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Conserved domains on  [gi|446147024|ref|WP_000224879|]
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MULTISPECIES: purine-nucleoside phosphorylase [Enterobacteriaceae]

Protein Classification

purine-nucleoside phosphorylase( domain architecture ID 10012601)

purine-nucleoside phosphorylase catalyzes the phosphorolysis of purine nucleoside to form the corresponding free purine base and pentose-1-phosphate

EC:  2.4.2.1
Gene Ontology:  GO:0004731|GO:0009164|GO:0042278
PubMed:  24479338

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
2-236 8.69e-175

DeoD-type purine-nucleoside phosphorylase;


:

Pssm-ID: 180275  Cd Length: 235  Bit Score: 479.74  E-value: 8.69e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024   2 ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDF 81
Cdd:PRK05819   1 MTPHINAKKGDIADTVLMPGDPLRAKYIAETFLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELITDY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  82 GVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGVDARVGNLFSADLFY 161
Cdd:PRK05819  81 GVKKLIRVGSCGALQEDVKVRDVVIAMGASTDSNVNRIRFKGHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLFY 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446147024 162 SPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLG 236
Cdd:PRK05819 161 NPDPEMFDVLEKYGVLGVEMEAAALYGLAAKYGVKALTILTVSDHIVTGEATTAEERQTTFNDMIEIALESAILG 235
 
Name Accession Description Interval E-value
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
2-236 8.69e-175

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 479.74  E-value: 8.69e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024   2 ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDF 81
Cdd:PRK05819   1 MTPHINAKKGDIADTVLMPGDPLRAKYIAETFLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELITDY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  82 GVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGVDARVGNLFSADLFY 161
Cdd:PRK05819  81 GVKKLIRVGSCGALQEDVKVRDVVIAMGASTDSNVNRIRFKGHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLFY 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446147024 162 SPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLG 236
Cdd:PRK05819 161 NPDPEMFDVLEKYGVLGVEMEAAALYGLAAKYGVKALTILTVSDHIVTGEATTAEERQTTFNDMIEIALESAILG 235
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 1-236 6.13e-168

Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside phosphorylase is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 440575  Cd Length: 236  Bit Score: 462.28  E-value: 6.13e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024   1 MATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITD 80
Cdd:COG0813    1 MMTPHIGAKKGDIAETVLLPGDPLRAKYIAETFLEDAVLVNEVRGMLGYTGTYKGKRVSVMGSGMGIPSISIYAYELITE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  81 FGVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGVDARVGNLFSADLF 160
Cdd:COG0813   81 YGVKNIIRVGTCGALQEDVKVRDVVIAMGASTDSNVNRQRFGGGDFAPIADFELLRKAVEAAKELGIKVHVGNVFSSDLF 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446147024 161 YSPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLG 236
Cdd:COG0813  161 YREDPDLLEKLAKYGVLAVEMEAAALYTLAAKYGKRALAILTVSDHLVTGEETTAEERQTTFNDMMEIALEAALKL 236
deoD TIGR00107
purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called ...
 5-236 9.88e-160

purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called inosine phosphorylase) is a purine salvage enzyme. Purine nucleosides, such as guanosine, inosine, or xanthosine, plus orthophosphate, can be converted to their respective purine bases (guanine, hypoxanthine, or xanthine) plus ribose-1-phosphate. This family of purine nucleoside phosphorylase is restricted to the bacteria. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 188024  Cd Length: 232  Bit Score: 441.52  E-value: 9.88e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024    5 HINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDFGVK 84
Cdd:TIGR00107   1 HINAKKGDIADVVLMPGDPLRAKYIAETFLEDVREVNEVRGMLGFTGTYKGKKISVMGHGMGIPSISIYVYELIKFYEVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024   85 KIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGVDARVGNLFSADLFYSPD 164
Cdd:TIGR00107  81 TIIRVGSCGAIRPDVKLRDVIIAMGASTDSKYNRVRFVEVDFAAIADFELVENAYDAAKAKGVDVHVGNVFSADAFYQPD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446147024  165 GEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLG 236
Cdd:TIGR00107 161 KDVFDLMAKYGILGVEMEAAALYANAAELGAKALTILTVSDHLVTHEATTAEERQTTFKDMIILALESVSQL 232
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 5-232 1.68e-154

purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas vaginalis PNP; Escherichia coli purine nucleoside phosphorylase (PNP)-I (or DeoD) accepts both 6-oxo and 6-amino purine nucleosides as substrates. Trichomonas vaginalis PNP has broad substrate specificity, having phosphorolytic catalytic activity with adenosine, inosine, and guanosine (with adenosine as the preferred substrate). This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350157  Cd Length: 228  Bit Score: 427.97  E-value: 1.68e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024   5 HINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDFGVK 84
Cdd:cd09006    1 HIEAKKGDIAKTVLMPGDPLRAKYIAETFLEDAKLVNSVRNMLGYTGTYKGKRVSVMGSGMGMPSIGIYAYELFKFYGVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  85 KIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGVDARVGNLFSADLFYSPD 164
Cdd:cd09006   81 NIIRIGTCGAYQPDLKLRDVVLAMGASTDSNYNRLRFGGGDFAPIADFELLRKAVETAKELGIPVHVGNVFSSDVFYDDD 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446147024 165 GEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALES 232
Cdd:cd09006  161 PELWKKLKKYGVLAVEMEAAALYTNAARLGKKALAILTVSDSLVTGEELSAEERETSFTNMIELALET 228
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 15-223 1.07e-37

Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase (PNP) Uridine phosphorylase (UdRPase) 5'-methylthioadenosine phosphorylase (MTA phosphorylase)


Pssm-ID: 426013  Cd Length: 233  Bit Score: 131.70  E-value: 1.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024   15 DVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSI-YTKELITDFGVKKIIRVGSCG 93
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAIlAAIRLLKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024   94 AVLPHVKLRDVVIGMGACTDSKVNRIRFKDHD------FAAIADFDMVRNAVDAAKALGVDARVGNLFSADLFYSPDGEM 167
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPLFGPEGGpyfpdmAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446147024  168 FDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDH--IRTHEQTTAAERQTTFN 223
Cdd:pfam01048 161 IRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSDLaaGGADGELTHEEVEEFAE 218
 
Name Accession Description Interval E-value
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
2-236 8.69e-175

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 479.74  E-value: 8.69e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024   2 ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDF 81
Cdd:PRK05819   1 MTPHINAKKGDIADTVLMPGDPLRAKYIAETFLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELITDY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  82 GVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGVDARVGNLFSADLFY 161
Cdd:PRK05819  81 GVKKLIRVGSCGALQEDVKVRDVVIAMGASTDSNVNRIRFKGHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLFY 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446147024 162 SPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLG 236
Cdd:PRK05819 161 NPDPEMFDVLEKYGVLGVEMEAAALYGLAAKYGVKALTILTVSDHIVTGEATTAEERQTTFNDMIEIALESAILG 235
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 1-236 6.13e-168

Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside phosphorylase is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 440575  Cd Length: 236  Bit Score: 462.28  E-value: 6.13e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024   1 MATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITD 80
Cdd:COG0813    1 MMTPHIGAKKGDIAETVLLPGDPLRAKYIAETFLEDAVLVNEVRGMLGYTGTYKGKRVSVMGSGMGIPSISIYAYELITE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  81 FGVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGVDARVGNLFSADLF 160
Cdd:COG0813   81 YGVKNIIRVGTCGALQEDVKVRDVVIAMGASTDSNVNRQRFGGGDFAPIADFELLRKAVEAAKELGIKVHVGNVFSSDLF 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446147024 161 YSPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLG 236
Cdd:COG0813  161 YREDPDLLEKLAKYGVLAVEMEAAALYTLAAKYGKRALAILTVSDHLVTGEETTAEERQTTFNDMMEIALEAALKL 236
deoD TIGR00107
purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called ...
 5-236 9.88e-160

purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called inosine phosphorylase) is a purine salvage enzyme. Purine nucleosides, such as guanosine, inosine, or xanthosine, plus orthophosphate, can be converted to their respective purine bases (guanine, hypoxanthine, or xanthine) plus ribose-1-phosphate. This family of purine nucleoside phosphorylase is restricted to the bacteria. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 188024  Cd Length: 232  Bit Score: 441.52  E-value: 9.88e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024    5 HINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDFGVK 84
Cdd:TIGR00107   1 HINAKKGDIADVVLMPGDPLRAKYIAETFLEDVREVNEVRGMLGFTGTYKGKKISVMGHGMGIPSISIYVYELIKFYEVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024   85 KIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGVDARVGNLFSADLFYSPD 164
Cdd:TIGR00107  81 TIIRVGSCGAIRPDVKLRDVIIAMGASTDSKYNRVRFVEVDFAAIADFELVENAYDAAKAKGVDVHVGNVFSADAFYQPD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446147024  165 GEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLG 236
Cdd:TIGR00107 161 KDVFDLMAKYGILGVEMEAAALYANAAELGAKALTILTVSDHLVTHEATTAEERQTTFKDMIILALESVSQL 232
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 5-232 1.68e-154

purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas vaginalis PNP; Escherichia coli purine nucleoside phosphorylase (PNP)-I (or DeoD) accepts both 6-oxo and 6-amino purine nucleosides as substrates. Trichomonas vaginalis PNP has broad substrate specificity, having phosphorolytic catalytic activity with adenosine, inosine, and guanosine (with adenosine as the preferred substrate). This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350157  Cd Length: 228  Bit Score: 427.97  E-value: 1.68e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024   5 HINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDFGVK 84
Cdd:cd09006    1 HIEAKKGDIAKTVLMPGDPLRAKYIAETFLEDAKLVNSVRNMLGYTGTYKGKRVSVMGSGMGMPSIGIYAYELFKFYGVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  85 KIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGVDARVGNLFSADLFYSPD 164
Cdd:cd09006   81 NIIRIGTCGAYQPDLKLRDVVLAMGASTDSNYNRLRFGGGDFAPIADFELLRKAVETAKELGIPVHVGNVFSSDVFYDDD 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446147024 165 GEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALES 232
Cdd:cd09006  161 PELWKKLKKYGVLAVEMEAAALYTNAARLGKKALAILTVSDSLVTGEELSAEERETSFTNMIELALET 228
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
1-233 1.68e-149

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 415.65  E-value: 1.68e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024   1 MATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITD 80
Cdd:PRK13374   1 MSTPHINAQPGDFAETVLMPGDPLRAKYIAETYLEDVVQVTDVRNMFGFTGTYKGKKVSVMGHGMGIPSMVIYVHELIAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  81 FGVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGVDARVGNLFSADLF 160
Cdd:PRK13374  81 FGVKNIIRVGSCGATQDDVKLMDVIIAQGASTDSKTNRIRFSGHDFAAIADYQLLEKAVETAREKGVPVKVGNVFSSDLF 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446147024 161 YSPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESV 233
Cdd:PRK13374 161 YDPDEDAIEAMERFGILGVDMEVAGLYGLAAYLGAEALAILTVSDHIITGEETTAEERQLSFNDMIEVALETA 233
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
 5-234 9.96e-80

purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside phosphorylase (PNP) catalyzes the reversible phosphorolysis of purine nucleosides. Thermus thermophiles PNP catalyzes the phosphorolysis of guanosine but not adenosine. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350165  Cd Length: 234  Bit Score: 239.13  E-value: 9.96e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024   5 HINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELItDFGVK 84
Cdd:cd17765    4 HIRAEPGDVAEAVLLPGDPGRATYIAETFFDGPRLYNDHRGLLGYTGTYKGKPVSVQTTGMGCPSAAIVVEELA-QLGVK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  85 KIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGVDARVGNLFSADLFYSPD 164
Cdd:cd17765   83 RLIRVGTCGGLSSGLQLGDLIVATAAVPADGTTRALLGGEPYAPAADFELVEALYRAARAAGMPVHVGPVATSDLFYDPT 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446147024 165 GEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQT-TAAERQTTFNDMIKIALESVL 234
Cdd:cd17765  163 PDGVKRWRRRGVLAVEMEASALFTLAALRGLRAGCILTVSDLIGDPERRiDDEELRAGVDRMTEVALEAVV 233
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 4-233 1.87e-64

Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 442068  Cd Length: 251  Bit Score: 200.78  E-value: 1.87e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024   4 PHINAEMGDFADVVLMPGDPLRAKYIAEtFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITdFGV 83
Cdd:COG2820   12 YHLGLKPGDVADYVILPGDPGRVELIAS-YLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIAVEELAA-LGA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  84 KKIIRVGSCGAVLPHVKLRDVVIGMGActdskvnrIRF-------KDHDFAAIADFDMVRNAVDAAKALGVDARVGNLFS 156
Cdd:COG2820   90 KTFIRVGTSGALQPDIPVGDLVIATGA--------VRLdgtsnfyAPAEYPAVADFELTRALVEAAEELGVDYHVGITAS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024 157 ADLFYSPDG----------EMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERqtTFNDMI 226
Cdd:COG2820  162 TDGFYAEQGrelrvdpdldEKLEAWRKLGVLNVEMETAALFTLARLRGHRAGSVLAVSANRVTGEFSKDPEE--AVERAI 239


