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Conserved domains on  [gi|24650443|ref|NP_651515|]
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uncharacterized protein Dmel_CG6330, isoform B [Drosophila melanogaster]

Protein Classification

uridine phosphorylase( domain architecture ID 13027119)

uridine phosphorylase catalyzes the reversible phosphorolysis of uracil ribosides and analogous compounds to their respective nucleobases and ribose 1-phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
38-312 0e+00

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: 540.58  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443  38 DILYHLALGSESHDLQEMFGDVKFVCMGGTPKRMENFAHFIMNEIGYKLPAGTQLQDISAYSYRYSMYKVGPVLCVSHGM 117
Cdd:cd17763   2 DFLYHLGLDTSSHDLKKMFGDVKFVCMGGSPGRMENFAEYLAKELGIKLPAGAALVNLSKTTDRYSMYKVGPVLSVSHGM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 118 GTPSVSILMHEMIKLMYHAKCKDPVFIRIGTCGGIGVDGGTVIITEDALDGQLRNSHEFTILGKTIHRPAKLDKKLAREL 197
Cdd:cd17763  82 GIPSLSILLHELIKLLHYAGCKDVTFIRIGTSGGIGVEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQLAEEL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 198 KSLASPDDPYDTIIGKTLCTNDFYEGQGRLDGAFCDFSENEKMAYLEKLRENGVVNIEMESTIFAALTHHAGIKAAVVCV 277
Cdd:cd17763 162 LECAKELDDFPTVIGKTMCANDFYEGQGRLDGAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIKAAVVCV 241
                       250       260       270
                ....*....|....*....|....*....|....*
gi 24650443 278 ALLNRLNGDQVNAPKEVMNEWQARPQILVSRYIRK 312
Cdd:cd17763 242 TLLNRLEGDQITSSKETLEEWQQRPQRLVSRYIKK 276
 
Name Accession Description Interval E-value
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
38-312 0e+00

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: 540.58  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443  38 DILYHLALGSESHDLQEMFGDVKFVCMGGTPKRMENFAHFIMNEIGYKLPAGTQLQDISAYSYRYSMYKVGPVLCVSHGM 117
Cdd:cd17763   2 DFLYHLGLDTSSHDLKKMFGDVKFVCMGGSPGRMENFAEYLAKELGIKLPAGAALVNLSKTTDRYSMYKVGPVLSVSHGM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 118 GTPSVSILMHEMIKLMYHAKCKDPVFIRIGTCGGIGVDGGTVIITEDALDGQLRNSHEFTILGKTIHRPAKLDKKLAREL 197
Cdd:cd17763  82 GIPSLSILLHELIKLLHYAGCKDVTFIRIGTSGGIGVEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQLAEEL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 198 KSLASPDDPYDTIIGKTLCTNDFYEGQGRLDGAFCDFSENEKMAYLEKLRENGVVNIEMESTIFAALTHHAGIKAAVVCV 277
Cdd:cd17763 162 LECAKELDDFPTVIGKTMCANDFYEGQGRLDGAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIKAAVVCV 241
                       250       260       270
                ....*....|....*....|....*....|....*
gi 24650443 278 ALLNRLNGDQVNAPKEVMNEWQARPQILVSRYIRK 312
Cdd:cd17763 242 TLLNRLEGDQITSSKETLEEWQQRPQRLVSRYIKK 276
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
29-316 1.01e-151

