NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|46015053|pdb|1OVG|C]
View 

Chain C, Purine nucleoside phosphorylase

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
1-235 4.77e-174

DeoD-type purine-nucleoside phosphorylase;


:

Pssm-ID: 180275  Cd Length: 235  Bit Score: 477.81  E-value: 4.77e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C         1 ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGVGIPSCSIYTKELITDF 80
Cdd:PRK05819   1 MTPHINAKKGDIADTVLMPGDPLRAKYIAETFLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELITDY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C        81 GVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFY 160
Cdd:PRK05819  81 GVKKLIRVGSCGALQEDVKVRDVVIAMGASTDSNVNRIRFKGHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLFY 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1OVG_C       161 SPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLG 235
Cdd:PRK05819 161 NPDPEMFDVLEKYGVLGVEMEAAALYGLAAKYGVKALTILTVSDHIVTGEATTAEERQTTFNDMIEIALESAILG 235
 
Name Accession Description Interval E-value
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
1-235 4.77e-174

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 477.81  E-value: 4.77e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C         1 ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGVGIPSCSIYTKELITDF 80
Cdd:PRK05819   1 MTPHINAKKGDIADTVLMPGDPLRAKYIAETFLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELITDY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C        81 GVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFY 160
Cdd:PRK05819  81 GVKKLIRVGSCGALQEDVKVRDVVIAMGASTDSNVNRIRFKGHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLFY 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1OVG_C       161 SPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLG 235
Cdd:PRK05819 161 NPDPEMFDVLEKYGVLGVEMEAAALYGLAAKYGVKALTILTVSDHIVTGEATTAEERQTTFNDMIEIALESAILG 235
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 1-235 2.11e-165

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: 455.73  E-value: 2.11e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C        1 ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGVGIPSCSIYTKELITDF 80
Cdd:COG0813   2 MTPHIGAKKGDIAETVLLPGDPLRAKYIAETFLEDAVLVNEVRGMLGYTGTYKGKRVSVMGSGMGIPSISIYAYELITEY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C       81 GVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFY 160
Cdd:COG0813  82 GVKNIIRVGTCGALQEDVKVRDVVIAMGASTDSNVNRQRFGGGDFAPIADFELLRKAVEAAKELGIKVHVGNVFSSDLFY 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1OVG_C      161 SPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLG 235
Cdd:COG0813 162 REDPDLLEKLAKYGVLAVEMEAAALYTLAAKYGKRALAILTVSDHLVTGEETTAEERQTTFNDMMEIALEAALKL 236
deoD TIGR00107
purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called ...
 4-235 3.78e-159

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: 439.98  E-value: 3.78e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C          4 HINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGVGIPSCSIYTKELITDFGVK 83
Cdd:TIGR00107   1 HINAKKGDIADVVLMPGDPLRAKYIAETFLEDVREVNEVRGMLGFTGTYKGKKISVMGHGMGIPSISIYVYELIKFYEVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C         84 KIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFYSPD 163
Cdd:TIGR00107  81 TIIRVGSCGAIRPDVKLRDVIIAMGASTDSKYNRVRFVEVDFAAIADFELVENAYDAAKAKGVDVHVGNVFSADAFYQPD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1OVG_C        164 GEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLG 235
Cdd:TIGR00107 161 KDVFDLMAKYGILGVEMEAAALYANAAELGAKALTILTVSDHLVTHEATTAEERQTTFKDMIILALESVSQL 232
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 4-231 1.55e-153

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: 425.66  E-value: 1.55e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C        4 HINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGVGIPSCSIYTKELITDFGVK 83
Cdd:cd09006   1 HIEAKKGDIAKTVLMPGDPLRAKYIAETFLEDAKLVNSVRNMLGYTGTYKGKRVSVMGSGMGMPSIGIYAYELFKFYGVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C       84 KIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFYSPD 163
Cdd:cd09006  81 NIIRIGTCGAYQPDLKLRDVVLAMGASTDSNYNRLRFGGGDFAPIADFELLRKAVETAKELGIPVHVGNVFSSDVFYDDD 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1OVG_C      164 GEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALES 231
Cdd:cd09006 161 PELWKKLKKYGVLAVEMEAAALYTNAARLGKKALAILTVSDSLVTGEELSAEERETSFTNMIELALET 228
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 14-222 2.42e-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: 130.54  E-value: 2.42e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C         14 DVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGVGIPSCSI-YTKELITDFGVKKIIRVGSCG 92
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAIlAAIRLLKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C         93 AVLPHVKLRDVVIGMGACTDSKVNRIRFKDHD------FAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFYSPDGEM 166
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPLFGPEGGpyfpdmAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
1OVG_C        167 FDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDH--IRTHEQTTAAERQTTFN 222
Cdd:pfam01048 161 IRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSDLaaGGADGELTHEEVEEFAE 218
 
Name Accession Description Interval E-value
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
1-235 4.77e-174

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 477.81  E-value: 4.77e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C         1 ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGVGIPSCSIYTKELITDF 80
Cdd:PRK05819   1 MTPHINAKKGDIADTVLMPGDPLRAKYIAETFLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELITDY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C        81 GVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFY 160
Cdd:PRK05819  81 GVKKLIRVGSCGALQEDVKVRDVVIAMGASTDSNVNRIRFKGHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLFY 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1OVG_C       161 SPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLG 235
Cdd:PRK05819 161 NPDPEMFDVLEKYGVLGVEMEAAALYGLAAKYGVKALTILTVSDHIVTGEATTAEERQTTFNDMIEIALESAILG 235
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 1-235 2.11e-165

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: 455.73  E-value: 2.11e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C        1 ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGVGIPSCSIYTKELITDF 80
Cdd:COG0813   2 MTPHIGAKKGDIAETVLLPGDPLRAKYIAETFLEDAVLVNEVRGMLGYTGTYKGKRVSVMGSGMGIPSISIYAYELITEY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C       81 GVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFY 160
Cdd:COG0813  82 GVKNIIRVGTCGALQEDVKVRDVVIAMGASTDSNVNRQRFGGGDFAPIADFELLRKAVEAAKELGIKVHVGNVFSSDLFY 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1OVG_C      161 SPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLG 235
Cdd:COG0813 162 REDPDLLEKLAKYGVLAVEMEAAALYTLAAKYGKRALAILTVSDHLVTGEETTAEERQTTFNDMMEIALEAALKL 236
deoD TIGR00107
purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called ...
 4-235 3.78e-159

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: 439.98  E-value: 3.78e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C          4 HINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGVGIPSCSIYTKELITDFGVK 83
Cdd:TIGR00107   1 HINAKKGDIADVVLMPGDPLRAKYIAETFLEDVREVNEVRGMLGFTGTYKGKKISVMGHGMGIPSISIYVYELIKFYEVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C         84 KIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFYSPD 163
Cdd:TIGR00107  81 TIIRVGSCGAIRPDVKLRDVIIAMGASTDSKYNRVRFVEVDFAAIADFELVENAYDAAKAKGVDVHVGNVFSADAFYQPD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1OVG_C        164 GEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLG 235
Cdd:TIGR00107 161 KDVFDLMAKYGILGVEMEAAALYANAAELGAKALTILTVSDHLVTHEATTAEERQTTFKDMIILALESVSQL 232
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 4-231 1.55e-153

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: 425.66  E-value: 1.55e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C        4 HINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGVGIPSCSIYTKELITDFGVK 83
Cdd:cd09006   1 HIEAKKGDIAKTVLMPGDPLRAKYIAETFLEDAKLVNSVRNMLGYTGTYKGKRVSVMGSGMGMPSIGIYAYELFKFYGVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C       84 KIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFYSPD 163
Cdd:cd09006  81 NIIRIGTCGAYQPDLKLRDVVLAMGASTDSNYNRLRFGGGDFAPIADFELLRKAVETAKELGIPVHVGNVFSSDVFYDDD 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1OVG_C      164 GEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALES 231
Cdd:cd09006 161 PELWKKLKKYGVLAVEMEAAALYTNAARLGKKALAILTVSDSLVTGEELSAEERETSFTNMIELALET 228
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
1-232 1.10e-147

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 411.03  E-value: 1.10e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C         1 ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGVGIPSCSIYTKELITDF 80
Cdd:PRK13374   2 STPHINAQPGDFAETVLMPGDPLRAKYIAETYLEDVVQVTDVRNMFGFTGTYKGKKVSVMGHGMGIPSMVIYVHELIATF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C        81 GVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFY 160
Cdd:PRK13374  82 GVKNIIRVGSCGATQDDVKLMDVIIAQGASTDSKTNRIRFSGHDFAAIADYQLLEKAVETAREKGVPVKVGNVFSSDLFY 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1OVG_C       161 SPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESV 232
Cdd:PRK13374 162 DPDEDAIEAMERFGILGVDMEVAGLYGLAAYLGAEALAILTVSDHIITGEETTAEERQLSFNDMIEVALETA 233
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
 4-233 4.93e-78

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: 234.51  E-value: 4.93e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C        4 HINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGVGIPSCSIYTKELItDFGVK 83
Cdd:cd17765   4 HIRAEPGDVAEAVLLPGDPGRATYIAETFFDGPRLYNDHRGLLGYTGTYKGKPVSVQTTGMGCPSAAIVVEELA-QLGVK 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C       84 KIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFYSPD 163
Cdd:cd17765  83 RLIRVGTCGGLSSGLQLGDLIVATAAVPADGTTRALLGGEPYAPAADFELVEALYRAARAAGMPVHVGPVATSDLFYDPT 162

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1OVG_C      164 GEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQT-TAAERQTTFNDMIKIALESVL 233
Cdd:cd17765 163 PDGVKRWRRRGVLAVEMEASALFTLAALRGLRAGCILTVSDLIGDPERRiDDEELRAGVDRMTEVALEAVV 233
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 3-232 1.83e-63

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 198.08  E-value: 1.83e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C        3 PHINAEMGDFADVVLMPGDPLRAKYIAEtFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGVGIPSCSIYTKELITdFGV 82
Cdd:COG2820  12 YHLGLKPGDVADYVILPGDPGRVELIAS-YLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIAVEELAA-LGA 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C       83 KKIIRVGSCGAVLPHVKLRDVVIGMGActdskvnrIRF-------KDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFS 155
Cdd:COG2820  90 KTFIRVGTSGALQPDIPVGDLVIATGA--------VRLdgtsnfyAPAEYPAVADFELTRALVEAAEELGVDYHVGITAS 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C      156 ADLFYSPDG----------EMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERqtTFNDMI 225
Cdd:COG2820 162 TDGFYAEQGrelrvdpdldEKLEAWRKLGVLNVEMETAALFTLARLRGHRAGSVLAVSANRVTGEFSKDPEE--AVERAI 239


                ....*..
1OVG_C      226 KIALESV 232
Cdd:COG2820 240 KVALEAL 246
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 3-232 3.44e-60

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: 189.19  E-value: 3.44e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C        3 PHINAEMGDFADVVLMPGDPLRAKYIAEtFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGVGIPSCSIYTKELItDFGV 82
Cdd:cd17767   1 YHIGLKPGDVAPYVLLPGDPGRVERIAE-LLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELA-QLGA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C       83 KKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRiRFKDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFYSP 162
Cdd:cd17767  79 KTFIRVGTCGALQPDIKLGDLVIATGAVRDEGTSK-HYVPPEYPAVADPEVVLALVEAAEELGVPYHVGITASKDSFYGG 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C      163 DG-----------EMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALES 231
Cdd:cd17767 158 QGrpgpglppelpELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAPDEEDVAAGEERAIRVALEA 237


                .
1OVG_C      232 V 232
Cdd:cd17767 238 L 238
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 15-230 1.23e-55

