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Conserved domains on  [gi|446329155|ref|WP_000407010|]
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MULTISPECIES: histidinol dehydrogenase [Bacillus]

Protein Classification

histidinol dehydrogenase( domain architecture ID 10792081)

histidinol dehydrogenase catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine

EC:  1.1.1.23
Gene Symbol:  hisD
SCOP:  4003347

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
hisD PRK00877
bifunctional histidinal dehydrogenase/ histidinol dehydrogenase; Reviewed
6-425 0e+00

bifunctional histidinal dehydrogenase/ histidinol dehydrogenase; Reviewed


:

Pssm-ID: 234853 [Multi-domain]  Cd Length: 425  Bit Score: 705.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155   6 EDFQKALSKikllRENANIieETVQRNVSEIVRNVRESGDEALSFYTKKFDGVKIKEFRVSEEEEKRASMFVENSFLEAL 85
Cdd:PRK00877  12 AEFRAALPR----RAREDD--EDVEAAVREILEDVRERGDAALLEYTEKFDGVELESLRVSEEEIEAAYERLDPELREAL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  86 QEAKKNIISYHEKQKRQSMFDCASEGIIRGQIIRPLENVGVYVPGGTASYPSSVLMNVLPAKLAGVKKIVMVTPPREGGI 165
Cdd:PRK00877  86 EEAAENIRAFHEAQKPESWDVETAPGVRLGQRWRPIERVGLYVPGGKAAYPSSVLMNAIPAKVAGVKEIVMVTPPPDGEI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 166 DPHILVAASLAGVDEIYTIGGAQAIAALAYGTESIPKVDKIVGPGNLYVALAKREVYGIVNIDMIAGPSEIVVIADETGN 245
Cdd:PRK00877 166 NPAILAAAALAGVDEVYKVGGAQAIAALAYGTESIPKVDKIVGPGNIYVTAAKRLVFGVVGIDMIAGPSEILVIADETAD 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 246 AKYIAADLLSQAEHDERATAICITTNIELAKKVEKEIERQLETLPRSEIARESINRNGAIFIVPSIDEALQLSNEIAPEH 325
Cdd:PRK00877 246 PDFVAADLLSQAEHDPDAQSILVTTSEELAEAVAAEVERQLATLPRAEIARASLEGQGAIILVDDLEEAIELSNAYAPEH 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 326 LELHIKEPMNALAYVKHAGSIFLGPYAPEPLGDYLAGPNHVLPTSGTARFFSPLSVDDFVKKSSFLSYTEEALRDVQHHI 405
Cdd:PRK00877 326 LEIQTEDPRALLDRIRNAGAIFLGPYTPESLGDYAAGPNHVLPTSGTARFSSGLSVYDFLKRSSVIELSKEGLKALGPAI 405
                        410       420
                 ....*....|....*....|
gi 446329155 406 VELANKEGLHAHARAIQIRF 425
Cdd:PRK00877 406 VTLAEAEGLDAHARAVRVRL 425
 
Name Accession Description Interval E-value
hisD PRK00877
bifunctional histidinal dehydrogenase/ histidinol dehydrogenase; Reviewed
6-425 0e+00

bifunctional histidinal dehydrogenase/ histidinol dehydrogenase; Reviewed


Pssm-ID: 234853 [Multi-domain]  Cd Length: 425  Bit Score: 705.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155   6 EDFQKALSKikllRENANIieETVQRNVSEIVRNVRESGDEALSFYTKKFDGVKIKEFRVSEEEEKRASMFVENSFLEAL 85
Cdd:PRK00877  12 AEFRAALPR----RAREDD--EDVEAAVREILEDVRERGDAALLEYTEKFDGVELESLRVSEEEIEAAYERLDPELREAL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  86 QEAKKNIISYHEKQKRQSMFDCASEGIIRGQIIRPLENVGVYVPGGTASYPSSVLMNVLPAKLAGVKKIVMVTPPREGGI 165
Cdd:PRK00877  86 EEAAENIRAFHEAQKPESWDVETAPGVRLGQRWRPIERVGLYVPGGKAAYPSSVLMNAIPAKVAGVKEIVMVTPPPDGEI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 166 DPHILVAASLAGVDEIYTIGGAQAIAALAYGTESIPKVDKIVGPGNLYVALAKREVYGIVNIDMIAGPSEIVVIADETGN 245
Cdd:PRK00877 166 NPAILAAAALAGVDEVYKVGGAQAIAALAYGTESIPKVDKIVGPGNIYVTAAKRLVFGVVGIDMIAGPSEILVIADETAD 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 246 AKYIAADLLSQAEHDERATAICITTNIELAKKVEKEIERQLETLPRSEIARESINRNGAIFIVPSIDEALQLSNEIAPEH 325
Cdd:PRK00877 246 PDFVAADLLSQAEHDPDAQSILVTTSEELAEAVAAEVERQLATLPRAEIARASLEGQGAIILVDDLEEAIELSNAYAPEH 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 326 LELHIKEPMNALAYVKHAGSIFLGPYAPEPLGDYLAGPNHVLPTSGTARFFSPLSVDDFVKKSSFLSYTEEALRDVQHHI 405
Cdd:PRK00877 326 LEIQTEDPRALLDRIRNAGAIFLGPYTPESLGDYAAGPNHVLPTSGTARFSSGLSVYDFLKRSSVIELSKEGLKALGPAI 405
                        410       420
                 ....*....|....*....|
gi 446329155 406 VELANKEGLHAHARAIQIRF 425
Cdd:PRK00877 406 VTLAEAEGLDAHARAVRVRL 425
HisD COG0141
Histidinol dehydrogenase [Amino acid transport and metabolism]; Histidinol dehydrogenase is ...
3-429 0e+00

Histidinol dehydrogenase [Amino acid transport and metabolism]; Histidinol dehydrogenase is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439911  Cd Length: 429  Bit Score: 695.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155   3 IVFEDFQKALSKIkLLRENANIieETVQRNVSEIVRNVRESGDEALSFYTKKFDGVKIKEFRVSEEEEKRASMFVENSFL 82
Cdd:COG0141    5 LDDADLSAELKAL-LKRPAADD--EDVEATVREILADVRARGDAALLEYTERFDGVDLESLRVSEEEIEAAYAALDPELR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  83 EALQEAKKNIISYHEKQKRQSMFDCASEGIIRGQIIRPLENVGVYVPGGTASYPSSVLMNVLPAKLAGVKKIVMVTPP-R 161
Cdd:COG0141   82 EALELAAENIRAFHEAQKPESWEVETEPGVVLGQRVTPIERVGLYVPGGKAPYPSSVLMNAIPAKVAGVKEIVMCTPPpK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 162 EGGIDPHILVAASLAGVDEIYTIGGAQAIAALAYGTESIPKVDKIVGPGNLYVALAKREVYGIVNIDMIAGPSEIVVIAD 241
Cdd:COG0141  162 DGKINPAVLAAAHLAGVDEIYKVGGAQAIAALAYGTETIPKVDKIVGPGNIYVAAAKRLVFGGVGIDMPAGPSEILVIAD 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 242 ETGNAKYIAADLLSQAEHDERATAICITTNIELAKKVEKEIERQLETLPRSEIARESINRNGAIFIVPSIDEALQLSNEI 321
Cdd:COG0141  242 ETADPEFVAADLLSQAEHDPDAQAILVTTSEELAEAVEAEVERQLATLPRAEIARKALEDNGAIILVDDLEEAIELANRY 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 322 APEHLELHIKEPMNALAYVKHAGSIFLGPYAPEPLGDYLAGPNHVLPTSGTARFFSPLSVDDFVKKSSFLSYTEEALRDV 401
Cdd:COG0141  322 APEHLELQTADPEALLERIRNAGAIFLGPYTPESLGDYAAGPNHVLPTGGTARFSSGLSVDDFLKRSSVQEYSEEGLAKL 401
                        410       420
                 ....*....|....*....|....*...
gi 446329155 402 QHHIVELANKEGLHAHARAIQIRFEEEE 429
Cdd:COG0141  402 APAIETLAEAEGLEAHARAVRIRLEKLG 429
Histidinol_dh pfam00815
Histidinol dehydrogenase;
27-425 0e+00

Histidinol dehydrogenase;


Pssm-ID: 459948  Cd Length: 410  Bit Score: 681.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155   27 ETVQRNVSEIVRNVRESGDEALSFYTKKFDGVKIK-EFRVSEEEEKRASMFVENSFLEALQEAKKNIISYHEKQKRQSM- 104
Cdd:pfam00815   9 DEVEETVREIIEDVRERGDAALLEYTEKFDGVELGvLLRVSEEEIEAAYAKLDPELKEAIELAAENIRAFHEAQKPSELw 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  105 FDCASEGIIRGQIIRPLENVGVYVPGGTASYPSSVLMNVLPAKLAGVKKIVMVTPP-REGGIDPHILVAASLAGVDEIYT 183
Cdd:pfam00815  89 VYETEPGVVLGQRVRPIERVGLYVPGGTAPYPSSVLMNAIPAKVAGVKEIVMCTPPqKDGKINPAILAAAHLAGVDEIYK 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  184 IGGAQAIAALAYGTESIPKVDKIVGPGNLYVALAKREVYGIVNIDMIAGPSEIVVIADETGNAKYIAADLLSQAEHDERA 263
Cdd:pfam00815 169 VGGAQAIAALAYGTETIPKVDKIVGPGNIYVTAAKRLVFGDVGIDMPAGPSEVLVIADETANPEFVAADLLSQAEHDPDA 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  264 TAICITTNIELAKKVEKEIERQLETLPRSEIARESINRNGAIFIVPSIDEALQLSNEIAPEHLELHIKEPMNALAYVKHA 343
Cdd:pfam00815 249 QAILVTTSEELAEAVEAEVERQLATLPRKEIARKSLENYGAIILVDDLEEAIELSNEYAPEHLELQTEDPEALLEKIRNA 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  344 GSIFLGPYAPEPLGDYLAGPNHVLPTSGTARFFSPLSVDDFVKKSSFLSYTEEALRDVQHHIVELANKEGLHAHARAIQI 423
Cdd:pfam00815 329 GSIFLGEYTPESLGDYAAGPNHVLPTSGTARFYSGLSVDDFLKKSSVQEYSKEGLKELGPAVETLAEAEGLEAHANAVRV 408

                  ..
gi 446329155  424 RF 425
Cdd:pfam00815 409 RL 410
Histidinol_dh cd06572
Histidinol dehydrogenase, HisD, E.C 1.1.1.23. Histidinol dehydrogenase catalyzes the last two ...
29-417 0e+00

Histidinol dehydrogenase, HisD, E.C 1.1.1.23. Histidinol dehydrogenase catalyzes the last two steps in the L-histidine biosynthesis pathway, which is conserved in bacteria, archaea, fungi, and plants. These last two steps are (i) the NAD-dependent oxidation of L-histidinol to L-histidinaldehyde, and (ii) the NAD-dependent oxidation of L-histidinaldehyde to L-histidine. In most fungi and in the unicellular choanoflagellate Monosiga bevicollis, the HisD domain is fused with units that catalyze the second and third biosynthesis steps in this same pathway.


Pssm-ID: 119329  Cd Length: 390  Bit Score: 644.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  29 VQRNVSEIVRNVRESGDEALSFYTKKFDGVKIKEFRVSEEEEKRASMFVENSFLEALQEAKKNIISYHEKQKRQSMFDCA 108
Cdd:cd06572    1 VEETVREIIEDVRERGDEALLEYTEKFDGVELESLRVSEEEIDAAYAAVDPELKEAIELAAENIRAFHEAQLPKDWEVET 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 109 SEGIIRGQIIRPLENVGVYVPGGTASYPSSVLMNVLPAKLAGVKKIVMVTPPR-EGGIDPHILVAASLAGVDEIYTIGGA 187
Cdd:cd06572   81 EPGVVLGQRYRPIERVGLYVPGGTAPYPSTVLMLAIPAKVAGVKEIVVVTPPRkDGKINPAILAAAKLAGVDEIYKVGGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 188 QAIAALAYGTESIPKVDKIVGPGNLYVALAKREVYGIVNIDMIAGPSEIVVIADETGNAKYIAADLLSQAEHDERATAIC 267
Cdd:cd06572  161 QAIAALAYGTETIPKVDKIVGPGNIYVTAAKRLVSGDVGIDMPAGPSEVLVIADETANPEFVAADLLSQAEHDPDSQAIL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 268 ITTNIELAKKVEKEIERQLETLPRSEIARESINRNGAIFIVPSIDEALQLSNEIAPEHLELHIKEPMNALAYVKHAGSIF 347
Cdd:cd06572  241 VTTSEELAEAVEEEVERQLAELPRREIAAKSLLDYGAIILVDDLEEAIELANEYAPEHLELQTEDPEELLEKIRNAGSIF 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 348 LGPYAPEPLGDYLAGPNHVLPTSGTARFFSPLSVDDFVKKSSFLSYTEEALRDVQHHIVELANKEGLHAH 417
Cdd:cd06572  321 LGPYTPEALGDYAAGPNHVLPTGGTARFYSGLSVDDFLKRITVQEYSKEGLRALAPAVATLAEAEGLEAH 390
hisD TIGR00069
histidinol dehydrogenase; This model describes a polypeptide sequence catalyzing the final ...
33-424 0e+00

histidinol dehydrogenase; This model describes a polypeptide sequence catalyzing the final step in histidine biosynthesis, found sometimes as an independent protein and sometimes as a part of a multifunctional protein. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 272887  Cd Length: 393  Bit Score: 634.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155   33 VSEIVRNVRESGDEALSFYTKKFDGVKIKEFRVSEEEEKRASMFVENSFLEALQEAKKNIISYHEKQKRQSMFDCASEGI 112
Cdd:TIGR00069   1 VKDIIEDVRARGDEALLEYTEKFDGVTLDSLRVSEEEIEAAYAAVDPELKEALELAAENIRAFHEAQLPRSWEVETEPGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  113 IRGQIIRPLENVGVYVPGGTASYPSSVLMNVLPAKLAGVKKIVMVTPP-REGGIDPHILVAASLAGVDEIYTIGGAQAIA 191
Cdd:TIGR00069  81 ILGQRVRPIERVGLYVPGGRAPYPSTVLMTAIPAKVAGVKEIVVCTPPgKDGEINPAVLAAAKLAGVDEVYKVGGAQAIA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  192 ALAYGTESIPKVDKIVGPGNLYVALAKREVYGIVNIDMIAGPSEIVVIADETGNAKYIAADLLSQAEHDERATAICITTN 271
Cdd:TIGR00069 161 ALAYGTETVPKVDKIVGPGNIYVTAAKKLVFGDVGIDMPAGPSEVLVIADETANPEFVAADLLSQAEHDPDAQAILVTTS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  272 IELAKKVEKEIERQLETLPRSEIARESINRNGAIFIVPSIDEALQLSNEIAPEHLELHIKEPMNALAYVKHAGSIFLGPY 351
Cdd:TIGR00069 241 EELAEAVQEEIERQLATLPRREIARKSLEDNGAIILVDDLEEAIEISNDYAPEHLELQTKNPEELLPKIRNAGSIFLGPY 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446329155  352 APEPLGDYLAGPNHVLPTSGTARFFSPLSVDDFVKKSSFLSYTEEALRDVQHHIVELANKEGLHAHARAIQIR 424
Cdd:TIGR00069 321 TPEAAGDYAAGPNHVLPTGGTARFYSGLSVLDFLKRITVQRLSKEGLAELAPAVETLAEAEGLDAHANSVRIR 393
 
Name Accession Description Interval E-value
hisD PRK00877
bifunctional histidinal dehydrogenase/ histidinol dehydrogenase; Reviewed
6-425 0e+00

bifunctional histidinal dehydrogenase/ histidinol dehydrogenase; Reviewed


Pssm-ID: 234853 [Multi-domain]  Cd Length: 425  Bit Score: 705.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155   6 EDFQKALSKikllRENANIieETVQRNVSEIVRNVRESGDEALSFYTKKFDGVKIKEFRVSEEEEKRASMFVENSFLEAL 85
Cdd:PRK00877  12 AEFRAALPR----RAREDD--EDVEAAVREILEDVRERGDAALLEYTEKFDGVELESLRVSEEEIEAAYERLDPELREAL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  86 QEAKKNIISYHEKQKRQSMFDCASEGIIRGQIIRPLENVGVYVPGGTASYPSSVLMNVLPAKLAGVKKIVMVTPPREGGI 165
Cdd:PRK00877  86 EEAAENIRAFHEAQKPESWDVETAPGVRLGQRWRPIERVGLYVPGGKAAYPSSVLMNAIPAKVAGVKEIVMVTPPPDGEI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 166 DPHILVAASLAGVDEIYTIGGAQAIAALAYGTESIPKVDKIVGPGNLYVALAKREVYGIVNIDMIAGPSEIVVIADETGN 245
Cdd:PRK00877 166 NPAILAAAALAGVDEVYKVGGAQAIAALAYGTESIPKVDKIVGPGNIYVTAAKRLVFGVVGIDMIAGPSEILVIADETAD 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 246 AKYIAADLLSQAEHDERATAICITTNIELAKKVEKEIERQLETLPRSEIARESINRNGAIFIVPSIDEALQLSNEIAPEH 325
Cdd:PRK00877 246 PDFVAADLLSQAEHDPDAQSILVTTSEELAEAVAAEVERQLATLPRAEIARASLEGQGAIILVDDLEEAIELSNAYAPEH 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 326 LELHIKEPMNALAYVKHAGSIFLGPYAPEPLGDYLAGPNHVLPTSGTARFFSPLSVDDFVKKSSFLSYTEEALRDVQHHI 405
Cdd:PRK00877 326 LEIQTEDPRALLDRIRNAGAIFLGPYTPESLGDYAAGPNHVLPTSGTARFSSGLSVYDFLKRSSVIELSKEGLKALGPAI 405
                        410       420
                 ....*....|....*....|
gi 446329155 406 VELANKEGLHAHARAIQIRF 425
Cdd:PRK00877 406 VTLAEAEGLDAHARAVRVRL 425
HisD COG0141
Histidinol dehydrogenase [Amino acid transport and metabolism]; Histidinol dehydrogenase is ...
3-429 0e+00

Histidinol dehydrogenase [Amino acid transport and metabolism]; Histidinol dehydrogenase is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439911  Cd Length: 429  Bit Score: 695.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155   3 IVFEDFQKALSKIkLLRENANIieETVQRNVSEIVRNVRESGDEALSFYTKKFDGVKIKEFRVSEEEEKRASMFVENSFL 82
Cdd:COG0141    5 LDDADLSAELKAL-LKRPAADD--EDVEATVREILADVRARGDAALLEYTERFDGVDLESLRVSEEEIEAAYAALDPELR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  83 EALQEAKKNIISYHEKQKRQSMFDCASEGIIRGQIIRPLENVGVYVPGGTASYPSSVLMNVLPAKLAGVKKIVMVTPP-R 161
Cdd:COG0141   82 EALELAAENIRAFHEAQKPESWEVETEPGVVLGQRVTPIERVGLYVPGGKAPYPSSVLMNAIPAKVAGVKEIVMCTPPpK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 162 EGGIDPHILVAASLAGVDEIYTIGGAQAIAALAYGTESIPKVDKIVGPGNLYVALAKREVYGIVNIDMIAGPSEIVVIAD 241
Cdd:COG0141  162 DGKINPAVLAAAHLAGVDEIYKVGGAQAIAALAYGTETIPKVDKIVGPGNIYVAAAKRLVFGGVGIDMPAGPSEILVIAD 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 242 ETGNAKYIAADLLSQAEHDERATAICITTNIELAKKVEKEIERQLETLPRSEIARESINRNGAIFIVPSIDEALQLSNEI 321
Cdd:COG0141  242 ETADPEFVAADLLSQAEHDPDAQAILVTTSEELAEAVEAEVERQLATLPRAEIARKALEDNGAIILVDDLEEAIELANRY 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 322 APEHLELHIKEPMNALAYVKHAGSIFLGPYAPEPLGDYLAGPNHVLPTSGTARFFSPLSVDDFVKKSSFLSYTEEALRDV 401
Cdd:COG0141  322 APEHLELQTADPEALLERIRNAGAIFLGPYTPESLGDYAAGPNHVLPTGGTARFSSGLSVDDFLKRSSVQEYSEEGLAKL 401
                        410       420
                 ....*....|....*....|....*...
gi 446329155 402 QHHIVELANKEGLHAHARAIQIRFEEEE 429
Cdd:COG0141  402 APAIETLAEAEGLEAHARAVRIRLEKLG 429
Histidinol_dh pfam00815
Histidinol dehydrogenase;
27-425 0e+00

Histidinol dehydrogenase;


Pssm-ID: 459948  Cd Length: 410  Bit Score: 681.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155   27 ETVQRNVSEIVRNVRESGDEALSFYTKKFDGVKIK-EFRVSEEEEKRASMFVENSFLEALQEAKKNIISYHEKQKRQSM- 104
Cdd:pfam00815   9 DEVEETVREIIEDVRERGDAALLEYTEKFDGVELGvLLRVSEEEIEAAYAKLDPELKEAIELAAENIRAFHEAQKPSELw 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  105 FDCASEGIIRGQIIRPLENVGVYVPGGTASYPSSVLMNVLPAKLAGVKKIVMVTPP-REGGIDPHILVAASLAGVDEIYT 183
Cdd:pfam00815  89 VYETEPGVVLGQRVRPIERVGLYVPGGTAPYPSSVLMNAIPAKVAGVKEIVMCTPPqKDGKINPAILAAAHLAGVDEIYK 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  184 IGGAQAIAALAYGTESIPKVDKIVGPGNLYVALAKREVYGIVNIDMIAGPSEIVVIADETGNAKYIAADLLSQAEHDERA 263
Cdd:pfam00815 169 VGGAQAIAALAYGTETIPKVDKIVGPGNIYVTAAKRLVFGDVGIDMPAGPSEVLVIADETANPEFVAADLLSQAEHDPDA 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  264 TAICITTNIELAKKVEKEIERQLETLPRSEIARESINRNGAIFIVPSIDEALQLSNEIAPEHLELHIKEPMNALAYVKHA 343
Cdd:pfam00815 249 QAILVTTSEELAEAVEAEVERQLATLPRKEIARKSLENYGAIILVDDLEEAIELSNEYAPEHLELQTEDPEALLEKIRNA 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  344 GSIFLGPYAPEPLGDYLAGPNHVLPTSGTARFFSPLSVDDFVKKSSFLSYTEEALRDVQHHIVELANKEGLHAHARAIQI 423
Cdd:pfam00815 329 GSIFLGEYTPESLGDYAAGPNHVLPTSGTARFYSGLSVDDFLKKSSVQEYSKEGLKELGPAVETLAEAEGLEAHANAVRV 408

                  ..
gi 446329155  424 RF 425
Cdd:pfam00815 409 RL 410
Histidinol_dh cd06572
Histidinol dehydrogenase, HisD, E.C 1.1.1.23. Histidinol dehydrogenase catalyzes the last two ...
29-417 0e+00

Histidinol dehydrogenase, HisD, E.C 1.1.1.23. Histidinol dehydrogenase catalyzes the last two steps in the L-histidine biosynthesis pathway, which is conserved in bacteria, archaea, fungi, and plants. These last two steps are (i) the NAD-dependent oxidation of L-histidinol to L-histidinaldehyde, and (ii) the NAD-dependent oxidation of L-histidinaldehyde to L-histidine. In most fungi and in the unicellular choanoflagellate Monosiga bevicollis, the HisD domain is fused with units that catalyze the second and third biosynthesis steps in this same pathway.


Pssm-ID: 119329  Cd Length: 390  Bit Score: 644.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  29 VQRNVSEIVRNVRESGDEALSFYTKKFDGVKIKEFRVSEEEEKRASMFVENSFLEALQEAKKNIISYHEKQKRQSMFDCA 108
Cdd:cd06572    1 VEETVREIIEDVRERGDEALLEYTEKFDGVELESLRVSEEEIDAAYAAVDPELKEAIELAAENIRAFHEAQLPKDWEVET 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 109 SEGIIRGQIIRPLENVGVYVPGGTASYPSSVLMNVLPAKLAGVKKIVMVTPPR-EGGIDPHILVAASLAGVDEIYTIGGA 187
Cdd:cd06572   81 EPGVVLGQRYRPIERVGLYVPGGTAPYPSTVLMLAIPAKVAGVKEIVVVTPPRkDGKINPAILAAAKLAGVDEIYKVGGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 188 QAIAALAYGTESIPKVDKIVGPGNLYVALAKREVYGIVNIDMIAGPSEIVVIADETGNAKYIAADLLSQAEHDERATAIC 267
Cdd:cd06572  161 QAIAALAYGTETIPKVDKIVGPGNIYVTAAKRLVSGDVGIDMPAGPSEVLVIADETANPEFVAADLLSQAEHDPDSQAIL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 268 ITTNIELAKKVEKEIERQLETLPRSEIARESINRNGAIFIVPSIDEALQLSNEIAPEHLELHIKEPMNALAYVKHAGSIF 347
Cdd:cd06572  241 VTTSEELAEAVEEEVERQLAELPRREIAAKSLLDYGAIILVDDLEEAIELANEYAPEHLELQTEDPEELLEKIRNAGSIF 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 348 LGPYAPEPLGDYLAGPNHVLPTSGTARFFSPLSVDDFVKKSSFLSYTEEALRDVQHHIVELANKEGLHAH 417
Cdd:cd06572  321 LGPYTPEALGDYAAGPNHVLPTGGTARFYSGLSVDDFLKRITVQEYSKEGLRALAPAVATLAEAEGLEAH 390
hisD TIGR00069
histidinol dehydrogenase; This model describes a polypeptide sequence catalyzing the final ...
33-424 0e+00

histidinol dehydrogenase; This model describes a polypeptide sequence catalyzing the final step in histidine biosynthesis, found sometimes as an independent protein and sometimes as a part of a multifunctional protein. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 272887  Cd Length: 393  Bit Score: 634.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155   33 VSEIVRNVRESGDEALSFYTKKFDGVKIKEFRVSEEEEKRASMFVENSFLEALQEAKKNIISYHEKQKRQSMFDCASEGI 112
Cdd:TIGR00069   1 VKDIIEDVRARGDEALLEYTEKFDGVTLDSLRVSEEEIEAAYAAVDPELKEALELAAENIRAFHEAQLPRSWEVETEPGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  113 IRGQIIRPLENVGVYVPGGTASYPSSVLMNVLPAKLAGVKKIVMVTPP-REGGIDPHILVAASLAGVDEIYTIGGAQAIA 191
Cdd:TIGR00069  81 ILGQRVRPIERVGLYVPGGRAPYPSTVLMTAIPAKVAGVKEIVVCTPPgKDGEINPAVLAAAKLAGVDEVYKVGGAQAIA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  192 ALAYGTESIPKVDKIVGPGNLYVALAKREVYGIVNIDMIAGPSEIVVIADETGNAKYIAADLLSQAEHDERATAICITTN 271
Cdd:TIGR00069 161 ALAYGTETVPKVDKIVGPGNIYVTAAKKLVFGDVGIDMPAGPSEVLVIADETANPEFVAADLLSQAEHDPDAQAILVTTS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  272 IELAKKVEKEIERQLETLPRSEIARESINRNGAIFIVPSIDEALQLSNEIAPEHLELHIKEPMNALAYVKHAGSIFLGPY 351
Cdd:TIGR00069 241 EELAEAVQEEIERQLATLPRREIARKSLEDNGAIILVDDLEEAIEISNDYAPEHLELQTKNPEELLPKIRNAGSIFLGPY 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446329155  352 APEPLGDYLAGPNHVLPTSGTARFFSPLSVDDFVKKSSFLSYTEEALRDVQHHIVELANKEGLHAHARAIQIR 424
Cdd:TIGR00069 321 TPEAAGDYAAGPNHVLPTGGTARFYSGLSVLDFLKRITVQRLSKEGLAELAPAVETLAEAEGLDAHANSVRIR 393
PRK12447 PRK12447
histidinol dehydrogenase; Reviewed
29-424 2.69e-157

histidinol dehydrogenase; Reviewed


Pssm-ID: 237103 [Multi-domain]  Cd Length: 426  Bit Score: 450.89  E-value: 2.69e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  29 VQRNVSEIVRNVRESGDEALSFYTKKFDGVKIKEFRVSEEEEKRASMFVENSFLEALQEAKKNIISYHEKQkRQSMFDCA 108
Cdd:PRK12447  22 VRETVEAILADIEARGDAAVREYSRKFDKWSPGSFRLSAAEIDAAVAKVPEQVKEDIRFAQDQVRRFAEAQ-RDSLQDLE 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 109 SE---GIIRGQIIRPLENVGVYVPGGTASYPSSVLMNVLPAKLAGVKKIVMVTPPREGGIDPHILVAASLAGVDEIYTIG 185
Cdd:PRK12447 101 VEtlpGVILGHRNIPVNSVGCYVPGGRYPLVASAHMSVLTAKVAGVKRVIACTPPFPGEPPPAIVAAMHLAGADEIYVLG 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 186 GAQAIAALAYGTESIPKVDKIVGPGNLYVALAKREVYGIVNIDMIAGPSEIVVIADETGNAKYIAADLLSQAEHDERATA 265
Cdd:PRK12447 181 GVQAVAAMAYGTETIKPVDMLVGPGNAYVAEAKRQLFGRVGIDLFAGPTETLVIADDTADPELVATDLLGQAEHGPNSPA 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 266 ICITTNIELAKKVEKEIERQLETLPRSEIARESINRNGAIFIVPSIDEALQLSNEIAPEHLELHIKEPMNALAYVKHAGS 345
Cdd:PRK12447 261 VLITTSRKLAEEVLAEIERLLAILPTADVASAAWRDYGEVILCDDLEEMVAEADRYASEHVQVMTEDPDWFLENMTNYGA 340
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446329155 346 IFLGPYAPEPLGDYLAGPNHVLPTSGTARFFSPLSVDDFVKKSSFLSYTEEALRDVQHHIVELANKEGLHAHARAIQIR 424
Cdd:PRK12447 341 LFLGERTNVAYGDKVIGTNHVLPTSGAARYTGGLWVGKFLKTVTYQRVTDEASAEIGEYCSRLCRLEGFEGHARQADIR 419
PLN02926 PLN02926
histidinol dehydrogenase
33-424 2.46e-131

histidinol dehydrogenase


Pssm-ID: 215500  Cd Length: 431  Bit Score: 384.93  E-value: 2.46e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  33 VSEIVRNVRESGDEALSFYTKKFDGVKIKEF--RVSEEEEKRASMFVEnsflEALQEAKKNIISYHEKQKRQSMFDCAS- 109
Cdd:PLN02926  34 VNPIVENVRSRGDAAVKEYTSKFDKVALDSVveRVSDLPDPVLDADVK----EAFDVAYDNIYAFHLAQKSTEKLEVETm 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 110 EGIIRGQIIRPLENVGVYVPGGTASYPSSVLMNVLPAKLAGVKKIVMVTPPR-EGGIDPHILVAASLAGVDEIYTIGGAQ 188
Cdd:PLN02926 110 PGVRCRRVARPIGAVGLYVPGGTAVLPSTALMLAVPAQIAGCKTVVLATPPRkDGSICPEVLYCAKKAGVTHILKAGGAQ 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 189 AIAALAYGTESIPKVDKIVGPGNLYVALAKREVYG---IVNIDMIAGPSEIVVIADETGNAKYIAADLLSQAEHDERATA 265
Cdd:PLN02926 190 AIAAMAWGTDSCPKVDKIFGPGNQYVTAAKMILQNseaMVSIDMPAGPSEVLVIADKTANPVHVAADLLSQAEHGPDSQV 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 266 ICITTNIELAKKVEKEIERQLETLPRSEIARESINRNGAIFiVPSIDEALQLSNEIAPEHLELHIKEPMNALAYVKHAGS 345
Cdd:PLN02926 270 VLVAVGDVDLDAIEEEVEKQCQSLPRGEIASKALGHSFIVV-ARDMAEAISFSNLYAPEHLIVNVEDAESWLDKIDNAGS 348
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446329155 346 IFLGPYAPEPLGDYLAGPNHVLPTSGTARFFSPLSVDDFVKKSSFLSYTEEALRDVQHHIVELANKEGLHAHARAIQIR 424
Cdd:PLN02926 349 VFLGRWTPESVGDYASGTNHVLPTYGYARMYGGVSLDSFLKYMTVQSLTEEGLQNLGPYVARMAEVEGLEAHKRAVTLR 427
PRK13770 PRK13770
histidinol dehydrogenase; Provisional
12-424 4.67e-129

histidinol dehydrogenase; Provisional


Pssm-ID: 172308  Cd Length: 416  Bit Score: 378.82  E-value: 4.67e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  12 LSKIKLLRE--NANIIEETVQRNVSEIVRNVRESGDEALSFYTKKFDGVKIKEFRVSEEEEKRASMFVENSFLEALQEAK 89
Cdd:PRK13770   2 LNAQQFLNQfsLEAPLDESLYPIIRDICQEVKVHGDKALKMYNLTFDHTKTDHLEISHEQIKAAFDTLDEKTKQALQQSY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  90 KNIISY-----HEKQKRQSMFDCAsegiirgQIIRPLENVGVYVPGGTASYPSSVLMNVLPAKLAGVKKIVMVTPPREGG 164
Cdd:PRK13770  82 ERIKAYqesikQTNQQLEESVECY-------EIYHPLESVGIYVPGGKASYPSTVLMTATLAQVAGVENIVVVTPPQPNG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 165 IDPHILVAASLAGVDEIYTIGGAQAIAALAYGTESIPKVDKIVGPGNLYVALAKREVYGIVNIDMIAGPSEIVVIADETG 244
Cdd:PRK13770 155 VSQEVLAACYITQVNQVFQVGGAQSIAALTYGTETIPKVDKIVGPGNQFVAYAKKYLFGQVGIDQIAGPTEIALIIDETA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 245 NAKYIAADLLSQAEHDERATAICITTNIELAKKVEKEIERQLETLPRSEIARESINRNGAIFIVPSIDEALQLSNEIAPE 324
Cdd:PRK13770 235 DLDAIVYDVFAQAEHDELARTYVISEDAQVLKDLESRIAKALPNVDRYDIVSKSIANQHYLIHASNFDEACHVMNTIAPE 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 325 HLELHIKEPMNALAYVKHAGSIFLGPYAPEPLGDYLAGPNHVLPTSGTARFFSPLSVDDFVKKSSFLSYTEEALRDVQHH 404
Cdd:PRK13770 315 HASIQTVNPQPYIEKVKYVGALFIGHYSPEVIGDYVAGPSHVLPTNRTARFTNGLSVNDFLTRNTVIHLSKDTFEQIADS 394
                        410       420
                 ....*....|....*....|
gi 446329155 405 IVELANKEGLHAHARAIQIR 424
Cdd:PRK13770 395 AQHIAHVEALYNHQQSILIR 414
PRK13769 PRK13769
histidinol dehydrogenase; Provisional
29-421 1.61e-43

histidinol dehydrogenase; Provisional


Pssm-ID: 172307  Cd Length: 368  Bit Score: 156.20  E-value: 1.61e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155  29 VQRNVSEIVRNVRESGDEALSFYTKKFDGVKIKEFRVseeeEKRASMfvENSFLEALQEAKKNIISYHEKQKRQSMFDCA 108
Cdd:PRK13769   9 VVKSVEKIVDDVAERGLQAALEYSERLDGVAPEAALV----EPRPGG--DPAVVAAALEAAKSLEALYSRLKPPEAVDFY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 109 SeGIIRGQIIRPLENVGVYVPggtASYPSSVLMNVLPAKLAGVKKIVMVTPPRegGIDPHILVAASLAGVDEIYTIGGAQ 188
Cdd:PRK13769  83 G-GVLRSVFWKPVRRAALYVP---ARYVSTLVMLAVPARAAGVEEIYVVTPPR--GVTGELLAVAKELGVKGVLAIGGPH 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 189 AiaaLAYGTESIpKVDKIVGPGNLYVALAKREVYGIVNIDMIAGPSEIVVIAdETGNAKYIAADLLSQAEHDERATAICI 268
Cdd:PRK13769 157 G---LAYAVFHM-GVDMVAGPGGLYVQAAKYVLSQYVGIDGIEGPTELVVYA-EGVPPEVAVRGALAQLEHGPTSFAYLL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446329155 269 TTNIELAKKVEkEIERqletlprseiaRESINRNGAIFI--VPSIDEALQLSNEIAPEHLELHIKEpmnALAY-VKHAGS 345
Cdd:PRK13769 232 STDAELLKAAE-EIYR-----------RERTSSMGPLEVrkVAGVEEAVRFIDEIAPEHLEVWGRR---EVAYrVRNVGA 296
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446329155 346 IFLGpyAPEPLGDYLAGPNHVLPTSGTARFFSPLSVDDFVKKSSFLSYTEEAlrDVQHHIVELANKEGLHAHARAI 421
Cdd:PRK13769 297 VSVN--MPSPYLDYVAGISHVLPTGGTARWRGIITPLTFMKPIGVAEAVGEL--ELAEAARRLAEYEGFQYHREAL 368
 
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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