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Conserved domains on  [gi|16950585|gb|AAL32279|]
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hypothetical protein [Trueperella pyogenes]

Protein Classification

metal-dependent hydrolase family protein( domain architecture ID 10101344)

metal-dependent hydrolase family protein having a conserved metal binding site, usually involving four histidines and one aspartic acid residue, similar to Zn-dependent arginine carboxypeptidase (protein Sgx9359b) derived from a DNA sequence isolated from the Sargasso Sea

EC:  3.-.-.-
Gene Ontology:  GO:0046872|GO:0016787
SCOP:  4001956|4002032

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
29-338 2.60e-77

Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.


:

Pssm-ID: 238624 [Multi-domain]  Cd Length: 342  Bit Score: 241.04  E-value: 2.60e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585  29 AVTSEEIRGYAYPGLLDAHTHPGMRRTPEPLALSE--------IRRRLAVLARHGITTVRDAGGQH-----DPKGAWEPG 95
Cdd:cd01299   1 AQVIDLGGKTLMPGLIDAHTHLGSDPGDLPLDLALpveyrtirATRQARAALRAGFTTVRDAGGADygllrDAIDAGLIP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585  96 LARVMHSGQHIARFKRYERYL------------AVDVEPADLPAEAVRQFEKGDGWIKIVGDWIDRSVGDTTP--LWPRQ 161
Cdd:cd01299  81 GPRVFASGRALSQTGGHGDPRglsglfpagglaAVVDGVEEVRAAVREQLRRGADQIKIMATGGVLSPGDPPPdtQFSEE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585 162 ALIDAVAGVHDVGGKVTVHTFATETVDDLLEAGVDGIEHGTGMTRDHLLEAAARGILVTPTVHQIRRFPEFAAKGARFAT 241
Cdd:cd01299 161 ELRAIVDEAHKAGLYVAAHAYGAEAIRRAIRAGVDTIEHGFLIDDETIELMKEKGIFLVPTLATYEALAAEGAAPGLPAD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585 242 YVERM-----LGMDAVRREHlalmvEVGTHFLMGSDT-AENVAEVNLVDELIDAVDDGMPADVVMAAASYAGRARIG--- 312
Cdd:cd01299 241 SAEKValvleAGRDALRRAH-----KAGVKIAFGTDAgFPVPPHGWNARELELLVKAGGTPAEALRAATANAAELLGlsd 315
                       330       340
                ....*....|....*....|....*..
gi 16950585 313 -FGVWSAGEPADVVIYREDPERNIETL 338
Cdd:cd01299 316 eLGVIEAGKLADLLVVDGDPLEDIAVL 342
 
Name Accession Description Interval E-value
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
29-338 2.60e-77

Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.


Pssm-ID: 238624 [Multi-domain]  Cd Length: 342  Bit Score: 241.04  E-value: 2.60e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585  29 AVTSEEIRGYAYPGLLDAHTHPGMRRTPEPLALSE--------IRRRLAVLARHGITTVRDAGGQH-----DPKGAWEPG 95
Cdd:cd01299   1 AQVIDLGGKTLMPGLIDAHTHLGSDPGDLPLDLALpveyrtirATRQARAALRAGFTTVRDAGGADygllrDAIDAGLIP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585  96 LARVMHSGQHIARFKRYERYL------------AVDVEPADLPAEAVRQFEKGDGWIKIVGDWIDRSVGDTTP--LWPRQ 161
Cdd:cd01299  81 GPRVFASGRALSQTGGHGDPRglsglfpagglaAVVDGVEEVRAAVREQLRRGADQIKIMATGGVLSPGDPPPdtQFSEE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585 162 ALIDAVAGVHDVGGKVTVHTFATETVDDLLEAGVDGIEHGTGMTRDHLLEAAARGILVTPTVHQIRRFPEFAAKGARFAT 241
Cdd:cd01299 161 ELRAIVDEAHKAGLYVAAHAYGAEAIRRAIRAGVDTIEHGFLIDDETIELMKEKGIFLVPTLATYEALAAEGAAPGLPAD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585 242 YVERM-----LGMDAVRREHlalmvEVGTHFLMGSDT-AENVAEVNLVDELIDAVDDGMPADVVMAAASYAGRARIG--- 312
Cdd:cd01299 241 SAEKValvleAGRDALRRAH-----KAGVKIAFGTDAgFPVPPHGWNARELELLVKAGGTPAEALRAATANAAELLGlsd 315
                       330       340
                ....*....|....*....|....*..
gi 16950585 313 -FGVWSAGEPADVVIYREDPERNIETL 338
Cdd:cd01299 316 eLGVIEAGKLADLLVVDGDPLEDIAVL 342
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
38-351 3.35e-24

Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 101.96  E-value: 3.35e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585  38 YAYPGLLDAHTHPGMRR------------TPEPLALSEIRRRLAVLARHGITTVRDA-GGQHDPKGAWEPGLA------R 98
Cdd:COG1228  62 TVLPGLIDAHTHLGLGGgravefeagggiTPTVDLVNPADKRLRRALAAGVTTVRDLpGGPLGLRDAIIAGESkllpgpR 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585  99 VMHSGQHIARFKRyerylAVDVEPADLPAEAVRQFEKGdgwikivGDWIDRSVGDTTPLWPRQALIDAVAGVHDVGGKVT 178
Cdd:COG1228 142 VLAAGPALSLTGG-----AHARGPEEARAALRELLAEG-------ADYIKVFAEGGAPDFSLEELRAILEAAHALGLPVA 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585 179 VHTFATETVDDLLEAGVDGIEHGTGMTRDHLLEAAARG-ILVTPTVhqirRFPEFAAKGARfATYVERMLGMDAVRREHL 257
Cdd:COG1228 210 AHAHQADDIRLAVEAGVDSIEHGTYLDDEVADLLAEAGtVVLVPTL----SLFLALLEGAA-APVAAKARKVREAALANA 284
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585 258 ALMVEVGTHFLMGSDT-AENVAEVNLVDELIDAVDDGM-PADVVMAAASYAGRArIGF----GVWSAGEPADVVIYREDP 331
Cdd:COG1228 285 RRLHDAGVPVALGTDAgVGVPPGRSLHRELALAVEAGLtPEEALRAATINAAKA-LGLdddvGSLEPGKLADLVLLDGDP 363
                       330       340
                ....*....|....*....|
gi 16950585 332 ERNIETLRNPLAVFAGGVRV 351
Cdd:COG1228 364 LEDIAYLEDVRAVMKDGRVV 383
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
38-351 8.84e-14

Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.


Pssm-ID: 460401 [Multi-domain]  Cd Length: 334  Bit Score: 71.38  E-value: 8.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585    38 YAYPGLLDAHTHPGM---RRTPEPLALSEIRRRLAVLA--RHGITTVRDAGGQHDPKGAWepgLARVMHSGQHIARFKRY 112
Cdd:pfam01979   1 IVLPGLIDAHVHLEMgllRGIPVPPEFAYEALRLGITTmlKSGTTTVLDMGATTSTGIEA---LLEAAEELPLGLRFLGP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585   113 ERYLAVDVEPADLPAEAvRQFEKGDGWIKIVGDwiDRSVGDTTPLWPRQ----ALIDAVAGVHDVGGKVTVHTFAT-ETV 187
Cdd:pfam01979  78 GCSLDTDGELEGRKALR-EKLKAGAEFIKGMAD--GVVFVGLAPHGAPTfsddELKAALEEAKKYGLPVAIHALETkGEV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585   188 DDLLEAGVDGIEHGTGMTR-------DHLLEAAARGILVTPTvhQIRRFPEfAAKGARFATYV--ERMLGMDavrREHLA 258
Cdd:pfam01979 155 EDAIAAFGGGIEHGTHLEVaesggllDIIKLILAHGVHLSPT--EANLLAE-HLKGAGVAHCPfsNSKLRSG---RIALR 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585   259 LMVEVGTHFLMGSDTAENVAEVNLVDELIDAV------DDGMPADVVMAAASYAGRARIGF----GVWSAGEPADVVIYR 328
Cdd:pfam01979 229 KALEDGVKVGLGTDGAGSGNSLNMLEELRLALelqfdpEGGLSPLEALRMATINPAKALGLddkvGSIEVGKDADLVVVD 308
                         330       340
                  ....*....|....*....|....*.
gi 16950585   329 EDPERNIETL---RNPLAVFAGGVRV 351
Cdd:pfam01979 309 LDPLAAFFGLkpdGNVKKVIVKGKIV 334
 
Name Accession Description Interval E-value
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
29-338 2.60e-77

Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.


Pssm-ID: 238624 [Multi-domain]  Cd Length: 342  Bit Score: 241.04  E-value: 2.60e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585  29 AVTSEEIRGYAYPGLLDAHTHPGMRRTPEPLALSE--------IRRRLAVLARHGITTVRDAGGQH-----DPKGAWEPG 95
Cdd:cd01299   1 AQVIDLGGKTLMPGLIDAHTHLGSDPGDLPLDLALpveyrtirATRQARAALRAGFTTVRDAGGADygllrDAIDAGLIP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585  96 LARVMHSGQHIARFKRYERYL------------AVDVEPADLPAEAVRQFEKGDGWIKIVGDWIDRSVGDTTP--LWPRQ 161
Cdd:cd01299  81 GPRVFASGRALSQTGGHGDPRglsglfpagglaAVVDGVEEVRAAVREQLRRGADQIKIMATGGVLSPGDPPPdtQFSEE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585 162 ALIDAVAGVHDVGGKVTVHTFATETVDDLLEAGVDGIEHGTGMTRDHLLEAAARGILVTPTVHQIRRFPEFAAKGARFAT 241
Cdd:cd01299 161 ELRAIVDEAHKAGLYVAAHAYGAEAIRRAIRAGVDTIEHGFLIDDETIELMKEKGIFLVPTLATYEALAAEGAAPGLPAD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585 242 YVERM-----LGMDAVRREHlalmvEVGTHFLMGSDT-AENVAEVNLVDELIDAVDDGMPADVVMAAASYAGRARIG--- 312
Cdd:cd01299 241 SAEKValvleAGRDALRRAH-----KAGVKIAFGTDAgFPVPPHGWNARELELLVKAGGTPAEALRAATANAAELLGlsd 315
                       330       340
                ....*....|....*....|....*..
gi 16950585 313 -FGVWSAGEPADVVIYREDPERNIETL 338
Cdd:cd01299 316 eLGVIEAGKLADLLVVDGDPLEDIAVL 342
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
38-351 3.35e-24

Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 101.96  E-value: 3.35e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585  38 YAYPGLLDAHTHPGMRR------------TPEPLALSEIRRRLAVLARHGITTVRDA-GGQHDPKGAWEPGLA------R 98
Cdd:COG1228  62 TVLPGLIDAHTHLGLGGgravefeagggiTPTVDLVNPADKRLRRALAAGVTTVRDLpGGPLGLRDAIIAGESkllpgpR 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585  99 VMHSGQHIARFKRyerylAVDVEPADLPAEAVRQFEKGdgwikivGDWIDRSVGDTTPLWPRQALIDAVAGVHDVGGKVT 178
Cdd:COG1228 142 VLAAGPALSLTGG-----AHARGPEEARAALRELLAEG-------ADYIKVFAEGGAPDFSLEELRAILEAAHALGLPVA 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585 179 VHTFATETVDDLLEAGVDGIEHGTGMTRDHLLEAAARG-ILVTPTVhqirRFPEFAAKGARfATYVERMLGMDAVRREHL 257
Cdd:COG1228 210 AHAHQADDIRLAVEAGVDSIEHGTYLDDEVADLLAEAGtVVLVPTL----SLFLALLEGAA-APVAAKARKVREAALANA 284
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585 258 ALMVEVGTHFLMGSDT-AENVAEVNLVDELIDAVDDGM-PADVVMAAASYAGRArIGF----GVWSAGEPADVVIYREDP 331
Cdd:COG1228 285 RRLHDAGVPVALGTDAgVGVPPGRSLHRELALAVEAGLtPEEALRAATINAAKA-LGLdddvGSLEPGKLADLVLLDGDP 363
                       330       340
                ....*....|....*....|
gi 16950585 332 ERNIETLRNPLAVFAGGVRV 351
Cdd:COG1228 364 LEDIAYLEDVRAVMKDGRVV 383
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
38-351 8.84e-14

Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.


Pssm-ID: 460401 [Multi-domain]  Cd Length: 334  Bit Score: 71.38  E-value: 8.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585    38 YAYPGLLDAHTHPGM---RRTPEPLALSEIRRRLAVLA--RHGITTVRDAGGQHDPKGAWepgLARVMHSGQHIARFKRY 112
Cdd:pfam01979   1 IVLPGLIDAHVHLEMgllRGIPVPPEFAYEALRLGITTmlKSGTTTVLDMGATTSTGIEA---LLEAAEELPLGLRFLGP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585   113 ERYLAVDVEPADLPAEAvRQFEKGDGWIKIVGDwiDRSVGDTTPLWPRQ----ALIDAVAGVHDVGGKVTVHTFAT-ETV 187
Cdd:pfam01979  78 GCSLDTDGELEGRKALR-EKLKAGAEFIKGMAD--GVVFVGLAPHGAPTfsddELKAALEEAKKYGLPVAIHALETkGEV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585   188 DDLLEAGVDGIEHGTGMTR-------DHLLEAAARGILVTPTvhQIRRFPEfAAKGARFATYV--ERMLGMDavrREHLA 258
Cdd:pfam01979 155 EDAIAAFGGGIEHGTHLEVaesggllDIIKLILAHGVHLSPT--EANLLAE-HLKGAGVAHCPfsNSKLRSG---RIALR 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585   259 LMVEVGTHFLMGSDTAENVAEVNLVDELIDAV------DDGMPADVVMAAASYAGRARIGF----GVWSAGEPADVVIYR 328
Cdd:pfam01979 229 KALEDGVKVGLGTDGAGSGNSLNMLEELRLALelqfdpEGGLSPLEALRMATINPAKALGLddkvGSIEVGKDADLVVVD 308
                         330       340
                  ....*....|....*....|....*.
gi 16950585   329 EDPERNIETL---RNPLAVFAGGVRV 351
Cdd:pfam01979 309 LDPLAAFFGLkpdGNVKKVIVKGKIV 334
Amidohydro_3 pfam07969
Amidohydrolase family;
42-273 2.04e-06

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 49.45  E-value: 2.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585    42 GLLDAHTHPGMRRTPEPLALSEIRRRLAVLARHGITTVRDAGGQHDPKGAWEPgLARVMHSGQHIARFKRYERYLAVdve 121
Cdd:pfam07969 131 GLLREGAYALPPLLAREAEAAAVAAALAALPGFGITSVDGGGGNVHSLDDYEP-LRELTAAEKLKELLDAPERLGLP--- 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585   122 padLPAEAVRqfekgDGWIKIVGDWIDRS------------VGDTTPLWPRQALIDAVAGVHDVGGKVTVHTFATETVDD 189
Cdd:pfam07969 207 ---HSIYELR-----IGAMKLFADGVLGSrtaaltepyfdaPGTGWPDFEDEALAELVAAARERGLDVAIHAIGDATIDT 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16950585   190 LLEA-----------GVDGIEHGTGMT--RDHLLEAAARgILVTPTVHQIRRFPEFAAKGARFATyvERMLGMDAVRreh 256
Cdd:pfam07969 279 ALDAfeavaeklgnqGRVRIEHAQGVVpyTYSQIERVAA-LGGAAGVQPVFDPLWGDWLQDRLGA--ERARGLTPVK--- 352
                         250
                  ....*....|....*..
gi 16950585   257 laLMVEVGTHFLMGSDT 273
Cdd:pfam07969 353 --ELLNAGVKVALGSDA 367
 
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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