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: 428.02  E-value: 1.01e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443    29 NSNIELMDQDILYHLALGSESHDLQEMFGDVKFVCMGGTPKRMENFAHFIMNEIGykLPAGTQLQDISAYSYRYSMYKVG 108
Cdd:TIGR01719   1 NPNLDKMKEDILYHFGINTSTHDFPAVFGDVKFVCMGGTPSRMKAFARYVGAELG--LSCGRDYPNISERGDRFAMYKVG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443   109 PVLCVSHGMGTPSVSILMHEMIKLMYHAKCKDPVFIRIGTCGGIGVDGGTVIITEDALDGQLRNSHEFTILGKTIHRPAK 188
Cdd:TIGR01719  79 PVLCVSHGMGIPSISIMLHELIKLLYYARCKNPTFIRIGTSGGIGVPPGTVVVSSEAVDACLKPEYEQIVLGKRVIRPTQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443   189 LDKKLARELKSLASP-DDPYDTIIGKTLCTNDFYEGQGRLDGAFCDFSENEKMAYLEKLRENGVVNIEMESTIFAALTHH 267
Cdd:TIGR01719 159 LDEALVQELLLCGAEgLDEFTTVSGNTMCTDDFYEGQGRLDGAFCEYTEKDKMAYLRKLYALGVRNIEMESSMFAAMTSR 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 24650443   268 AGIKAAVVCVALLNRLNGDQVNAPKEVMNEWQARPQILVSRYIRKVLTH 316
Cdd:TIGR01719 239 AGFKAAVVCVTLLNRLEGDQITITRDQLHEFEQRPQRLVSRYIKKKLSK 287
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
60-311 6.93e-35

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: 127.46  E-value: 6.93e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443    60 KFVCMGGTPKRMENFAHFIMNEIgyklPAGTQlqdISAYSYRYSMYKVGPVLCVSHGMGTPSVSILmhEMIKLMYHAKCK 139
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDET----PVGPP---SRGGKFYTGTLGGVPVVLVRHGIGPPNAAIL--AAIRLLKEFGVD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443   140 dpVFIRIGTCGGI--GVDGGTVIITEDALDGQLRNSHEFTILGKT--IHRPAKLDKKLARELKSLASpDDPYDTIIGKTL 215
Cdd:pfam01048  72 --AIIRTGTAGGLnpDLKVGDVVIPTDAINHDGRSPLFGPEGGPYfpDMAPAPADPELRALAKEAAE-RLGIPVHRGVYA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443   216 CTNDFYEGQGrldgafcdfsenekmAYLEKLRENGVVNIEMESTIFAALTHHAGIKAAVVCVaLLNRLNGD-----QVNA 290
Cdd:pfam01048 149 TGDGFYFETP---------------AEIRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRV-VSDLAAGGadgelTHEE 212
                         250       260
                  ....*....|....*....|.
gi 24650443   291 PKEVMNEWQARPQILVSRYIR 311
Cdd:pfam01048 213 VEEFAERAAERAAALLLALLA 233
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
30-297 8.04e-31

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 117.19  E-value: 8.04e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443  30 SNIELMDqDILYHLALGseshdlQEMFGDVKFVCmgGTPKRMENFAHFiMNEI-------GYKLPAGTqlqdisaysyry 102
Cdd:COG2820   2 KESELPD-GSQYHLGLK------PGDVADYVILP--GDPGRVELIASY-LDDVelvaenrEFRTYTGT------------ 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 103 smYKVGPVLCVSHGMGTPSVSILMHEMIKLMyhAKckdpVFIRIGTCGGI--GVDGGTVIITEDA--LDGQLRN--SHEF 176
Cdd:COG2820  60 --YKGKRITVISTGIGGPSAAIAVEELAALG--AK----TFIRVGTSGALqpDIPVGDLVIATGAvrLDGTSNFyaPAEY 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 177 tilgktihrPAKLDKKLARELKSLASPDDpYDTIIGKTLCTNDFYEGQGRLDGAFCDFseNEKMAYLEKLrenGVVNIEM 256
Cdd:COG2820 132 ---------PAVADFELTRALVEAAEELG-VDYHVGITASTDGFYAEQGRELRVDPDL--DEKLEAWRKL---GVLNVEM 196
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 24650443 257 E-STIFaALTHHAGIKAAVVCVALLNRLNGDQVNAPKEVMNE 297
Cdd:COG2820 197 EtAALF-TLARLRGHRAGSVLAVSANRVTGEFSKDPEEAVER 237
PRK11178 PRK11178
uridine phosphorylase; Provisional
109-282 9.67e-11

