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Conserved domains on  [gi|449448800|ref|XP_004142153|]
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protein PHOTOSYSTEM I ASSEMBLY 2, chloroplastic isoform X1 [Cucumis sativus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK14276 super family cl36351
chaperone protein DnaJ; Provisional
 101-156 2.41e-07

chaperone protein DnaJ; Provisional


The actual alignment was detected with superfamily member PRK14276:

Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 49.70  E-value: 2.41e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449448800 101 CRNCGGSGA------VLCDMCGGTG-----KWKALNRKRAKdvyefTECPNCYGRGKLV---CPVCLGTG 156
Cdd:PRK14276 149 CHTCNGSGAkpgtspVTCGKCHGSGvitvdTQTPLGMMRRQ-----VTCDVCHGTGKEIkepCQTCHGTG 213
 
Name Accession Description Interval E-value
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 101-156 2.41e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 49.70  E-value: 2.41e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449448800 101 CRNCGGSGA------VLCDMCGGTG-----KWKALNRKRAKdvyefTECPNCYGRGKLV---CPVCLGTG 156
Cdd:PRK14276 149 CHTCNGSGAkpgtspVTCGKCHGSGvitvdTQTPLGMMRRQ-----VTCDVCHGTGKEIkepCQTCHGTG 213
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 101-156 1.78e-04

Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of DnaJ/Hsp40 (heat shock protein 40). DnaJ proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonin family. Hsp40 proteins are characterized by the presence of an N-terminal J domain, which mediates the interaction with Hsp70. This central domain contains four repeats of a CxxCxGxG motif and binds to two Zinc ions. It has been implicated in substrate binding.


Pssm-ID: 199908 [Multi-domain]  Cd Length: 65  Bit Score: 38.01  E-value: 1.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449448800 101 CRNCGGSGA------VLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLV---CPVCLGTG 156
Cdd:cd10719    1 CPTCNGSGAkpgtkpKTCPTCGGSGQVRQVQGTGFGFFQTQTTCPTCGGTGKIIkdpCPKCKGKG 65
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 101-156 2.95e-04

DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four repeats of the motif CXXCXGXG where X is any amino acid. The isolated cysteine rich domain folds in zinc dependent fashion. Each set of two repeats binds one unit of zinc. Although this domain has been implicated in substrate binding, no evidence of specific interaction between the isolated DNAJ cysteine rich domain and various hydrophobic peptides has been found.


Pssm-ID: 459904 [Multi-domain]  Cd Length: 65  Bit Score: 37.54  E-value: 2.95e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449448800  101 CRNCGGSGA------VLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLV---CPVCLGTG 156
Cdd:pfam00684   1 CPTCNGSGAkpgtkpTTCPTCGGTGQVRRVQQTGPGFFQMQSTCPTCGGTGKIIkdpCKKCKGKG 65
 
Name Accession Description Interval E-value
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 101-156 2.41e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 49.70  E-value: 2.41e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449448800 101 CRNCGGSGA------VLCDMCGGTG-----KWKALNRKRAKdvyefTECPNCYGRGKLV---CPVCLGTG 156
Cdd:PRK14276 149 CHTCNGSGAkpgtspVTCGKCHGSGvitvdTQTPLGMMRRQ-----VTCDVCHGTGKEIkepCQTCHGTG 213
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 76-156 9.41e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 47.74  E-value: 9.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449448800  76 SVTLMKSYGGtVTEAIanTMDGKPACRNCGGSGA------VLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLV- 148
Cdd:PRK14278 120 RLDLEECATG-VTKQV--TVDTAVLCDRCHGKGTagdskpVTCDTCGGRGEVQTVQRSFLGQVMTSRPCPTCRGVGEVIp 196

                         90
                 ....*....|
gi 449448800 149 --CPVCLGTG 156
Cdd:PRK14278 197 dpCHECAGDG 206
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 101-156 1.42e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 47.23  E-value: 1.42e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 449448800 101 CRNCGGSGA-----VLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKL---VCPVCLGTG 156
Cdd:PRK14290 152 CPDCSGTGAkngklITCPTCHGTGQQRIVRGQGFFRMVTVTTCRTCGGRGRIpeeKCPRCNGTG 215
PRK14295 PRK14295
molecular chaperone DnaJ;
75-156 1.64e-06

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 47.15  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449448800  75 SSVTLmksyggTVTEAIANT-----MDGKPACRNCGGSGAV------LCDMCGGTGKwkalnRKRAKDVYEFTE-CPNCY 142
Cdd:PRK14295 144 SEVTL------SFTEAIDGAtvplrLTSQAPCPACSGTGAKngttprVCPTCSGTGQ-----VSRNSGGFSLSEpCPDCK 212

                         90
                 ....*....|....*..
gi 449448800 143 GRGKLV---CPVCLGTG 156
Cdd:PRK14295 213 GRGLIAddpCLVCKGSG 229
PRK14293 PRK14293
molecular chaperone DnaJ;
101-156 2.68e-06

