NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|500942211|ref|WP_012027381|]
View 

purine-nucleoside phosphorylase [Streptococcus suis]

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;
1-237 3.52e-154

DeoD-type purine-nucleoside phosphorylase;


:

Pssm-ID: 180275  Cd Length: 235  Bit Score: 427.35  E-value: 3.52e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211   1 MSIHISAKPGEIADKILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGIPSISIYAHELINEY 80
Cdd:PRK05819   1 MTPHINAKKGDIADTVLMPGDPLRAKYIAETFLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELITDY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  81 GVKKLIRVGTAGSLNEDVHVRELVLAQAAATNSRMINIDWPEYDLPQIADFDLLDKAYHIAKELNMTTHVGNVLSSDSFY 160
Cdd:PRK05819  81 GVKKLIRVGSCGALQEDVKVRDVVIAMGASTDSNVNRIRFKGHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLFY 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500942211 161 SPKlFSRNLELGQLGVKAVEMEAAALYYLGAKFGVQTLAIMTISDSLVNpEEDTTAEERQNTFTDMMKVGLETLIAE 237
Cdd:PRK05819 161 NPD-PEMFDVLEKYGVLGVEMEAAALYGLAAKYGVKALTILTVSDHIVT-GEATTAEERQTTFNDMIEIALESAILG 235
 
Name Accession Description Interval E-value
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
1-237 3.52e-154

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 427.35  E-value: 3.52e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211   1 MSIHISAKPGEIADKILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGIPSISIYAHELINEY 80
Cdd:PRK05819   1 MTPHINAKKGDIADTVLMPGDPLRAKYIAETFLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELITDY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  81 GVKKLIRVGTAGSLNEDVHVRELVLAQAAATNSRMINIDWPEYDLPQIADFDLLDKAYHIAKELNMTTHVGNVLSSDSFY 160
Cdd:PRK05819  81 GVKKLIRVGSCGALQEDVKVRDVVIAMGASTDSNVNRIRFKGHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLFY 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500942211 161 SPKlFSRNLELGQLGVKAVEMEAAALYYLGAKFGVQTLAIMTISDSLVNpEEDTTAEERQNTFTDMMKVGLETLIAE 237
Cdd:PRK05819 161 NPD-PEMFDVLEKYGVLGVEMEAAALYGLAAKYGVKALTILTVSDHIVT-GEATTAEERQTTFNDMIEIALESAILG 235
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
1-236 3.46e-150

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: 417.21  E-value: 3.46e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211   1 MSIHISAKPGEIADKILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGIPSISIYAHELINEY 80
Cdd:COG0813    2 MTPHIGAKKGDIAETVLLPGDPLRAKYIAETFLEDAVLVNEVRGMLGYTGTYKGKRVSVMGSGMGIPSISIYAYELITEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  81 GVKKLIRVGTAGSLNEDVHVRELVLAQAAATNSRMINIDWPEYDLPQIADFDLLDKAYHIAKELNMTTHVGNVLSSDSFY 160
Cdd:COG0813   82 GVKNIIRVGTCGALQEDVKVRDVVIAMGASTDSNVNRQRFGGGDFAPIADFELLRKAVEAAKELGIKVHVGNVFSSDLFY 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500942211 161 SPKLfSRNLELGQLGVKAVEMEAAALYYLGAKFGVQTLAIMTISDSLVNPEEdTTAEERQNTFTDMMKVGLETLIA 236
Cdd:COG0813  162 REDP-DLLEKLAKYGVLAVEMEAAALYTLAAKYGKRALAILTVSDHLVTGEE-TTAEERQTTFNDMMEIALEAALK 235
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
4-233 9.20e-141

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: 393.31  E-value: 9.20e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211   4 HISAKPGEIADKILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGIPSISIYAHELINEYGVK 83
Cdd:cd09006    1 HIEAKKGDIAKTVLMPGDPLRAKYIAETFLEDAKLVNSVRNMLGYTGTYKGKRVSVMGSGMGMPSIGIYAYELFKFYGVK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  84 KLIRVGTAGSLNEDVHVRELVLAQAAATNSRMINIDWPEYDLPQIADFDLLDKAYHIAKELNMTTHVGNVLSSDSFYSPK 163
Cdd:cd09006   81 NIIRIGTCGAYQPDLKLRDVVLAMGASTDSNYNRLRFGGGDFAPIADFELLRKAVETAKELGIPVHVGNVFSSDVFYDDD 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211 164 lFSRNLELGQLGVKAVEMEAAALYYLGAKFGVQTLAIMTISDSLVNPEEdTTAEERQNTFTDMMKVGLET 233
Cdd:cd09006  161 -PELWKKLKKYGVLAVEMEAAALYTNAARLGKKALAILTVSDSLVTGEE-LSAEERETSFTNMIELALET 228
deoD TIGR00107
purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called ...
4-232 1.95e-93

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: 273.57  E-value: 1.95e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211    4 HISAKPGEIADKILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGIPSISIYAHELINEYGVK 83
Cdd:TIGR00107   1 HINAKKGDIADVVLMPGDPLRAKYIAETFLEDVREVNEVRGMLGFTGTYKGKKISVMGHGMGIPSISIYVYELIKFYEVK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211   84 KLIRVGTAGSLNEDVHVRELVLAQAAATNSRMINIDWPEYDLPQIADFDLLDKAYHIAKELNMTTHVGNVLSSDSFYSPK 163
Cdd:TIGR00107  81 TIIRVGSCGAIRPDVKLRDVIIAMGASTDSKYNRVRFVEVDFAAIADFELVENAYDAAKAKGVDVHVGNVFSADAFYQPD 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500942211  164 LFSRNLeLGQLGVKAVEMEAAALYYLGAKFGVQTLAIMTISDSLVNPEEdTTAEERQNTFTDMMKVGLE 232
Cdd:TIGR00107 161 KDVFDL-MAKYGILGVEMEAAALYANAAELGAKALTILTVSDHLVTHEA-TTAEERQTTFKDMIILALE 227
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
16-236 1.01e-43

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: 147.11  E-value: 1.01e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211   16 ILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGIPSISI-YAHELINEYGVKKLIRVGTAGSL 94
Cdd:pfam01048   3 AIIGGSPEELALLAELLDDETPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAIlAAIRLLKEFGVDAIIRTGTAGGL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211   95 NEDVHVRELVLAQAAA---TNSRMINIDWPEYDLPQ---IADFDLLDKAYHIAKELNMTTHVGNVLSSDSFYSPKLfSRN 168
Cdd:pfam01048  83 NPDLKVGDVVIPTDAInhdGRSPLFGPEGGPYFPDMapaPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETP-AEI 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500942211  169 LELGQLGVKAVEMEAAALYYLGAKFGVQTLAIMTISDSLVnpeEDTTAEERQNTFTDMMKVGLETLIA 236
Cdd:pfam01048 162 RLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSDLAA---GGADGELTHEEVEEFAERAAERAAA 226
 
Name Accession Description Interval E-value
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
1-237 3.52e-154

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 427.35  E-value: 3.52e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211   1 MSIHISAKPGEIADKILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGIPSISIYAHELINEY 80
Cdd:PRK05819   1 MTPHINAKKGDIADTVLMPGDPLRAKYIAETFLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELITDY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  81 GVKKLIRVGTAGSLNEDVHVRELVLAQAAATNSRMINIDWPEYDLPQIADFDLLDKAYHIAKELNMTTHVGNVLSSDSFY 160
Cdd:PRK05819  81 GVKKLIRVGSCGALQEDVKVRDVVIAMGASTDSNVNRIRFKGHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLFY 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500942211 161 SPKlFSRNLELGQLGVKAVEMEAAALYYLGAKFGVQTLAIMTISDSLVNpEEDTTAEERQNTFTDMMKVGLETLIAE 237
Cdd:PRK05819 161 NPD-PEMFDVLEKYGVLGVEMEAAALYGLAAKYGVKALTILTVSDHIVT-GEATTAEERQTTFNDMIEIALESAILG 235
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
1-236 3.46e-150

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: 417.21  E-value: 3.46e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211   1 MSIHISAKPGEIADKILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGIPSISIYAHELINEY 80
Cdd:COG0813    2 MTPHIGAKKGDIAETVLLPGDPLRAKYIAETFLEDAVLVNEVRGMLGYTGTYKGKRVSVMGSGMGIPSISIYAYELITEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  81 GVKKLIRVGTAGSLNEDVHVRELVLAQAAATNSRMINIDWPEYDLPQIADFDLLDKAYHIAKELNMTTHVGNVLSSDSFY 160
Cdd:COG0813   82 GVKNIIRVGTCGALQEDVKVRDVVIAMGASTDSNVNRQRFGGGDFAPIADFELLRKAVEAAKELGIKVHVGNVFSSDLFY 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500942211 161 SPKLfSRNLELGQLGVKAVEMEAAALYYLGAKFGVQTLAIMTISDSLVNPEEdTTAEERQNTFTDMMKVGLETLIA 236
Cdd:COG0813  162 REDP-DLLEKLAKYGVLAVEMEAAALYTLAAKYGKRALAILTVSDHLVTGEE-TTAEERQTTFNDMMEIALEAALK 235
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
4-233 9.20e-141

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: 393.31  E-value: 9.20e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211   4 HISAKPGEIADKILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGIPSISIYAHELINEYGVK 83
Cdd:cd09006    1 HIEAKKGDIAKTVLMPGDPLRAKYIAETFLEDAKLVNSVRNMLGYTGTYKGKRVSVMGSGMGMPSIGIYAYELFKFYGVK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  84 KLIRVGTAGSLNEDVHVRELVLAQAAATNSRMINIDWPEYDLPQIADFDLLDKAYHIAKELNMTTHVGNVLSSDSFYSPK 163
Cdd:cd09006   81 NIIRIGTCGAYQPDLKLRDVVLAMGASTDSNYNRLRFGGGDFAPIADFELLRKAVETAKELGIPVHVGNVFSSDVFYDDD 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211 164 lFSRNLELGQLGVKAVEMEAAALYYLGAKFGVQTLAIMTISDSLVNPEEdTTAEERQNTFTDMMKVGLET 233
Cdd:cd09006  161 -PELWKKLKKYGVLAVEMEAAALYTNAARLGKKALAILTVSDSLVTGEE-LSAEERETSFTNMIELALET 228
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
1-233 3.15e-107

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 308.57  E-value: 3.15e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211   1 MSIHISAKPGEIADKILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGIPSISIYAHELINEY 80
Cdd:PRK13374   2 STPHINAQPGDFAETVLMPGDPLRAKYIAETYLEDVVQVTDVRNMFGFTGTYKGKKVSVMGHGMGIPSMVIYVHELIATF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  81 GVKKLIRVGTAGSLNEDVHVRELVLAQAAATNSRMINIDWPEYDLPQIADFDLLDKAYHIAKELNMTTHVGNVLSSDSFY 160
Cdd:PRK13374  82 GVKNIIRVGSCGATQDDVKLMDVIIAQGASTDSKTNRIRFSGHDFAAIADYQLLEKAVETAREKGVPVKVGNVFSSDLFY 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500942211 161 SPK--LFSRnleLGQLGVKAVEMEAAALYYLGAKFGVQTLAIMTISDSLVNPEEdTTAEERQNTFTDMMKVGLET 233
Cdd:PRK13374 162 DPDedAIEA---MERFGILGVDMEVAGLYGLAAYLGAEALAILTVSDHIITGEE-TTAEERQLSFNDMIEVALET 232
deoD TIGR00107
purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called ...
4-232 1.95e-93

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: 273.57  E-value: 1.95e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211    4 HISAKPGEIADKILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGIPSISIYAHELINEYGVK 83
Cdd:TIGR00107   1 HINAKKGDIADVVLMPGDPLRAKYIAETFLEDVREVNEVRGMLGFTGTYKGKKISVMGHGMGIPSISIYVYELIKFYEVK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211   84 KLIRVGTAGSLNEDVHVRELVLAQAAATNSRMINIDWPEYDLPQIADFDLLDKAYHIAKELNMTTHVGNVLSSDSFYSPK 163
Cdd:TIGR00107  81 TIIRVGSCGAIRPDVKLRDVIIAMGASTDSKYNRVRFVEVDFAAIADFELVENAYDAAKAKGVDVHVGNVFSADAFYQPD 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500942211  164 LFSRNLeLGQLGVKAVEMEAAALYYLGAKFGVQTLAIMTISDSLVNPEEdTTAEERQNTFTDMMKVGLE 232
Cdd:TIGR00107 161 KDVFDL-MAKYGILGVEMEAAALYANAAELGAKALTILTVSDHLVTHEA-TTAEERQTTFKDMIILALE 227
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
1-236 3.38e-85

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: 253.00  E-value: 3.38e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211   1 MSIHISAKPGEIADKILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGIPSISIYAHELInEY 80
Cdd:cd17765    1 MPIHIRAEPGDVAEAVLLPGDPGRATYIAETFFDGPRLYNDHRGLLGYTGTYKGKPVSVQTTGMGCPSAAIVVEELA-QL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  81 GVKKLIRVGTAGSLNEDVHVRELVLAQAAATNSRMINIDWPEYDLPQIADFDLLDKAYHIAKELNMTTHVGNVLSSDSFY 160
Cdd:cd17765   80 GVKRLIRVGTCGGLSSGLQLGDLIVATAAVPADGTTRALLGGEPYAPAADFELVEALYRAARAAGMPVHVGPVATSDLFY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500942211 161 SPKlFSRNLELGQLGVKAVEMEAAALYYLGAKFGVQTLAIMTISDSLVNPEEDTTAEERQNTFTDMMKVGLETLIA 236
Cdd:cd17765  160 DPT-PDGVKRWRRRGVLAVEMEASALFTLAALRGLRAGCILTVSDLIGDPERRIDDEELRAGVDRMTEVALEAVVA 234
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
4-235 3.32e-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: 3.32e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211   4 HISAKPGEIADKILLPGDPLRAKFIAEnFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGIPSISIYAHELINeYGVK 83
Cdd:cd17767    2 HIGLKPGDVAPYVLLPGDPGRVERIAE-LLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELAQ-LGAK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  84 KLIRVGTAGSLNEDVHVRELVLAQAAA----TNSRMInidWPEYdlPQIADFDLLDKAYHIAKELNMTTHVGNVLSSDSF 159
Cdd:cd17767   80 TFIRVGTCGALQPDIKLGDLVIATGAVrdegTSKHYV---PPEY--PAVADPEVVLALVEAAEELGVPYHVGITASKDSF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211 160 Y------SPKLFSRNLE----LGQLGVKAVEMEAAALYYLGAKFGVQTLAIMTISDSLVNpEEDTTAEERQNTFTDMMKV 229
Cdd:cd17767  155 YggqgrpGPGLPPELPElleeWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVT-DEAPDEEDVAAGEERAIRV 233

                 ....*.
gi 500942211 230 GLETLI 235
Cdd:cd17767  234 ALEALK 239
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
4-235 4.95e-61

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 191.92  E-value: 4.95e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211   4 HISAKPGEIADKILLPGDPLRAKFIAEnFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGIPSISIYAHELINeYGVK 83
Cdd:COG2820   13 HLGLKPGDVADYVILPGDPGRVELIAS-YLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIAVEELAA-LGAK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  84 KLIRVGTAGSLNEDVHVRELVLAQAAATNSRMIN-IDWPEYdlPQIADFDLLDKAYHIAKELNMTTHVGNVLSSDSFYSP 162
Cdd:COG2820   91 TFIRVGTSGALQPDIPVGDLVIATGAVRLDGTSNfYAPAEY--PAVADFELTRALVEAAEELGVDYHVGITASTDGFYAE 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211 163 KLFSRNL---------ELGQLGVKAVEMEAAALYYLGAKFGVQTLAIMTISDslvNPEEDTTAEERQNTFTDMMKVGLET 233
Cdd:COG2820  169 QGRELRVdpdldekleAWRKLGVLNVEMETAALFTLARLRGHRAGSVLAVSA---NRVTGEFSKDPEEAVERAIKVALEA 245

                 ..
gi 500942211 234 LI 235
Cdd:COG2820  246 LK 247
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
16-233 7.97e-58

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: 182.49  E-value: 7.97e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  16 ILLPGDPLRAKFIAEnFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGIPSISIYAHELInEYGVKKLIRVGTAGSLN 95
Cdd:cd09005    2 AIIPGDPERVDVIDS-KLENPQKVSSFRGYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEELC-ALGVDTIIRVGSCGALR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  96 EDVHVRELVLAQAAATNSRMINIDWPEYDLPQIADFDLLDKAYHIAKELNMTTHVGNVLSSDSFY-SPKLFSRNleLGQL 174
Cdd:cd09005   80 EDIKVGDLVIADGAIRGDGVTPYYVVGPPFAPEADPELTAALEEAAKELGLTVHVGTVWTTDAFYrETREESEK--LRKL 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 500942211 175 GVKAVEMEAAALYYLGAKFGVQTLAIMTISDSLVNPEEDTTAEERQNTFTDMMKVGLET 233
Cdd:cd09005  158 GALAVEMETSALATLAHLRGVKAASILAVSDNLITGEIGFVDEFLSEAEKKAIEIALDA 216
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
14-234 2.00e-49

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: 161.24  E-value: 2.00e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  14 DKILLPGDPLRAKFIAEnFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGIPSISIYAHELInEYGVKKLIRVGTAGS 93
Cdd:cd17764    1 ERVIAVGDPGRVELLST-LLEDPRLVNENRGLLVYTGKYKGEEVTIATHGIGGPSAAIVFEELI-MLGAKVIIRLGTAGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  94 LNEDVHVRELVLAQAAA-TNSRMINIDWPEYDLPQIADFDLLDKAYHIAKELNMTTHVGNVLSSDSFYS-PKLFSRnlEL 171
Cdd:cd17764   79 LVPELRVGDIVVATGASyYPGGGLGQYFPDVCPPASPDPELTLELVESLSKRGLKYYVGPVFSSDAFYAeDEEFAE--RW 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500942211 172 GQLGVKAVEMEAAALYYLGAKFGVQTLAIMTISDSLVNPEEDT-TAEERQNTFTDMMKVGLETL 234
Cdd:cd17764  157 SSLGFIAVEMECATLFTLGWLRGVKAGAVLVVSDNLVKGGKLMlTKEELEEKVMKAAKAVLEAL 220
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
16-236 1.01e-43

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: 147.11  E-value: 1.01e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211   16 ILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGIPSISI-YAHELINEYGVKKLIRVGTAGSL 94
Cdd:pfam01048   3 AIIGGSPEELALLAELLDDETPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAIlAAIRLLKEFGVDAIIRTGTAGGL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211   95 NEDVHVRELVLAQAAA---TNSRMINIDWPEYDLPQ---IADFDLLDKAYHIAKELNMTTHVGNVLSSDSFYSPKLfSRN 168
Cdd:pfam01048  83 NPDLKVGDVVIPTDAInhdGRSPLFGPEGGPYFPDMapaPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETP-AEI 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500942211  169 LELGQLGVKAVEMEAAALYYLGAKFGVQTLAIMTISDSLVnpeEDTTAEERQNTFTDMMKVGLETLIA 236
Cdd:pfam01048 162 RLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSDLAA---GGADGELTHEEVEEFAERAAERAAA 226
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
2-234 3.10e-26

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: 102.55  E-value: 3.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211   2 SI-HISAKPGEIADKILLPGDPLRAKFIAENFleDAVCF-NEVRNMFGYTGTYKGHRVSVMGTGMGIPSISIYAHEL--I 77
Cdd:cd00436    9 SIyHLHLKPEDLADTIILVGDPGRVPKVSKHF--DSIEFkKQNREFVTHTGTYKGKRITVISTGIGTDNIDIVLNELdaL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  78 NEYGVK-----------KLIRVGTAGSLNEDVHVRELVLAQAAatnsrmINID-------WPEYD---------LPQIAD 130
Cdd:cd00436   87 VNIDFKtrtpkeektslNIIRLGTSGALQPDIPVGSLVISSYA------IGLDnllnfydHPNTDeeaelenafIAHTSW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211 131 FDLLDKAYHIAKELNMT-------THVGNVLSSDSFYSP-------KLFSRNL--ELGQLGVKAV-----EMEAAALYYL 189
Cdd:cd00436  161 FKGKPRPYVVKASPELLdaltgvgYVVGITATAPGFYGPqgrqlrlPLADPDLldKLSSFSYGGLritnfEMETSAIYGL 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 500942211 190 GAKFGVQTLAIMTIsdsLVNPEEDTTAEERQNTFTDMMKVGLETL 234
Cdd:cd00436  241 SRLLGHRALSICAI---IANRATGEFSKDYKKAVEKLIEKVLEAL 282
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
48-205 1.17e-22

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: 92.28  E-value: 1.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  48 YTGTYKGHRVSVMGTGMGIPSISIYAHELINEYGVKKLIRVGTAGSLNEDVHVRELVLAQAA------ATNSRMINIDWP 121
Cdd:COG0775   34 YLGTLGGKEVVLVNSGIGKVNAATATTLLIARFRPDAVINTGVAGGLDPDLKIGDVVLATEVvqhdvdVTAFGYPRGQVP 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211 122 EYDLPQIADFDLLDKAYHIAKELNMTTHVGNVLSSDSFYSPKLFSRNLELGQLGVKAVEMEAAALYYLGAKFGVQTLAIM 201
Cdd:COG0775  114 GMPALFEADPALLEAAKEAAKESGLKVVTGTIATGDRFVWSAEEKRRLRERFPGALAVDMEGAAIAQVCYRFGVPFLVIR 193

                 ....
gi 500942211 202 TISD 205
Cdd:COG0775  194 AISD 197
PRK11178 PRK11178
uridine phosphorylase; Provisional
17-214 2.62e-21

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 88.95  E-value: 2.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  17 LLPGDPLRAKFIAEnFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGIPSISIYAHELiNEYGVKKLIRVGTAGSLNE 96
Cdd:PRK11178  21 IVPGDPERVEKIAA-LMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEEL-AQLGVRTFLRIGTTGAIQP 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  97 DVHVRELVLAQAAatnsrmINID-----WPEYDLPQIADFDLLDKAYHIAKELNMTTHVGNVLSSDSFY---------SP 162
Cdd:PRK11178  99 HINVGDVLVTTAS------VRLDgaslhFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYpgqerydtySG 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500942211 163 KLFSR---NLELGQ-LGVKAVEMEAAALYYLGAKFGVQtlAIMtISDSLVN------PEEDT 214
Cdd:PRK11178 173 RVVRRfkgSMEEWQaMGVMNYEMESATLLTMCASQGLR--AGM-VAGVIVNrtqqeiPNAET 231
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
48-218 3.60e-21

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: 87.94  E-value: 3.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  48 YTGTYKGHRVSVMGTGMGIPSISIYAHELINEYGVKKLIRVGTAGSLNEDVHVRELVLAqaaatnSRMINID----WPEY 123
Cdd:cd09008   32 YEGTLGGKEVVLVQSGIGKVNAAIATQLLIDRFKPDAIINTGVAGGLDPDLKIGDVVIA------TKVVYHDvdatAFGY 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211 124 DLPQI--------ADFDLLDKAYHIAKELNMTTHVGNVLSSDSFYSPKLFSRNLeLGQLGVKAVEMEAAALYYLGAKFGV 195
Cdd:cd09008  106 EGGQPpgmpayfpADPELLELAKKAAKELGPKVHTGLIASGDQFVASSEKKEEL-RENFPALAVEMEGAAIAQVCYLNGV 184
                        170       180
                 ....*....|....*....|...
gi 500942211 196 QTLAIMTISDsLVNPEEDTTAEE 218
Cdd:cd09008  185 PFLVIRSISD-LADGEADEDFEE 206
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
16-191 4.64e-21

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: 88.40  E-value: 4.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  16 ILLPGDPLRAKFIAENFLEDAVCFnEV---RNMFGYTGTYKGHRVSVMGTGMGIPSI--------SIYAHELIneygvkk 84
Cdd:cd17769    3 IITVGDPARARLIAKLLDKEPKVF-ELtseRGFLTITGRYKGVPVSIVAIGMGAPMMdffvrearAVVDGPMA------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  85 LIRVGTAGSLNEDVHVRELVLAQAAATNSRmiNIDWPEYD-------------LPQIADFDLLDKAYHIAKELNMTTHVG 151
Cdd:cd17769   75 IIRLGSCGSLDPDVPVGSVVVPSASVAVTR--NYDDDDFAgpstssekpylisKPVPADPELSELLESELKASLGGEVVV 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 500942211 152 NVL--SSDSFYS-----------------PKLFSRNLELGQLgvkavEMEAAALYYLGA 191
Cdd:cd17769  153 EGLnaSADSFYSsqgrqdpnfpdhnenliDKLLKRYPGAASL-----EMETFHLFHLAR 206
NP-I_spr0068 cd09007
uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed ...
16-233 1.13e-20

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: 86.38  E-value: 1.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  16 ILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGIPSISIYAHELInEYGVKKLIRVGTAGSLN 95
Cdd:cd09007    6 VLVFSGDLLEYLLEEYGAEKIGELSSAGHTPLYRLEYDGEEVGVVGPPVGAPAAVLVLEELI-ALGAKKFIVVGSCGSLD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  96 EDVHVRELVLAQAA----------ATNSRMInidwpeydlpqIADFDLLDKAYHIAKELNMTTHVGNVLSSDSFY--SPK 163
Cdd:cd09007   85 PDLAVGDIILPTSAlrdegtsyhyLPPSRYI-----------EPDPELLDALEEALEKAGIPYVRGKTWTTDAPYreTRA 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500942211 164 LFSRnleLGQLGVKAVEMEAAALYYLGAKFGVQTLAIMTISDSLVNPEEDT-TAEERQNTFTDMMKVGLET 233
Cdd:cd09007  154 KVAR---RRAEGCLAVEMEAAALFAVAQFRGVELAQLLYVSDSLAGEEWDPrGRDEGKDAREKALELALEA 221
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
5-205 3.10e-15

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 72.08  E-value: 3.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211   5 ISAKPGEIAdkillpgdPLRAKfiaenfLEDAVCFNEVRNMFgYTGTYKGHRVSVMGTGMGIPSISIYAHELINEYGVKK 84
Cdd:PRK05584   6 IGAMEEEVT--------LLLDK------LENAQTITLAGREF-YTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  85 LIRVGTAGSLNEDVHVRELVLAQ--------AAAtnsrminIDWPEYDLPQ-----IADFDLLDKAYHIAKELNMTTHVG 151
Cdd:PRK05584  71 VINTGVAGGLAPGLKVGDVVVADelvqhdvdVTA-------FGYPYGQVPGlpaafKADEKLVALAEKAAKELNLNVHRG 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 500942211 152 NVLSSDSFYSPKLFSRNLELGQLGVKAVEMEAAALYYLGAKFGVQTLAIMTISD 205
Cdd:PRK05584 144 LIASGDQFIAGAEKVAAIRAEFPDALAVEMEGAAIAQVCHEFGVPFVVVRAISD 197
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
48-205 2.68e-14

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: 69.24  E-value: 2.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  48 YTGTYKGHRVSVMGTGMGIPSISIYAHELINEYGVKKLIRVGTAGSLNEDVHVRELVLAQAAAtnsrminiDWPEYDLPQ 127
Cdd:cd17877   32 YRGTLGGHPVVLVESGMGKANAARAAQLLLEHFQPDLIISTGFAGGLDPGLAVGDLVIADRVL--------YHDGDVPAG 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211 128 IA-DFDLLDKAYHIAKELNMTTHVGNVLSSDSF-----YSPKLFSRNlelgqlGVKAVEMEAAALYYLGAKFGVQTLAIM 201
Cdd:cd17877  104 LEaDEKLVALAEELAAGLNLKVHRGTIITVDAIvrksaEKAALAARF------PALAVDMESAAIAQVAAARGIPFLAIR 177

                 ....
gi 500942211 202 TISD 205
Cdd:cd17877  178 AISD 181
PRK14697 PRK14697
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; ...
48-206 2.66e-08

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


Pssm-ID: 184794  Cd Length: 233  Bit Score: 52.71  E-value: 2.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  48 YTGTYKGHRVSVMGTGMGIPSISIYAHELINEYGVKKLIRVGTAGSLNEDVHVRELVLAQaaatnsrmiNIDWPEYDLPQ 127
Cdd:PRK14697  35 YVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLHPDVKVGDIVIST---------NVTHHDVSKTQ 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211 128 IADFDLLDKAYHIAKEL-------------NMTTHVGNVLSSDSFYSPKLFSRNLeLGQLGVKAVEMEAAALYYLGAKFG 194
Cdd:PRK14697 106 MKNLFPFQEEFIASKELvelarkacnssslHIEIHEGRIVSGECFVEDSKLKAKL-IDEYAPHCTEMEGAAIGHVAYINE 184
                        170
                 ....*....|..
gi 500942211 195 VQTLAIMTISDS 206
Cdd:PRK14697 185 VPFLVIRCISDS 196
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
16-196 3.57e-08

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: 52.84  E-value: 3.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211   16 ILLPGDPLRAKFIAENFLEDAV--CFNEVRNMFGYT---GTYKGHRVSVMGTGMGIPSISIYAHELIN---EYGVKK--L 85
Cdd:TIGR01719  34 VCMGGTPSRMKAFARYVGAELGlsCGRDYPNISERGdrfAMYKVGPVLCVSHGMGIPSISIMLHELIKllyYARCKNptF 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211   86 IRVGTAGSLNEDVHVrelVLAQAAATNSRMinidWPEYDL---------PQIADFDLLDKAYHIAKELN--MTTHVGNVL 154
Cdd:TIGR01719 114 IRIGTSGGIGVPPGT---VVVSSEAVDACL----KPEYEQivlgkrvirPTQLDEALVQELLLCGAEGLdeFTTVSGNTM 186
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 500942211  155 SSDSFY-------------SPKLFSRNLE-LGQLGVKAVEMEAAALYYLGAKFGVQ 196
Cdd:TIGR01719 187 CTDDFYegqgrldgafceyTEKDKMAYLRkLYALGVRNIEMESSMFAAMTSRAGFK 242
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
63-186 1.88e-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: 47.53  E-value: 1.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  63 GMGIPSISIYAHELIneygvkKL-----------IRVGTAGSLneDVHVRELVLAQAAATNsrMINidwPEYDL------ 125
Cdd:cd17763   80 GMGIPSLSILLHELI------KLlhyagckdvtfIRIGTSGGI--GVEPGTVVITTEAVDG--ELE---PFYEQvilgkv 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211 126 ---PQIADFDLLDKAYHIAKELNMTTHV-GNVLSSDSFY---------------SPKL-FSRnlELGQLGVKAVEMEAAA 185
Cdd:cd17763  147 vkrPAVLDAQLAEELLECAKELDDFPTViGKTMCANDFYegqgrldgafcdyteEDKMaFLQ--KLYDAGVRNIEMESLC 224

                 .
gi 500942211 186 L 186
Cdd:cd17763  225 F 225
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
49-205 2.59e-06

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: 47.02  E-value: 2.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211   49 TGTYKGHRVSVMGTGMGIPSISIYAHELINEYGVKKLIRVGTAGSLNEDVHVRELVLaqaaATNSRMINIDWPEYD---- 124
Cdd:TIGR01704  34 TGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLAPTLKVGDIVV----SDEARYHDADVTAFGyeyg 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  125 ----LPQ--IADFDLLDKAYHIAKELNMTTHVGNVLSSDSFYSPKLFSRNLELGQLGVKAVEMEAAALYYLGAKFGVQTL 198
Cdd:TIGR01704 110 qlpgCPAgfKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKIRHNFPQAIAVEMEATAIAHVCHNFNVPFV 189

                  ....*..
gi 500942211  199 AIMTISD 205
Cdd:TIGR01704 190 VVRAISD 196
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
48-206 5.27e-06

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


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 46.54  E-value: 5.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  48 YTGTYKGHRVSVMGTGMGIPSISIYAHELINEYGVKKLIRVGTAGSLNEDVHVRELVLAQAAA----TNSRMINIdWPeY 123
Cdd:PRK06698  35 YVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLHPDVKVGDIVISTNVThhdvSKTQMKNL-FP-F 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211 124 DLPQIADFDLLDKAYHI--AKELNMTTHVGNVLSSDSFYSPKLFSRNLeLGQLGVKAVEMEAAALYYLGAKFGVQTLAIM 201
Cdd:PRK06698 113 QEEFIASKELVELARKAcnSSSLHMEIHEGRIVSGECFVEDSKLKAKL-IDEYAPHCTEMEGAAIGHVAYINEVPFLVIR 191

                 ....*
gi 500942211 202 TISDS 206
Cdd:PRK06698 192 CISDS 196
PLN02584 PLN02584
5'-methylthioadenosine nucleosidase
48-221 5.93e-04

5'-methylthioadenosine nucleosidase


Pssm-ID: 178196  Cd Length: 249  Bit Score: 39.99  E-value: 5.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211  48 YTGTYKGHRVSVMGTG----MGIPSISIYAHELINEYGVKKL-----IRVGTAGSLN-EDVHVRELVLAQAAATNSRMIN 117
Cdd:PLN02584  47 YSGTHKGLRVHVVCPGkdkaLGVDSVGTVPASLVTYAAIQALkpdliINAGTAGGFKaKGAAIGDVFLATAVANHDRRIP 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500942211 118 IdwPEYDLPQIADFDLLdKAYHIAKELNMTThvGNVLSSDSFYSPKLFSRNLELGQLGVKavEMEAAALYYLGAKFGVQT 197
Cdd:PLN02584 127 I--PVFDKYGVGTRDAF-PTPNLIKALGLKE--GVLSTGNSLDMTEQDEESIKANDATVK--DMEGAAVAYVADLLKVPA 199
                        170       180
                 ....*....|....*....|....
gi 500942211 198 LAIMTISDsLVNPEEDTTAEERQN 221
Cdd:PLN02584 200 IFVKAVTD-IVDGDKPTAEEFLEN 222
 
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