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 61.21  E-value: 9.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443  109 PVLCVSHGMGTPSVSILMHEMIKLMYHakckdpVFIRIGTCGGI--GVDGGTVIITEDA--LDGQlrnSHEFTILgktiH 184
Cdd:PRK11178  59 PVIVCSTGIGGPSTSIAVEELAQLGVR------TFLRIGTTGAIqpHINVGDVLVTTASvrLDGA---SLHFAPL----E 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443  185 RPAKLDKKLARELKSlASPDDPYDTIIGKTLCTNDFYEGQGRLDgafcDFSENEKMAY---LEKLRENGVVNIEMES--- 258
Cdd:PRK11178 126 FPAVADFECTTALVE-AAKSIGATTHVGVTASSDTFYPGQERYD----TYSGRVVRRFkgsMEEWQAMGVMNYEMESatl 200
                        170       180
                 ....*....|....*....|....*
gi 24650443  259 -TIFAALthhaGIKAAVVCVALLNR 282
Cdd:PRK11178 201 lTMCASQ----GLRAGMVAGVIVNR 221
 
Name Accession Description Interval E-value
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
38-312 0e+00

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: 540.58  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443  38 DILYHLALGSESHDLQEMFGDVKFVCMGGTPKRMENFAHFIMNEIGYKLPAGTQLQDISAYSYRYSMYKVGPVLCVSHGM 117
Cdd:cd17763   2 DFLYHLGLDTSSHDLKKMFGDVKFVCMGGSPGRMENFAEYLAKELGIKLPAGAALVNLSKTTDRYSMYKVGPVLSVSHGM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 118 GTPSVSILMHEMIKLMYHAKCKDPVFIRIGTCGGIGVDGGTVIITEDALDGQLRNSHEFTILGKTIHRPAKLDKKLAREL 197
Cdd:cd17763  82 GIPSLSILLHELIKLLHYAGCKDVTFIRIGTSGGIGVEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQLAEEL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 198 KSLASPDDPYDTIIGKTLCTNDFYEGQGRLDGAFCDFSENEKMAYLEKLRENGVVNIEMESTIFAALTHHAGIKAAVVCV 277
Cdd:cd17763 162 LECAKELDDFPTVIGKTMCANDFYEGQGRLDGAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIKAAVVCV 241
                       250       260       270
                ....*....|....*....|....*....|....*
gi 24650443 278 ALLNRLNGDQVNAPKEVMNEWQARPQILVSRYIRK 312
Cdd:cd17763 242 TLLNRLEGDQITSSKETLEEWQQRPQRLVSRYIKK 276
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
29-316 1.01e-151

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: 428.02  E-value: 1.01e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443    29 NSNIELMDQDILYHLALGSESHDLQEMFGDVKFVCMGGTPKRMENFAHFIMNEIGykLPAGTQLQDISAYSYRYSMYKVG 108
Cdd:TIGR01719   1 NPNLDKMKEDILYHFGINTSTHDFPAVFGDVKFVCMGGTPSRMKAFARYVGAELG--LSCGRDYPNISERGDRFAMYKVG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443   109 PVLCVSHGMGTPSVSILMHEMIKLMYHAKCKDPVFIRIGTCGGIGVDGGTVIITEDALDGQLRNSHEFTILGKTIHRPAK 188
Cdd:TIGR01719  79 PVLCVSHGMGIPSISIMLHELIKLLYYARCKNPTFIRIGTSGGIGVPPGTVVVSSEAVDACLKPEYEQIVLGKRVIRPTQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443   189 LDKKLARELKSLASP-DDPYDTIIGKTLCTNDFYEGQGRLDGAFCDFSENEKMAYLEKLRENGVVNIEMESTIFAALTHH 267
Cdd:TIGR01719 159 LDEALVQELLLCGAEgLDEFTTVSGNTMCTDDFYEGQGRLDGAFCEYTEKDKMAYLRKLYALGVRNIEMESSMFAAMTSR 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 24650443   268 AGIKAAVVCVALLNRLNGDQVNAPKEVMNEWQARPQILVSRYIRKVLTH 316
Cdd:TIGR01719 239 AGFKAAVVCVTLLNRLEGDQITITRDQLHEFEQRPQRLVSRYIKKKLSK 287
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
60-311 6.93e-35

