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Conserved domains on  [gi|89353281|ref|NP_001034796|]
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endosome-associated-trafficking regulator 1 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
261-433 1.16e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 1.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89353281    261 DRHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEMVRTLERKLEakMIKEEsdyhdlesvVQQVEQNLELMTKRAVK 340
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ--ILRER---------LANLERQLEELEAQLEE 327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89353281    341 AENHVVKLKQEISLLQAQVSNFQRENEALRcGQGASLTVVKQNADVALQNLRVVMNSAQASIKQLVSGAETLNlvAEILK 420
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKEELESLE-AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN--NEIER 404
                          170
                   ....*....|...
gi 89353281    421 SIDRISEVKDEEE 433
Cdd:TIGR02168  405 LEARLERLEDRRE 417
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
261-433 1.16e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 1.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89353281    261 DRHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEMVRTLERKLEakMIKEEsdyhdlesvVQQVEQNLELMTKRAVK 340
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ--ILRER---------LANLERQLEELEAQLEE 327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89353281    341 AENHVVKLKQEISLLQAQVSNFQRENEALRcGQGASLTVVKQNADVALQNLRVVMNSAQASIKQLVSGAETLNlvAEILK 420
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKEELESLE-AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN--NEIER 404
                          170
                   ....*....|...
gi 89353281    421 SIDRISEVKDEEE 433
Cdd:TIGR02168  405 LEARLERLEDRRE 417
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
258-433 2.03e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 2.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89353281 258 SLGDRHLRTLQISYDALKDENSKLRRKLNEvqsfseAQTEMvRTLERKLEAKmiKEEsdyhdlesvVQQVEQNLELMTKR 337
Cdd:COG4372  27 AALSEQLRKALFELDKLQEELEQLREELEQ------AREEL-EQLEEELEQA--RSE---------LEQLEEELEELNEQ 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89353281 338 AVKAENHVVKLKQEISLLQAQVSNFQRENEALRcGQGASLTVVKQNADVALQNLRVVMNSAQASIKQLVSGAETL-NLVA 416
Cdd:COG4372  89 LQAAQAELAQAQEELESLQEEAEELQEELEELQ-KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLqEELA 167
                       170
                ....*....|....*..
gi 89353281 417 EILKSIDRISEVKDEEE 433
Cdd:COG4372 168 ALEQELQALSEAEAEQA 184
AAA_13 pfam13166
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
264-361 5.84e-03

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.


Pssm-ID: 463796 [Multi-domain]  Cd Length: 712  Bit Score: 38.89  E-value: 5.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89353281   264 LRTLQISYDALKDE---NSKLRRKLNEVQSFSEAQTEMVRTLER-----------------KLEAKMIKE-ESDYHDLES 322
Cdd:pfam13166 337 LDGLRRALEAKRKDpfkSIELDSVDAKIESINDLVASINELIAKhneitdnfeeeknkakkKLRLHLVEEfKSEIDEYKD 416
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 89353281   323 VVQQVEQNLELMTKRAVKAENHVVKLKQEISLLQAQVSN 361
Cdd:pfam13166 417 KYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRD 455
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
261-433 1.16e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 1.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89353281    261 DRHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEMVRTLERKLEakMIKEEsdyhdlesvVQQVEQNLELMTKRAVK 340
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ--ILRER---------LANLERQLEELEAQLEE 327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89353281    341 AENHVVKLKQEISLLQAQVSNFQRENEALRcGQGASLTVVKQNADVALQNLRVVMNSAQASIKQLVSGAETLNlvAEILK 420
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKEELESLE-AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN--NEIER 404
                          170
                   ....*....|...
gi 89353281    421 SIDRISEVKDEEE 433
Cdd:TIGR02168  405 LEARLERLEDRRE 417
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
258-433 2.03e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 2.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89353281 258 SLGDRHLRTLQISYDALKDENSKLRRKLNEvqsfseAQTEMvRTLERKLEAKmiKEEsdyhdlesvVQQVEQNLELMTKR 337
Cdd:COG4372  27 AALSEQLRKALFELDKLQEELEQLREELEQ------AREEL-EQLEEELEQA--RSE---------LEQLEEELEELNEQ 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89353281 338 AVKAENHVVKLKQEISLLQAQVSNFQRENEALRcGQGASLTVVKQNADVALQNLRVVMNSAQASIKQLVSGAETL-NLVA 416
Cdd:COG4372  89 LQAAQAELAQAQEELESLQEEAEELQEELEELQ-KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLqEELA 167
                       170
                ....*....|....*..
gi 89353281 417 EILKSIDRISEVKDEEE 433
Cdd:COG4372 168 ALEQELQALSEAEAEQA 184
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
272-386 7.31e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 7.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89353281    272 DALKDE----NSKLRRKLNEVQSFSEAQTEMVRTLERkLEAKMIKEESDYHDLESVVQQVEQNLELMTKRAVKAENHVVK 347
Cdd:TIGR02169  395 EKLKREinelKRELDRLQEELQRLSEELADLNAAIAG-IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 89353281    348 LKQEISLLQAQVSNFQRENEALRCGQGASLTVVKQNADV 386
Cdd:TIGR02169  474 LKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
290-422 1.88e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 1.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89353281 290 SFSEAQTEMVRTLERKLEA--KMIKE-ESDYHDLESVVQQVEQNLELMTKRAVKAENHVVKLKQEISLLQAQVSNFQREN 366
Cdd:COG4942  13 LAAAAQADAAAEAEAELEQlqQEIAElEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 89353281 367 EALRcgqgASLTvvKQNADVALQNLRVVMNSAQASIKQLVSGAETLNLV--AEILKSI 422
Cdd:COG4942  93 AELR----AELE--AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVrrLQYLKYL 144
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
320-434 4.19e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 4.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89353281 320 LESVVQQ-VEQNLELMTKRAVKA----ENHVVKLKQEISLLQAQVSNFQRENEALRCGQGASLTVVK-QNADVALQNLRV 393
Cdd:COG3206 154 ANALAEAyLEQNLELRREEARKAleflEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQlSELESQLAEARA 233
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 89353281 394 VMNSAQASIKQLVSGAETLNLVAEILKSIDRISEVKDEEED 434
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAE 274
AAA_13 pfam13166
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
264-361 5.84e-03

