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Conserved domains on  [gi|755498001|ref|XP_011237507|]
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uridine phosphorylase 2 isoform X1 [Mus musculus]

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 ...
 166-399 2.03e-155

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: 439.66  E-value: 2.03e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 166 EDILYHLDLGTKTHNLPAMFGDVKFVCVGGSPNRMKAFAQFMHKELRLEGD-GEDIEDICAGTDRYCMFKTGPVLSVSHG 244
Cdd:cd17763    1 VDFLYHLGLDTSSHDLKKMFGDVKFVCMGGSPGRMENFAEYLAKELGIKLPaGAALVNLSKTTDRYSMYKVGPVLSVSHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 245 MGIPSISIMLHELIKLLHHAHCCDVTIIRIGTSGGIGIAPGSVVITDTAVDSFFKPRFEQVILDNVVTRSTELDKELAND 324
Cdd:cd17763   81 MGIPSLSILLHELIKLLHYAGCKDVTFIRIGTSGGIGVEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQLAEE 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755498001 325 LFNCSREIPNVPTLIGHTMCTYDFYEGQGRLDGALCSFSREKKLDYLKRAYRAGVRNIEMESTVFAAMCGLCGLR 399
Cdd:cd17763  161 LLECAKELDDFPTVIGKTMCANDFYEGQGRLDGAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIK 235
 
Name Accession Description Interval E-value
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
 166-399 2.03e-155

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: 439.66  E-value: 2.03e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 166 EDILYHLDLGTKTHNLPAMFGDVKFVCVGGSPNRMKAFAQFMHKELRLEGD-GEDIEDICAGTDRYCMFKTGPVLSVSHG 244
Cdd:cd17763    1 VDFLYHLGLDTSSHDLKKMFGDVKFVCMGGSPGRMENFAEYLAKELGIKLPaGAALVNLSKTTDRYSMYKVGPVLSVSHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 245 MGIPSISIMLHELIKLLHHAHCCDVTIIRIGTSGGIGIAPGSVVITDTAVDSFFKPRFEQVILDNVVTRSTELDKELAND 324
Cdd:cd17763   81 MGIPSLSILLHELIKLLHYAGCKDVTFIRIGTSGGIGVEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQLAEE 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755498001 325 LFNCSREIPNVPTLIGHTMCTYDFYEGQGRLDGALCSFSREKKLDYLKRAYRAGVRNIEMESTVFAAMCGLCGLR 399
Cdd:cd17763  161 LLECAKELDDFPTVIGKTMCANDFYEGQGRLDGAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIK 235
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
 158-399 5.99e-115

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: 337.50  E-value: 5.99e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001  158 NPYLEGMDEDILYHLDLGTKTHNLPAMFGDVKFVCVGGSPNRMKAFAQFMHKELRLEgDGEDIEDICAGTDRYCMFKTGP 237
Cdd:TIGR01719   1 NPNLDKMKEDILYHFGINTSTHDFPAVFGDVKFVCMGGTPSRMKAFARYVGAELGLS-CGRDYPNISERGDRFAMYKVGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001  238 VLSVSHGMGIPSISIMLHELIKLLHHAHCCDVTIIRIGTSGGIGIAPGSVVITDTAVDSFFKPRFEQVILDNVVTRSTEL 317
Cdd:TIGR01719  80 VLCVSHGMGIPSISIMLHELIKLLYYARCKNPTFIRIGTSGGIGVPPGTVVVSSEAVDACLKPEYEQIVLGKRVIRPTQL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001  318 DKELANDLFNCSRE-IPNVPTLIGHTMCTYDFYEGQGRLDGALCSFSREKKLDYLKRAYRAGVRNIEMESTVFAAMCGLC 396
Cdd:TIGR01719 160 DEALVQELLLCGAEgLDEFTTVSGNTMCTDDFYEGQGRLDGAFCEYTEKDKMAYLRKLYALGVRNIEMESSMFAAMTSRA 239


                  ...
gi 755498001  397 GLR 399
Cdd:TIGR01719 240 GFK 242
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 165-408 2.45e-23

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 97.93  E-value: 2.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 165 DEDILYHLDLGtkthnlPAMFGDVKFVCvgGSPNRMKAFAQFMhkelrlegdgEDIEDIcAGTDRYCMFkTG-----PVL 239
Cdd:COG2820    7 PDGSQYHLGLK------PGDVADYVILP--GDPGRVELIASYL----------DDVELV-AENREFRTY-TGtykgkRIT 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 240 SVSHGMGIPSISIMLHELIKLlhHAHccdvTIIRIGTSGGI--GIAPGSVVITDTAVdsffkpRFEQ-----VILDNVVT 312
Cdd:COG2820   67 VISTGIGGPSAAIAVEELAAL--GAK----TFIRVGTSGALqpDIPVGDLVIATGAV------RLDGtsnfyAPAEYPAV 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 313 RSTELDKELANDLfncsrEIPNVPTLIGHTMCTYDFYEGQGRLDGALCSFsrEKKLDYLKrayRAGVRNIEMESTVFAAM 392
Cdd:COG2820  135 ADFELTRALVEAA-----EELGVDYHVGITASTDGFYAEQGRELRVDPDL--DEKLEAWR---KLGVLNVEMETAALFTL 204

                        250
                 ....*....|....*.
gi 755498001 393 CGLCGLRVVPMSANSV 408
Cdd:COG2820  205 ARLRGHRAGSVLAVSA 220
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 189-401 5.07e-21

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: 91.25  E-value: 5.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001  189 KFVCVGGSPNRMKAFAQFMHKELRLEgdgedieDICAGTDRY-CMFKTGPVLSVSHGMGIPSISIMlhELIKLLHHAHCc 267
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVG-------PPSRGGKFYtGTLGGVPVVLVRHGIGPPNAAIL--AAIRLLKEFGV- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001  268 dVTIIRIGTSGGI--GIAPGSVVITDTAVD-----SFFKPRFEQVILDnvvTRSTELDKELANDLFNCSREIpNVPTLIG 340
Cdd:pfam01048  71 -DAIIRTGTAGGLnpDLKVGDVVIPTDAINhdgrsPLFGPEGGPYFPD---MAPAPADPELRALAKEAAERL-GIPVHRG 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755498001  341 HTMCTYDFYegqgrldgalcsFSREKKLDYLKrayRAGVRNIEMESTVFAAMCGLCGLRVV 401
Cdd:pfam01048 146 VYATGDGFY------------FETPAEIRLLR---RLGADAVEMETAAEAQVAREAGIPFA 191
PRK11178 PRK11178
uridine phosphorylase; Provisional
 170-399 1.17e-11

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 64.29  E-value: 1.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 170 YHLDLgTKthnlpAMFGDVKFVCVGGSPNRMKAFAQFM--------HKEL---RLEGDGEdiedicagtdrycmfktgPV 238
Cdd:PRK11178   5 FHLGL-TK-----ADLQGATLAIVPGDPERVEKIAALMdnpvflasHREFtswRAELDGK------------------PV 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 239 LSVSHGMGIPSISIMLHELIKLLHHahccdvTIIRIGTSGGI--GIAPGSVVITDTAV-----DSFFKP-RFEQVIldnv 310
Cdd:PRK11178  61 IVCSTGIGGPSTSIAVEELAQLGVR------TFLRIGTTGAIqpHINVGDVLVTTASVrldgaSLHFAPlEFPAVA---- 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 311 vtrstelDKELANDLFNCSREIpNVPTLIGHTMCTYDFYEGQGRLDgalcSFSrekkldylKRAYRA-----------GV 379
Cdd:PRK11178 131 -------DFECTTALVEAAKSI-GATTHVGVTASSDTFYPGQERYD----TYS--------GRVVRRfkgsmeewqamGV 190

                        250       260
                 ....*....|....*....|
gi 755498001 380 RNIEMESTVFAAMCGLCGLR 399
Cdd:PRK11178 191 MNYEMESATLLTMCASQGLR 210
 
Name Accession Description Interval E-value
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
 166-399 2.03e-155

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: 439.66  E-value: 2.03e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 166 EDILYHLDLGTKTHNLPAMFGDVKFVCVGGSPNRMKAFAQFMHKELRLEGD-GEDIEDICAGTDRYCMFKTGPVLSVSHG 244
Cdd:cd17763    1 VDFLYHLGLDTSSHDLKKMFGDVKFVCMGGSPGRMENFAEYLAKELGIKLPaGAALVNLSKTTDRYSMYKVGPVLSVSHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 245 MGIPSISIMLHELIKLLHHAHCCDVTIIRIGTSGGIGIAPGSVVITDTAVDSFFKPRFEQVILDNVVTRSTELDKELAND 324
Cdd:cd17763   81 MGIPSLSILLHELIKLLHYAGCKDVTFIRIGTSGGIGVEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQLAEE 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755498001 325 LFNCSREIPNVPTLIGHTMCTYDFYEGQGRLDGALCSFSREKKLDYLKRAYRAGVRNIEMESTVFAAMCGLCGLR 399
Cdd:cd17763  161 LLECAKELDDFPTVIGKTMCANDFYEGQGRLDGAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIK 235
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
 158-399 5.99e-115

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: 337.50  E-value: 5.99e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001  158 NPYLEGMDEDILYHLDLGTKTHNLPAMFGDVKFVCVGGSPNRMKAFAQFMHKELRLEgDGEDIEDICAGTDRYCMFKTGP 237
Cdd:TIGR01719   1 NPNLDKMKEDILYHFGINTSTHDFPAVFGDVKFVCMGGTPSRMKAFARYVGAELGLS-CGRDYPNISERGDRFAMYKVGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001  238 VLSVSHGMGIPSISIMLHELIKLLHHAHCCDVTIIRIGTSGGIGIAPGSVVITDTAVDSFFKPRFEQVILDNVVTRSTEL 317
Cdd:TIGR01719  80 VLCVSHGMGIPSISIMLHELIKLLYYARCKNPTFIRIGTSGGIGVPPGTVVVSSEAVDACLKPEYEQIVLGKRVIRPTQL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001  318 DKELANDLFNCSRE-IPNVPTLIGHTMCTYDFYEGQGRLDGALCSFSREKKLDYLKRAYRAGVRNIEMESTVFAAMCGLC 396
Cdd:TIGR01719 160 DEALVQELLLCGAEgLDEFTTVSGNTMCTDDFYEGQGRLDGAFCEYTEKDKMAYLRKLYALGVRNIEMESSMFAAMTSRA 239


                  ...
gi 755498001  397 GLR 399
Cdd:TIGR01719 240 GFK 242
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 190-410 1.88e-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: 113.92  E-value: 1.88e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 190 FVCVGGSPNRMKAFAQFMhkelrlegdgEDIEDICAGtDRYCMFkTG-----PVLSVSHGMGIPSISIMLHELIkllhhA 264
Cdd:cd09005    1 YAIIPGDPERVDVIDSKL----------ENPQKVSSF-RGYTMY-TGkyngkRVTVVNGGMGSPSAAIVVEELC-----A 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 265 HCCDvTIIRIGTSGGIG--IAPGSVVITDTAVDSFFKPRFEQVILDnvvtRSTELDKELANDLFNCSREIpNVPTLIGHT 342
Cdd:cd09005   64 LGVD-TIIRVGSCGALRedIKVGDLVIADGAIRGDGVTPYYVVGPP----FAPEADPELTAALEEAAKEL-GLTVHVGTV 137

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755498001 343 MCTYDFYEGQGrldgalcsfsrekklDYLKRAYRAGVRNIEMESTVFAAMCGLCGLRVVPMSANSVRL 410
Cdd:cd09005  138 WTTDAFYRETR---------------EESEKLRKLGALAVEMETSALATLAHLRGVKAASILAVSDNL 190
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 165-408 2.45e-23

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 97.93  E-value: 2.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 165 DEDILYHLDLGtkthnlPAMFGDVKFVCvgGSPNRMKAFAQFMhkelrlegdgEDIEDIcAGTDRYCMFkTG-----PVL 239
Cdd:COG2820    7 PDGSQYHLGLK------PGDVADYVILP--GDPGRVELIASYL----------DDVELV-AENREFRTY-TGtykgkRIT 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 240 SVSHGMGIPSISIMLHELIKLlhHAHccdvTIIRIGTSGGI--GIAPGSVVITDTAVdsffkpRFEQ-----VILDNVVT 312
Cdd:COG2820   67 VISTGIGGPSAAIAVEELAAL--GAK----TFIRVGTSGALqpDIPVGDLVIATGAV------RLDGtsnfyAPAEYPAV 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 313 RSTELDKELANDLfncsrEIPNVPTLIGHTMCTYDFYEGQGRLDGALCSFsrEKKLDYLKrayRAGVRNIEMESTVFAAM 392
Cdd:COG2820  135 ADFELTRALVEAA-----EELGVDYHVGITASTDGFYAEQGRELRVDPDL--DEKLEAWR---KLGVLNVEMETAALFTL 204

                        250
                 ....*....|....*.
gi 755498001 393 CGLCGLRVVPMSANSV 408
Cdd:COG2820  205 ARLRGHRAGSVLAVSA 220
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 170-400 1.33e-21

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: 92.89  E-value: 1.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 170 YHLDLGTkthnlpamfGDV-KFVCVGGSPNRMKAFAQFMhkelrlegdgEDIEDIcaGTDRycMFKTG-------PVLSV 241
Cdd:cd17767    1 YHIGLKP---------GDVaPYVLLPGDPGRVERIAELL----------DDAEEV--ADNR--EYRTYtgtykgvPVSVC 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 242 SHGMGIPSISIMLHELIKLlhHAHccdvTIIRIGTSGGI--GIAPGSVVITDTAVdsffkpRFEQVildnvvtrSTEL-- 317
Cdd:cd17767   58 STGIGGPSAAIAVEELAQL--GAK----TFIRVGTCGALqpDIKLGDLVIATGAV------RDEGT--------SKHYvp 117

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 318 -------DKELANDLFNCSREIpNVPTLIGhTMCTYD-FYEGQGRLDGALCSFSREkKLDYLKrayRAGVRNIEME-STV 388
Cdd:cd17767  118 peypavaDPEVVLALVEAAEEL-GVPYHVG-ITASKDsFYGGQGRPGPGLPPELPE-LLEEWQ---RAGVLNSEMEsAAL 191

                        250
                 ....*....|..
gi 755498001 389 FaAMCGLCGLRV 400
Cdd:cd17767  192 F-TLASLRGVRA 202
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 189-401 5.07e-21

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: 91.25  E-value: 5.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001  189 KFVCVGGSPNRMKAFAQFMHKELRLEgdgedieDICAGTDRY-CMFKTGPVLSVSHGMGIPSISIMlhELIKLLHHAHCc 267
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVG-------PPSRGGKFYtGTLGGVPVVLVRHGIGPPNAAIL--AAIRLLKEFGV- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001  268 dVTIIRIGTSGGI--GIAPGSVVITDTAVD-----SFFKPRFEQVILDnvvTRSTELDKELANDLFNCSREIpNVPTLIG 340
Cdd:pfam01048  71 -DAIIRTGTAGGLnpDLKVGDVVIPTDAINhdgrsPLFGPEGGPYFPD---MAPAPADPELRALAKEAAERL-GIPVHRG 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755498001  341 HTMCTYDFYegqgrldgalcsFSREKKLDYLKrayRAGVRNIEMESTVFAAMCGLCGLRVV 401
Cdd:pfam01048 146 VYATGDGFY------------FETPAEIRLLR---RLGADAVEMETAAEAQVAREAGIPFA 191
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 240-386 3.43e-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: 65.50  E-value: 3.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 240 SV-SHGMGIPSISIMLHELIKllHHahccDV-TIIRIGTSGGIG--IAPGSVVITDTAV-DSFFkprfeQVILDNVVTRS 314
Cdd:cd09006   55 SVmGSGMGMPSIGIYAYELFK--FY----GVkNIIRIGTCGAYQpdLKLRDVVLAMGAStDSNY-----NRLRFGGGDFA 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755498001 315 TELDKELANDLFNCSREIpNVPTLIGHTMCTYDFYegqgrldgalcsfsrEKKLDYLKRAYRAGVRNIEMES 386
Cdd:cd09006  124 PIADFELLRKAVETAKEL-GIPVHVGNVFSSDVFY---------------DDDPELWKKLKKYGVLAVEMEA 179
PRK11178 PRK11178
uridine phosphorylase; Provisional
 170-399 1.17e-11

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 64.29  E-value: 1.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 170 YHLDLgTKthnlpAMFGDVKFVCVGGSPNRMKAFAQFM--------HKEL---RLEGDGEdiedicagtdrycmfktgPV 238
Cdd:PRK11178   5 FHLGL-TK-----ADLQGATLAIVPGDPERVEKIAALMdnpvflasHREFtswRAELDGK------------------PV 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 239 LSVSHGMGIPSISIMLHELIKLLHHahccdvTIIRIGTSGGI--GIAPGSVVITDTAV-----DSFFKP-RFEQVIldnv 310
Cdd:PRK11178  61 IVCSTGIGGPSTSIAVEELAQLGVR------TFLRIGTTGAIqpHINVGDVLVTTASVrldgaSLHFAPlEFPAVA---- 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 311 vtrstelDKELANDLFNCSREIpNVPTLIGHTMCTYDFYEGQGRLDgalcSFSrekkldylKRAYRA-----------GV 379
Cdd:PRK11178 131 -------DFECTTALVEAAKSI-GATTHVGVTASSDTFYPGQERYD----TYS--------GRVVRRfkgsmeewqamGV 190

                        250       260
                 ....*....|....*....|
gi 755498001 380 RNIEMESTVFAAMCGLCGLR 399
Cdd:PRK11178 191 MNYEMESATLLTMCASQGLR 210
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 239-400 5.10e-11

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: 62.44  E-value: 5.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 239 LSV-SHGMGIPSISIMLHELIKLLhhahccDV-TIIRIGTSGGI--GIAPGSVVITDTAV-DS-FFKPRFEQVILdnvvt 312
Cdd:COG0813   58 VSVmGSGMGIPSISIYAYELITEY------GVkNIIRVGTCGALqeDVKVRDVVIAMGAStDSnVNRQRFGGGDF----- 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 313 rSTELDKELANDLFNCSREIpNVPTLIGHTMCTYDFYegqgrldgalcsfsrEKKLDYLKRAYRAGVRNIEMES----TV 388
Cdd:COG0813  127 -APIADFELLRKAVEAAKEL-GIKVHVGNVFSSDLFY---------------REDPDLLEKLAKYGVLAVEMEAaalyTL 189

                        170
                 ....*....|....*
gi 755498001 389 fAAMCG---LCGLRV 400
Cdd:COG0813  190 -AAKYGkraLAILTV 203
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
 241-398 8.65e-11

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: 62.10  E-value: 8.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 241 VSHGMGIPSISIMLHELikllhHA-HCCD------------VTIIRIGTSGGI--GIAPGSVVITDTAV--DSF-----F 298
Cdd:cd00436   67 ISTGIGTDNIDIVLNEL-----DAlVNIDfktrtpkeektsLNIIRLGTSGALqpDIPVGSLVISSYAIglDNLlnfydH 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 299 KPRFEQVILDNVVTRSTELDKELAN--------DLFNCsreIPNVPTLIGHTMCTYDFYEGQGR----------LDGALC 360
Cdd:cd00436  142 PNTDEEAELENAFIAHTSWFKGKPRpyvvkaspELLDA---LTGVGYVVGITATAPGFYGPQGRqlrlpladpdLLDKLS 218

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 755498001 361 SFSrekkldylkraYRaGVR--NIEMEStvfAAMCGLCGL 398
Cdd:cd00436  219 SFS-----------YG-GLRitNFEMET---SAIYGLSRL 243
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
 239-395 2.24e-09

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: 57.32  E-value: 2.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 239 LSV-SHGMGIPSISIMLHELIKLLHHahccdvTIIRIGTSGGI--GIAPGSVVITDTAVDSFFKPRfeqvILDNVVTRST 315
Cdd:cd17765   57 VSVqTTGMGCPSAAIVVEELAQLGVK------RLIRVGTCGGLssGLQLGDLIVATAAVPADGTTR----ALLGGEPYAP 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 316 ELDKELANDLFNCSREIpNVPTLIGHTMCTYDFYEGQgrldgalcsfsrekkLDYLKRAYRAGVRNIEME-STVF--AAM 392
Cdd:cd17765  127 AADFELVEALYRAARAA-GMPVHVGPVATSDLFYDPT---------------PDGVKRWRRRGVLAVEMEaSALFtlAAL 190


                 ...
gi 755498001 393 CGL 395
Cdd:cd17765  191 RGL 193
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
 232-386 4.16e-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: 56.82  E-value: 4.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 232 MFKTGPVLSVSHGMGIPSISIMLHELikllhhAHCCD--VTIIRIGTSGGIG--IAPGSVVITDTAV-------DSFFKP 300
Cdd:cd17769   40 RYKGVPVSIVAIGMGAPMMDFFVREA------RAVVDgpMAIIRLGSCGSLDpdVPVGSVVVPSASVavtrnydDDDFAG 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 301 RFEQVILDNVVTRSTELDKELANDLF-NCSREIPNVPTLIGHTMCTYDFYEGQGRLDGalcSF--SREKKLDYLKRAYRa 377
Cdd:cd17769  114 PSTSSEKPYLISKPVPADPELSELLEsELKASLGGEVVVEGLNASADSFYSSQGRQDP---NFpdHNENLIDKLLKRYP- 189


                 ....*....
gi 755498001 378 GVRNIEMES 386
Cdd:cd17769  190 GAASLEMET 198
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
240-280 3.53e-07

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 51.01  E-value: 3.53e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 755498001 240 SV-SHGMGIPSISIMLHELIKLLhhahccDV-TIIRIGTSGGI 280
Cdd:PRK05819  58 SVmGTGMGIPSISIYANELITDY------GVkKLIRVGSCGAL 94
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
 233-293 5.87e-06

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: 46.83  E-value: 5.87e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755498001 233 FKTGPVLSVSHGMGIPSISIMLHELIKLlhHAHccdvTIIRIGTSGGI--GIAPGSVVITDTA 293
Cdd:cd17764   38 YKGEEVTIATHGIGGPSAAIVFEELIML--GAK----VIIRLGTAGGLvpELRVGDIVVATGA 94
deoD TIGR00107
purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called ...
 243-280 1.66e-04

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: 42.84  E-value: 1.66e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 755498001  243 HGMGIPSISIMLHELIKLLhhahccDV-TIIRIGTSGGI 280
Cdd:TIGR00107  59 HGMGIPSISIYVYELIKFY------EVkTIIRVGSCGAI 91
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
178-280 2.95e-04

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 42.01  E-value: 2.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498001 178 THNLPAMFGDV-KFVCVGGSPNRMKAFAQ-FMhkelrlegdgEDIEDICA--GTDRYCMFKTGPVLSV-SHGMGIPSISI 252
Cdd:PRK13374   3 TPHINAQPGDFaETVLMPGDPLRAKYIAEtYL----------EDVVQVTDvrNMFGFTGTYKGKKVSVmGHGMGIPSMVI 72

                         90       100
                 ....*....|....*....|....*....
gi 755498001 253 MLHELIkllhhaHCCDV-TIIRIGTSGGI 280
Cdd:PRK13374  73 YVHELI------ATFGVkNIIRVGSCGAT 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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