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: 177.10  E-value: 1.23e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C       15 VVLMPGDPLRAKYIAEtFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGVGIPSCSIYTKELItDFGVKKIIRVGSCGAV 94
Cdd:cd09005   1 YAIIPGDPERVDVIDS-KLENPQKVSSFRGYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEELC-ALGVDTIIRVGSCGAL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C       95 LPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFYSPDGEMFDVMEKYG 174
Cdd:cd09005  79 REDIKVGDLVIADGAIRGDGVTPYYVVGPPFAPEADPELTAALEEAAKELGLTVHVGTVWTTDAFYRETREESEKLRKLG 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
1OVG_C      175 ILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAE-RQTTFNDMIKIALE 230
Cdd:cd09005 159 ALAVEMETSALATLAHLRGVKAASILAVSDNLITGEIGFVDEfLSEAEKKAIEIALD 215
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
 16-232 5.79e-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: 152.38  E-value: 5.79e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C       16 VLMPGDPLRAKYIAETfLEDAREVNNVRGMLGFTGTYKGRKISVMGHGVGIPSCSIYTKELITdFGVKKIIRVGSCGAVL 95
Cdd:cd17764   3 VIAVGDPGRVELLSTL-LEDPRLVNENRGLLVYTGKYKGEEVTIATHGIGGPSAAIVFEELIM-LGAKVIIRLGTAGGLV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C       96 PHVKLRDVVIGMGA-CTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFYSPDGEMFDVMEKYG 174
Cdd:cd17764  81 PELRVGDIVVATGAsYYPGGGLGQYFPDVCPPASPDPELTLELVESLSKRGLKYYVGPVFSSDAFYAEDEEFAERWSSLG 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C      175 ILGVEMEAAGIYGVAAEFGAKALTICTVSDHI--RTHEQTTAAERQTTFNDMIKIALESV 232
Cdd:cd17764 161 FIAVEMECATLFTLGWLRGVKAGAVLVVSDNLvkGGKLMLTKEELEEKVMKAAKAVLEAL 220
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 14-222 2.42e-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: 130.54  E-value: 2.42e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C         14 DVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGVGIPSCSI-YTKELITDFGVKKIIRVGSCG 92
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAIlAAIRLLKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C         93 AVLPHVKLRDVVIGMGACTDSKVNRIRFKDHD------FAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFYSPDGEM 166
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPLFGPEGGpyfpdmAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
1OVG_C        167 FDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDH--IRTHEQTTAAERQTTFN 222
Cdd:pfam01048 161 IRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSDLaaGGADGELTHEEVEEFAE 218
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
 4-230 1.45e-25

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: 101.01  E-value: 1.45e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C        4 HINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNvRGMLGFTGTYKGRKISVMGHGVGIPSCSIY----------- 72
Cdd:cd00436  12 HLHLKPEDLADTIILVGDPGRVPKVSKHFDSIEFKKQN-REFVTHTGTYKGKRITVISTGIGTDNIDIVlneldalvnid 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C       73 --TKELITDFGVKKIIRVGSCGAVLPHVKLRDVV-----IGM-GAC----TDSKVNRIRFKDHDFAAIADFDMVRN--AV 138
Cdd:cd00436  91 fkTRTPKEEKTSLNIIRLGTSGALQPDIPVGSLVissyaIGLdNLLnfydHPNTDEEAELENAFIAHTSWFKGKPRpyVV 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C      139 DAAKAL-----GIDARVGNLFSADLFYSPDG----------EMFDVMEKYGILGV-----EMEAAGIYGVAAEFGAKALT 198
Cdd:cd00436 171 KASPELldaltGVGYVVGITATAPGFYGPQGrqlrlpladpDLLDKLSSFSYGGLritnfEMETSAIYGLSRLLGHRALS 250

                       250       260       270
                ....*....|....*....|....*....|..
1OVG_C      199 ICTVSDHIRTHEQTTAAERqtTFNDMIKIALE 230
Cdd:cd00436 251 ICAIIANRATGEFSKDYKK--AVEKLIEKVLE 280
PRK11178 PRK11178
uridine phosphorylase; Provisional
 13-230 1.74e-23

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 94.72  E-value: 1.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C        13 ADVVLMPGDPLRAKYIAE-----TFLEDAREVNNVRGMLGftgtykGRKISVMGHGVGIPSCSIYTKELiTDFGVKKIIR 87
Cdd:PRK11178  17 ATLAIVPGDPERVEKIAAlmdnpVFLASHREFTSWRAELD------GKPVIVCSTGIGGPSTSIAVEEL-AQLGVRTFLR 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C        88 VGSCGAVLPHVKLRDVVIGMGACTDSKVNRiRFKDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFYsPDGEMF 167
Cdd:PRK11178  90 IGTTGAIQPHINVGDVLVTTASVRLDGASL-HFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFY-PGQERY 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C       168 DV------------MEKY---GILGVEMEAAGIYGVAAEFGAKALTICTVsdhI--RTHEQT-TAAERQTTFNDMIKIAL 229
Cdd:PRK11178 168 DTysgrvvrrfkgsMEEWqamGVMNYEMESATLLTMCASQGLRAGMVAGV---IvnRTQQEIpNAETMKQTESHAVKIVV 244


