPHMPIEEKVPYMVEWWTKSHALLIGQGLQKEAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317  99 KEIVAESDVMLKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVYHPNVKVVSNFMDFDETGVLKGFKGELIHVF 178
Cdd:pfam05822  81 AEVVAESDIMLRDGTHEFFDDLQQLNVPVLIFSAGLGDVLEEVLRQANVMHPNVKVVSNFMDFDDDGVLNGFKGPLIHTF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317 179 NKHDGALRNTEYFNQLKDNSNIILLGDSQGDLRMADGVANVEHILKIGYLNDRVDELLEKYMDSYDIVLVQDESLEVANS 258
Cdd:pfam05822 161 NKNETVLDGTEYFDQLHTRDNIILLGDSLGDLGMADGVPSVEHILKIGFLNDKVEENLDKYMDAFDIVLVDDQTMDVPNA 240

                  ....*.
gi 1747199317 259 ILQKIL 264
Cdd:pfam05822 241 ILEMIL 246
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
90-213 1.02e-07

Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model represents a subfamily of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at a an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included. Subfamily IA includes the enzyme phosphoserine phosphatase (TIGR00338) as well as three hypothetical equivalogs. Many members of these hypothetical equivalogs have been annotated as PSPase-like or PSPase-family proteins. In particular, the hypothetical equivalog which appears to be most closely related to PSPase contains only Archaea (while TIGR00338 contains only eukaryotes and bacteria) of which some are annotated as PSPases. Although this is a reasonable conjecture, none of these sequences has sufficient evidence for this assignment. If such should be found, this model should be retired while the PSPase model should be broadened to include these sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273653 [Multi-domain]  Cd Length: 177  Bit Score: 50.43  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317  90 QQALPKAKLKEIVAESDVMLKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVyhpnVKVVSNFMDFDETGVLKG 169
Cdd:TIGR01488  55 LHRSRSEEVAKEFLARQVALRPGARELISWLKERGIDTVIVSGGFDFFVEPVAEKLGI----DDVFANRLEFDDNGLLTG 130
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1747199317 170 FKGELIHVFNKHDGaLRNTEYFNQLK-DNSNIILLGDSQGDLRMA 213
Cdd:TIGR01488 131 PIEGQVNPEGECKG-KVLKELLEESKiTLKKIIAVGDSVNDLPML 174
HAD_PSP_eu cd04309
phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human ...
95-210 1.58e-05

phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human PSP, EC 3.1.3.3, catalyzes the third and final of the L-serine biosynthesis pathway, the Mg2+-dependent hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, L-serine is a precursor for the biosynthesis of glycine. HPSP regulates the levels of glycine and D-serine (converted from L-serine), the putative co-agonists for the glycine site of the NMDA receptor in the brain. Plant 3-PSP catalyzes the conversion of 3-phosphoserine to serine in the last step of the plastidic pathway of serine biosynthesis. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319801 [Multi-domain]  Cd Length: 202  Bit Score: 44.58  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317  95 KAKLKEIVAESDVMLKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVyhPNVKVVSNFMDFDETGVLKGFkgEL 174
Cdd:cd04309    59 KEQVDEFLEEHPPRLTPGVEELVSRLKARGVEVYLISGGFRELIEPVASQLGI--PLENVFANRLLFDFNGEYAGF--DE 134
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1747199317 175 IHVFNKHDGALRNTEYFNQLKDNSNIILLGDSQGDL 210
Cdd:cd04309   135 TQPTSRSGGKAKVIEQLKEKHHYKRVIMIGDGATDL 170
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
114-213 9.47e-05

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 40.84  E-value: 9.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317 114 ENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVYHPNVKVVSNfmdfDETGVLKGFKGELIHVFNKhdgalrnteyfnQ 193
Cdd:cd01427    13 VELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGS----DGGGTPKPKPKPLLLLLLK------------L 76
                          90       100
                  ....*....|....*....|
gi 1747199317 194 LKDNSNIILLGDSQGDLRMA 213
Cdd:cd01427    77 GVDPEEVLFVGDSENDIEAA 96
HAD_Pase cd07524
phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like ...
91-239 9.81e-05

phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like superfamily; Bacillus subtilis recycles two toxic byproducts of polyamine metabolism, methylthioadenosine and methylthioribose, into methionine by a salvage pathway. The sixth reaction in this pathway is catalyzed by B. subtilis MtnX: the dephosphorylation of 2- hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HKMTP- 1-P) into 1,2-dihydroxy-3-keto-5-methylthiopentene. The hydrolysis of HK-MTP-1-P is a two-step mechanism involving the formation of a transiently phosphorylated aspartyl intermediate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319826 [Multi-domain]  Cd Length: 211  Bit Score: 42.32  E-value: 9.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747199317  91 QALPKAKLKEI--VAESDVMLKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVyhPNVKVVSNFMDFDetgvlk 168
Cdd:cd07524    53 ELLPSSLKDEIieFLEKTAKIRPGFKEFVAFCQEHGIPFIIVSGGMDFFIEPLLEGLVI--EKIAIYCNGSDFS------ 124
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1747199317 169 gfkGELIHVFNKHDGALRNTE------YFNQL-KDNSNIILLGDSQGDLRMAdgvANVEHILKIGYLNDRVDELLEKY 239
Cdd:cd07524   125 ---GEQIHIDWPHECDCTNGCgcckssIIRKYsKPRPFIIVIGDSVTDLEAA---KEADLVFARDGLILKCEEENLPY 196
 
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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