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 46.52  E-value: 2.68e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449448800 101 CRNCGGSGA------VLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLV---CPVCLGTG 156
Cdd:PRK14293 146 CETCRGSGAkpgtgpTTCSTCGGAGQVRRATRTPFGSFTQVSECPTCNGTGQVIedpCDACGGQG 210
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 100-156 3.89e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 45.91  E-value: 3.89e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 449448800 100 ACRNCGGSGA------VLCDMCGGTGkwkalnRKRAKDVYeFT---ECPNCYGRGKLV---CPVCLGTG 156
Cdd:PRK10767 144 TCDTCHGSGAkpgtspKTCPTCHGAG------QVRMQQGF-FTvqqTCPTCHGRGKIIkdpCKKCHGQG 205
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 100-157 4.73e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 45.75  E-value: 4.73e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 449448800 100 ACRNCGGSGA------VLCDMCGGTGKWKalnrkRAKDVYEF-TECPNCYGRGKLV---CPVCLGTGL 157
Cdd:PRK14286 152 SCVDCNGSGAskgsspTTCPDCGGSGQIR-----RTQGFFSVaTTCPTCRGKGTVIsnpCKTCGGQGL 214
PLN03165 PLN03165
chaperone protein dnaJ-related; Provisional
 101-157 6.54e-06

chaperone protein dnaJ-related; Provisional


Pssm-ID: 178709 [Multi-domain]  Cd Length: 111  Bit Score: 43.27  E-value: 6.54e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 449448800 101 CRNCGGSGAVLCDMCGGTGkwkALNRKRAKDVYEFTECPNCYGRGKLVCPVCLGTGL 157
Cdd:PLN03165  44 CFPCSGTGAQVCRFCVGSG---NVTVELGGGEKEVSKCINCDGAGSLTCTTCQGSGI 97
PRK14297 PRK14297
molecular chaperone DnaJ;
101-156 7.29e-06

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 45.16  E-value: 7.29e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449448800 101 CRNCGGSGA------VLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLV---CPVCLGTG 156
Cdd:PRK14297 151 CETCNGTGAkpgtspKTCDKCGGTGQIRVQRNTPLGSFVSTTTCDKCGGSGKVIedpCNKCHGKG 215
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 76-156 8.00e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 45.14  E-value: 8.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449448800  76 SVTLMKSYGGTVTEAIANTMDgkpACRNCGGSGA------VLCDMCGGTGKWKalnrkRAKDVYEF-TECPNCYGRGKLV 148
Cdd:PRK14294 125 TLPFLEAAFGTEKEIRIQKLE---TCEECHGSGCepgtspTTCPQCGGSGQVT-----QSQGFFSIrTTCPRCRGMGKVI 196

                         90
                 ....*....|.
gi 449448800 149 ---CPVCLGTG 156
Cdd:PRK14294 197 vspCKTCHGQG 207
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 77-156 2.11e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 43.72  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449448800  77 VTLMKSYGGtvtEAIANTMDGKPACRNC-------GGSGAVLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLV- 148
Cdd:PRK14292 121 ITLEQARAG---EEVEVEVDRLTECEHChgsrtepGGKPPKTCPTCRGAGAVRAQARTIFGVVETQQPCPTCRGEGQIIt 197

                         90
                 ....*....|
gi 449448800 149 --CPVCLGTG 156
Cdd:PRK14292 198 dpCTVCRGRG 207
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 101-157 6.22e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 42.50  E-value: 6.22e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 449448800 101 CRNCGGS------GAVLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLV---CPVCLGTGL 157
Cdd:PRK14283 149 CPVCNGSraepgsEVKTCPTCGGTGQVKQVRNTILGQMMNVTTCPDCQGEGKIVekpCSNCHGKGV 214
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 101-156 7.34e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 42.04  E-value: 7.34e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 449448800 101 CRNCGGSGAV------LCDMCGGTGKwkalnRKRAKDVYEF-TECPNCYGRGKLV---CPVCLGTG 156
Cdd:PRK14301 147 CDDCGGSGAApgtspeTCRHCGGSGQ-----VRQSQGFFQIaVPCPVCRGEGRVIthpCPKCKGSG 207
PRK14289 PRK14289
molecular chaperone DnaJ;
100-157 9.07e-05

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 42.13  E-value: 9.07e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 449448800 100 ACRNCGGSGA------VLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLV---CPVCLGTGL 157
Cdd:PRK14289 156 PCSHCHGTGAegnngsETCPTCKGSGSVTRVQNTILGTMQTQSTCPTCNGEGKIIkkkCKKCGGEGI 222
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 101-156 1.78e-04

Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of DnaJ/Hsp40 (heat shock protein 40). DnaJ proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonin family. Hsp40 proteins are characterized by the presence of an N-terminal J domain, which mediates the interaction with Hsp70. This central domain contains four repeats of a CxxCxGxG motif and binds to two Zinc ions. It has been implicated in substrate binding.