                 .
1OVG_C       230 E 230
Cdd:PRK11178 245 E 245
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 33-206 8.78e-15

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: 70.60  E-value: 8.78e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C       33 LEDAREVNNVRGMLGFTGTYKGRKISVMGHGVGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKLRDVVIGmgactd 112
Cdd:cd09008  17 LLENVEEETIAGRTFYEGTLGGKEVVLVQSGIGKVNAAIATQLLIDRFKPDAIINTGVAGGLDPDLKIGDVVIA------ 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C      113 skvNRIRFkdHDFAAI-----------------ADFDMVRNAVDAAKALGIDARVGNLFSADLFYSpDGEMFD-VMEKYG 174
Cdd:cd09008  91 ---TKVVY--HDVDATafgyeggqppgmpayfpADPELLELAKKAAKELGPKVHTGLIASGDQFVA-SSEKKEeLRENFP 164

                       170       180       190
                ....*....|....*....|....*....|..
1OVG_C      175 ILGVEMEAAGIYGVAAEFGAKALTICTVSDHI 206
Cdd:cd09008 165 ALAVEMEGAAIAQVCYLNGVPFLVIRSISDLA 196
NP-I_spr0068 cd09007
uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed ...
 48-230 2.35e-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: 69.43  E-value: 2.35e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C       48 FTGTYKGRKISVMGHGVGIPSCSIYTKELITdFGVKKIIRVGSCGAVLPHVKLRDVVIGMGActdskvnrIRfkD----- 122
Cdd:cd09007  38 YRLEYDGEEVGVVGPPVGAPAAVLVLEELIA-LGAKKFIVVGSCGSLDPDLAVGDIILPTSA--------LR--Degtsy 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C      123 H-----DFAAiADFDMVRNAVDAAKALGIDARVGNLFSADLFYSpdgEMFDVMEKY---GILGVEMEAAGIYGVAAEFGA 194
Cdd:cd09007 107 HylppsRYIE-PDPELLDALEEALEKAGIPYVRGKTWTTDAPYR---ETRAKVARRraeGCLAVEMEAAALFAVAQFRGV 182

                       170       180       190
                ....*....|....*....|....*....|....*...
1OVG_C      195 KALTICTVSDHI--RTHEQTTAAERQTTFNDMIKIALE 230
Cdd:cd09007 183 ELAQLLYVSDSLagEEWDPRGRDEGKDAREKALELALE 220
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 33-204 2.67e-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: 2.67e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C       33 LEDAREVNnVRGMLGFTGTYKGRKISVMGHGVGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKLRDVVIGmgactd 112
Cdd:COG0775  20 LEDKKEVQ-IAGFTFYLGTLGGKEVVLVNSGIGKVNAATATTLLIARFRPDAVINTGVAGGLDPDLKIGDVVLA------ 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C      113 skvNRIRFKDHDFAAI---------------ADFDMVRNAVDAAKALGIDARVGNLFSADLFYSPDGEMFDVMEKY-GIL 176
Cdd:COG0775  93 ---TEVVQHDVDVTAFgyprgqvpgmpalfeADPALLEAAKEAAKESGLKVVTGTIATGDRFVWSAEEKRRLRERFpGAL 169

                       170       180
                ....*....|....*....|....*...
1OVG_C      177 GVEMEAAGIYGVAAEFGAKALTICTVSD 204
Cdd:COG0775 170 AVDMEGAAIAQVCYRFGVPFLVIRAISD 197
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
 20-217 4.37e-14

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: 69.53  E-value: 4.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C       20 GDPLRAKYIAETFLEDA--REVNNVRGMLGFTGTYKGRKISVMGHGVGIPSCsiytkelitDFGVKK----------IIR 87
Cdd:cd17769   7 GDPARARLIAKLLDKEPkvFELTSERGFLTITGRYKGVPVSIVAIGMGAPMM---------DFFVREaravvdgpmaIIR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C       88 VGSCGAVLPHVKLRDVVIGMGACTdskVNRIRFKDHDFAA--------------IADFD--------MVRNAVDAAKALG 145
Cdd:cd17769  78 LGSCGSLDPDVPVGSVVVPSASVA---VTRNYDDDDFAGPstssekpyliskpvPADPElselleseLKASLGGEVVVEG 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C      146 IDArvgnlfSADLFYSPDG---EMFD---------VMEKY-GILGVEMEAAGIYGVAAEFGAKALTICTVSDHIR----- 207
Cdd:cd17769 155 LNA------SADSFYSSQGrqdPNFPdhnenlidkLLKRYpGAASLEMETFHLFHLARCSRPAQGKIRAAAAHMVfanrt 228

