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Conserved domains on  [gi|320544292|ref|NP_001188991|]
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uncharacterized protein Dmel_CG3788, isoform B [Drosophila melanogaster]

Protein Classification

nucleoside phosphorylase-I family protein; purine-nucleoside phosphorylase( domain architecture ID 10019827)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
57-345 0e+00

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: 522.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292   57 NPCLKCLQPDILYHLGLNTETTDFPKVFGDVRFVCMGGTPGRMENFAYYVMQEIGLKInaATKLRNISEAGQRFSLFKVG 136
Cdd:TIGR01719   1 NPNLDKMKEDILYHFGINTSTHDFPAVFGDVKFVCMGGTPSRMKAFARYVGAELGLSC--GRDYPNISERGDRFAMYKVG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292  137 PVLCASHGMGCPSISILLHELIKMMYHAKCKDPVFIRIGTSGGIGVEPGTVIISSEAIDGRLNPVHEILVHGVSVQHASQ 216
Cdd:TIGR01719  79 PVLCVSHGMGIPSISIMLHELIKLLYYARCKNPTFIRIGTSGGIGVPPGTVVVSSEAVDACLKPEYEQIVLGKRVIRPTQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292  217 LDESLADEIKMCHDPCKDKYEAVIGRTLCAHDFYEGQSRLDGAFCEYTPEMKKSYLETLQSQQVKNIEMESLAFAALTSR 296
Cdd:TIGR01719 159 LDEALVQELLLCGAEGLDEFTTVSGNTMCTDDFYEGQGRLDGAFCEYTEKDKMAYLRKLYALGVRNIEMESSMFAAMTSR 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 320544292  297 ANIRGAVVCVAILNRLNGDQIKTPHDVLSKWEKRPQELVARYIRKVLYH 345
Cdd:TIGR01719 239 AGFKAAVVCVTLLNRLEGDQITITRDQLHEFEQRPQRLVSRYIKKKLSK 287
 
Name Accession Description Interval E-value
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
57-345 0e+00

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: 522.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292   57 NPCLKCLQPDILYHLGLNTETTDFPKVFGDVRFVCMGGTPGRMENFAYYVMQEIGLKInaATKLRNISEAGQRFSLFKVG 136
Cdd:TIGR01719   1 NPNLDKMKEDILYHFGINTSTHDFPAVFGDVKFVCMGGTPSRMKAFARYVGAELGLSC--GRDYPNISERGDRFAMYKVG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292  137 PVLCASHGMGCPSISILLHELIKMMYHAKCKDPVFIRIGTSGGIGVEPGTVIISSEAIDGRLNPVHEILVHGVSVQHASQ 216
Cdd:TIGR01719  79 PVLCVSHGMGIPSISIMLHELIKLLYYARCKNPTFIRIGTSGGIGVPPGTVVVSSEAVDACLKPEYEQIVLGKRVIRPTQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292  217 LDESLADEIKMCHDPCKDKYEAVIGRTLCAHDFYEGQSRLDGAFCEYTPEMKKSYLETLQSQQVKNIEMESLAFAALTSR 296
Cdd:TIGR01719 159 LDEALVQELLLCGAEGLDEFTTVSGNTMCTDDFYEGQGRLDGAFCEYTEKDKMAYLRKLYALGVRNIEMESSMFAAMTSR 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 320544292  297 ANIRGAVVCVAILNRLNGDQIKTPHDVLSKWEKRPQELVARYIRKVLYH 345
Cdd:TIGR01719 239 AGFKAAVVCVTLLNRLEGDQITITRDQLHEFEQRPQRLVSRYIKKKLSK 287
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
65-341 9.32e-178

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: 494.74  E-value: 9.32e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292  65 PDILYHLGLNTETTDFPKVFGDVRFVCMGGTPGRMENFAYYVMQEIGLKINAATKLRNISEAGQRFSLFKVGPVLCASHG 144
Cdd:cd17763    1 VDFLYHLGLDTSSHDLKKMFGDVKFVCMGGSPGRMENFAEYLAKELGIKLPAGAALVNLSKTTDRYSMYKVGPVLSVSHG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 145 MGCPSISILLHELIKMMYHAKCKDPVFIRIGTSGGIGVEPGTVIISSEAIDGRLNPVHEILVHGVSVQHASQLDESLADE 224
Cdd:cd17763   81 MGIPSLSILLHELIKLLHYAGCKDVTFIRIGTSGGIGVEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQLAEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 225 IKMCHDPCKDkYEAVIGRTLCAHDFYEGQSRLDGAFCEYTPEMKKSYLETLQSQQVKNIEMESLAFAALTSRANIRGAVV 304
Cdd:cd17763  161 LLECAKELDD-FPTVIGKTMCANDFYEGQGRLDGAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIKAAVV 239
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 320544292 305 CVAILNRLNGDQIKTPHDVLSKWEKRPQELVARYIRK 341
Cdd:cd17763  240 CVTLLNRLEGDQITSSKETLEEWQQRPQRLVSRYIKK 276
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
88-340 3.78e-28

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: 110.13  E-value: 3.78e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292   88 RFVCMGGTPGRMENFAyyvmQEIGLKINAATKLRniseaGQRFSLFKVG--PVLCASHGMGCPSISILL-HELIKMMyha 164
Cdd:pfam01048   1 KIAIIGGSPEELALLA----ELLDDETPVGPPSR-----GGKFYTGTLGgvPVVLVRHGIGPPNAAILAaIRLLKEF--- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292  165 kcKDPVFIRIGTSGGI--GVEPGTVIISSEAI--DGRLNPVHEILVHGVSVQHASQLDESLADEIKmcHDPCKDKYEAVI 240
Cdd:pfam01048  69 --GVDAIIRTGTAGGLnpDLKVGDVVIPTDAInhDGRSPLFGPEGGPYFPDMAPAPADPELRALAK--EAAERLGIPVHR 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292  241 GRTLCAHDFYEGQsrldgafceytpemkKSYLETLQSQQVKNIEMESLAFAALTSRANIRGAVVCVaILNRLNGDQIKTP 320
Cdd:pfam01048 145 GVYATGDGFYFET---------------PAEIRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRV-VSDLAAGGADGEL 208
                         250       260
                  ....*....|....*....|....*
gi 320544292  321 -----HDVLSKWEKRPQELVARYIR 340
Cdd:pfam01048 209 theevEEFAERAAERAAALLLALLA 233
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
137-343 3.04e-26

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 105.25  E-value: 3.04e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 137 PVLCASHGMGCPSISILLHELIKMMyhAKckdpVFIRIGTSGGI--GVEPGTVIISSEAI--DGRLN---PVHEILVHGV 209
Cdd:COG2820   64 RITVISTGIGGPSAAIAVEELAALG--AK----TFIRVGTSGALqpDIPVGDLVIATGAVrlDGTSNfyaPAEYPAVADF 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 210 SVQHAsqldesLADEIKmchdpcKDKYEAVIGRTLCAHDFYEGQSRLDgafceYTPEMKKSYLETLQSQQVKNIEMESLA 289
Cdd:COG2820  138 ELTRA------LVEAAE------ELGVDYHVGITASTDGFYAEQGREL-----RVDPDLDEKLEAWRKLGVLNVEMETAA 200
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 320544292 290 FAALTSRANIRGAVVCVAILNRLNGDQIKTPHDVlskwekrpqelVARYIRKVL 343
Cdd:COG2820  201 LFTLARLRGHRAGSVLAVSANRVTGEFSKDPEEA-----------VERAIKVAL 243
PRK11178 PRK11178
uridine phosphorylase; Provisional
137-343 6.72e-10

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 58.90  E-value: 6.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 137 PVLCASHGMGCPSISILLHELIKMMYHakckdpVFIRIGTSGGI--GVEPGTVIISSEAIdgRLNpvheilvhGVSvQHA 214
Cdd:PRK11178  59 PVIVCSTGIGGPSTSIAVEELAQLGVR------TFLRIGTTGAIqpHINVGDVLVTTASV--RLD--------GAS-LHF 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 215 SQLD-ESLADEIKMC--HDPCKDKYEAV-IGRTLCAHDFYEGQSRLDgAFCEYTPEMKKSYLETLQSQQVKNIEMESLAF 290
Cdd:PRK11178 122 APLEfPAVADFECTTalVEAAKSIGATThVGVTASSDTFYPGQERYD-TYSGRVVRRFKGSMEEWQAMGVMNYEMESATL 200
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 320544292 291 AALTSRANIRGAVVCVAILNRLngdQIKTP-HDVLSKWEKRPQELVARYIRKVL 343
Cdd:PRK11178 201 LTMCASQGLRAGMVAGVIVNRT---QQEIPnAETMKQTESHAVKIVVEAARRLL 251
 
Name Accession Description Interval E-value
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
57-345 0e+00

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: 522.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292   57 NPCLKCLQPDILYHLGLNTETTDFPKVFGDVRFVCMGGTPGRMENFAYYVMQEIGLKInaATKLRNISEAGQRFSLFKVG 136
Cdd:TIGR01719   1 NPNLDKMKEDILYHFGINTSTHDFPAVFGDVKFVCMGGTPSRMKAFARYVGAELGLSC--GRDYPNISERGDRFAMYKVG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292  137 PVLCASHGMGCPSISILLHELIKMMYHAKCKDPVFIRIGTSGGIGVEPGTVIISSEAIDGRLNPVHEILVHGVSVQHASQ 216
Cdd:TIGR01719  79 PVLCVSHGMGIPSISIMLHELIKLLYYARCKNPTFIRIGTSGGIGVPPGTVVVSSEAVDACLKPEYEQIVLGKRVIRPTQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292  217 LDESLADEIKMCHDPCKDKYEAVIGRTLCAHDFYEGQSRLDGAFCEYTPEMKKSYLETLQSQQVKNIEMESLAFAALTSR 296
Cdd:TIGR01719 159 LDEALVQELLLCGAEGLDEFTTVSGNTMCTDDFYEGQGRLDGAFCEYTEKDKMAYLRKLYALGVRNIEMESSMFAAMTSR 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 320544292  297 ANIRGAVVCVAILNRLNGDQIKTPHDVLSKWEKRPQELVARYIRKVLYH 345
Cdd:TIGR01719 239 AGFKAAVVCVTLLNRLEGDQITITRDQLHEFEQRPQRLVSRYIKKKLSK 287
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
65-341 9.32e-178

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: 494.74  E-value: 9.32e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292  65 PDILYHLGLNTETTDFPKVFGDVRFVCMGGTPGRMENFAYYVMQEIGLKINAATKLRNISEAGQRFSLFKVGPVLCASHG 144
Cdd:cd17763    1 VDFLYHLGLDTSSHDLKKMFGDVKFVCMGGSPGRMENFAEYLAKELGIKLPAGAALVNLSKTTDRYSMYKVGPVLSVSHG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 145 MGCPSISILLHELIKMMYHAKCKDPVFIRIGTSGGIGVEPGTVIISSEAIDGRLNPVHEILVHGVSVQHASQLDESLADE 224
Cdd:cd17763   81 MGIPSLSILLHELIKLLHYAGCKDVTFIRIGTSGGIGVEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQLAEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 225 IKMCHDPCKDkYEAVIGRTLCAHDFYEGQSRLDGAFCEYTPEMKKSYLETLQSQQVKNIEMESLAFAALTSRANIRGAVV 304
Cdd:cd17763  161 LLECAKELDD-FPTVIGKTMCANDFYEGQGRLDGAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIKAAVV 239
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 320544292 305 CVAILNRLNGDQIKTPHDVLSKWEKRPQELVARYIRK 341
Cdd:cd17763  240 CVTLLNRLEGDQITSSKETLEEWQQRPQRLVSRYIKK 276
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
88-340 3.78e-28

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: 110.13  E-value: 3.78e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292   88 RFVCMGGTPGRMENFAyyvmQEIGLKINAATKLRniseaGQRFSLFKVG--PVLCASHGMGCPSISILL-HELIKMMyha 164
Cdd:pfam01048   1 KIAIIGGSPEELALLA----ELLDDETPVGPPSR-----GGKFYTGTLGgvPVVLVRHGIGPPNAAILAaIRLLKEF--- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292  165 kcKDPVFIRIGTSGGI--GVEPGTVIISSEAI--DGRLNPVHEILVHGVSVQHASQLDESLADEIKmcHDPCKDKYEAVI 240
Cdd:pfam01048  69 --GVDAIIRTGTAGGLnpDLKVGDVVIPTDAInhDGRSPLFGPEGGPYFPDMAPAPADPELRALAK--EAAERLGIPVHR 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292  241 GRTLCAHDFYEGQsrldgafceytpemkKSYLETLQSQQVKNIEMESLAFAALTSRANIRGAVVCVaILNRLNGDQIKTP 320
Cdd:pfam01048 145 GVYATGDGFYFET---------------PAEIRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRV-VSDLAAGGADGEL 208
                         250       260
                  ....*....|....*....|....*
gi 320544292  321 -----HDVLSKWEKRPQELVARYIR 340
Cdd:pfam01048 209 theevEEFAERAAERAAALLLALLA 233
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
137-343 3.04e-26

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 105.25  E-value: 3.04e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 137 PVLCASHGMGCPSISILLHELIKMMyhAKckdpVFIRIGTSGGI--GVEPGTVIISSEAI--DGRLN---PVHEILVHGV 209
Cdd:COG2820   64 RITVISTGIGGPSAAIAVEELAALG--AK----TFIRVGTSGALqpDIPVGDLVIATGAVrlDGTSNfyaPAEYPAVADF 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 210 SVQHAsqldesLADEIKmchdpcKDKYEAVIGRTLCAHDFYEGQSRLDgafceYTPEMKKSYLETLQSQQVKNIEMESLA 289
Cdd:COG2820  138 ELTRA------LVEAAE------ELGVDYHVGITASTDGFYAEQGREL-----RVDPDLDEKLEAWRKLGVLNVEMETAA 200
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 320544292 290 FAALTSRANIRGAVVCVAILNRLNGDQIKTPHDVlskwekrpqelVARYIRKVL 343
Cdd:COG2820  201 LFTLARLRGHRAGSVLAVSANRVTGEFSKDPEEA-----------VERAIKVAL 243
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
137-318 2.17e-23

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: 97.13  E-value: 2.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 137 PVLCASHGMGCPSISILLHELIkmmyhaKCKDPVFIRIGTSGGI--GVEPGTVIISSEAIdgRLNpvheilvhGVSVQHA 214
Cdd:cd17767   53 PVSVCSTGIGGPSAAIAVEELA------QLGAKTFIRVGTCGALqpDIKLGDLVIATGAV--RDE--------GTSKHYV 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 215 SQLDESLAD-EIKMC-HDPCKD-KYEAVIGRTLCAHDFYEGQSRLDGAFceytPEMKKSYLETLQSQQVKNIEMESLAFA 291
Cdd:cd17767  117 PPEYPAVADpEVVLAlVEAAEElGVPYHVGITASKDSFYGGQGRPGPGL----PPELPELLEEWQRAGVLNSEMESAALF 192
                        170       180
                 ....*....|....*....|....*..
gi 320544292 292 ALTSRANIRGAVVCVAILNRLNGDQIK 318
Cdd:cd17767  193 TLASLRGVRAGAVLAVVGNRVTDEAPD 219
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
89-335 1.82e-21

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: 91.58  E-value: 1.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292  89 FVCMGGTPGRMENFAyyvmqeiglkinaaTKLRNISEAGQRFSL------FKVGPVLCASHGMGCPSISILLHELIKMmy 162
Cdd:cd09005    1 YAIIPGDPERVDVID--------------SKLENPQKVSSFRGYtmytgkYNGKRVTVVNGGMGSPSAAIVVEELCAL-- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 163 haKCKdpVFIRIGTSGGIG--VEPGTVIISSEAIDG----RLNPVHEILvhgvsvqhASQLDESLADEIkmcHDPCKD-K 235
Cdd:cd09005   65 --GVD--TIIRVGSCGALRedIKVGDLVIADGAIRGdgvtPYYVVGPPF--------APEADPELTAAL---EEAAKElG 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 236 YEAVIGRTLCAHDFYEGQsrldGAFCEytpEMKKSYletlqsqqVKNIEMESLAFAALTSRANIRGAVVCVAILNRLNGD 315
Cdd:cd09005  130 LTVHVGTVWTTDAFYRET----REESE---KLRKLG--------ALAVEMETSALATLAHLRGVKAASILAVSDNLITGE 194
                        250       260
                 ....*....|....*....|
gi 320544292 316 QIkTPHDVLSKWEKRPQELV 335
Cdd:cd09005  195 IG-FVDEFLSEAEKKAIEIA 213
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
137-343 1.46e-14

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: 73.28  E-value: 1.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 137 PVLCASHGMGCPSISILLHEL-----I---KMMYHAKCKDPVFIRIGTSGGI--GVEPGTVIISSEAI--DGRLN----- 199
Cdd:cd00436   63 RITVISTGIGTDNIDIVLNELdalvnIdfkTRTPKEEKTSLNIIRLGTSGALqpDIPVGSLVISSYAIglDNLLNfydhp 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 200 -PVHEILVHGVSVQH-----------ASQLDESLADEIKmchdpckdKYEAVIGRTLCAHDFYEGQSR---LDGAFceyt 264
Cdd:cd00436  143 nTDEEAELENAFIAHtswfkgkprpyVVKASPELLDALT--------GVGYVVGITATAPGFYGPQGRqlrLPLAD---- 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 265 PEMkksyLETLQS-----QQVKNIEMESLAFAALTSRANIRGAVVCVAILNRLNGdqiktphdvlsKWEKRPQELVARYI 339
Cdd:cd00436  211 PDL----LDKLSSfsyggLRITNFEMETSAIYGLSRLLGHRALSICAIIANRATG-----------EFSKDYKKAVEKLI 275

                 ....
gi 320544292 340 RKVL 343
Cdd:cd00436  276 EKVL 279
PRK11178 PRK11178
uridine phosphorylase; Provisional
137-343 6.72e-10

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 58.90  E-value: 6.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 137 PVLCASHGMGCPSISILLHELIKMMYHakckdpVFIRIGTSGGI--GVEPGTVIISSEAIdgRLNpvheilvhGVSvQHA 214
Cdd:PRK11178  59 PVIVCSTGIGGPSTSIAVEELAQLGVR------TFLRIGTTGAIqpHINVGDVLVTTASV--RLD--------GAS-LHF 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 215 SQLD-ESLADEIKMC--HDPCKDKYEAV-IGRTLCAHDFYEGQSRLDgAFCEYTPEMKKSYLETLQSQQVKNIEMESLAF 290
Cdd:PRK11178 122 APLEfPAVADFECTTalVEAAKSIGATThVGVTASSDTFYPGQERYD-TYSGRVVRRFKGSMEEWQAMGVMNYEMESATL 200
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 320544292 291 AALTSRANIRGAVVCVAILNRLngdQIKTP-HDVLSKWEKRPQELVARYIRKVL 343
Cdd:PRK11178 201 LTMCASQGLRAGMVAGVIVNRT---QQEIPnAETMKQTESHAVKIVVEAARRLL 251
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
142-305 8.88e-10

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: 58.18  E-value: 8.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 142 SHGMGCPSISILLHELIKmMYHAKCkdpvFIRIGTSGGIG--VEPGTVIISSEA------IDGRLNPVHEILVHgvsvqh 213
Cdd:cd09006   58 GSGMGMPSIGIYAYELFK-FYGVKN----IIRIGTCGAYQpdLKLRDVVLAMGAstdsnyNRLRFGGGDFAPIA------ 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 214 asqlDESLadeIKMCHDPCKDK-YEAVIGRTLCAHDFYegqsrldgafcEYTPEMKKsyleTLQSQQVKNIEMESLAFAA 292
Cdd:cd09006  127 ----DFEL---LRKAVETAKELgIPVHVGNVFSSDVFY-----------DDDPELWK----KLKKYGVLAVEMEAAALYT 184
                        170
                 ....*....|...
gi 320544292 293 LTSRANIRGAVVC 305
Cdd:cd09006  185 NAARLGKKALAIL 197
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
143-305 1.89e-09

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: 57.43  E-value: 1.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 143 HGMGCPSISILLHELIKmMYHAKckdpVFIRIGTSGGI--GVEPGTVIISSEA------IDGRLNPVHEILVHgvsvqha 214
Cdd:COG0813   63 SGMGIPSISIYAYELIT-EYGVK----NIIRVGTCGALqeDVKVRDVVIAMGAstdsnvNRQRFGGGDFAPIA------- 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 215 sqlDESLADEIkmcHDPCKDK-YEAVIGRTLCAHDFYegqsrldgafcEYTPEMkksyLETLQSQQVKNIEMESLAFAAL 293
Cdd:COG0813  131 ---DFELLRKA---VEAAKELgIKVHVGNVFSSDLFY-----------REDPDL----LEKLAKYGVLAVEMEAAALYTL 189
                        170
                 ....*....|..
gi 320544292 294 TSRANIRGAVVC 305
Cdd:COG0813  190 AAKYGKRALAIL 201
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
137-193 4.78e-09

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: 56.08  E-value: 4.78e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 320544292 137 PVLCASHGMGCPSISILLHELIkmMYHAKckdpVFIRIGTSGGI--GVEPGTVIISSEA 193
Cdd:cd17764   42 EVTIATHGIGGPSAAIVFEELI--MLGAK----VIIRLGTAGGLvpELRVGDIVVATGA 94
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
170-317 7.42e-09

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: 56.05  E-value: 7.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 170 VFIRIGTSGGIG--VEPGTVIISSEAI--------DGRLNPVHEI----LVHGvsVQHAsqlDESLADEIKMCHDPCKDK 235
Cdd:cd17769   74 AIIRLGSCGSLDpdVPVGSVVVPSASVavtrnyddDDFAGPSTSSekpyLISK--PVPA---DPELSELLESELKASLGG 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 236 YEAVIGRTLCAHDFYEGQSRLDGAFceytPEMKKSYLETLQSQ--QVKNIEMES-----LAFAALTSRANIRGAVVCVAI 308
Cdd:cd17769  149 EVVVEGLNASADSFYSSQGRQDPNF----PDHNENLIDKLLKRypGAASLEMETfhlfhLARCSRPAQGKIRAAAAHMVF 224

                 ....*....
gi 320544292 309 LNRLNGDQI 317
Cdd:cd17769  225 ANRTSNDFI 233
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
137-194 4.20e-08

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: 53.46  E-value: 4.20e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 137 PVLCASHGMGCPSISILLHELIkmMYHAKckdpVFIRIGTSGGI--GVEPGTVIISSEAI 194
Cdd:cd17765   56 PVSVQTTGMGCPSAAIVVEELA--QLGVK----RLIRVGTCGGLssGLQLGDLIVATAAV 109
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
143-305 6.76e-06

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 46.77  E-value: 6.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 143 HGMGCPSISILLHELIKmMYHAKckdpVFIRIGTSGGIG--VEPGTVIISSEA------IDGRLNPVH-------EILVH 207
Cdd:PRK05819  62 TGMGIPSISIYANELIT-DYGVK----KLIRVGSCGALQedVKVRDVVIAMGAstdsnvNRIRFKGHDfapiadfDLLRK 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544292 208 GVSVqhasqldeslADEIKMchdpckdkyEAVIGRTLCAHDFYEGQsrldgafceytPEMkksyLETLQSQQVKNIEMES 287
Cdd:PRK05819 137 AYDA----------AKEKGI---------TVHVGNVFSADLFYNPD-----------PEM----FDVLEKYGVLGVEMEA 182
                        170
                 ....*....|....*...
gi 320544292 288 LAFAALTSRANIRGAVVC 305
Cdd:PRK05819 183 AALYGLAAKYGVKALTIL 200
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
143-180 1.14e-03

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 40.08  E-value: 1.14e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 320544292 143 HGMGCPSISILLHELIKMMyhaKCKDpvFIRIGTSGGI 180
Cdd:PRK13374  63 HGMGIPSMVIYVHELIATF---GVKN--IIRVGSCGAT 95
 
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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