NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1622965932|ref|XP_028682326|]
View 

prolyl 4-hydroxylase subunit alpha-1 isoform X4 [Macaca mulatta]

Protein Classification

prolyl 4-hydroxylase( domain architecture ID 20591303)

prolyl 4-hydroxylase catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins

CATH:  2.60.120.620
EC:  1.14.11.2
Gene Ontology:  GO:0004656|GO:0005506

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 258-431 3.63e-53

Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor.


:

Pssm-ID: 214780  Cd Length: 165  Bit Score: 175.65  E-value: 3.63e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622965932  258 SDAEIEIVKDLAKPRLRRATISNPITGDLETVHYRISKSAWLSGYE-NPVVSRINMRIQDLTGL---DVSTAEELQVANY 333
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGIGNPNETSQYRQSNGTWLELLErDLVIERIRQRLADFLGLlagLPLSAEDAQVARY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622965932  334 GVGGQYEPHFDFARKdepdafkelgtGNRIATWLFYMSDVSAGGATVFPE----VGASVWPKKGTAVFWYNlfasgeGDY 409
Cdd:smart00702  81 GPGGHYGPHVDNFLY-----------GDRIATFILYLNDVEEGGELVFPGlrlmVVATVKPKKGDLLFFPS------GHG 143

                          170       180
                   ....*....|....*....|..
gi 1622965932  410 STRHAACPVLVGNKWVSNKWLH 431
Cdd:smart00702 144 RSLHGVCPVTRGSRWAITGWIR 165
P4Ha_N pfam08336
Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are ...
 1-68 2.27e-22

Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are eukaryotic proteins, and include all three isoforms of the prolyl 4-hydroxylase alpha subunit. This enzyme (EC:1.14.11.2) is important in the post-translational modification of collagen, as it catalyzes the formation of 4-hydroxyproline. In vertebrates, the complete enzyme is an alpha2-beta2 tetramer; the beta-subunit is identical to protein disulphide isomerase. The function of the N-terminal region featured in this family does not seem to be known.


:

Pssm-ID: 462433  Cd Length: 135  Bit Score: 92.34  E-value: 2.27e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622965932   1 MKRLNTEWSELENLVLKDMSDGFISNLTIQRQY---FPNDEDQVGAAKALLRLQDTYNLDTDTISKGNLPG 68
Cdd:pfam08336  65 IKRLHQDWPKWEKLMKTNQAVGFLEQLTEMRSRllkLPTDEDLEGAAEALLRLQDTYNLDPSDLANGNLNG 135
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 77-158 3.93e-04

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 40.56  E-value: 3.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622965932  77 AEDCFELGKVAYTEADYyhtelwmEQALRQLDEGEISTIDKVSVLDYLSYAVYQQGDLDKALVLTKKLLELDPEHQRANG 156
Cdd:COG4783     4 AEALYALAQALLLAGDY-------DEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARL 76


                  ..
gi 1622965932 157 NL 158
Cdd:COG4783    77 NL 78
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 258-431 3.63e-53

Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor.


Pssm-ID: 214780  Cd Length: 165  Bit Score: 175.65  E-value: 3.63e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622965932  258 SDAEIEIVKDLAKPRLRRATISNPITGDLETVHYRISKSAWLSGYE-NPVVSRINMRIQDLTGL---DVSTAEELQVANY 333
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGIGNPNETSQYRQSNGTWLELLErDLVIERIRQRLADFLGLlagLPLSAEDAQVARY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622965932  334 GVGGQYEPHFDFARKdepdafkelgtGNRIATWLFYMSDVSAGGATVFPE----VGASVWPKKGTAVFWYNlfasgeGDY 409
Cdd:smart00702  81 GPGGHYGPHVDNFLY-----------GDRIATFILYLNDVEEGGELVFPGlrlmVVATVKPKKGDLLFFPS------GHG 143

                          170       180
                   ....*....|....*....|..
gi 1622965932  410 STRHAACPVLVGNKWVSNKWLH 431
Cdd:smart00702 144 RSLHGVCPVTRGSRWAITGWIR 165
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
 247-436 2.92e-34

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 130.17  E-value: 2.92e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622965932 247 KPRIIRFHDIISDAEIEIVKDLAKPRLRRATISNPITGDLETVHYRISKSAWLSGYENPVVSRINMRIQDLTGLDVSTAE 326
Cdd:PLN00052   53 QPRIFVYKGFLSDAECDHLVKLAKKKIQRSMVADNKSGKSVMSEVRTSSGMFLDKRQDPVVSRIEERIAAWTFLPEENAE 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622965932 327 ELQVANYGVGGQYEPHFDFARkdepDAFKELGTGNRIATWLFYMSDVSAGGATVFPEV------------------GASV 388
Cdd:PLN00052  133 NIQILRYEHGQKYEPHFDYFH----DKINQALGGHRYATVLMYLSTVDKGGETVFPNAegwenqpkddtfsecahkGLAV 208