                       250
                ....*....|....*
1OVG_C      208 -----THEQTTAAER 217
Cdd:cd17769 229 sndfiSPERVHELER 243
PRK14697 PRK14697
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; ...
 37-228 4.28e-10

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


Pssm-ID: 184794  Cd Length: 233  Bit Score: 58.10  E-value: 4.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C        37 REVNNVRGMLGFTGTYKGRKISVMGHGVGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKLRDVVIGMGAcTDSKVN 116
Cdd:PRK14697  24 QEEQIIAGMPFYVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLHPDVKVGDIVISTNV-THHDVS 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C       117 RIRFKD-----HDFAAIADF-DMVRNAVDAAkALGIDARVGNLFSADLFYSPDGEMFDVMEKYGILGVEMEAAGIYGVAA 190
Cdd:PRK14697 103 KTQMKNlfpfqEEFIASKELvELARKACNSS-SLHIEIHEGRIVSGECFVEDSKLKAKLIDEYAPHCTEMEGAAIGHVAY 181

                        170       180       190
                 ....*....|....*....|....*....|....*...
1OVG_C       191 EFGAKALTICTVSDhirtheqTTAAERQTTFNDMIKIA 228
Cdd:PRK14697 182 INEVPFLVIRCISD-------SADDEAQISYDDFAKTA 212
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
21-204 3.95e-09

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 55.13  E-value: 3.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C        21 DPLRAKyiaetfLEDAREVNnVRGMLGFTGTYKGRKISVMGHGVGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKL 100
Cdd:PRK05584  14 TLLLDK------LENAQTIT-LAGREFYTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDAVINTGVAGGLAPGLKV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C       101 RDVVIGmgactdskvNRIRFKDHDFAAI---------------ADFDMVRNAVDAAKALGIDARVGNLFSADLFYSpDGE 165
Cdd:PRK05584  87 GDVVVA---------DELVQHDVDVTAFgypygqvpglpaafkADEKLVALAEKAAKELNLNVHRGLIASGDQFIA-GAE 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
1OVG_C       166 MFDVMEK--YGILGVEMEAAGIYGVAAEFGAKALTICTVSD 204
Cdd:PRK05584 157 KVAAIRAefPDALAVEMEGAAIAQVCHEFGVPFVVVRAISD 197
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
 37-228 5.12e-08

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


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 52.71  E-value: 5.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C        37 REVNNVRGMLGFTGTYKGRKISVMGHGVGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKLRDVVIGMGAC-TDSKV 115
Cdd:PRK06698  24 QEEQIIAGMPFYVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLHPDVKVGDIVISTNVThHDVSK 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C       116 NRIR----FKDHDFAAIADFDMVRNAVDAAkALGIDARVGNLFSADLFYSPDGEMFDVMEKYGILGVEMEAAGIYGVAAE 191
Cdd:PRK06698 104 TQMKnlfpFQEEFIASKELVELARKACNSS-SLHMEIHEGRIVSGECFVEDSKLKAKLIDEYAPHCTEMEGAAIGHVAYI 182

                        170       180       190
                 ....*....|....*....|....*....|....*..
1OVG_C       192 FGAKALTICTVSDhirtheqTTAAERQTTFNDMIKIA 228
Cdd:PRK06698 183 NEVPFLVIRCISD-------SADDEAQISYDDFAKTA 212
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 48-204 1.61e-07