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.


Pssm-ID: 463796 [Multi-domain]  Cd Length: 712  Bit Score: 38.89  E-value: 5.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89353281   264 LRTLQISYDALKDE---NSKLRRKLNEVQSFSEAQTEMVRTLER-----------------KLEAKMIKE-ESDYHDLES 322
Cdd:pfam13166 337 LDGLRRALEAKRKDpfkSIELDSVDAKIESINDLVASINELIAKhneitdnfeeeknkakkKLRLHLVEEfKSEIDEYKD 416
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 89353281   323 VVQQVEQNLELMTKRAVKAENHVVKLKQEISLLQAQVSN 361
Cdd:pfam13166 417 KYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRD 455
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
274-435 6.18e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 6.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89353281 274 LKDENSKLRRKLNEvQSFSEAQTEMVRTLERKLEAKMIKEESDYHDLESVVQQVEQNLELMTKRAVKAENHVVKLKQEIS 353
Cdd:COG4372  82 LEELNEQLQAAQAE-LAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE 160
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89353281 354 LLQAQVSNFQRENEALRcgqgasltvvKQNADVALQNLRVVMNSAQASIKQLVSGAETLNLVAEILKSIDRISEVKDEEE 433
Cdd:COG4372 161 SLQEELAALEQELQALS----------EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAK 230

                ..
gi 89353281 434 DS 435
Cdd:COG4372 231 LG 232
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
307-413 7.69e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 36.46  E-value: 7.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89353281   307 EAKMIKEESDyhDLESVVQQVEQNLELMTKRAVKAENhvvklkqeisllqaqvsNFQREnealrcgqgasltVVKQNADV 386
Cdd:pfam07926   9 EIKRLKEEAA--DAEAQLQKLQEDLEKQAEIAREAQQ-----------------NYERE-------------LVLHAEDI 56
                          90       100
                  ....*....|....*....|....*...
gi 89353281   387 -ALQNLRVVMNSAQASIKQLVSGAETLN 413
Cdd:pfam07926  57 kALQALREELNELKAEIAELKAEAESAK 84
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
257-365 7.73e-03

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 37.57  E-value: 7.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89353281   257 ESLGDRHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEMVRTLERKLEakmikeesdyhdLESVVQQVEQNLELMTK 336
Cdd:pfam15619  98 LRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLE------------LENKSFRRQLAAEKKKH 165
                          90       100
                  ....*....|....*....|....*....
gi 89353281   337 RAVKAEnhVVKLKQEISLLQAQVSNFQRE 365
Cdd:pfam15619 166 KEAQEE--VKILQEEIERLQQKLKEKERE 192
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
248-370 9.21e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.21  E-value: 9.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89353281 248 PSADFAVHGESLGD--RHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEMVRTLERKLEAKMIKEESdyhdLESVVQ 325
Cdd:COG4942 120 PPLALLLSPEDFLDavRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA----LEALKA 195
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 89353281 326 QVEQNLELMTKRAVKAENHVVKLKQEISLLQAQVSNFQRENEALR 370
Cdd:COG4942 196 ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
264-434 9.48e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 9.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89353281 264 LRTLQISYDALKDENskLRRKLNEVqsfsEAQTEMVRTLERKLEAKMIKEESDYHDLESVVQQVEQNLELMTKRAVKAEN 343
Cdd:COG1196 222 LKELEAELLLLKLRE--LEAELEEL----EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89353281 344 HVVKLKQEISLLQAQVSNFQRENEALRC------GQGASLTVVKQNADVALQNLRVVMNSAQASIKQLVsgAETLNLVAE 417
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEelaeleEELEELEEELEELEEELEEAEEELEEAEAELAEAE--EALLEAEAE 373
                       170
                ....*....|....*..
gi 89353281 418 ILKSIDRISEVKDEEED 434
Cdd:COG1196 374 LAEAEEELEELAEELLE 390
 
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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