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: 127.46  E-value: 6.93e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443    60 KFVCMGGTPKRMENFAHFIMNEIgyklPAGTQlqdISAYSYRYSMYKVGPVLCVSHGMGTPSVSILmhEMIKLMYHAKCK 139
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDET----PVGPP---SRGGKFYTGTLGGVPVVLVRHGIGPPNAAIL--AAIRLLKEFGVD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443   140 dpVFIRIGTCGGI--GVDGGTVIITEDALDGQLRNSHEFTILGKT--IHRPAKLDKKLARELKSLASpDDPYDTIIGKTL 215
Cdd:pfam01048  72 --AIIRTGTAGGLnpDLKVGDVVIPTDAINHDGRSPLFGPEGGPYfpDMAPAPADPELRALAKEAAE-RLGIPVHRGVYA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443   216 CTNDFYEGQGrldgafcdfsenekmAYLEKLRENGVVNIEMESTIFAALTHHAGIKAAVVCVaLLNRLNGD-----QVNA 290
Cdd:pfam01048 149 TGDGFYFETP---------------AEIRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRV-VSDLAAGGadgelTHEE 212
                         250       260
                  ....*....|....*....|.
gi 24650443   291 PKEVMNEWQARPQILVSRYIR 311
Cdd:pfam01048 213 VEEFAERAAERAAALLLALLA 233
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
30-297 8.04e-31

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 117.19  E-value: 8.04e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443  30 SNIELMDqDILYHLALGseshdlQEMFGDVKFVCmgGTPKRMENFAHFiMNEI-------GYKLPAGTqlqdisaysyry 102
Cdd:COG2820   2 KESELPD-GSQYHLGLK------PGDVADYVILP--GDPGRVELIASY-LDDVelvaenrEFRTYTGT------------ 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 103 smYKVGPVLCVSHGMGTPSVSILMHEMIKLMyhAKckdpVFIRIGTCGGI--GVDGGTVIITEDA--LDGQLRN--SHEF 176
Cdd:COG2820  60 --YKGKRITVISTGIGGPSAAIAVEELAALG--AK----TFIRVGTSGALqpDIPVGDLVIATGAvrLDGTSNFyaPAEY 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 177 tilgktihrPAKLDKKLARELKSLASPDDpYDTIIGKTLCTNDFYEGQGRLDGAFCDFseNEKMAYLEKLrenGVVNIEM 256
Cdd:COG2820 132 ---------PAVADFELTRALVEAAEELG-VDYHVGITASTDGFYAEQGRELRVDPDL--DEKLEAWRKL---GVLNVEM 196
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 24650443 257 E-STIFaALTHHAGIKAAVVCVALLNRLNGDQVNAPKEVMNE 297
Cdd:COG2820 197 EtAALF-TLARLRGHRAGSVLAVSANRVTGEFSKDPEEAVER 237
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
61-300 9.84e-29

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: 110.46  E-value: 9.84e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443  61 FVCMGGTPKRMENFAHFIMNeigyklpagTQLQDisaYSYRYSMYKVG----PVLCVSHGMGTPSVSILMHEMIKLmyha 136
Cdd:cd09005   1 YAIIPGDPERVDVIDSKLEN---------PQKVS---SFRGYTMYTGKyngkRVTVVNGGMGSPSAAIVVEELCAL---- 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 137 KCKdpVFIRIGTCGGIG--VDGGTVIITEDALDGQlRNSHEFtilGKTIHRPAKLDKKLARELKSlASPDDPYDTIIGKT 214
Cdd:cd09005  65 GVD--TIIRVGSCGALRedIKVGDLVIADGAIRGD-GVTPYY---VVGPPFAPEADPELTAALEE-AAKELGLTVHVGTV 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 215 LCTNDFYEGQgrldgafcdfsenekMAYLEKLRENGVVNIEMESTIFAALTHHAGIKAAVVCVALLNRLNGDQvnapkEV 294
Cdd:cd09005 138 WTTDAFYRET---------------REESEKLRKLGALAVEMETSALATLAHLRGVKAASILAVSDNLITGEI-----GF 197

                ....*.
gi 24650443 295 MNEWQA 300
Cdd:cd09005 198 VDEFLS 203
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
109-301 1.96e-24

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: 99.44  E-value: 1.96e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 109 PVLCVSHGMGTPSVSILMHEMIKlmyhakCKDPVFIRIGTCGGI--GVDGGTVIITEDA--LDGQLRN----------SH 174
Cdd:cd17767  53 PVSVCSTGIGGPSAAIAVEELAQ------LGAKTFIRVGTCGALqpDIKLGDLVIATGAvrDEGTSKHyvppeypavaDP 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 175 EFTilgktihrpAKLdKKLARELKSlaspddPYDTiiGKTLCTNDFYEGQGRLDGAFCDFSENekmaYLEKLRENGVVNI 254
Cdd:cd17767 127 EVV---------LAL-VEAAEELGV------PYHV--GITASKDSFYGGQGRPGPGLPPELPE----LLEEWQRAGVLNS 184
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 24650443 255 EME-STIFaALTHHAGIKAAVVCVALLNRLNGDQVNapKEVMNEWQAR 301
Cdd:cd17767 185 EMEsAALF-TLASLRGVRAGAVLAVVGNRVTDEAPD--EEDVAAGEER 229
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
109-297 1.01e-17

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: 81.75  E-value: 1.01e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 109 PVLCVSHGMGTPSVSILMHEMIKL--------MYHAKCKDPVFIRIGTCGG----IGVDggTVIITEDA--LDG-----Q 169
Cdd:cd00436  63 RITVISTGIGTDNIDIVLNELDALvnidfktrTPKEEKTSLNIIRLGTSGAlqpdIPVG--SLVISSYAigLDNllnfyD 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 170 LRNSHEFTILGKTIHRPAKLDKKLARELKSLASPD-----DPYDTIIGKTLCTNDFYEGQGR---LDGAFCDFseNEKma 241
Cdd:cd00436 141 HPNTDEEAELENAFIAHTSWFKGKPRPYVVKASPElldalTGVGYVVGITATAPGFYGPQGRqlrLPLADPDL--LDK-- 216
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24650443 242 yLEKLRENG--VVNIEMESTIFAALTHHAGIKAAVVCVALLNRLNGDQVNAPKEVMNE 297
Cdd:cd00436 217 -LSSFSYGGlrITNFEMETSAIYGLSRLLGHRALSICAIIANRATGEFSKDYKKAVEK 273
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
104-301 1.15e-17

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: 81.47  E-value: 1.15e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 104 MYKVGPVLCVSHGMGTPSV--------SILMHEMiklmyhakckdpVFIRIGTCGGIGVDG--GTVIITEDALdGQLRNS 173
Cdd:cd17769  40 RYKGVPVSIVAIGMGAPMMdffvrearAVVDGPM------------AIIRLGSCGSLDPDVpvGSVVVPSASV-AVTRNY 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 174 HEFTILGK--------TIHRPAKLDKKLAREL-KSLASPDDPYDTIIGKTLCTNDFYEGQGRLDGAFCDfsENEKMayLE 244
Cdd:cd17769 107 DDDDFAGPstssekpyLISKPVPADPELSELLeSELKASLGGEVVVEGLNASADSFYSSQGRQDPNFPD--HNENL--ID 182
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24650443 245 KL--RENGVVNIEMESTIFAAL----THHAG-IKAAVVCVALLNRLNGDQV-NAPKEVMNEWQAR 301
Cdd:cd17769 183 KLlkRYPGAASLEMETFHLFHLarcsRPAQGkIRAAAAHMVFANRTSNDFIsPERVHELERWAGR 247
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
105-301 1.00e-13

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: 69.64  E-value: 1.00e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 105 YKVGPVLCVSHGMGTPSVSILMHEMIKLMYHakckdpVFIRIGTCGGI--GVDGGTVIITEDA--LDGQLRnshefTILG 180
Cdd:cd17765  52 YKGKPVSVQTTGMGCPSAAIVVEELAQLGVK------RLIRVGTCGGLssGLQLGDLIVATAAvpADGTTR-----ALLG 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 181 KTIHRPA---KLDKKLARELKSLASPddpydTIIGKTLCTNDFYEgqGRLDGAfcdfsenekmaylEKLRENGVVNIEME 257
Cdd:cd17765 121 GEPYAPAadfELVEALYRAARAAGMP-----VHVGPVATSDLFYD--PTPDGV-------------KRWRRRGVLAVEME 180
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 24650443 258 STIFAALTHHAGIKAAVVCVAlLNRLNGDQVNAPKEVMNEWQAR 301
Cdd:cd17765 181 ASALFTLAALRGLRAGCILTV-SDLIGDPERRIDDEELRAGVDR 223
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
57-276 2.73e-12

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: 65.52  E-value: 2.73e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443  57 GDV-KFVCMGGTPKRmenfAHFImneigyklpAGTQLQDISAYSYRYSM------YKVGPVLCVSHGMGTPSVSILMHEM 129
Cdd:COG0813  11 GDIaETVLLPGDPLR----AKYI---------AETFLEDAVLVNEVRGMlgytgtYKGKRVSVMGSGMGIPSISIYAYEL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 130 IKlMYHAKckdpVFIRIGTCGGI--GVDGGTVII-----TEDALDGQLRNSHEFTILGktihrpaklDKKLARELKSLAS 202
Cdd:COG0813  78 IT-EYGVK----NIIRVGTCGALqeDVKVRDVVIamgasTDSNVNRQRFGGGDFAPIA---------DFELLRKAVEAAK 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24650443 203 PDDpYDTIIGKTLCTNDFYegqgrldgafcdfseNEKMAYLEKLRENGVVNIEMESTIFAALTHHAGIKAAVVC 276
Cdd:COG0813 144 ELG-IKVHVGNVFSSDLFY---------------REDPDLLEKLAKYGVLAVEMEAAALYTLAAKYGKRALAIL 201
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
114-276 4.05e-12

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: 64.73  E-value: 4.05e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 114 SHGMGTPSVSILMHEMIKlMYHAKCkdpvFIRIGTCGGIG--VDGGTVIITEDALDgqlrNSHEFTILGKTIHRPAKLDK 191
Cdd:cd09006  58 GSGMGMPSIGIYAYELFK-FYGVKN----IIRIGTCGAYQpdLKLRDVVLAMGAST----DSNYNRLRFGGGDFAPIADF 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 192 KLARELKSLASpDDPYDTIIGKTLCTNDFYegqgrldgafcdfseNEKMAYLEKLRENGVVNIEMESTIFAALTHHAGIK 271
Cdd:cd09006 129 ELLRKAVETAK-ELGIPVHVGNVFSSDVFY---------------DDDPELWKKLKKYGVLAVEMEAAALYTNAARLGKK 192

                ....*
gi 24650443 272 AAVVC 276
Cdd:cd09006 193 ALAIL 197
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
105-297 5.19e-11

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: 61.47  E-value: 5.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 105 YKVGPVLCVSHGMGTPSVSILMHEMIKLmyHAKckdpVFIRIGTCGGI--GVDGGTVIITEDALdgqLRNSHEFTILGKT 182
Cdd:cd17764  38 YKGEEVTIATHGIGGPSAAIVFEELIML--GAK----VIIRLGTAGGLvpELRVGDIVVATGAS---YYPGGGLGQYFPD 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443 183 IHRPAKLDKKLAREL-KSLASPDDPYdtIIGKTLCTNDFYegqgrldgafcdfSENEkmAYLEKLRENGVVNIEMESTIF 261
Cdd:cd17764 109 VCPPASPDPELTLELvESLSKRGLKY--YVGPVFSSDAFY-------------AEDE--EFAERWSSLGFIAVEMECATL 171
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 24650443 262 AALTHHAGIKAAVVCVALLNRLNGDQVNAPKEVMNE 297
Cdd:cd17764 172 FTLGWLRGVKAGAVLVVSDNLVKGGKLMLTKEELEE 207
PRK11178 PRK11178
uridine phosphorylase; Provisional
109-282 9.67e-11