                 ....*..
gi 446147024 227 KIALESV 233
Cdd:COG2820  240 KVALEAL 246
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 4-233 3.20e-61

uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine phosphorylase (UP) is specific for pyrimidines, and is involved in pyrimidine salvage and in the maintenance of uridine homeostasis. In addition to E. coli Udp, this subfamily includes Shewanella oneidensis MR-1 UP and Plasmodium falciparum purine nucleoside phosphorylase (PfPNP). PfPNP is an outlier in terms of genetic distance from the other families of PNPs. PfPNP is catalytically active for inosine and guanosine, and in addition, has a weak UP activity. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350167  Cd Length: 239  Bit Score: 191.89  E-value: 3.20e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024   4 PHINAEMGDFADVVLMPGDPLRAKYIAEtFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELItDFGV 83
Cdd:cd17767    1 YHIGLKPGDVAPYVLLPGDPGRVERIAE-LLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELA-QLGA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  84 KKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRiRFKDHDFAAIADFDMVRNAVDAAKALGVDARVGNLFSADLFYSP 163
Cdd:cd17767   79 KTFIRVGTCGALQPDIKLGDLVIATGAVRDEGTSK-HYVPPEYPAVADPEVVLALVEAAEELGVPYHVGITASKDSFYGG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024 164 DG-----------EMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALES 232
Cdd:cd17767  158 QGrpgpglppelpELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAPDEEDVAAGEERAIRVALEA 237


                 .
gi 446147024 233 V 233
Cdd:cd17767  238 L 238
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 16-231 4.08e-56

nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases such as purine nucleoside phosphorylase (PNP, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases such as AMP nucleosidase (AMN, EC 3.2.2.4) and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). Members of this family display different physiologically relevant quaternary structures: hexameric (trimer-of-dimers arrangement of Shewanella oneidensis MR-1 UP); homotrimeric (human PNP and Escherichia coli PNPII or XapA); hexameric (with some evidence for co-existence of a trimeric form) such as E. coli PNPI (DeoD); or homodimeric such as human and Trypanosoma brucei UP. The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350156  Cd Length: 216  Bit Score: 178.25  E-value: 4.08e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  16 VVLMPGDPLRAKYIAEtFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELItDFGVKKIIRVGSCGAV 95
Cdd:cd09005    1 YAIIPGDPERVDVIDS-KLENPQKVSSFRGYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEELC-ALGVDTIIRVGSCGAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  96 LPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGVDARVGNLFSADLFYSPDGEMFDVMEKYG 175
Cdd:cd09005   79 REDIKVGDLVIADGAIRGDGVTPYYVVGPPFAPEADPELTAALEEAAKELGLTVHVGTVWTTDAFYRETREESEKLRKLG 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446147024 176 ILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAE-RQTTFNDMIKIALE 231
Cdd:cd09005  159 ALAVEMETSALATLAHLRGVKAASILAVSDNLITGEIGFVDEfLSEAEKKAIEIALD 215
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
 17-233 2.72e-46

5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP) catalyzes the reversible phosphorolysis of 5'-deoxy-5'-methylthioadenosine (MTA) to adenine and 5-methylthio-D-ribose-1-phosphate. Sulfolobus solfataricus MTAPI will utilize inosine, guanosine, and adenosine as substrates, in addition to MTA. Two MTAPs have been isolated from S. solfataricus: SsMTAP1 and SsMTAPII, SsMTAPII belongs to a different subfamily of the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-I family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350164  Cd Length: 220  Bit Score: 153.15  E-value: 2.72e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  17 VLMPGDPLRAKYIAETfLEDAREVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITdFGVKKIIRVGSCGAVL 96
Cdd:cd17764    3 VIAVGDPGRVELLSTL-LEDPRLVNENRGLLVYTGKYKGEEVTIATHGIGGPSAAIVFEELIM-LGAKVIIRLGTAGGLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  97 PHVKLRDVVIGMGA-CTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGVDARVGNLFSADLFYSPDGEMFDVMEKYG 175
Cdd:cd17764   81 PELRVGDIVVATGAsYYPGGGLGQYFPDVCPPASPDPELTLELVESLSKRGLKYYVGPVFSSDAFYAEDEEFAERWSSLG 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024 176 ILGVEMEAAGIYGVAAEFGAKALTICTVSDHI--RTHEQTTAAERQTTFNDMIKIALESV 233
Cdd:cd17764  161 FIAVEMECATLFTLGWLRGVKAGAVLVVSDNLvkGGKLMLTKEELEEKVMKAAKAVLEAL 220
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 15-223 1.07e-37

Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase (PNP) Uridine phosphorylase (UdRPase) 5'-methylthioadenosine phosphorylase (MTA phosphorylase)


