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Conserved domains on  [gi|446568050|ref|WP_000645396|]
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mannitol-1-phosphate 5-dehydrogenase [Salmonella enterica]

Protein Classification

mannitol-1-phosphate 5-dehydrogenase( domain architecture ID 11479775)

mannitol-1-phosphate 5-dehydrogenase catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway

EC:  1.1.1.17
Gene Ontology:  GO:0008926|GO:0019594
PubMed:  14367396

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRK02318 PRK02318
mannitol-1-phosphate 5-dehydrogenase; Provisional
1-382 0e+00

mannitol-1-phosphate 5-dehydrogenase; Provisional


:

Pssm-ID: 235031 [Multi-domain]  Cd Length: 381  Bit Score: 685.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050   1 MKALHFGAGNIGRGFIGKLLADAGIQLTFADVNQVVLDALNARHSYQVHVVGENEQVDTVSGVNAVSSIG-DDVVDLIAH 79
Cdd:PRK02318   1 MKAVHFGAGNIGRGFIGKLLADNGFEVTFVDVNQELIDALNKRKSYQVIVVGENEQVETVSNVSAINSADeEAVIEAIAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050  80 VDLITTAVGPVVLERIAPAIAKGLVKRKAQGVDAPLNIIACENMVRGTTQLKGHVMNALAGGDKAWVEQHVGFVDSAVDR 159
Cdd:PRK02318  81 ADLVTTAVGPNILPFIAPLIAKGLKKRKAQGNTKPLNIIACENMIRGTSFLKKHVLKALSEDEKAWLEEHVGFVDSAVDR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050 160 IVPpsASATHDPLEVTVETFSEWIVDKTQFKGALPTIPGMELTDNLMAFVERKLFTLNTGHAITAYLGKLAGHQTIRDAI 239
Cdd:PRK02318 161 IVP--AQKNEDPLDVTVEPFSEWIVDKTQFKGALPKIKGMEYVDNLMPFIERKLFTVNTGHATTAYLGYLKGYKTIREAI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050 240 LDESIRAVVKGAMEESGAVLIKRYGFDADKHAAYIQKILGRFENPYLKDDVERVGRQPLRKLSAGDRLIKPLLGTLEYGL 319
Cdd:PRK02318 239 LDPSIRAVVKGALEESGAVLIKKYGFDKEEHAAYIEKILGRFENPYLSDDVERVGRQPLRKLGANDRLIKPLLGLKEYGL 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446568050 320 PHVNLVKGIAAAMHFRSEEDPQAQELAALIDEKGPQAALAQISGLDANSDVVAEAVNAYNATK 382
Cdd:PRK02318 319 PHSNLLKGIAAALHFDDENDPQAVELQALIAEKGLEAALAEITGLDADSELVEEIVKAYNALK 381
 
Name Accession Description Interval E-value
PRK02318 PRK02318
mannitol-1-phosphate 5-dehydrogenase; Provisional
1-382 0e+00

mannitol-1-phosphate 5-dehydrogenase; Provisional


Pssm-ID: 235031 [Multi-domain]  Cd Length: 381  Bit Score: 685.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050   1 MKALHFGAGNIGRGFIGKLLADAGIQLTFADVNQVVLDALNARHSYQVHVVGENEQVDTVSGVNAVSSIG-DDVVDLIAH 79
Cdd:PRK02318   1 MKAVHFGAGNIGRGFIGKLLADNGFEVTFVDVNQELIDALNKRKSYQVIVVGENEQVETVSNVSAINSADeEAVIEAIAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050  80 VDLITTAVGPVVLERIAPAIAKGLVKRKAQGVDAPLNIIACENMVRGTTQLKGHVMNALAGGDKAWVEQHVGFVDSAVDR 159
Cdd:PRK02318  81 ADLVTTAVGPNILPFIAPLIAKGLKKRKAQGNTKPLNIIACENMIRGTSFLKKHVLKALSEDEKAWLEEHVGFVDSAVDR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050 160 IVPpsASATHDPLEVTVETFSEWIVDKTQFKGALPTIPGMELTDNLMAFVERKLFTLNTGHAITAYLGKLAGHQTIRDAI 239
Cdd:PRK02318 161 IVP--AQKNEDPLDVTVEPFSEWIVDKTQFKGALPKIKGMEYVDNLMPFIERKLFTVNTGHATTAYLGYLKGYKTIREAI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050 240 LDESIRAVVKGAMEESGAVLIKRYGFDADKHAAYIQKILGRFENPYLKDDVERVGRQPLRKLSAGDRLIKPLLGTLEYGL 319
Cdd:PRK02318 239 LDPSIRAVVKGALEESGAVLIKKYGFDKEEHAAYIEKILGRFENPYLSDDVERVGRQPLRKLGANDRLIKPLLGLKEYGL 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446568050 320 PHVNLVKGIAAAMHFRSEEDPQAQELAALIDEKGPQAALAQISGLDANSDVVAEAVNAYNATK 382
Cdd:PRK02318 319 PHSNLLKGIAAALHFDDENDPQAVELQALIAEKGLEAALAEITGLDADSELVEEIVKAYNALK 381
Mannitol_dh_C pfam08125
Mannitol dehydrogenase C-terminal domain;
148-374 1.18e-83

Mannitol dehydrogenase C-terminal domain;


Pssm-ID: 369700  Cd Length: 246  Bit Score: 255.00  E-value: 1.18e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050  148 QHVGFVDSAVDRIVPPS----------ASATHDPLEVTVETFSEWIVDKTQFKG-ALPTIPGMELTDNLMAFVERKLFTL 216
Cdd:pfam08125   1 DNVGFPNTMVDRIVPATtddelakiaqALGVEDPLPVTVEPFRQWVIEDNFVKGrPLLEKVGVEYVEDVDPYEERKLRIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050  217 NTGHAITAYLGKLAGHQTIRDAILDESIRAVVKGAMEESGAVLIKRYgfDADKHAAYIQKILGRFENPYLKDDVERVGR- 295
Cdd:pfam08125  81 NGGHATLAYLGYLAGYQTIHEAMLDPEIRAFVKGVMTEEVAPLLAKV--PGDDLEAYADKIIERFSNPYIKDTVWRVARd 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050  296 ----QPLRKLSAGDRLIK--PLLGTLEYG-LPHVNLVKGIAAAMHFRSEEDPQAQEL--AALIDEKGPQAALAQISGLDA 366
Cdd:pfam08125 159 gsqkLPQRKLPSLRRHIRagPLPELLALGvAGWMRYLQGVDEGGNYIDPEDPQAQELqaAAIIAKERPAAVLAEVSGLGD 238

                  ....*...
gi 446568050  367 NSDVVAEA 374
Cdd:pfam08125 239 DLAQNSEF 246
MtlD COG0246
Mannitol-1-phosphate/altronate dehydrogenases [Carbohydrate transport and metabolism];
4-378 1.34e-34

Mannitol-1-phosphate/altronate dehydrogenases [Carbohydrate transport and metabolism];


Pssm-ID: 440016 [Multi-domain]  Cd Length: 492  Bit Score: 132.97  E-value: 1.34e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050   4 LHFGAGNIGRGFIG----KLLAD-------AGIQLTFADvnqVVLDALNAR-HSYQVHVVG-----ENEQVDTVSGVNAV 66
Cdd:COG0246   31 VHFGVGNFHRAHQAwytdRLLNAgdfdwgiVGVGLRSGD---ALRDALAAQdGLYTLVERGpdgveEARVIGSISEVLVA 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050  67 SSIGDDVVDLIAH-----VDLITTAVG--------------PVVLERIAP---------AIAKGLVKRKAQGvDAPLNII 118
Cdd:COG0246  108 PEDPEAVLALLADpalriVSLTITEKGycldpatgeldldhPDIQADLANpapprsapgKLTAALYRRRAAG-LKPFTVL 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050 119 ACENMVRGTTQLKGHVMNALAGGDKA---WVEQHVGFVDSAVDRIVPPSASAT----------HDPLEVTVETFSEWIV- 184
Cdd:COG0246  187 SCDNLPHNGDVLREAVLAFARLWDPEladWIEENVTFPNTMVDRIVPATTDEDrarlaaelgyEDAAPVVAEPFRQWVIe 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050 185 DKtqFKGALPTI--PGMELTDNLMAFVERKLFTLNTGHAITAYLGKLAGHQTIRDAILDESIRAVVKGAM-EESGAVLIK 261
Cdd:COG0246  267 DD--FPAGRPPLekAGVQFVDDVAPYEEMKLRLLNGSHTALAYLGYLAGYETVAEAMADPLLRAFVRRLMlEEIIPTLPP 344
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050 262 RYGFDADkhaAYIQKILGRFENPYLKDDVERVGRQPLRKLSAgdRLIKPLLGTLEYGLPHVNLVKGIAAAMHF---RSEE 338
Cdd:COG0246  345 PPGVDLE---AYADAVLERFANPAIRHTLARIALDGSQKLPQ--RLLPTLRDYLAAGRDPKRLALAVAAWLRYlrgVDDD 419
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446568050 339 -------DPQAQELAALIDEKG-----PQAALA--QISGLD-ANSDVVAEAVNAY 378
Cdd:COG0246  420 gepielsDPLADELAALAAAADdpadlVRAFLAleAIFGDDlADDPGFVEAVTAA 474
 
Name Accession Description Interval E-value
PRK02318 PRK02318
mannitol-1-phosphate 5-dehydrogenase; Provisional
1-382 0e+00

mannitol-1-phosphate 5-dehydrogenase; Provisional


Pssm-ID: 235031 [Multi-domain]  Cd Length: 381  Bit Score: 685.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050   1 MKALHFGAGNIGRGFIGKLLADAGIQLTFADVNQVVLDALNARHSYQVHVVGENEQVDTVSGVNAVSSIG-DDVVDLIAH 79
Cdd:PRK02318   1 MKAVHFGAGNIGRGFIGKLLADNGFEVTFVDVNQELIDALNKRKSYQVIVVGENEQVETVSNVSAINSADeEAVIEAIAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050  80 VDLITTAVGPVVLERIAPAIAKGLVKRKAQGVDAPLNIIACENMVRGTTQLKGHVMNALAGGDKAWVEQHVGFVDSAVDR 159
Cdd:PRK02318  81 ADLVTTAVGPNILPFIAPLIAKGLKKRKAQGNTKPLNIIACENMIRGTSFLKKHVLKALSEDEKAWLEEHVGFVDSAVDR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050 160 IVPpsASATHDPLEVTVETFSEWIVDKTQFKGALPTIPGMELTDNLMAFVERKLFTLNTGHAITAYLGKLAGHQTIRDAI 239
Cdd:PRK02318 161 IVP--AQKNEDPLDVTVEPFSEWIVDKTQFKGALPKIKGMEYVDNLMPFIERKLFTVNTGHATTAYLGYLKGYKTIREAI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050 240 LDESIRAVVKGAMEESGAVLIKRYGFDADKHAAYIQKILGRFENPYLKDDVERVGRQPLRKLSAGDRLIKPLLGTLEYGL 319
Cdd:PRK02318 239 LDPSIRAVVKGALEESGAVLIKKYGFDKEEHAAYIEKILGRFENPYLSDDVERVGRQPLRKLGANDRLIKPLLGLKEYGL 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446568050 320 PHVNLVKGIAAAMHFRSEEDPQAQELAALIDEKGPQAALAQISGLDANSDVVAEAVNAYNATK 382
Cdd:PRK02318 319 PHSNLLKGIAAALHFDDENDPQAVELQALIAEKGLEAALAEITGLDADSELVEEIVKAYNALK 381
Mannitol_dh_C pfam08125
Mannitol dehydrogenase C-terminal domain;
148-374 1.18e-83

Mannitol dehydrogenase C-terminal domain;


Pssm-ID: 369700  Cd Length: 246  Bit Score: 255.00  E-value: 1.18e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050  148 QHVGFVDSAVDRIVPPS----------ASATHDPLEVTVETFSEWIVDKTQFKG-ALPTIPGMELTDNLMAFVERKLFTL 216
Cdd:pfam08125   1 DNVGFPNTMVDRIVPATtddelakiaqALGVEDPLPVTVEPFRQWVIEDNFVKGrPLLEKVGVEYVEDVDPYEERKLRIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050  217 NTGHAITAYLGKLAGHQTIRDAILDESIRAVVKGAMEESGAVLIKRYgfDADKHAAYIQKILGRFENPYLKDDVERVGR- 295
Cdd:pfam08125  81 NGGHATLAYLGYLAGYQTIHEAMLDPEIRAFVKGVMTEEVAPLLAKV--PGDDLEAYADKIIERFSNPYIKDTVWRVARd 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050  296 ----QPLRKLSAGDRLIK--PLLGTLEYG-LPHVNLVKGIAAAMHFRSEEDPQAQEL--AALIDEKGPQAALAQISGLDA 366
Cdd:pfam08125 159 gsqkLPQRKLPSLRRHIRagPLPELLALGvAGWMRYLQGVDEGGNYIDPEDPQAQELqaAAIIAKERPAAVLAEVSGLGD 238

                  ....*...
gi 446568050  367 NSDVVAEA 374
Cdd:pfam08125 239 DLAQNSEF 246
MtlD COG0246
Mannitol-1-phosphate/altronate dehydrogenases [Carbohydrate transport and metabolism];
4-378 1.34e-34

Mannitol-1-phosphate/altronate dehydrogenases [Carbohydrate transport and metabolism];


Pssm-ID: 440016 [Multi-domain]  Cd Length: 492  Bit Score: 132.97  E-value: 1.34e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050   4 LHFGAGNIGRGFIG----KLLAD-------AGIQLTFADvnqVVLDALNAR-HSYQVHVVG-----ENEQVDTVSGVNAV 66
Cdd:COG0246   31 VHFGVGNFHRAHQAwytdRLLNAgdfdwgiVGVGLRSGD---ALRDALAAQdGLYTLVERGpdgveEARVIGSISEVLVA 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050  67 SSIGDDVVDLIAH-----VDLITTAVG--------------PVVLERIAP---------AIAKGLVKRKAQGvDAPLNII 118
Cdd:COG0246  108 PEDPEAVLALLADpalriVSLTITEKGycldpatgeldldhPDIQADLANpapprsapgKLTAALYRRRAAG-LKPFTVL 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050 119 ACENMVRGTTQLKGHVMNALAGGDKA---WVEQHVGFVDSAVDRIVPPSASAT----------HDPLEVTVETFSEWIV- 184
Cdd:COG0246  187 SCDNLPHNGDVLREAVLAFARLWDPEladWIEENVTFPNTMVDRIVPATTDEDrarlaaelgyEDAAPVVAEPFRQWVIe 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050 185 DKtqFKGALPTI--PGMELTDNLMAFVERKLFTLNTGHAITAYLGKLAGHQTIRDAILDESIRAVVKGAM-EESGAVLIK 261
Cdd:COG0246  267 DD--FPAGRPPLekAGVQFVDDVAPYEEMKLRLLNGSHTALAYLGYLAGYETVAEAMADPLLRAFVRRLMlEEIIPTLPP 344
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050 262 RYGFDADkhaAYIQKILGRFENPYLKDDVERVGRQPLRKLSAgdRLIKPLLGTLEYGLPHVNLVKGIAAAMHF---RSEE 338
Cdd:COG0246  345 PPGVDLE---AYADAVLERFANPAIRHTLARIALDGSQKLPQ--RLLPTLRDYLAAGRDPKRLALAVAAWLRYlrgVDDD 419
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446568050 339 -------DPQAQELAALIDEKG-----PQAALA--QISGLD-ANSDVVAEAVNAY 378
Cdd:COG0246  420 gepielsDPLADELAALAAAADdpadlVRAFLAleAIFGDDlADDPGFVEAVTAA 474
Mannitol_dh pfam01232
Mannitol dehydrogenase Rossmann domain;
1-123 6.73e-28

Mannitol dehydrogenase Rossmann domain;


Pssm-ID: 395986 [Multi-domain]  Cd Length: 151  Bit Score: 107.11  E-value: 6.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050    1 MKALHFGAGNIGRG---FIGKLLADAGIQLTFADVNQVVLDA---LNARHSYQVHVVG--ENEQVDTVSGVNAVSSIGDD 72
Cdd:pfam01232   1 MRIVHFGAGNFHRAhqaFIGDLLAENGFDWGIVDVNLRVVDAreaLNAQDGLYTVIEDgeEGRQARLVGSVNAVNSVEED 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446568050   73 VVDLIA-----HVDLITTAVGP----------VVLERIAPAIAKG------LVKRKAQGvDAPLNIIACENM 123
Cdd:pfam01232  81 LEALIElmaepQADIVSTTVTEggidatgqldNDLPDIAADLAKPeylveaLKRRRAAG-LKPLTIIACDNM 151
PRK15037 PRK15037
D-mannonate oxidoreductase; Provisional
99-345 4.60e-21

D-mannonate oxidoreductase; Provisional


Pssm-ID: 184997 [Multi-domain]  Cd Length: 486  Bit Score: 94.33  E-value: 4.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050  99 IAKGLVKRKAQGVDApLNIIACENMVRGTTQLKGHVMNALAGGD---KAWVEQHVGFVDSAVDRIVPPSASAT------- 168
Cdd:PRK15037 165 IVEALRLRREKGLKA-FTVMSCDNVRENGHVAKVAVLGLAQARDpqlAAWIEENVTFPCTMVDRIVPAATPETlqeiadq 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050 169 ---HDPLEVTVETFSEWIVDKtQFKGALP--TIPGMELTDNLMAFVERKLFTLNTGHAITAYLGKLAGHQTIRDAILDES 243
Cdd:PRK15037 244 lgvYDPCAIACEPFRQWVIED-NFVNGRPdwDKVGAQFVADVVPFEMMKLRMLNGSHSFLAYLGYLGGYETIADTMTNPA 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050 244 IR-AVVKGAMEESGAVLIKRYGFDADkhaAYIQKILGRFENPYLKDDVERVGRQPLRKLSagDRLIKPLLGTLEYGLPHV 322
Cdd:PRK15037 323 YRkAAFALMMQEQAPTLSMPEGTDLN---AYATLLIERFSNPSLRHRTWQIAMDGSQKLP--QRLLDPVRLHLQNGGSWR 397
                        250       260
                 ....*....|....*....|...
gi 446568050 323 NLVKGIAAAMHFRSEEDPQAQEL 345
Cdd:PRK15037 398 HLALGVAGWMRYTQGVDEQGNAI 420
PRK03643 PRK03643
tagaturonate reductase;
98-378 7.68e-18

tagaturonate reductase;


Pssm-ID: 235147 [Multi-domain]  Cd Length: 471  Bit Score: 84.51  E-value: 7.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050  98 AIAKGLVkrkaqgvdaplnIIACENMVRGTTQLKGHVM-----NALAGGDKAWVEQHVGFVDSAVDRIVP--PSASAT-- 168
Cdd:PRK03643 159 AADKGLI------------IIPCELIDYNGEKLKEIVLryaqeWNLPEAFIQWLEEANTFCSTLVDRIVTgyPRDEAAal 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050 169 ------HDPLEVTVETFSEWIVDKTQF-KGALP---TIPGMELTDNLMAFVERKLFTLNTGHAITAYLGKLAGHQTIRDA 238
Cdd:PRK03643 227 eeelgyEDGLLDTAEPFYLWVIEGPKSlAKELPfdkAGLNVLIVDDIKPYRERKVRILNGAHTALVPVAYLAGLDTVGEA 306
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568050 239 ILDESIRAVVKGAMEESgavLIKRYGFDADKHAAYIQKILGRFENPYLKDDVERVGRQPLRKLSAgdRLIKPLLGTLE-Y 317
Cdd:PRK03643 307 MEDAEIGAFVEKAIYEE---IIPVLDLPEDELESFAEAVLDRFRNPFIKHQLLSIALNSMSKFRT--RILPQLLAYQErK 381
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446568050 318 G-LPhVNLVKGIAAAMHF-RSEEDPQAQELAaliDEKGPQAALAQI-SGLDANSDVVAEAVNAY 378
Cdd:PRK03643 382 GtLP-ARLTFALAALIAFyRGERNGETYPIQ---DDAHWLERFKQLwSQVDDGEISLAELVAAV 441
 
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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