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1622965932 389 WPKKGTAVFWYNLFASGEGDYSTRHAACPVLVGNKWVSNKWLHERGQE 436
Cdd:PLN00052  209 KPVKGDAVLFFSLHIDGVPDPLSLHGSCPVIEGEKWSAPKWIHIRSYE 256
P4Ha_N pfam08336
Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are ...
 1-68 2.27e-22

Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are eukaryotic proteins, and include all three isoforms of the prolyl 4-hydroxylase alpha subunit. This enzyme (EC:1.14.11.2) is important in the post-translational modification of collagen, as it catalyzes the formation of 4-hydroxyproline. In vertebrates, the complete enzyme is an alpha2-beta2 tetramer; the beta-subunit is identical to protein disulphide isomerase. The function of the N-terminal region featured in this family does not seem to be known.


Pssm-ID: 462433  Cd Length: 135  Bit Score: 92.34  E-value: 2.27e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622965932   1 MKRLNTEWSELENLVLKDMSDGFISNLTIQRQY---FPNDEDQVGAAKALLRLQDTYNLDTDTISKGNLPG 68
Cdd:pfam08336  65 IKRLHQDWPKWEKLMKTNQAVGFLEQLTEMRSRllkLPTDEDLEGAAEALLRLQDTYNLDPSDLANGNLNG 135
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 328-431 2.04e-20

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily.


Pssm-ID: 463943  Cd Length: 94  Bit Score: 85.51  E-value: 2.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622965932 328 LQVANYGVGGQYEPHFDFARKDEpdafkelGTGNRIATWLFYMSDVSA--GGATVF--PEVGASVWPKKGTAVFWYNlfa 403
Cdd:pfam13640   1 LQLARYGDGGFYKPHLDFFEGAE-------GGGQRRLTVVLYLNDWEEeeGGELVLydGDGVEDIKPKKGRLVLFPS--- 70

                          90       100
                  ....*....|....*....|....*...
gi 1622965932 404 sgegDYSTRHAACPVLVGNKWVSNKWLH 431
Cdd:pfam13640  71 ----SELSLHEVLPVTGGERWSITGWFR 94
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 77-158 3.93e-04

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 40.56  E-value: 3.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622965932  77 AEDCFELGKVAYTEADYyhtelwmEQALRQLDEGEISTIDKVSVLDYLSYAVYQQGDLDKALVLTKKLLELDPEHQRANG 156
Cdd:COG4783     4 AEALYALAQALLLAGDY-------DEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARL 76


                  ..
gi 1622965932 157 NL 158
Cdd:COG4783    77 NL 78
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 258-431 3.63e-53

Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor.


Pssm-ID: 214780  Cd Length: 165  Bit Score: 175.65  E-value: 3.63e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622965932  258 SDAEIEIVKDLAKPRLRRATISNPITGDLETVHYRISKSAWLSGYE-NPVVSRINMRIQDLTGL---DVSTAEELQVANY 333
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGIGNPNETSQYRQSNGTWLELLErDLVIERIRQRLADFLGLlagLPLSAEDAQVARY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622965932  334 GVGGQYEPHFDFARKdepdafkelgtGNRIATWLFYMSDVSAGGATVFPE----VGASVWPKKGTAVFWYNlfasgeGDY 409
Cdd:smart00702  81 GPGGHYGPHVDNFLY-----------GDRIATFILYLNDVEEGGELVFPGlrlmVVATVKPKKGDLLFFPS------GHG 143

                          170       180
                   ....*....|....*....|..
gi 1622965932  410 STRHAACPVLVGNKWVSNKWLH 431
Cdd:smart00702 144 RSLHGVCPVTRGSRWAITGWIR 165
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
 247-436 2.92e-34

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 130.17  E-value: 2.92e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622965932 247 KPRIIRFHDIISDAEIEIVKDLAKPRLRRATISNPITGDLETVHYRISKSAWLSGYENPVVSRINMRIQDLTGLDVSTAE 326
Cdd:PLN00052   53 QPRIFVYKGFLSDAECDHLVKLAKKKIQRSMVADNKSGKSVMSEVRTSSGMFLDKRQDPVVSRIEERIAAWTFLPEENAE 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622965932 327 ELQVANYGVGGQYEPHFDFARkdepDAFKELGTGNRIATWLFYMSDVSAGGATVFPEV------------------GASV 388
Cdd:PLN00052  133 NIQILRYEHGQKYEPHFDYFH----DKINQALGGHRYATVLMYLSTVDKGGETVFPNAegwenqpkddtfsecahkGLAV 208

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1622965932 389 WPKKGTAVFWYNLFASGEGDYSTRHAACPVLVGNKWVSNKWLHERGQE 436
Cdd:PLN00052  209 KPVKGDAVLFFSLHIDGVPDPLSLHGSCPVIEGEKWSAPKWIHIRSYE 256
P4Ha_N pfam08336
Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are ...
 1-68 2.27e-22

Prolyl 4-Hydroxylase alpha-subunit, N-terminal region; The members of this family are eukaryotic proteins, and include all three isoforms of the prolyl 4-hydroxylase alpha subunit. This enzyme (EC:1.14.11.2) is important in the post-translational modification of collagen, as it catalyzes the formation of 4-hydroxyproline. In vertebrates, the complete enzyme is an alpha2-beta2 tetramer; the beta-subunit is identical to protein disulphide isomerase. The function of the N-terminal region featured in this family does not seem to be known.


Pssm-ID: 462433  Cd Length: 135  Bit Score: 92.34  E-value: 2.27e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622965932   1 MKRLNTEWSELENLVLKDMSDGFISNLTIQRQY---FPNDEDQVGAAKALLRLQDTYNLDTDTISKGNLPG 68
Cdd:pfam08336  65 IKRLHQDWPKWEKLMKTNQAVGFLEQLTEMRSRllkLPTDEDLEGAAEALLRLQDTYNLDPSDLANGNLNG 135
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 328-431 2.04e-20

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily.


Pssm-ID: 463943  Cd Length: 94  Bit Score: 85.51  E-value: 2.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622965932 328 LQVANYGVGGQYEPHFDFARKDEpdafkelGTGNRIATWLFYMSDVSA--GGATVF--PEVGASVWPKKGTAVFWYNlfa 403
Cdd:pfam13640   1 LQLARYGDGGFYKPHLDFFEGAE-------GGGQRRLTVVLYLNDWEEeeGGELVLydGDGVEDIKPKKGRLVLFPS--- 70

                          90       100
                  ....*....|....*....|....*...
gi 1622965932 404 sgegDYSTRHAACPVLVGNKWVSNKWLH 431
Cdd:pfam13640  71 ----SELSLHEVLPVTGGERWSITGWFR 94
2OG-FeII_Oxy pfam03171
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 325-432 1.75e-07

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily. This family includes the C-terminal of prolyl 4-hydroxylase alpha subunit. The holoenzyme has the activity EC:1.14.11.2 catalysing the reaction: Procollagen L-proline + 2-oxoglutarate + O2 <=> procollagen trans- 4-hydroxy-L-proline + succinate + CO2. The full enzyme consists of a alpha2 beta2 complex with the alpha subunit contributing most of the parts of the active site. The family also includes lysyl hydrolases, isopenicillin synthases and AlkB.


Pssm-ID: 397334 [Multi-domain]  Cd Length: 101  Bit Score: 48.99  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622965932 325 AEELQVANYgvggqYEPHfdfarkdePDAFKELGTG-NRIATWLFYMSDVSAGGATVF--------PEVGASVWPKKGTA 395
Cdd:pfam03171   1 PDQCLVLNY-----YPPH--------PDPDLTLGLGpHTDASILTILLQDDVGGLQVFkdgkwidvPPLPGALVVNIGDQ 67

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1622965932 396 V-FWYNLFasgegDYSTRHAACPVLVG-NKWVSNKWLHE 432
Cdd:pfam03171  68 LeLLSNGR-----YKSVLHRVLPVNKGkERISIAFFLRP 101
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 77-158 3.93e-04

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 40.56  E-value: 3.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622965932  77 AEDCFELGKVAYTEADYyhtelwmEQALRQLDEGEISTIDKVSVLDYLSYAVYQQGDLDKALVLTKKLLELDPEHQRANG 156
Cdd:COG4783     4 AEALYALAQALLLAGDY-------DEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARL 76


                  ..
gi 1622965932 157 NL 158
Cdd:COG4783    77 NL 78
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 101-158 1.91e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 38.79  E-value: 1.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622965932 101 EQALRQLDEGEISTIDKVSVLDYLSYAVYQQGDLDKALVLTKKLLELDPEHQRANGNL 158
Cdd:COG5010    71 EESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNL 128
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 77-158 1.98e-03

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 38.45  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622965932  77 AEDCFELGKVAYTEADYYHTELWMEQALRqLDEgeistiDKVSVLDYLSYAVYQQGDLDKALVLTKKLLELDPEHQRANG 156
Cdd:COG4235    17 AEGWLLLGRAYLRLGRYDEALAAYEKALR-LDP------DNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALY 89


                  ..
gi 1622965932 157 NL 158
Cdd:COG4235    90 LL 91
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 83-158 7.22e-03

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 36.71  E-value: 7.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622965932  83 LGKVAYTEADYyhtelwmEQALRQLDEGEISTIDKVSVLDYLSYAVYQQGDLDKALVLTKKLLELDPEHQRANGNL 158
Cdd:COG4783    44 LGEILLQLGDL-------DEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRL 112
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH