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Conserved domains on  [gi|664506076|ref|WP_031024513|]
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MULTISPECIES: hypothetical protein [Streptomyces]

Protein Classification

Pfs family protein( domain architecture ID 10002400)

Pfs family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 10-151 5.05e-18

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: 79.18  E-value: 5.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076  10 LLIACALGIEQFALRR----------GGRTT-----PGGPVTVLRTGMGPAAAERSVTRVLAdpALHGAAVLATGFCAGL 74
Cdd:COG0775    3 IGIIGAMEEEVAALLEaledkkevqiAGFTFylgtlGGKEVVLVNSGIGKVNAATATTLLIA--RFRPDAVINTGVAGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076  75 ASGMHPGDLVVAEETRD----------PRGSVPCVGTELLV-KELVRTV------PGRTVHTGPLTGSDHVVRGHERSDL 137
Cdd:COG0775   81 DPDLKIGDVVLATEVVQhdvdvtafgyPRGQVPGMPALFEAdPALLEAAkeaakeSGLKVVTGTIATGDRFVWSAEEKRR 160

                        170
                 ....*....|....*..
gi 664506076 138 LA---TGAIAVDMESAA 151
Cdd:COG0775  161 LRerfPGALAVDMEGAA 177
 
Name Accession Description Interval E-value
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 10-151 5.05e-18

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: 79.18  E-value: 5.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076  10 LLIACALGIEQFALRR----------GGRTT-----PGGPVTVLRTGMGPAAAERSVTRVLAdpALHGAAVLATGFCAGL 74
Cdd:COG0775    3 IGIIGAMEEEVAALLEaledkkevqiAGFTFylgtlGGKEVVLVNSGIGKVNAATATTLLIA--RFRPDAVINTGVAGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076  75 ASGMHPGDLVVAEETRD----------PRGSVPCVGTELLV-KELVRTV------PGRTVHTGPLTGSDHVVRGHERSDL 137
Cdd:COG0775   81 DPDLKIGDVVLATEVVQhdvdvtafgyPRGQVPGMPALFEAdPALLEAAkeaakeSGLKVVTGTIATGDRFVWSAEEKRR 160

                        170
                 ....*....|....*..
gi 664506076 138 LA---TGAIAVDMESAA 151
Cdd:COG0775  161 LRerfPGALAVDMEGAA 177
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 32-151 1.84e-17

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: 77.33  E-value: 1.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076  32 GGPVTVLRTGMGPAAAERSVTRVL--ADPALhgaaVLATGFCAGLASGMHPGDLVVAEETRDPRGSVP--CVGTELLVK- 106
Cdd:cd17877   38 GHPVVLVESGMGKANAARAAQLLLehFQPDL----IISTGFAGGLDPGLAVGDLVIADRVLYHDGDVPagLEADEKLVAl 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 664506076 107 -ELVRTVPGRTVHTGPLTGSDHVVRGHERSDLLA--TGAIAVDMESAA 151
Cdd:cd17877  114 aEELAAGLNLKVHRGTIITVDAIVRKSAEKAALAarFPALAVDMESAA 161
HpnG TIGR03468
hopanoid-associated phosphorylase; The sequences in this family are members of the pfam01048 ...
 22-151 7.90e-14

hopanoid-associated phosphorylase; The sequences in this family are members of the pfam01048 family of phosphorylases typically acting on nucleotide-sugar substrates. The genes of the family modeled here are generally in the same locus with genes involved in the biosynthesis and elaboration of hopene, the cyclization product of the polyisoprenoid squalene. This gene is adjacent to the genes PhnA-E and squalene-hopene cyclase (which would be HpnF) in Zymomonas mobilis and their association with hopene biosynthesis has been noted in the literature. Extending the gene symbol sequence, we suggest the symbol HpnG for the product of this gene. Hopanoids are known to be components of the plasma membrane and to have polar sugar head groups in Z. mobilis and other species.


Pssm-ID: 274594  Cd Length: 212  Bit Score: 67.36  E-value: 7.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076   22 ALRRGGRTTPGGPVTVLRTGMGPAAAERSVTRVLADPAlhgAAVLATGFCAGLASGMHPGDLVVAEETRDPRGSVPCvgT 101
Cdd:TIGR03468   9 GLAFEARIAAGPGLLVCLSGGGPERARAAAARLMAAGA---AGLVSFGTAGALDPALQPGDLVVPEEVRADGDRFPT--D 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 664506076  102 ELLVKELVRTVPGRT-VHTGPLTGSDHVVRGHERSDLL--ATGAIAVDMESAA 151
Cdd:TIGR03468  84 PAWRRRLLEALPAGLrVHRGVLAASDTVVSTAAAKAALarATGAAAVDMESGA 136
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 32-151 2.02e-08

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: 52.73  E-value: 2.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076   32 GGPVTVLRTGMGPA-AAERSVTRVLAdpaLHGA-AVLATGFCAGLASGMHPGDLVVAEETRDPRGSVPCVGTEL------ 103
Cdd:pfam01048  41 GVPVVLVRHGIGPPnAAILAAIRLLK---EFGVdAIIRTGTAGGLNPDLKVGDVVIPTDAINHDGRSPLFGPEGgpyfpd 117

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 664506076  104 ---------LVKELVRTVP--GRTVHTGPLTGSDHVVRG-HERSDLLAT-GAIAVDMESAA 151
Cdd:pfam01048 118 mapapadpeLRALAKEAAErlGIPVHRGVYATGDGFYFEtPAEIRLLRRlGADAVEMETAA 178
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
32-151 8.66e-07

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 47.81  E-value: 8.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076  32 GGPVTVLRTGMGPAAAERSVTrVLADpALHGAAVLATGFCAGLASGMHPGDLVVAEETR----------DPRGSVPCVGT 101
Cdd:PRK05584  40 GHEVVLVLSGIGKVAAALTAT-ILIE-HFKVDAVINTGVAGGLAPGLKVGDVVVADELVqhdvdvtafgYPYGQVPGLPA 117

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076 102 -----ELLVKELVRTVP--GRTVHTGPLTGSDHVVRGHERSDLLAT---GAIAVDMESAA 151
Cdd:PRK05584 118 afkadEKLVALAEKAAKelNLNVHRGLIASGDQFIAGAEKVAAIRAefpDALAVEMEGAA 177
 
Name Accession Description Interval E-value
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 10-151 5.05e-18

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: 79.18  E-value: 5.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076  10 LLIACALGIEQFALRR----------GGRTT-----PGGPVTVLRTGMGPAAAERSVTRVLAdpALHGAAVLATGFCAGL 74
Cdd:COG0775    3 IGIIGAMEEEVAALLEaledkkevqiAGFTFylgtlGGKEVVLVNSGIGKVNAATATTLLIA--RFRPDAVINTGVAGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076  75 ASGMHPGDLVVAEETRD----------PRGSVPCVGTELLV-KELVRTV------PGRTVHTGPLTGSDHVVRGHERSDL 137
Cdd:COG0775   81 DPDLKIGDVVLATEVVQhdvdvtafgyPRGQVPGMPALFEAdPALLEAAkeaakeSGLKVVTGTIATGDRFVWSAEEKRR 160

                        170
                 ....*....|....*..
gi 664506076 138 LA---TGAIAVDMESAA 151
Cdd:COG0775  161 LRerfPGALAVDMEGAA 177
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 32-151 1.84e-17

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: 77.33  E-value: 1.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076  32 GGPVTVLRTGMGPAAAERSVTRVL--ADPALhgaaVLATGFCAGLASGMHPGDLVVAEETRDPRGSVP--CVGTELLVK- 106
Cdd:cd17877   38 GHPVVLVESGMGKANAARAAQLLLehFQPDL----IISTGFAGGLDPGLAVGDLVIADRVLYHDGDVPagLEADEKLVAl 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 664506076 107 -ELVRTVPGRTVHTGPLTGSDHVVRGHERSDLLA--TGAIAVDMESAA 151
Cdd:cd17877  114 aEELAAGLNLKVHRGTIITVDAIVRKSAEKAALAarFPALAVDMESAA 161
adenosylhopane_nucleosidase_HpnG-like cd17768
adenosylhopane nucleosidase which cleaves adenine from adenosylhopane to form ribosyl hopane; ...
 23-151 4.22e-16

adenosylhopane nucleosidase which cleaves adenine from adenosylhopane to form ribosyl hopane; similar to Burkholderia cenocepacia HpnG; adenosylhopane nucleosidase HpnG, catalyzes the second step in hopanoid side-chain biosynthesis. Hopanoids are bacterial membrane lipids. This CD belongs to the PNP_UDP_1 superfamily which includes members which accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. PNP_UDP_1 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). Superfamily members have different physiologically relevant quaternary structures: hexameric such as the trimer-of-dimers arrangement of Shewanella oneidensis MR-1 UP, homotrimeric such as human PNP and Escherichia coli PNPII (XapA), homohexameric (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 PNP_UDP_2 (nucleoside phosphorylase-II family) is a different structural family.


Pssm-ID: 350168  Cd Length: 188  Bit Score: 72.96  E-value: 4.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076  23 LRRGGRTTPGGPVTVLRTGMGPAAAERSVTRVLADPAlhgAAVLATGFCAGLASGMHPGDLVVAEETRDPRGSVPCvgTE 102
Cdd:cd17768   11 LKFEARIAIGDGLLVILSGAGPERARRAAERLLAAGA---RALISFGVAGGLDPALKPGDLVLPEAVVADGERYPT--DP 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 664506076 103 LLVKELVRTVPGR-TVHTGPLTGSDHVV--RGHERSDLLATGAIAVDMESAA 151
Cdd:cd17768   86 AWRRRLLRALPAGlRVVAGPLAGSDAPVlsVADKAALHAATGAVAVDMESGA 137
HpnG TIGR03468
hopanoid-associated phosphorylase; The sequences in this family are members of the pfam01048 ...
 22-151 7.90e-14

hopanoid-associated phosphorylase; The sequences in this family are members of the pfam01048 family of phosphorylases typically acting on nucleotide-sugar substrates. The genes of the family modeled here are generally in the same locus with genes involved in the biosynthesis and elaboration of hopene, the cyclization product of the polyisoprenoid squalene. This gene is adjacent to the genes PhnA-E and squalene-hopene cyclase (which would be HpnF) in Zymomonas mobilis and their association with hopene biosynthesis has been noted in the literature. Extending the gene symbol sequence, we suggest the symbol HpnG for the product of this gene. Hopanoids are known to be components of the plasma membrane and to have polar sugar head groups in Z. mobilis and other species.


Pssm-ID: 274594  Cd Length: 212  Bit Score: 67.36  E-value: 7.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076   22 ALRRGGRTTPGGPVTVLRTGMGPAAAERSVTRVLADPAlhgAAVLATGFCAGLASGMHPGDLVVAEETRDPRGSVPCvgT 101
Cdd:TIGR03468   9 GLAFEARIAAGPGLLVCLSGGGPERARAAAARLMAAGA---AGLVSFGTAGALDPALQPGDLVVPEEVRADGDRFPT--D 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 664506076  102 ELLVKELVRTVPGRT-VHTGPLTGSDHVVRGHERSDLL--ATGAIAVDMESAA 151
Cdd:TIGR03468  84 PAWRRRLLEALPAGLrVHRGVLAASDTVVSTAAAKAALarATGAAAVDMESGA 136
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 32-151 3.75e-09

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: 54.43  E-value: 3.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076  32 GGPVTVLRTGMGPAAAERSVTRVLA--DPAlhgaAVLATGFCAGLASGMHPGDLVVAEETR---------DPRGSVPCVG 100
Cdd:cd09008   38 GKEVVLVQSGIGKVNAAIATQLLIDrfKPD----AIINTGVAGGLDPDLKIGDVVIATKVVyhdvdatafGYEGGQPPGM 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664506076 101 TEL---------LVKELVRTVPGRtVHTGPLTGSDHVVRGHERSDLLAT--GAIAVDMESAA 151
Cdd:cd09008  114 PAYfpadpelleLAKKAAKELGPK-VHTGLIASGDQFVASSEKKEELREnfPALAVEMEGAA 174
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 32-151 2.02e-08

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: 52.73  E-value: 2.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076   32 GGPVTVLRTGMGPA-AAERSVTRVLAdpaLHGA-AVLATGFCAGLASGMHPGDLVVAEETRDPRGSVPCVGTEL------ 103
Cdd:pfam01048  41 GVPVVLVRHGIGPPnAAILAAIRLLK---EFGVdAIIRTGTAGGLNPDLKVGDVVIPTDAINHDGRSPLFGPEGgpyfpd 117

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 664506076  104 ---------LVKELVRTVP--GRTVHTGPLTGSDHVVRG-HERSDLLAT-GAIAVDMESAA 151
Cdd:pfam01048 118 mapapadpeLRALAKEAAErlGIPVHRGVYATGDGFYFEtPAEIRLLRRlGADAVEMETAA 178
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
32-151 8.66e-07