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: 50.37  E-value: 1.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C       48 FTGTYKGRKISVMGHGVGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKLRDVVIGmgactdskvNRIRFKDHDFAA 127
Cdd:cd17877  32 YRGTLGGHPVVLVESGMGKANAARAAQLLLEHFQPDLIISTGFAGGLDPGLAVGDLVIA---------DRVLYHDGDVPA 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C      128 I--ADFDMVRNAVDAAKALGIDARVGNLFSADLFY-SPDGEMFdVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSD 204
Cdd:cd17877 103 GleADEKLVALAEELAAGLNLKVHRGTIITVDAIVrKSAEKAA-LAARFPALAVDMESAAIAQVAAARGIPFLAIRAISD 181
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
 1-200 2.67e-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: 47.06  E-value: 2.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C          1 ATPHINAEMGDfADVVLMPGDPLRAKYIAETFLEDA--REVNNVRGMLGFTGTYKGRKIS---VMGHGVGIPSCSIYTKE 75
Cdd:TIGR01719  20 STHDFPAVFGD-VKFVCMGGTPSRMKAFARYVGAELglSCGRDYPNISERGDRFAMYKVGpvlCVSHGMGIPSISIMLHE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C         76 LITDF---GVKK--IIRVGSCGAVlpHVKLRDVVI---GMGACTDSKVNRIRFKDHDF-AAIADFDMVRNAVDAAKAL-- 144
Cdd:TIGR01719  99 LIKLLyyaRCKNptFIRIGTSGGI--GVPPGTVVVsseAVDACLKPEYEQIVLGKRVIrPTQLDEALVQELLLCGAEGld 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1OVG_C        145 GIDARVGNLFSADLFYSP----DGEMFDVMEK-----------YGILGVEMEAAGIYGVAAEFGAKALTIC 200
Cdd:TIGR01719 177 EFTTVSGNTMCTDDFYEGqgrlDGAFCEYTEKdkmaylrklyaLGVRNIEMESSMFAAMTSRAGFKAAVVC 247
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
 12-200 1.97e-05

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: 44.45  E-value: 1.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C       12 FADV--VLMPGDPLRAKYIAETFLEDAR-EVNNVRGMLGFTGT------YK-GRKISVmGHGVGIPSCSIYTKELI---- 77
Cdd:cd17763  20 FGDVkfVCMGGSPGRMENFAEYLAKELGiKLPAGAALVNLSKTtdrysmYKvGPVLSV-SHGMGIPSLSILLHELIkllh 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C       78 ----TDFgvkKIIRVGSCGAVlpHVKLRDVVIgmgacTDSKVN---------RIRFKDHDFAAIADFDMVRNAVDAAKAL 144
Cdd:cd17763  99 yagcKDV---TFIRIGTSGGI--GVEPGTVVI-----TTEAVDgelepfyeqVILGKVVKRPAVLDAQLAEELLECAKEL 168

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1OVG_C      145 G-IDARVGNLFSADLFYSP----DG--------EMFDVMEK---YGILGVEMEAAGIYGVAAEFGAKALTIC 200
Cdd:cd17763 169 DdFPTVIGKTMCANDFYEGqgrlDGafcdyteeDKMAFLQKlydAGVRNIEMESLCFAAFCHRAGIKAAVVC 240
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
 49-204 1.81e-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: 41.63  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C         49 TGTYKGRKISVMGHGVGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKLRDVVIGmgacTDSKVNRIRFKDHDF--- 125
Cdd:TIGR01704  34 TGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLAPTLKVGDIVVS----DEARYHDADVTAFGYeyg 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C        126 -------AAIADFDMVRNAVDAAKALGIDARVGNLFSADLFYSPDGEMFDVMEKYGIL-GVEMEAAGIYGVAAEFGAKAL 197
Cdd:TIGR01704 110 qlpgcpaGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKIRHNFPQAiAVEMEATAIAHVCHNFNVPFV 189


                  ....*..
1OVG_C        198 TICTVSD 204
Cdd:TIGR01704 190 VVRAISD 196
PRK04148 PRK04148
hypothetical protein; Provisional
 96-175 7.05e-03

hypothetical protein; Provisional


Pssm-ID: 235226  Cd Length: 134  Bit Score: 35.75  E-value: 7.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1OVG_C        96 PHVKLRDVV-IGMGACTDskvNRIRFKDHDFAAIAdFDMVRNAVDAAKALGIDARVGNLFS--------ADLFYS----P 162
Cdd:PRK04148  13 EKGKNKKIVeLGIGFYFK---VAKKLKESGFDVIV-IDINEKAVEKAKKLGLNAFVDDLFNpnleiyknAKLIYSirppR 88

                         90
                 ....*....|....*
1OVG_C       163 DGEMF--DVMEKYGI 175
Cdd:PRK04148  89 DLQPFilELAKKINV 103
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH