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Conserved domains on  [gi|2477813389|gb|KAJ8244981|]
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hypothetical protein LV160_000565 [Aspergillus fumigatus]

Protein Classification

signal recognition particle receptor subunit beta( domain architecture ID 10134869)

signal recognition particle (SRP) receptor subunit beta, together with SRP subunit alpha, forms the heterodimeric SRP receptor that binds SRP to regulate protein translocation across the ER membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
 53-318 4.12e-49

Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.


:

Pssm-ID: 206691 [Multi-domain]  Cd Length: 202  Bit Score: 162.49  E-value: 4.12e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477813389  53 SNFLLLGPSGAGKTALLSLLESKTSRlakatqtthtsqtstSAIVSLPPSVPTasnryrsvndysVKDVSKNPVRYRLKD 132
Cdd:cd04105     1 PTVLLLGPSDSGKTALFTKLTTGKVR---------------STVTSIEPNVAS------------FYSNSSKGKKLTLVD 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477813389 133 TPGHGKLReaqglselvSMATAKDKKLkLRAVIFMVDTAALTEEntLRDTASYLHDVLLAlqkralkrgksSAKVASEIP 212
Cdd:cd04105    54 VPGHEKLR---------DKLLEYLKAS-LKAIVFVVDSATFQKN--IRDVAEFLYDILTD-----------LEKIKNKIP 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477813389 213 VLVAANKQDLFTALPPGSVREKLETEIDRIRKSKSKGLMNASEDTATVEDEDDTLGsidaqDNFSFRLLEDEvgvkvdvv 292
Cdd:cd04105   111 ILIACNKQDLFTAKPAKKIKELLEKEINTLRESRSKSLESLDGDDGSKDTLGDKGG-----KDFEFDQLEGE-------- 177

                         250       260
                  ....*....|....*....|....*....
gi 2477813389 293 ggvvKGDEEGNI---GAGVRRWEEWIGQC 318
Cdd:cd04105   178 ----VDFVEGSVkksKGGIDDIEEWIDEL 202
 
Name Accession Description Interval E-value
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
 53-318 4.12e-49

Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.


Pssm-ID: 206691 [Multi-domain]  Cd Length: 202  Bit Score: 162.49  E-value: 4.12e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477813389  53 SNFLLLGPSGAGKTALLSLLESKTSRlakatqtthtsqtstSAIVSLPPSVPTasnryrsvndysVKDVSKNPVRYRLKD 132
Cdd:cd04105     1 PTVLLLGPSDSGKTALFTKLTTGKVR---------------STVTSIEPNVAS------------FYSNSSKGKKLTLVD 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477813389 133 TPGHGKLReaqglselvSMATAKDKKLkLRAVIFMVDTAALTEEntLRDTASYLHDVLLAlqkralkrgksSAKVASEIP 212
Cdd:cd04105    54 VPGHEKLR---------DKLLEYLKAS-LKAIVFVVDSATFQKN--IRDVAEFLYDILTD-----------LEKIKNKIP 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477813389 213 VLVAANKQDLFTALPPGSVREKLETEIDRIRKSKSKGLMNASEDTATVEDEDDTLGsidaqDNFSFRLLEDEvgvkvdvv 292
Cdd:cd04105   111 ILIACNKQDLFTAKPAKKIKELLEKEINTLRESRSKSLESLDGDDGSKDTLGDKGG-----KDFEFDQLEGE-------- 177

                         250       260
                  ....*....|....*....|....*....
gi 2477813389 293 ggvvKGDEEGNI---GAGVRRWEEWIGQC 318
Cdd:cd04105   178 ----VDFVEGSVkksKGGIDDIEEWIDEL 202
SRPRB pfam09439
Signal recognition particle receptor beta subunit; The beta subunit of the signal recognition ...
 55-282 6.50e-26

Signal recognition particle receptor beta subunit; The beta subunit of the signal recognition particle receptor (SRP) is a transmembrane GTPase which anchors the alpha subunit to the endoplasmic reticulum membrane.


Pssm-ID: 462797 [Multi-domain]  Cd Length: 181  Bit Score: 101.37  E-value: 6.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477813389  55 FLLLGPSGAGKTALLSLLESKTSRLAkatqtthtsqtstsaIVSLPPSvptASNRYRSVNDYSVKdvsknpvryrLKDTP 134
Cdd:pfam09439   6 VIIAGLCDSGKTSLFTLLTTDSVRPT---------------VTSQEPS---AAYRYMLNKGNSFT----------LIDFP 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477813389 135 GHGKLReaQGLSElvsmaTAKDKKlKLRAVIFMVDTAALTEEntLRDTASYLHDVLLALQKRALKrgkssakvaseIPVL 214
Cdd:pfam09439  58 GHVKLR--YKLLE-----TLKDSS-SLKGIVFVVDSTIFPKE--VTDTAEFLYDILSITELLKNG-----------IDIL 116

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2477813389 215 VAANKQDLFTALPPGSVREKLETEIDRIRKSKSKGLMNASEDtatvEDEDDTLGsiDAQDNFSFRLLE 282
Cdd:pfam09439 117 IACNKQESFTARPPKKIKQALEKEINTIRERRSKALSGLDGS----EDLSAVLG--KKGKGFKFDQLE 178
 
Name Accession Description Interval E-value
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
 53-318 4.12e-49

Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.


Pssm-ID: 206691 [Multi-domain]  Cd Length: 202  Bit Score: 162.49  E-value: 4.12e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477813389  53 SNFLLLGPSGAGKTALLSLLESKTSRlakatqtthtsqtstSAIVSLPPSVPTasnryrsvndysVKDVSKNPVRYRLKD 132
Cdd:cd04105     1 PTVLLLGPSDSGKTALFTKLTTGKVR---------------STVTSIEPNVAS------------FYSNSSKGKKLTLVD 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477813389 133 TPGHGKLReaqglselvSMATAKDKKLkLRAVIFMVDTAALTEEntLRDTASYLHDVLLAlqkralkrgksSAKVASEIP 212
Cdd:cd04105    54 VPGHEKLR---------DKLLEYLKAS-LKAIVFVVDSATFQKN--IRDVAEFLYDILTD-----------LEKIKNKIP 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477813389 213 VLVAANKQDLFTALPPGSVREKLETEIDRIRKSKSKGLMNASEDTATVEDEDDTLGsidaqDNFSFRLLEDEvgvkvdvv 292
Cdd:cd04105   111 ILIACNKQDLFTAKPAKKIKELLEKEINTLRESRSKSLESLDGDDGSKDTLGDKGG-----KDFEFDQLEGE-------- 177

                         250       260
                  ....*....|....*....|....*....
gi 2477813389 293 ggvvKGDEEGNI---GAGVRRWEEWIGQC 318
Cdd:cd04105   178 ----VDFVEGSVkksKGGIDDIEEWIDEL 202
SRPRB pfam09439
Signal recognition particle receptor beta subunit; The beta subunit of the signal recognition ...
 55-282 6.50e-26

Signal recognition particle receptor beta subunit; The beta subunit of the signal recognition particle receptor (SRP) is a transmembrane GTPase which anchors the alpha subunit to the endoplasmic reticulum membrane.


Pssm-ID: 462797 [Multi-domain]  Cd Length: 181  Bit Score: 101.37  E-value: 6.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477813389  55 FLLLGPSGAGKTALLSLLESKTSRLAkatqtthtsqtstsaIVSLPPSvptASNRYRSVNDYSVKdvsknpvryrLKDTP 134
Cdd:pfam09439   6 VIIAGLCDSGKTSLFTLLTTDSVRPT---------------VTSQEPS---AAYRYMLNKGNSFT----------LIDFP 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477813389 135 GHGKLReaQGLSElvsmaTAKDKKlKLRAVIFMVDTAALTEEntLRDTASYLHDVLLALQKRALKrgkssakvaseIPVL 214
Cdd:pfam09439  58 GHVKLR--YKLLE-----TLKDSS-SLKGIVFVVDSTIFPKE--VTDTAEFLYDILSITELLKNG-----------IDIL 116

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2477813389 215 VAANKQDLFTALPPGSVREKLETEIDRIRKSKSKGLMNASEDtatvEDEDDTLGsiDAQDNFSFRLLE 282
Cdd:pfam09439 117 IACNKQESFTARPPKKIKQALEKEINTIRERRSKALSGLDGS----EDLSAVLG--KKGKGFKFDQLE 178
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 56-262 1.14e-05

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 44.75  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477813389  56 LLLGPSGAGKTALL-SLLESKTSrlakatqtthtsqtstsaIVSLPPSVPTASNRYRsvndysvKDVSKNPVRYRLKDTP 134
Cdd:cd00882     1 VVVGRGGVGKSSLLnALLGGEVG------------------EVSDVPGTTRDPDVYV-------KELDKGKVKLVLVDTP 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477813389 135 GHGKLReaqglsELVSMATAKDKKLKLRAVIFMVDtaaLTEENTLRDTASYLHDvllalqkralkrgkssAKVASEIPVL 214
Cdd:cd00882    56 GLDEFG------GLGREELARLLLRGADLILLVVD---STDRESEEDAKLLILR----------------RLRKEGIPII 110

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2477813389 215 VAANKQDlftaLPPGSVREKLETEIDRIRKSKSKGLMNASEDTATVED 262
Cdd:cd00882   111 LVGNKID----LLEEREVEELLRLEELAKILGVPVFEVSAKTGEGVDE 154
Arl3 cd04155
Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most ...
 163-241 1.66e-04

Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most Arf family members in the N-terminal extension. In is inactive, GDP-bound form, the N-terminal extension forms an elongated loop that is hydrophobically anchored into the membrane surface; however, it has been proposed that this region might form a helix in the GTP-bound form. The delta subunit of the rod-specific cyclic GMP phosphodiesterase type 6 (PDEdelta) is an Arl3 effector. Arl3 binds microtubules in a regulated manner to alter specific aspects of cytokinesis via interactions with retinitis pigmentosa 2 (RP2). It has been proposed that RP2 functions in concert with Arl3 to link the cell membrane and the cytoskeleton in photoreceptors as part of the cell signaling or vesicular transport machinery. In mice, the absence of Arl3 is associated with abnormal epithelial cell proliferation and cyst formation.


Pssm-ID: 206721 [Multi-domain]  Cd Length: 174  Bit Score: 41.61  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477813389 163 AVIFMVDTAaltEENTLRDTASYLHDVLLALQKRalkrgkssakvasEIPVLVAANKQDLFTALPPGSVREKLE--TEID 240
Cdd:cd04155    85 VLIYVIDSA---DRKRFEEAGQELVELLEEEKLA-------------GVPVLVFANKQDLLTAAPAEEVAEALNlhDIRD 148


                  .
gi 2477813389 241 R 241
Cdd:cd04155   149 R 149
Arl9_Arfrp2_like cd04162
Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first ...
 56-244 1.09e-03

Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first identified as part of the Human Cancer Genome Project. It maps to chromosome 4q12 and is sometimes referred to as Arfrp2 (Arf-related protein 2). This is a novel subfamily identified in human cancers that is uncharacterized to date.


Pssm-ID: 133362 [Multi-domain]  Cd Length: 164  Bit Score: 38.97  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477813389  56 LLLGPSGAGKTALLSLLESKTSRLAkatqtthtsqtstsaivslppSVPTASnryrsvndYSVKDVSKNPVRYRLKDTPG 135
Cdd:cd04162     3 LVLGLDGAGKTSLLHSLSSERSLES---------------------VVPTTG--------FNSVAIPTQDAIMELLEIGG 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477813389 136 HGKLReaQGLSELVSmatakdkklKLRAVIFMVDTAALTEENTLRDtasYLHDvllALQKralkrgkssakvASEIPVLV 215
Cdd:cd04162    54 SQNLR--KYWKRYLS---------GSQGLIFVVDSADSERLPLARQ---ELHQ---LLQH------------PPDLPLVV 104

                         170       180       190
                  ....*....|....*....|....*....|
gi 2477813389 216 AANKQDLFTALPPGSVREKLE-TEIDRIRK 244
Cdd:cd04162   105 LANKQDLPAARSVQEIHKELElEPIARGRR 134
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
 56-236 2.30e-03

ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.


Pssm-ID: 206644 [Multi-domain]  Cd Length: 158  Bit Score: 37.94  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477813389  56 LLLGPSGAGKTALLSLLESKtsrlakatqtthtsqtstsaivSLPPSVPTasnryrsvNDYSVKDVSKNPVRYRLKDTPG 135
Cdd:cd00878     3 LMLGLDGAGKTTILYKLKLG----------------------EVVTTIPT--------IGFNVETVEYKNVKFTVWDVGG 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477813389 136 HGKLR--------EAQGLselvsmatakdkklklravIFMVDTAalteeNTLR--DTASYLHDVLlalqkralkrgksSA 205
Cdd:cd00878    53 QDKIRplwkhyyeNTDGL-------------------IFVVDSS-----DRERieEAKNELHKLL-------------NE 95

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2477813389 206 KVASEIPVLVAANKQDLFTALPPGSVREKLE 236
Cdd:cd00878    96 EELKGAPLLILANKQDLPGALTESELIELLG 126
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
 56-244 8.93e-03

ADP-ribosylation factor family; Pfam combines a number of different Prosite families together


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 36.43  E-value: 8.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477813389  56 LLLGPSGAGKTALLSLLESKTsrlakatqtthtsqtstsaIVSLPPSVptasnryrsvnDYSVKDVSKNPVRYRLKDTPG 135
Cdd:pfam00025   4 LILGLDNAGKTTILYKLKLGE-------------------IVTTIPTI-----------GFNVETVTYKNVKFTVWDVGG 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477813389 136 HGKLREAQglselvsmataKDKKLKLRAVIFMVDTAALTEentLRDTASYLHDVLlalQKRALKRgkssakvaseIPVLV 215
Cdd:pfam00025  54 QESLRPLW-----------RNYFPNTDAVIFVVDSADRDR---IEEAKEELHALL---NEEELAD----------APLLI 106

                         170       180
                  ....*....|....*....|....*....
gi 2477813389 216 AANKQDLFTALPPGSVREKLETEIDRIRK 244
Cdd:pfam00025 107 LANKQDLPGAMSEAEIRELLGLHELKDRP 135
 
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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