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 47.81  E-value: 8.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076  32 GGPVTVLRTGMGPAAAERSVTrVLADpALHGAAVLATGFCAGLASGMHPGDLVVAEETR----------DPRGSVPCVGT 101
Cdd:PRK05584  40 GHEVVLVLSGIGKVAAALTAT-ILIE-HFKVDAVINTGVAGGLAPGLKVGDVVVADELVqhdvdvtafgYPYGQVPGLPA 117

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076 102 -----ELLVKELVRTVP--GRTVHTGPLTGSDHVVRGHERSDLLAT---GAIAVDMESAA 151
Cdd:PRK05584 118 afkadEKLVALAEKAAKelNLNVHRGLIASGDQFIAGAEKVAAIRAefpDALAVEMEGAA 177
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 32-151 2.10e-06

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: 46.51  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076  32 GGPVTVLRTGMGPAAAeRSVTRVLAdpaLHGA-AVLATGFCAGLASGMHPGDLVVAEET-RDPRGSV-----PCVGTEL- 103
Cdd:cd09005   39 GKRVTVVNGGMGSPSA-AIVVEELC---ALGVdTIIRVGSCGALREDIKVGDLVIADGAiRGDGVTPyyvvgPPFAPEAd 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 664506076 104 --LVKELVRTVP--GRTVHTGPLTGSDHVVRGH--ERSDLLATGAIAVDMESAA 151
Cdd:cd09005  115 peLTAALEEAAKelGLTVHVGTVWTTDAFYRETreESEKLRKLGALAVEMETSA 168
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 32-158 3.28e-06

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 46.31  E-value: 3.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076  32 GGPVTVLRTGMGPAAAERsvtrVLADPALHGA-AVLATGFCAGLASGMHPGDLVVAEET-RDPRGS-------VPCVGTE 102
Cdd:COG2820   62 GKRITVISTGIGGPSAAI----AVEELAALGAkTFIRVGTSGALQPDIPVGDLVIATGAvRLDGTSnfyapaeYPAVADF 137

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 664506076 103 LLVKELVRTVP--GRTVHTGPLTGSDHVVRGHERSDLL------------ATGAIAVDMESAATL-LSAVR 158
Cdd:COG2820  138 ELTRALVEAAEelGVDYHVGITASTDGFYAEQGRELRVdpdldekleawrKLGVLNVEMETAALFtLARLR 208
PRK07077 PRK07077
phosphorylase;
7-149 5.23e-06

phosphorylase;


Pssm-ID: 235926  Cd Length: 238  Bit Score: 45.80  E-value: 5.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076   7 PAPLLIACALGIEqfalrrgGRTTPGGPVTVLRTGMGPAAaERSVTRVLadPALHGAAVLATGFCAGLASGMHPGDLVVA 86
Cdd:PRK07077   9 PRPVLAVTGMAFE-------ARIAAGPGVEVVCAARADRL-ERALLAAF--DARGCAGIVSFGVAGGLDPDLAPGDLVVA 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 664506076  87 EETRDPRGSVPCVG--TELLVKELVRTVPGRTVHTGPLTGSDHVVRGHERSDLL--ATGAIAVDMES 149
Cdd:PRK07077  79 TAVDAPFGRVDTDArwSARLAAALELTPVARRVVRGGLAGVEAPVVGAAAKAALhrATGALAVDMES 145
futalosine_nucleosidase_MqnB cd17766
futalosine nucleosidase which catalyzes the hydrolysis of futalosine to ...
 9-151 1.08e-05

futalosine nucleosidase which catalyzes the hydrolysis of futalosine to dehypoxanthinylfutalosine and a hypoxanthine base; similar to Thermus thermophiles MqnB; Futalosine nucleosidase (MqnB, EC 3.2.2.26, also known as futalosine hydrolase) functions in an alternative menaquinone biosynthetic pathway (the futalosine pathway) which operates in some bacteria, including Streptomyces coelicolor and Thermus thermophiles. This domain model belongs to the PNP_UDP_1 superfamily which includes members which accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. PNP_UDP_1 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). Superfamily members have different physiologically relevant quaternary structures: hexameric such as the trimer-of-dimers arrangement of Shewanella oneidensis MR-1 UP, homotrimeric such as human PNP and Escherichia coli PNPII (XapA), homohexomeric (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 PNP_UDP_2 (nucleoside phosphorylase-II family) is a different structural family.


Pssm-ID: 350166  Cd Length: 217  Bit Score: 44.45  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076   9 PLLIACALG---------IEQFALRRGgrTTPGGPVTVLRTGMGPAAAERSVTRVLAdpALHGAAVLATGfCAG--LASG 77
Cdd:cd17766    1 MILIVTAVPletnlerveAEREAVLRG--LLGDQRVDVLVAGVGPVNAAAATALLLE--RHPPDLVINAG-IAGafPGSG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076  78 MHPGDLVVAEE---------TRD--------PRGSVPCVGTELLVKELVRTVP---GRTVHTGPL------TGSDhvvrg 131
Cdd:cd17766   76 LSVGDLVVASEeiaadlgveTPEgflsldelGFGLLRIGTDPYLNRFPLSALLlaaGLQVKTGPFltvstvTGTA----- 150

                        170       180
                 ....*....|....*....|..
gi 664506076 132 hERSDLLA--TGAIAVDMESAA 151
Cdd:cd17766  151 -ERAAELQrrFPAIAENMEGAA 171
AMN cd17762
AMP nucleosidase; AMP nucleosidase (AMN) catalyzes the hydrolysis of AMP to ribose 5-phosphate ...
 35-150 1.15e-04

AMP nucleosidase; AMP nucleosidase (AMN) catalyzes the hydrolysis of AMP to ribose 5-phosphate and adenine. It is a prokaryotic enzyme which plays a role in purine nucleoside salvage and intracellular AMP level regulation. AMN is active as a homohexamer; each monomer is comprised of a catalytic domain and a putative regulatory domain. This model represents the catalytic domain. AMN 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: 350162  Cd Length: 242  Bit Score: 41.77  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076  35 VTVLRTGMGPAAAeRSVTRVLAdpALHGAAVLATGFCAGLASGMHPGDLVVA------EETRD---PRG--SVPCVGTEL 103
Cdd:cd17762   61 ITIINFGVGSPNA-ATITDLLA--VLRPKAVLMLGHCGGLRNSQEIGDFVLPiaairgEGTSDdylPPEvpALPSFELQR 137

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 664506076 104 LVKELVRTVpGRTVHTGP-LTGSDHVVRGHERS--DLLATGAIAVDMESA 150
Cdd:cd17762  138 ALSDALREV-GLDYRTGTvYTTDRRNWEFDEAFkeYLRESRAIAIDMESA 186
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
 32-151 2.06e-04

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: 41.14  E-value: 2.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076  32 GGPVTVLRTGMGPAaaerSVTRVLADPALHGAAVLA-TGFCAGLASGMHPGDLVVAEET--RDPRGSVPCVGTEL----- 103
Cdd:cd17765   54 GKPVSVQTTGMGCP----SAAIVVEELAQLGVKRLIrVGTCGGLSSGLQLGDLIVATAAvpADGTTRALLGGEPYapaad 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 664506076 104 --LVKELVRT--VPGRTVHTGPLTGSDHVVRGHERSD--LLATGAIAVDMESAA 151
Cdd:cd17765  130 feLVEALYRAarAAGMPVHVGPVATSDLFYDPTPDGVkrWRRRGVLAVEMEASA 183
PRK08236 PRK08236
hypothetical protein; Provisional
 9-88 1.22e-03

hypothetical protein; Provisional


Pssm-ID: 236194  Cd Length: 212  Bit Score: 38.50  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076   9 PLLIACALGIEQFALRRGGRTTPGgpVTVLRTGMGPAAAERSVTRVLADPALHGAAVLATGFCAGLASGMHPGDLVVAEE 88
Cdd:PRK08236   3 RVLVVTAVPAERDAVLRGLGNDSR--FDVLAAGVGPAAAAASTARALAAAAAPYDLVVSAGIAGGFPGKAEVGSLVVADE 80
PRK06714 PRK06714
S-adenosylhomocysteine nucleosidase; Validated
 68-151 9.17e-03

S-adenosylhomocysteine nucleosidase; Validated


Pssm-ID: 168652  Cd Length: 236  Bit Score: 36.05  E-value: 9.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664506076  68 TGFCAGLASGMHPGDLVVAEET-----------------RDPRGSvPCVGTELLVKELVRTVPGRTVHTGPLTGSDHVVR 130
Cdd:PRK06714  75 TGICGSLSNKVKNGHIVVALNAiqhdvtaagsgedvfnlYNGRTA-PIETTKSLVRRIKKIRSYDPIHFGTFLSGDQRIR 153

                         90       100
                 ....*....|....*....|...
gi 664506076 131 GHERSDLLAT--GAIAVDMESAA 151
Cdd:PRK06714 154 SSEMRYLLHTvyGALAVDQEVAA 176
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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