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 61.21  E-value: 9.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443  109 PVLCVSHGMGTPSVSILMHEMIKLMYHakckdpVFIRIGTCGGI--GVDGGTVIITEDA--LDGQlrnSHEFTILgktiH 184
Cdd:PRK11178  59 PVIVCSTGIGGPSTSIAVEELAQLGVR------TFLRIGTTGAIqpHINVGDVLVTTASvrLDGA---SLHFAPL----E 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443  185 RPAKLDKKLARELKSlASPDDPYDTIIGKTLCTNDFYEGQGRLDgafcDFSENEKMAY---LEKLRENGVVNIEMES--- 258
Cdd:PRK11178 126 FPAVADFECTTALVE-AAKSIGATTHVGVTASSDTFYPGQERYD----TYSGRVVRRFkgsMEEWQAMGVMNYEMESatl 200
                        170       180
                 ....*....|....*....|....*
gi 24650443  259 -TIFAALthhaGIKAAVVCVALLNR 282
Cdd:PRK11178 201 lTMCASQ----GLRAGMVAGVIVNR 221
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
104-276 6.82e-08

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 52.55  E-value: 6.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443  104 MYKVGPVLCVSHGMGTPSVSILMHEMIKlMYHAKckdpVFIRIGTCGGIG--VDGGTVIITEDA-LDGQLrNSHEFtilg 180
Cdd:PRK05819  51 TYKGKRVSVMGTGMGIPSISIYANELIT-DYGVK----KLIRVGSCGALQedVKVRDVVIAMGAsTDSNV-NRIRF---- 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443  181 KTIHRPAKLDKKLARELKSLASpDDPYDTIIGKTLCTNDFYegqgrldgafcdfseNEKMAYLEKLRENGVVNIEMESTI 260
Cdd:PRK05819 121 KGHDFAPIADFDLLRKAYDAAK-EKGITVHVGNVFSADLFY---------------NPDPEMFDVLEKYGVLGVEMEAAA 184
                        170
                 ....*....|....*.
gi 24650443  261 FAALTHHAGIKAAVVC 276
Cdd:PRK05819 185 LYGLAAKYGVKALTIL 200
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
62-276 1.14e-06

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 48.94  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443   62 VCMGGTPKRmenfAHFImneigyklpAGTQLQDISAYSYRYSM------YKVGPVLCVSHGMGTPSVSILMHEmikLMYH 135
Cdd:PRK13374  17 VLMPGDPLR----AKYI---------AETYLEDVVQVTDVRNMfgftgtYKGKKVSVMGHGMGIPSMVIYVHE---LIAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443  136 AKCKDpvFIRIGTCGGI--GVDGGTVIITEDA-----------LDGQLRNSHEFTILGKTIhrpakldkKLARELkslas 202
Cdd:PRK13374  81 FGVKN--IIRVGSCGATqdDVKLMDVIIAQGAstdsktnrirfSGHDFAAIADYQLLEKAV--------ETAREK----- 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24650443  203 pDDPYDtiIGKTLCTNDFYegqgrldgafcdfSENEKMayLEKLRENGVVNIEMESTIFAALTHHAGIKAAVVC 276
Cdd:PRK13374 146 -GVPVK--VGNVFSSDLFY-------------DPDEDA--IEAMERFGILGVDMEVAGLYGLAAYLGAEALAIL 201
deoD TIGR00107
purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called ...
56-276 5.69e-06

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: 46.69  E-value: 5.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443    56 FGDVkfVCMGGTPKRmenfAHFImneigyklpAGTQLQDISAYSYRYSM------YKVGPVLCVSHGMGTPSVSILMHEM 129
Cdd:TIGR00107   9 IADV--VLMPGDPLR----AKYI---------AETFLEDVREVNEVRGMlgftgtYKGKKISVMGHGMGIPSISIYVYEL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650443   130 IKlMYHAKckdpVFIRIGTCGGIGVDGG---TVIITEDALDGQLRNsheftILGKTIHRPAKLDKKLARelkslaspdDP 206
Cdd:TIGR00107  74 IK-FYEVK----TIIRVGSCGAIRPDVKlrdVIIAMGASTDSKYNR-----VRFVEVDFAAIADFELVE---------NA 134
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24650443   207 YDTIIGKTLctnDFYEGQgrldgAFC-DFSENEKMAYLEKLRENGVVNIEMESTIFAALTHHAGIKAAVVC 276
Cdd:TIGR00107 135 YDAAKAKGV---DVHVGN-----VFSaDAFYQPDKDVFDLMAKYGILGVEMEAAALYANAAELGAKALTIL 197
 
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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