Pssm-ID: 426013  Cd Length: 233  Bit Score: 131.70  E-value: 1.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024   15 DVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSI-YTKELITDFGVKKIIRVGSCG 93
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAIlAAIRLLKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024   94 AVLPHVKLRDVVIGMGACTDSKVNRIRFKDHD------FAAIADFDMVRNAVDAAKALGVDARVGNLFSADLFYSPDGEM 167
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPLFGPEGGpyfpdmAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446147024  168 FDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDH--IRTHEQTTAAERQTTFN 223
Cdd:pfam01048 161 IRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSDLaaGGADGELTHEEVEEFAE 218
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
 5-231 2.55e-27

uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes the reversible phosphorolysis of uracil ribosides and analogous compounds to their respective nucleobases and ribose 1-phosphate. Trypanosoma brucei UP has a high specificity for uracil-containing (deoxy)nucleosides, and may function as a dimer. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350155  Cd Length: 282  Bit Score: 105.63  E-value: 2.55e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024   5 HINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNvRGMLGFTGTYKGRKISVMGHGMGIPSCSIY----------- 73
Cdd:cd00436   12 HLHLKPEDLADTIILVGDPGRVPKVSKHFDSIEFKKQN-REFVTHTGTYKGKRITVISTGIGTDNIDIVlneldalvnid 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  74 --TKELITDFGVKKIIRVGSCGAVLPHVKLRDVV-----IGM-GAC----TDSKVNRIRFKDHDFAAIADFDMVRN--AV 139
Cdd:cd00436   91 fkTRTPKEEKTSLNIIRLGTSGALQPDIPVGSLVissyaIGLdNLLnfydHPNTDEEAELENAFIAHTSWFKGKPRpyVV 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024 140 DAAKAL-----GVDARVGNLFSADLFYSPDG----------EMFDVMEKYGILGV-----EMEAAGIYGVAAEFGAKALT 199
Cdd:cd00436  171 KASPELldaltGVGYVVGITATAPGFYGPQGrqlrlpladpDLLDKLSSFSYGGLritnfEMETSAIYGLSRLLGHRALS 250

                        250       260       270
                 ....*....|....*....|....*....|..
gi 446147024 200 ICTVSDHIRTHEQTTAAERqtTFNDMIKIALE 231
Cdd:cd00436  251 ICAIIANRATGEFSKDYKK--AVEKLIEKVLE 280
PRK11178 PRK11178
uridine phosphorylase; Provisional
 14-231 7.83e-23

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 93.18  E-value: 7.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  14 ADVVLMPGDPLRAKYIAE-----TFLEDAREVNNVRGMLGftgtykGRKISVMGHGMGIPSCSIYTKELiTDFGVKKIIR 88
Cdd:PRK11178  17 ATLAIVPGDPERVEKIAAlmdnpVFLASHREFTSWRAELD------GKPVIVCSTGIGGPSTSIAVEEL-AQLGVRTFLR 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  89 VGSCGAVLPHVKLRDVVIGMGACTDSKVNRiRFKDHDFAAIADFDMVRNAVDAAKALGVDARVGNLFSADLFYsPDGEMF 168
Cdd:PRK11178  90 IGTTGAIQPHINVGDVLVTTASVRLDGASL-HFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFY-PGQERY 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024 169 DV------------MEKY---GILGVEMEAAGIYGVAAEFGAKALTICTVsdhI--RTHEQT-TAAERQTTFNDMIKIAL 230
Cdd:PRK11178 168 DTysgrvvrrfkgsMEEWqamGVMNYEMESATLLTMCASQGLRAGMVAGV---IvnRTQQEIpNAETMKQTESHAVKIVV 244


                 .
gi 446147024 231 E 231
Cdd:PRK11178 245 E 245
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
 21-218 5.52e-16

nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily is composed of mostly uncharacterized proteins with similarity to Toxoplasma gondii uridine phosphorylase (TgUPase). Toxoplasma gondii appears to have a single non-specific uridine phosphorylase which catalyzes the reversible phosphorolysis of uridine, deoxyuridine and thymidine, rather than the two distinct enzymes of mammalian cells: uridine phosphorylase (nucleoside phosphorylase-I family) and thymidine phosphorylase (nucleoside phosphorylase-II family). TgUPase is a potential target for intervention against toxoplasmosis. It belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350169  Cd Length: 255  Bit Score: 74.54  E-value: 5.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  21 GDPLRAKYIAETFLEDA--REVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCsiytkelitDFGVKK----------IIR 88
Cdd:cd17769    7 GDPARARLIAKLLDKEPkvFELTSERGFLTITGRYKGVPVSIVAIGMGAPMM---------DFFVREaravvdgpmaIIR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  89 VGSCGAVLPHVKLRDVVIGMGACTdskVNRIRFKDHDFAA--------------IADFD--------MVRNAVDAAKALG 146
Cdd:cd17769   78 LGSCGSLDPDVPVGSVVVPSASVA---VTRNYDDDDFAGPstssekpyliskpvPADPElselleseLKASLGGEVVVEG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024 147 VDArvgnlfSADLFYSPDG---EMFD---------VMEKY-GILGVEMEAAGIYGVAAEFGAKALTICTVSDHIR----- 208
Cdd:cd17769  155 LNA------SADSFYSSQGrqdPNFPdhnenlidkLLKRYpGAASLEMETFHLFHLARCSRPAQGKIRAAAAHMVfanrt 228

                        250
                 ....*....|....*
gi 446147024 209 -----THEQTTAAER 218
Cdd:cd17769  229 sndfiSPERVHELER 243
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 34-207 2.20e-14

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both bacterial and plant 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidases (MTANs): bacterial MTANs show comparable efficiency in hydrolyzing MTA and SAH, while plant enzymes are highly specific for MTA and are unable to metabolize SAH or show significantly reduced activity towards SAH. MTAN is involved in methionine and S-adenosyl-methionine recycling, polyamine biosynthesis, and bacterial quorum sensing. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350159  Cd Length: 222  Bit Score: 69.83  E-value: 2.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  34 LEDAREVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKLRDVVIGmgactd 113
Cdd:cd09008   17 LLENVEEETIAGRTFYEGTLGGKEVVLVQSGIGKVNAAIATQLLIDRFKPDAIINTGVAGGLDPDLKIGDVVIA------ 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024 114 skvNRIRFkdHDFAAI-----------------ADFDMVRNAVDAAKALGVDARVGNLFSADLFYSpDGEMFD-VMEKYG 175
Cdd:cd09008   91 ---TKVVY--HDVDATafgyeggqppgmpayfpADPELLELAKKAAKELGPKVHTGLIASGDQFVA-SSEKKEeLRENFP 164

                        170       180       190
                 ....*....|....*....|....*....|..
gi 446147024 176 ILGVEMEAAGIYGVAAEFGAKALTICTVSDHI 207
Cdd:cd09008  165 ALAVEMEGAAIAQVCYLNGVPFLVIRSISDLA 196
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 34-205 3.03e-14

Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase MtnN and futalosine hydrolase MqnB [Nucleotide transport and metabolism, Coenzyme transport and metabolism]; Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase MtnN and futalosine hydrolase MqnB is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440538  Cd Length: 231  Bit Score: 69.55  E-value: 3.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  34 LEDAREVNnVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKLRDVVIGmgactd 113
Cdd:COG0775   20 LEDKKEVQ-IAGFTFYLGTLGGKEVVLVNSGIGKVNAATATTLLIARFRPDAVINTGVAGGLDPDLKIGDVVLA------ 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024 114 skvNRIRFKDHDFAAI---------------ADFDMVRNAVDAAKALGVDARVGNLFSADLFYSPDGEMFDVMEKY-GIL 177
Cdd:COG0775   93 ---TEVVQHDVDVTAFgyprgqvpgmpalfeADPALLEAAKEAAKESGLKVVTGTIATGDRFVWSAEEKRRLRERFpGAL 169

                        170       180
                 ....*....|....*....|....*...
gi 446147024 178 GVEMEAAGIYGVAAEFGAKALTICTVSD 205
Cdd:COG0775  170 AVDMEGAAIAQVCYRFGVPFLVIRAISD 197
NP-I_spr0068 cd09007
uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed ...
 49-231 7.40e-14

uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed of uncharacterized members including Streptococcus pneumoniae hypothetical protein spr0068. The nucleoside phosphorylase-I (NP-I) family members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases such as purine nucleoside phosphorylase (PNP, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases such as AMP nucleosidase (AMN, EC 3.2.2.4) and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). Members of the NP-I family display different physiologically relevant quaternary structures: hexameric (trimer-of-dimers arrangement of Shewanella oneidensis MR-1 UP); homotrimeric (human PNP and Escherichia coli PNPII or XapA); hexameric (with some evidence for co-existence of a trimeric form) such as E. coli PNPI (DeoD); or homodimeric such as human and Trypanosoma brucei UP. The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350158 [Multi-domain]  Cd Length: 221  Bit Score: 68.28  E-value: 7.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  49 FTGTYKGRKISVMGHGMGIPSCSIYTKELITdFGVKKIIRVGSCGAVLPHVKLRDVVIGMGActdskvnrIRfkD----- 123
Cdd:cd09007   38 YRLEYDGEEVGVVGPPVGAPAAVLVLEELIA-LGAKKFIVVGSCGSLDPDLAVGDIILPTSA--------LR--Degtsy 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024 124 H-----DFAAiADFDMVRNAVDAAKALGVDARVGNLFSADLFYSpdgEMFDVMEKY---GILGVEMEAAGIYGVAAEFGA 195
Cdd:cd09007  107 HylppsRYIE-PDPELLDALEEALEKAGIPYVRGKTWTTDAPYR---ETRAKVARRraeGCLAVEMEAAALFAVAQFRGV 182

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446147024 196 KALTICTVSDHI--RTHEQTTAAERQTTFNDMIKIALE 231
Cdd:cd09007  183 ELAQLLYVSDSLagEEWDPRGRDEGKDAREKALELALE 220
PRK14697 PRK14697
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; ...
 38-229 3.22e-09

bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Provisional


Pssm-ID: 184794  Cd Length: 233  Bit Score: 55.40  E-value: 3.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  38 REVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKLRDVVIGMGAcTDSKVN 117
Cdd:PRK14697  24 QEEQIIAGMPFYVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLHPDVKVGDIVISTNV-THHDVS 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024 118 RIRFKD-----HDFAAIADF-DMVRNAVDAAkALGVDARVGNLFSADLFYSPDGEMFDVMEKYGILGVEMEAAGIYGVAA 191
Cdd:PRK14697 103 KTQMKNlfpfqEEFIASKELvELARKACNSS-SLHIEIHEGRIVSGECFVEDSKLKAKLIDEYAPHCTEMEGAAIGHVAY 181

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446147024 192 EFGAKALTICTVSDhirtheqTTAAERQTTFNDMIKIA 229
Cdd:PRK14697 182 INEVPFLVIRCISD-------SADDEAQISYDDFAKTA 212
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
22-205 2.52e-08

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 52.82  E-value: 2.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  22 DPLRAKyiaetfLEDAREVNnVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKL 101
Cdd:PRK05584  14 TLLLDK------LENAQTIT-LAGREFYTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDAVINTGVAGGLAPGLKV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024 102 RDVVIGmgactdskvNRIRFKDHDFAAI---------------ADFDMVRNAVDAAKALGVDARVGNLFSADLFYSpDGE 166
Cdd:PRK05584  87 GDVVVA---------DELVQHDVDVTAFgypygqvpglpaafkADEKLVALAEKAAKELNLNVHRGLIASGDQFIA-GAE 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446147024 167 MFDVMEK--YGILGVEMEAAGIYGVAAEFGAKALTICTVSD 205
Cdd:PRK05584 157 KVAAIRAefPDALAVEMEGAAIAQVCHEFGVPFVVVRAISD 197
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 49-205 3.31e-08

nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both bacterial and plant 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidases (MTANs), as well as futalosine nucleosidase and adenosylhopane nucleosidase. Bacterial MTANs show comparable efficiency in hydrolyzing MTA and SAH, while plant enzymes are highly specific for MTA and are unable to metabolize SAH or show significantly reduced activity towards SAH. MTAN is involved in methionine and S-adenosyl-methionine recycling, polyamine biosynthesis, and bacterial quorum sensing. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350170 [Multi-domain]  Cd Length: 210  Bit Score: 52.29  E-value: 3.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  49 FTGTYKGRKISVMGHGMGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKLRDVVIGmgactdskvNRIRFKDHDFAA 128
Cdd:cd17877   32 YRGTLGGHPVVLVESGMGKANAARAAQLLLEHFQPDLIISTGFAGGLDPGLAVGDLVIA---------DRVLYHDGDVPA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024 129 I--ADFDMVRNAVDAAKALGVDARVGNLFSADLFY-SPDGEMFdVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSD 205
Cdd:cd17877  103 GleADEKLVALAEELAAGLNLKVHRGTIITVDAIVrKSAEKAA-LAARFPALAVDMESAAIAQVAAARGIPFLAIRAISD 181
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
 38-229 1.94e-07

bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 51.17  E-value: 1.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  38 REVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKLRDVVIGMGAC-TDSKV 116
Cdd:PRK06698  24 QEEQIIAGMPFYVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLHPDVKVGDIVISTNVThHDVSK 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024 117 NRIR----FKDHDFAAIADFDMVRNAVDAAkALGVDARVGNLFSADLFYSPDGEMFDVMEKYGILGVEMEAAGIYGVAAE 192
Cdd:PRK06698 104 TQMKnlfpFQEEFIASKELVELARKACNSS-SLHMEIHEGRIVSGECFVEDSKLKAKLIDEYAPHCTEMEGAAIGHVAYI 182

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446147024 193 FGAKALTICTVSDhirtheqTTAAERQTTFNDMIKIA 229
Cdd:PRK06698 183 NEVPFLVIRCISD-------SADDEAQISYDDFAKTA 212
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
 2-201 1.11e-06

uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine phosphorylases. Genes from human and mouse have been characterized. This enzyme is a member of the PHP/UDP subfamily (pfam01048) and is closely related to the bacterial uridine (TIGR01718) and inosine (TIGR00107) phosphorylase equivalogs. In addition to the eukaryotes, a gene from Mycobacterium leprae is included in this equivalog and may have resulted from lateral gene transfer. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 130780 [Multi-domain]  Cd Length: 287  Bit Score: 48.22  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024    2 ATPHINAEMGDfADVVLMPGDPLRAKYIAETFLEDA--REVNNVRGMLGFTGTYKGRKIS---VMGHGMGIPSCSIYTKE 76
Cdd:TIGR01719  20 STHDFPAVFGD-VKFVCMGGTPSRMKAFARYVGAELglSCGRDYPNISERGDRFAMYKVGpvlCVSHGMGIPSISIMLHE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024   77 LITDF---GVKK--IIRVGSCGAVlpHVKLRDVVI---GMGACTDSKVNRIRFKDHDFAAiADFDmvRNAVDAAKALGVD 148
Cdd:TIGR01719  99 LIKLLyyaRCKNptFIRIGTSGGI--GVPPGTVVVsseAVDACLKPEYEQIVLGKRVIRP-TQLD--EALVQELLLCGAE 173

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446147024  149 AR------VGNLFSADLFYSP----DGEMFDVMEK-----------YGILGVEMEAAGIYGVAAEFGAKALTIC 201
Cdd:TIGR01719 174 GLdefttvSGNTMCTDDFYEGqgrlDGAFCEYTEKdkmaylrklyaLGVRNIEMESSMFAAMTSRAGFKAAVVC 247
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
 13-201 3.27e-06

uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes the reversible phosphorolysis of uracil ribosides and analogous compounds to their respective nucleobases and ribose 1-phosphate. Human UPP1 has a role in the activation of pyrimidine nucleoside analogues used in chemotherapy, such as 5-fluorouracil. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350163  Cd Length: 276  Bit Score: 46.76  E-value: 3.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  13 FADV--VLMPGDPLRAKYIAETFLEDAR-EVNNVRGMLGFTGT------YK-GRKISVmGHGMGIPSCSIYTKELI---- 78
Cdd:cd17763   20 FGDVkfVCMGGSPGRMENFAEYLAKELGiKLPAGAALVNLSKTtdrysmYKvGPVLSV-SHGMGIPSLSILLHELIkllh 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  79 ----TDFgvkKIIRVGSCGAVlpHVKLRDVVIgmgacTDSKVN---------RIRFKDHDFAAIADFDMVRNAVDAAKAL 145
Cdd:cd17763   99 yagcKDV---TFIRIGTSGGI--GVEPGTVVI-----TTEAVDgelepfyeqVILGKVVKRPAVLDAQLAEELLECAKEL 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446147024 146 G-VDARVGNLFSADLFYSP----DG--------EMFDVMEK---YGILGVEMEAAGIYGVAAEFGAKALTIC 201
Cdd:cd17763  169 DdFPTVIGKTMCANDFYEGqgrlDGafcdyteeDKMAFLQKlydAGVRNIEMESLCFAAFCHRAGIKAAVVC 240
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
 50-205 1.93e-04

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase which acts on its two substrates at the same active site. This enzyme is involved in the recycling of the components of S-adenosylmethionine after it has donated one of its two non-ribose sulfur ligands to an acceptor. In the case of 5-methylthioadenosine this represents the first step of the methionine salvage pathway in bacteria. This enzyme is widely distributed in bacteria, especially those that lack adenosylhomocysteinase (EC 3.3.1.1). One clade of bacteria including Agrobacterium, Mesorhizobium, Sinorhizobium and Brucella includes sequences annotated as MTA/SAH nucleotidase, but differs significantly in homology and has no independent experimental evidence. There are homologs of this enzyme in plants, some of which score between trusted and noise cutoffs here, but there is no experimental evidence to validate this function at this time. [Central intermediary metabolism, Other, Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 130765  Cd Length: 228  Bit Score: 41.24  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024   50 TGTYKGRKISVMGHGMGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKLRDVVIGmgacTDSKVNRIRFKDHDF--- 126
Cdd:TIGR01704  34 TGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLAPTLKVGDIVVS----DEARYHDADVTAFGYeyg 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147024  127 -------AAIADFDMVRNAVDAAKALGVDARVGNLFSADLFYSPDGEMFDVMEKYGIL-GVEMEAAGIYGVAAEFGAKAL 198
Cdd:TIGR01704 110 qlpgcpaGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKIRHNFPQAiAVEMEATAIAHVCHNFNVPFV 189


                  ....*..
gi 446147024  199 TICTVSD 205
Cdd:TIGR01704 190 VVRAISD 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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