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Conserved domains on  [gi|566006152|ref|NP_001274358|]
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uridine phosphorylase 1 isoform b [Homo sapiens]

Protein Classification

nucleoside phosphorylase-I family protein( domain architecture ID 762)

nucleoside phosphorylase-I family protein

CATH:  3.40.50.1580
PubMed:  11743878

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NP-I super family cl00303
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 10-168 7.18e-100

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.


The actual alignment was detected with superfamily member cd17763:

Pssm-ID: 444819  Cd Length: 276  Bit Score: 288.66  E-value: 7.18e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566006152  10 LEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTDLNKKLVQELLLCSAELSEFTTVVGNTMCTLDFYEGQGRLDGALCS 89
Cdd:cd17763  118 VEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQLAEELLECAKELDDFPTVIGKTMCANDFYEGQGRLDGAFCD 197

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 566006152  90 YTEKDKQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVCVTLLNRLEGDQISSPRNVLSEYQQRPQRLVSYFIKK 168
Cdd:cd17763  198 YTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIKAAVVCVTLLNRLEGDQITSSKETLEEWQQRPQRLVSRYIKK 276
 
Name Accession Description Interval E-value
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
 10-168 7.18e-100

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: 288.66  E-value: 7.18e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566006152  10 LEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTDLNKKLVQELLLCSAELSEFTTVVGNTMCTLDFYEGQGRLDGALCS 89
Cdd:cd17763  118 VEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQLAEELLECAKELDDFPTVIGKTMCANDFYEGQGRLDGAFCD 197

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 566006152  90 YTEKDKQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVCVTLLNRLEGDQISSPRNVLSEYQQRPQRLVSYFIKK 168
Cdd:cd17763  198 YTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIKAAVVCVTLLNRLEGDQITSSKETLEEWQQRPQRLVSRYIKK 276
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
 10-172 5.05e-96

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: 279.34  E-value: 5.05e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566006152   10 LEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTDLNKKLVQELLLCSAE-LSEFTTVVGNTMCTLDFYEGQGRLDGALC 88
Cdd:TIGR01719 124 VPPGTVVVSSEAVDACLKPEYEQIVLGKRVIRPTQLDEALVQELLLCGAEgLDEFTTVSGNTMCTDDFYEGQGRLDGAFC 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566006152   89 SYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVCVTLLNRLEGDQISSPRNVLSEYQQRPQRLVSYFIKK 168
Cdd:TIGR01719 204 EYTEKDKMAYLRKLYALGVRNIEMESSMFAAMTSRAGFKAAVVCVTLLNRLEGDQITITRDQLHEFEQRPQRLVSRYIKK 283


                  ....
gi 566006152  169 KLSK 172
Cdd:TIGR01719 284 KLSK 287
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 44-149 7.30e-14

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 67.11  E-value: 7.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566006152  44 DLNKKLVQelllcSAELSEFTTVVGNTMCTLDFYEGQGRLDgalcsYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMCSA 123
Cdd:COG2820  138 ELTRALVE-----AAEELGVDYHVGITASTDGFYAEQGREL-----RVDPDLDEKLEAWRKLGVLNVEMETAALFTLARL 207

                         90       100
                 ....*....|....*....|....*.
gi 566006152 124 CGLQAAVVCVTLLNRLEGDQISSPRN 149
Cdd:COG2820  208 RGHRAGSVLAVSANRVTGEFSKDPEE 233
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 9-167 1.03e-10

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: 58.12  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566006152    9 SLEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTD--LNKKLVQELLLCSAELsEFTTVVGNTMCTLDFYEGQgrldga 86
Cdd:pfam01048  85 DLKVGDVVIPTDAINHDGRSPLFGPEGGPYFPDMAPapADPELRALAKEAAERL-GIPVHRGVYATGDGFYFET------ 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566006152   87 lcsytekdkQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVCVtLLNRLEGD-----QISSPRNVLSEYQQRPQRL 161
Cdd:pfam01048 158 ---------PAEIRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRV-VSDLAAGGadgelTHEEVEEFAERAAERAAAL 227


                  ....*.
gi 566006152  162 VSYFIK 167
Cdd:pfam01048 228 LLALLA 233
PRK11178 PRK11178
uridine phosphorylase; Provisional
 64-138 5.19e-07

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 47.73  E-value: 5.19e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 566006152  64 TTVVGNTMCTLDFYEGQGRLDgALCSYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVCVTLLNR 138
Cdd:PRK11178 148 TTHVGVTASSDTFYPGQERYD-TYSGRVVRRFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNR 221
 
Name Accession Description Interval E-value
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
 10-168 7.18e-100

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: 288.66  E-value: 7.18e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566006152  10 LEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTDLNKKLVQELLLCSAELSEFTTVVGNTMCTLDFYEGQGRLDGALCS 89
Cdd:cd17763  118 VEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQLAEELLECAKELDDFPTVIGKTMCANDFYEGQGRLDGAFCD 197

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 566006152  90 YTEKDKQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVCVTLLNRLEGDQISSPRNVLSEYQQRPQRLVSYFIKK 168
Cdd:cd17763  198 YTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIKAAVVCVTLLNRLEGDQITSSKETLEEWQQRPQRLVSRYIKK 276
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
 10-172 5.05e-96

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: 279.34  E-value: 5.05e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566006152   10 LEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTDLNKKLVQELLLCSAE-LSEFTTVVGNTMCTLDFYEGQGRLDGALC 88
Cdd:TIGR01719 124 VPPGTVVVSSEAVDACLKPEYEQIVLGKRVIRPTQLDEALVQELLLCGAEgLDEFTTVSGNTMCTDDFYEGQGRLDGAFC 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566006152   89 SYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVCVTLLNRLEGDQISSPRNVLSEYQQRPQRLVSYFIKK 168
Cdd:TIGR01719 204 EYTEKDKMAYLRKLYALGVRNIEMESSMFAAMTSRAGFKAAVVCVTLLNRLEGDQITITRDQLHEFEQRPQRLVSRYIKK 283


                  ....
gi 566006152  169 KLSK 172
Cdd:TIGR01719 284 KLSK 287
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 9-165 1.23e-27

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: 102.75  E-value: 1.23e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566006152   9 SLEPGTVVITEQAVDTCFKAEFEqivlGKRVIRKTDLNKKLVQELLLCSAELsEFTTVVGNTMCTLDFYEGQgrldgalc 88
Cdd:cd09005   81 DIKVGDLVIADGAIRGDGVTPYY----VVGPPFAPEADPELTAALEEAAKEL-GLTVHVGTVWTTDAFYRET-------- 147

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 566006152  89 sytekdkQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVCVTLLNRLEGDqISSPRNVLSEYQQRPQRLVSYF 165
Cdd:cd09005  148 -------REESEKLRKLGALAVEMETSALATLAHLRGVKAASILAVSDNLITGE-IGFVDEFLSEAEKKAIEIALDA 216
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 44-149 7.30e-14

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 67.11  E-value: 7.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566006152  44 DLNKKLVQelllcSAELSEFTTVVGNTMCTLDFYEGQGRLDgalcsYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMCSA 123
Cdd:COG2820  138 ELTRALVE-----AAEELGVDYHVGITASTDGFYAEQGREL-----RVDPDLDEKLEAWRKLGVLNVEMETAALFTLARL 207

                         90       100
                 ....*....|....*....|....*.
gi 566006152 124 CGLQAAVVCVTLLNRLEGDQISSPRN 149
Cdd:COG2820  208 RGHRAGSVLAVSANRVTGEFSKDPEE 233
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 9-167 1.03e-10

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: 58.12  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566006152    9 SLEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTD--LNKKLVQELLLCSAELsEFTTVVGNTMCTLDFYEGQgrldga 86
Cdd:pfam01048  85 DLKVGDVVIPTDAINHDGRSPLFGPEGGPYFPDMAPapADPELRALAKEAAERL-GIPVHRGVYATGDGFYFET------ 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566006152   87 lcsytekdkQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVCVtLLNRLEGD-----QISSPRNVLSEYQQRPQRL 161
Cdd:pfam01048 158 ---------PAEIRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRV-VSDLAAGGadgelTHEEVEEFAERAAERAAAL 227


                  ....*.
gi 566006152  162 VSYFIK 167
Cdd:pfam01048 228 LLALLA 233
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 54-144 1.43e-09

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: 55.14  E-value: 1.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566006152  54 LLCSAELSEFTTVVGnTMCTLD-FYEGQGRLDgalcSYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVC 132
Cdd:cd17767  132 LVEAAEELGVPYHVG-ITASKDsFYGGQGRPG----PGLPPELPELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVL 206

                         90
                 ....*....|..
gi 566006152 133 VTLLNRLEGDQI 144
Cdd:cd17767  207 AVVGNRVTDEAP 218
PRK11178 PRK11178
uridine phosphorylase; Provisional
 64-138 5.19e-07

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 47.73  E-value: 5.19e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 566006152  64 TTVVGNTMCTLDFYEGQGRLDgALCSYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVCVTLLNR 138
Cdd:PRK11178 148 TTHVGVTASSDTFYPGQERYD-TYSGRVVRRFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNR 221
 
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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