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Conserved domains on  [gi|639310398|ref|WP_024592675|]
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MULTISPECIES: 4-hydroxy-tetrahydrodipicolinate reductase [Pseudoalteromonas]

Protein Classification

4-hydroxy-tetrahydrodipicolinate reductase( domain architecture ID 11416656)

4-hydroxy-tetrahydrodipicolinate reductase catalyzes the NAD(P)-dependent conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate in amino acid biosynthesis pathways

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DapB COG0289
4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; ...
5-264 3.24e-117

4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; 4-hydroxy-tetrahydrodipicolinate reductase is part of the Pathway/BioSystem: Lysine biosynthesis


:

Pssm-ID: 440058 [Multi-domain]  Cd Length: 257  Bit Score: 335.93  E-value: 3.24e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398   5 RIGVFGANGRMGLALLEAATIKEQTQLTGAYVRSSSSllGINVNQVnsAADNSVSFSEETTIDNVDVLIDFTLPAGMKNH 84
Cdd:COG0289    2 KIAVAGASGRMGRELIRAVLEAPDLELVAAIDRPGSP--GQDAGEL--ALGVPVTDDLEEALAKADVVIDFTHPEATLEN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398  85 LKTAVAQKIPMVIGTTGLTSDDMALLHDAAKHIPIVFARNYSVGVNVLLNLVQTAATKFGDDLDIEIFEAHHRHKIDAPS 164
Cdd:COG0289   78 LEAALEAGVPVVIGTTGFSEEQLAELEEAAKGIPVLIAPNFSLGVNLLFKLAEEAAKYLGDDYDIEIIEAHHRQKVDAPS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398 165 GTALAIGESIAQAKGWDHDEVAVYDRSQVETAKSQNEIGYSVLRGGDIVGEHTAYFATMGERLELTHKASSRMTFALGAV 244
Cdd:COG0289  158 GTALKLAEAIAEARGRDLDDVAVYGREGITGARKKGEIGIHSVRGGDIVGEHTVIFAGEGERIEIRHDASSRESFAPGAL 237
                        250       260
                 ....*....|....*....|
gi 639310398 245 RAASWLKNKPVGLYDMQDVL 264
Cdd:COG0289  238 LAARWLAGKPPGLYGMEDVL 257
 
Name Accession Description Interval E-value
DapB COG0289
4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; ...
5-264 3.24e-117

4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; 4-hydroxy-tetrahydrodipicolinate reductase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440058 [Multi-domain]  Cd Length: 257  Bit Score: 335.93  E-value: 3.24e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398   5 RIGVFGANGRMGLALLEAATIKEQTQLTGAYVRSSSSllGINVNQVnsAADNSVSFSEETTIDNVDVLIDFTLPAGMKNH 84
Cdd:COG0289    2 KIAVAGASGRMGRELIRAVLEAPDLELVAAIDRPGSP--GQDAGEL--ALGVPVTDDLEEALAKADVVIDFTHPEATLEN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398  85 LKTAVAQKIPMVIGTTGLTSDDMALLHDAAKHIPIVFARNYSVGVNVLLNLVQTAATKFGDDLDIEIFEAHHRHKIDAPS 164
Cdd:COG0289   78 LEAALEAGVPVVIGTTGFSEEQLAELEEAAKGIPVLIAPNFSLGVNLLFKLAEEAAKYLGDDYDIEIIEAHHRQKVDAPS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398 165 GTALAIGESIAQAKGWDHDEVAVYDRSQVETAKSQNEIGYSVLRGGDIVGEHTAYFATMGERLELTHKASSRMTFALGAV 244
Cdd:COG0289  158 GTALKLAEAIAEARGRDLDDVAVYGREGITGARKKGEIGIHSVRGGDIVGEHTVIFAGEGERIEIRHDASSRESFAPGAL 237
                        250       260
                 ....*....|....*....|
gi 639310398 245 RAASWLKNKPVGLYDMQDVL 264
Cdd:COG0289  238 LAARWLAGKPPGLYGMEDVL 257
dapB TIGR00036
4-hydroxy-tetrahydrodipicolinate reductase; [Amino acid biosynthesis, Aspartate family]
5-265 1.30e-89

4-hydroxy-tetrahydrodipicolinate reductase; [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 129147 [Multi-domain]  Cd Length: 266  Bit Score: 266.58  E-value: 1.30e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398    5 RIGVFGANGRMGLALLEAATIKEQTQLTGAYVRSSSSLLGINVNQVNSAADNSVSFSE--ETTIDNVDVLIDFTLPAGMK 82
Cdd:TIGR00036   3 KVAVAGAAGRMGRELIKAALAAEGLQLVAAFERHGSSLQGTDAGELAGIGKVGVPVTDdlEAVETDPDVLIDFTTPEGVL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398   83 NHLKTAVAQKIPMVIGTTGLTSDDMALLHDAA--KHIPIVFARNYSVGVNVLLNLVQTAATKFGDdLDIEIFEAHHRHKI 160
Cdd:TIGR00036  83 NHLKFALEHGVRLVVGTTGFSEEDKQELADLAekAGIAAVIAPNFSIGVNLMFKLLEKAAKYLGD-YDIEIIELHHRHKK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398  161 DAPSGTALAIGESIAQAKGWDHDEVAVYDRSQVETAKSQNEIGYSVLRGGDIVGEHTAYFATMGERLELTHKASSRMTFA 240
Cdd:TIGR00036 162 DAPSGTALKTAEMIAEARGERLKNVAVTEREGLTGERGREEIGIHAVRGGDVVGEHTVMFAGDGERLEITHRASSRACFA 241
                         250       260
                  ....*....|....*....|....*
gi 639310398  241 LGAVRAASWLKNKPVGLYDMQDVLD 265
Cdd:TIGR00036 242 NGAVRAARWLADKEAGVYDMEDVLD 266
DapB_C pfam05173
Dihydrodipicolinate reductase, C-terminus; Dihydrodipicolinate reductase (DapB) reduces the ...
135-264 1.37e-52

Dihydrodipicolinate reductase, C-terminus; Dihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for both protein and cell wall biosynthesis. The C-terminal domain of DapB has been proposed to be the substrate- binding domain.


Pssm-ID: 461568  Cd Length: 122  Bit Score: 166.91  E-value: 1.37e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398  135 LVQTAATKFGDDLDIEIFEAHHRHKIDAPSGTALAIGESIAQAKGWDHDEVAVYDRsqvetaksqNEIGYSVLRGGDIVG 214
Cdd:pfam05173   2 LAKEAAKLLGDAYDVEIIESHHNQKKDAPSGTALKLAEAIAELGARKNKWARGAAR---------DGIGIHSVRGGGVVG 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 639310398  215 EHTAYFATMGERLELTHKASSRMTFALGAVRAASWLKNKPVGLYDMQDVL 264
Cdd:pfam05173  73 EHTVLFAGDGERIEITHDAHSREIFAPGALLAARWLAGKKPGLYGMEDVL 122
DHDPR_N cd02274
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ...
5-124 2.56e-33

N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; DHDPR (EC 1.17.1.8), also called 4-hydroxy-tetrahydrodipicolinate reductase, or HTPA reductase, is a product of an essential gene referred to as dapB. It catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). DHDPR could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. DHDPR is a component of the biosynthetic pathway that generates meso-diaminopimelate, a component of bacterial cell walls, and the amino acid L-lysine in various bacteria, archaea, cyanobacteria and higher plants. The enzyme is a homotetramer where each monomer is composed of two domains, an N-terminal NAD(P)-binding domain which forms a Rossmann fold, and a C-terminal substrate-binding domain that forms an open, mixed alpha-beta sandwich.


Pssm-ID: 467611 [Multi-domain]  Cd Length: 139  Bit Score: 118.05  E-value: 2.56e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398   5 RIGVFGANGRMGLALLEAATIKEQTQLTGAYVRSSSSLLGINV-NQVNSAADNSVSFSEETTIDNVDVLIDFTLPAGMKN 83
Cdd:cd02274    2 KVAVAGATGRMGRELVKAILEAPDLELVGAVDRPGSGLLGGDAgGLAGIGTGVIVSLDLELAAADADVVIDFTTPEATLE 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 639310398  84 HLKTAVAQKIPMVIGTTGLTSDDMALLHDAAKHIPIVFARN 124
Cdd:cd02274   82 NLEAAAKAGVPLVIGTTGFSEEQLAEIEEAAKKIPVVIAPN 122
PLN02775 PLN02775
Probable dihydrodipicolinate reductase
5-264 1.77e-11

Probable dihydrodipicolinate reductase


Pssm-ID: 178374  Cd Length: 286  Bit Score: 62.75  E-value: 1.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398   5 RIGVFGANGRMGLALLEAATIKE----QTQLTGAYVRSSS-SLLGINVNQVNSAADNSVSFSEETTIDNVdVLIDFTLPA 79
Cdd:PLN02775  13 PIMVNGCTGKMGHAVAEAAVSAGlqlvPVSFTGPAGVGVTvEVCGVEVRLVGPSEREAVLSSVKAEYPNL-IVVDYTLPD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398  80 GMKNHLKTAVAQKIPMVIGTTGltsDDMALLHD--AAKHIPIVFARNYSVGVNVLLNLVQTAATKFGDDLD---IEIFEA 154
Cdd:PLN02775  92 AVNDNAELYCKNGLPFVMGTTG---GDRDRLLKdvEESGVYAVIAPQMGKQVVAFQAAMEIMAEQFPGAFSgytLEVVES 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398 155 HHRHKIDApSGTALAIGESIaQAKGWDHDEVAVY----DRSQVETAKSQNEigysVLRGGdivGEHTAYFATMGE--RLE 228
Cdd:PLN02775 169 HQATKLDT-SGTAKAVISSF-RKLGVSFDMDQIElirdPKQQLEGVGVPEE----HLNGH---AFHTYRLTSPDGtvSFE 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 639310398 229 LTHKASSRMTFALGAVRAASWLKNK-----PVGLYDMQDVL 264
Cdd:PLN02775 240 FQHNVCGRSIYAEGTVDAVLFLAKKiaegaDKRIYNMIDVL 280
 
Name Accession Description Interval E-value
DapB COG0289
4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; ...
5-264 3.24e-117

4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; 4-hydroxy-tetrahydrodipicolinate reductase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440058 [Multi-domain]  Cd Length: 257  Bit Score: 335.93  E-value: 3.24e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398   5 RIGVFGANGRMGLALLEAATIKEQTQLTGAYVRSSSSllGINVNQVnsAADNSVSFSEETTIDNVDVLIDFTLPAGMKNH 84
Cdd:COG0289    2 KIAVAGASGRMGRELIRAVLEAPDLELVAAIDRPGSP--GQDAGEL--ALGVPVTDDLEEALAKADVVIDFTHPEATLEN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398  85 LKTAVAQKIPMVIGTTGLTSDDMALLHDAAKHIPIVFARNYSVGVNVLLNLVQTAATKFGDDLDIEIFEAHHRHKIDAPS 164
Cdd:COG0289   78 LEAALEAGVPVVIGTTGFSEEQLAELEEAAKGIPVLIAPNFSLGVNLLFKLAEEAAKYLGDDYDIEIIEAHHRQKVDAPS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398 165 GTALAIGESIAQAKGWDHDEVAVYDRSQVETAKSQNEIGYSVLRGGDIVGEHTAYFATMGERLELTHKASSRMTFALGAV 244
Cdd:COG0289  158 GTALKLAEAIAEARGRDLDDVAVYGREGITGARKKGEIGIHSVRGGDIVGEHTVIFAGEGERIEIRHDASSRESFAPGAL 237
                        250       260
                 ....*....|....*....|
gi 639310398 245 RAASWLKNKPVGLYDMQDVL 264
Cdd:COG0289  238 LAARWLAGKPPGLYGMEDVL 257
dapB TIGR00036
4-hydroxy-tetrahydrodipicolinate reductase; [Amino acid biosynthesis, Aspartate family]
5-265 1.30e-89

4-hydroxy-tetrahydrodipicolinate reductase; [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 129147 [Multi-domain]  Cd Length: 266  Bit Score: 266.58  E-value: 1.30e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398    5 RIGVFGANGRMGLALLEAATIKEQTQLTGAYVRSSSSLLGINVNQVNSAADNSVSFSE--ETTIDNVDVLIDFTLPAGMK 82
Cdd:TIGR00036   3 KVAVAGAAGRMGRELIKAALAAEGLQLVAAFERHGSSLQGTDAGELAGIGKVGVPVTDdlEAVETDPDVLIDFTTPEGVL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398   83 NHLKTAVAQKIPMVIGTTGLTSDDMALLHDAA--KHIPIVFARNYSVGVNVLLNLVQTAATKFGDdLDIEIFEAHHRHKI 160
Cdd:TIGR00036  83 NHLKFALEHGVRLVVGTTGFSEEDKQELADLAekAGIAAVIAPNFSIGVNLMFKLLEKAAKYLGD-YDIEIIELHHRHKK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398  161 DAPSGTALAIGESIAQAKGWDHDEVAVYDRSQVETAKSQNEIGYSVLRGGDIVGEHTAYFATMGERLELTHKASSRMTFA 240
Cdd:TIGR00036 162 DAPSGTALKTAEMIAEARGERLKNVAVTEREGLTGERGREEIGIHAVRGGDVVGEHTVMFAGDGERLEITHRASSRACFA 241
                         250       260
                  ....*....|....*....|....*
gi 639310398  241 LGAVRAASWLKNKPVGLYDMQDVLD 265
Cdd:TIGR00036 242 NGAVRAARWLADKEAGVYDMEDVLD 266
DapB_C pfam05173
Dihydrodipicolinate reductase, C-terminus; Dihydrodipicolinate reductase (DapB) reduces the ...
135-264 1.37e-52

Dihydrodipicolinate reductase, C-terminus; Dihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for both protein and cell wall biosynthesis. The C-terminal domain of DapB has been proposed to be the substrate- binding domain.


Pssm-ID: 461568  Cd Length: 122  Bit Score: 166.91  E-value: 1.37e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398  135 LVQTAATKFGDDLDIEIFEAHHRHKIDAPSGTALAIGESIAQAKGWDHDEVAVYDRsqvetaksqNEIGYSVLRGGDIVG 214
Cdd:pfam05173   2 LAKEAAKLLGDAYDVEIIESHHNQKKDAPSGTALKLAEAIAELGARKNKWARGAAR---------DGIGIHSVRGGGVVG 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 639310398  215 EHTAYFATMGERLELTHKASSRMTFALGAVRAASWLKNKPVGLYDMQDVL 264
Cdd:pfam05173  73 EHTVLFAGDGERIEITHDAHSREIFAPGALLAARWLAGKKPGLYGMEDVL 122
DapB_N pfam01113
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the ...
5-125 6.23e-36

Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for both protein and cell wall biosynthesis. The N-terminal domain of DapB binds the dinucleotide NADPH.


Pssm-ID: 460069 [Multi-domain]  Cd Length: 121  Bit Score: 124.27  E-value: 6.23e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398    5 RIGVFGANGRMGLALLEAATIKEQTQLTGAYVRSSSSLLGINVNQVnSAADNSVSFSEETTIDNVDVLIDFTLPAGMKNH 84
Cdd:pfam01113   2 KIAVAGASGRMGRELIKAVLEAPDLELVAAVDRPGSSLLGSDAGEL-APLGVPVTDDLEEVLADADVLIDFTTPEATLEN 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 639310398   85 LKTAVAQKIPMVIGTTGLTSDDMALLHDAAKHIPIVFARNY 125
Cdd:pfam01113  81 LEFALKHGVPLVIGTTGFTEEQLAELKEAAKKIPIVIAPNF 121
DHDPR_N cd02274
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ...
5-124 2.56e-33

N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; DHDPR (EC 1.17.1.8), also called 4-hydroxy-tetrahydrodipicolinate reductase, or HTPA reductase, is a product of an essential gene referred to as dapB. It catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). DHDPR could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. DHDPR is a component of the biosynthetic pathway that generates meso-diaminopimelate, a component of bacterial cell walls, and the amino acid L-lysine in various bacteria, archaea, cyanobacteria and higher plants. The enzyme is a homotetramer where each monomer is composed of two domains, an N-terminal NAD(P)-binding domain which forms a Rossmann fold, and a C-terminal substrate-binding domain that forms an open, mixed alpha-beta sandwich.


Pssm-ID: 467611 [Multi-domain]  Cd Length: 139  Bit Score: 118.05  E-value: 2.56e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398   5 RIGVFGANGRMGLALLEAATIKEQTQLTGAYVRSSSSLLGINV-NQVNSAADNSVSFSEETTIDNVDVLIDFTLPAGMKN 83
Cdd:cd02274    2 KVAVAGATGRMGRELVKAILEAPDLELVGAVDRPGSGLLGGDAgGLAGIGTGVIVSLDLELAAADADVVIDFTTPEATLE 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 639310398  84 HLKTAVAQKIPMVIGTTGLTSDDMALLHDAAKHIPIVFARN 124
Cdd:cd02274   82 NLEAAAKAGVPLVIGTTGFSEEQLAEIEEAAKKIPVVIAPN 122
PLN02775 PLN02775
Probable dihydrodipicolinate reductase
5-264 1.77e-11

Probable dihydrodipicolinate reductase


Pssm-ID: 178374  Cd Length: 286  Bit Score: 62.75  E-value: 1.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398   5 RIGVFGANGRMGLALLEAATIKE----QTQLTGAYVRSSS-SLLGINVNQVNSAADNSVSFSEETTIDNVdVLIDFTLPA 79
Cdd:PLN02775  13 PIMVNGCTGKMGHAVAEAAVSAGlqlvPVSFTGPAGVGVTvEVCGVEVRLVGPSEREAVLSSVKAEYPNL-IVVDYTLPD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398  80 GMKNHLKTAVAQKIPMVIGTTGltsDDMALLHD--AAKHIPIVFARNYSVGVNVLLNLVQTAATKFGDDLD---IEIFEA 154
Cdd:PLN02775  92 AVNDNAELYCKNGLPFVMGTTG---GDRDRLLKdvEESGVYAVIAPQMGKQVVAFQAAMEIMAEQFPGAFSgytLEVVES 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310398 155 HHRHKIDApSGTALAIGESIaQAKGWDHDEVAVY----DRSQVETAKSQNEigysVLRGGdivGEHTAYFATMGE--RLE 228
Cdd:PLN02775 169 HQATKLDT-SGTAKAVISSF-RKLGVSFDMDQIElirdPKQQLEGVGVPEE----HLNGH---AFHTYRLTSPDGtvSFE 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 639310398 229 LTHKASSRMTFALGAVRAASWLKNK-----PVGLYDMQDVL 264
Cdd:PLN02775 240 FQHNVCGRSIYAEGTVDAVLFLAKKiaegaDKRIYNMIDVL 280
 
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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