Pssm-ID: 199908 [Multi-domain]  Cd Length: 65  Bit Score: 38.01  E-value: 1.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449448800 101 CRNCGGSGA------VLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLV---CPVCLGTG 156
Cdd:cd10719    1 CPTCNGSGAkpgtkpKTCPTCGGSGQVRQVQGTGFGFFQTQTTCPTCGGTGKIIkdpCPKCKGKG 65
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 101-156 2.95e-04

DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four repeats of the motif CXXCXGXG where X is any amino acid. The isolated cysteine rich domain folds in zinc dependent fashion. Each set of two repeats binds one unit of zinc. Although this domain has been implicated in substrate binding, no evidence of specific interaction between the isolated DNAJ cysteine rich domain and various hydrophobic peptides has been found.


Pssm-ID: 459904 [Multi-domain]  Cd Length: 65  Bit Score: 37.54  E-value: 2.95e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449448800  101 CRNCGGSGA------VLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLV---CPVCLGTG 156
Cdd:pfam00684   1 CPTCNGSGAkpgtkpTTCPTCGGTGQVRRVQQTGPGFFQMQSTCPTCGGTGKIIkdpCKKCKGKG 65
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 101-156 3.16e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 40.22  E-value: 3.16e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 449448800 101 CRNCGGSGAVlcdmcggtgkwkalNRKRAKDVYEF---TECPNCYGRGKLV---CPVCLGTG 156
Cdd:PRK14298 161 CPTCGGTGQV--------------TTTRSTPLGQFvttTTCSTCHGRGQVIespCPVCSGTG 208
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 77-157 7.69e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 39.37  E-value: 7.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449448800  77 VTLMKSYGGTVTEAianTMDGKPACRNCGG------SGAVLCDMCGGTGKwkalNRKRAKDVYEFTECPNCYGRGKL--V 148
Cdd:PRK14291 138 ISLEEAYTGTTVSL---EVPRYVPCEACGGtgydpgSGEKVCPTCGGSGE----IYQRGGFFRISQTCPTCGGEGVLreP 210


                 ....*....
gi 449448800 149 CPVCLGTGL 157
Cdd:PRK14291 211 CSKCNGRGL 219
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 101-156 9.52e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 39.01  E-value: 9.52e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 449448800 101 CRNCGG------SGAVLCDMCGGTGKWKALNRK-RAKDVYEFTeCPNCYGRGKL---VCPVCLGTG 156
Cdd:PRK14282 155 CPHCGGtgvepgSGYVTCPKCHGTGRIREERRSfFGVFVSERT-CERCGGTGKIpgeYCHECGGSG 219
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 101-156 1.91e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 38.05  E-value: 1.91e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 449448800 101 CRNC------GGSGAVLCDMCGGTGKwkalnRKRAKDVYEFTE-CPNCYGRGKLV---CPVCLGTG 156
Cdd:PRK14285 149 CESClgkkseKGTSPSICNMCNGSGR-----VMQGGGFFRVTTtCPKCYGNGKIIsnpCKSCKGKG 209
DnaJ_C pfam01556
DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It ...
 76-161 5.15e-03

DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It is always found associated with pfam00226 and pfam00684. DnaJ is a chaperone associated with the Hsp70 heat-shock system involved in protein folding and renaturation after stress. The two C-terminal domains CTDI and CTDII, both incorporated in this family are necessary for maintaining the J-domains in their specific relative positions. Structural analysis of PDB:1nlt shows that PF00684 is nested within this DnaJ C-terminal region.


Pssm-ID: 460251 [Multi-domain]  Cd Length: 213  Bit Score: 36.46  E-value: 5.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449448800   76 SVTLMKSYGGTVTEAianTMDGKPACRNCGGSGA------VLCDMCGGTGKWkalnRKRAKDVYEFTECPNCYGRGKLV- 148
Cdd:pfam01556   6 ELTLEEAYFGCTKKI---KITRNVICDTCGGSGAkpgtspKTCPCCGGGGQV----RRQFGFFSTCTCCPCCGGGGKIId 78

                          90
                  ....*....|....*
gi 449448800  149 --CPVCLGTGLPNNK 161
Cdd:pfam01556  79 kcCKCCGGGGVVEKK 93
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 97-161 5.83e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 36.74  E-value: 5.83e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 449448800  97 GKPACRNCGGSGAV------LCDMCGGTGKwkaLNRKRAKDVYEFTeCPNCYGRGKLV---CPVCLGTGLPNNK 161
Cdd:PRK14284 157 GYKSCDACSGSGANssqgikVCDRCKGSGQ---VVQSRGFFSMAST-CPECGGEGRVItdpCSVCRGQGRIKDK 226
PLN03165 PLN03165
chaperone protein dnaJ-related; Provisional
 85-131 7.50e-03

chaperone protein dnaJ-related; Provisional


Pssm-ID: 178709 [Multi-domain]  Cd Length: 111  Bit Score: 34.79  E-value: 7.50e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 449448800  85 GTVTEAIANTMDGKPACRNCGGSGAVLCDMCGGTG-KWKALNRKRAKD 131
Cdd:PLN03165  62 GNVTVELGGGEKEVSKCINCDGAGSLTCTTCQGSGiQPRYLDRREFKD 109
 
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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