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Conserved domains on  [gi|663530302|gb|AIF20292|]
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5-deoxyadenosylcobinamide phosphate nucleotidyltransferase (ispD) [uncultured marine thaumarchaeote KM3_89_A10]

Protein Classification

COG2266 family protein( domain architecture ID 10006293)

COG2266 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 1-187 3.79e-64

GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


:

Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 195.49  E-value: 3.79e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530302   1 MAGGKGSRMEFPapEKLLLE-YEKPIIFHVIDSLNDShCFSKVFAATSLNSPDTKRVLEEKGIETLDTQGNGYVNDLNFL 79
Cdd:COG2266    1 MAGGKGTRLGGG--EKPLLEiCGKPMIDRVIDALEES-CIDKIYVAVSPNTPKTREYLKERGVEVIETPGEGYVEDLNEA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530302  80 LQKIDGFVFVVSGDLPLLDEEIIQKLVE--FNSESVWTSFLVSKEFLNSLGLESNLLVKHDStECVYTGISIINADKIKn 157
Cdd:COG2266   78 LESISGPVLVVPADLPLLTPEIIDDIIDayLESGKPSLTVVVPAALKRELGVSPDTTFEIDG-ELVPTGINIVDGSDGE- 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 663530302 158 lnlVNENYVILNDKRIAFNLNTNEDFELLN 187
Cdd:COG2266  156 ---QEETNLVLDDPRLALNVNTPEDLKLAE 182
 
Name Accession Description Interval E-value
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 1-187 3.79e-64

GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 195.49  E-value: 3.79e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530302   1 MAGGKGSRMEFPapEKLLLE-YEKPIIFHVIDSLNDShCFSKVFAATSLNSPDTKRVLEEKGIETLDTQGNGYVNDLNFL 79
Cdd:COG2266    1 MAGGKGTRLGGG--EKPLLEiCGKPMIDRVIDALEES-CIDKIYVAVSPNTPKTREYLKERGVEVIETPGEGYVEDLNEA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530302  80 LQKIDGFVFVVSGDLPLLDEEIIQKLVE--FNSESVWTSFLVSKEFLNSLGLESNLLVKHDStECVYTGISIINADKIKn 157
Cdd:COG2266   78 LESISGPVLVVPADLPLLTPEIIDDIIDayLESGKPSLTVVVPAALKRELGVSPDTTFEIDG-ELVPTGINIVDGSDGE- 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 663530302 158 lnlVNENYVILNDKRIAFNLNTNEDFELLN 187
Cdd:COG2266  156 ---QEETNLVLDDPRLALNVNTPEDLKLAE 182
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 1-107 2.36e-10

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 56.43  E-value: 2.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530302    1 MAGGKGSRMEFPapeKLLLEY-EKPIIFHVIDSLndSHCFSKVFAATslNSPDTKRVLEEKGIETL--DTQGNGYVNDLN 77
Cdd:pfam12804   4 LAGGRSSRMGGD---KALLPLgGKPLLERVLERL--RPAGDEVVVVA--NDEEVLAALAGLGVPVVpdPDPGQGPLAGLL 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 663530302   78 FLLQKIDG--FVFVVSGDLPLLDEEIIQKLVE 107
Cdd:pfam12804  77 AALRAAPGadAVLVLACDMPFLTPELLRRLLA 108
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 2-108 8.74e-10

MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 55.27  E-value: 8.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530302   2 AGGKGSRMEFPapeKLLLEYE-KPIIFHVIDSLndSHCFSKVFaatsLNSPDTKRVLEEKGIETL--DTQGNGYVNDLNF 78
Cdd:cd02503    7 AGGKSRRMGGD---KALLELGgKPLLEHVLERL--KPLVDEVV----ISANRDQERYALLGVPVIpdEPPGKGPLAGILA 77

                         90       100       110
                 ....*....|....*....|....*....|.
gi 663530302  79 LLQKIDG-FVFVVSGDLPLLDEEIIQKLVEF 108
Cdd:cd02503   78 ALRAAPAdWVLVLACDMPFLPPELLERLLAA 108
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
 1-189 6.27e-05

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional


Pssm-ID: 237727 [Multi-domain]  Cd Length: 366  Bit Score: 42.43  E-value: 6.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530302   1 MAGGKGSRMEfpAPEKLLLEYE-KPIIFHVIDSLndshcfSKVFAATSLNspdtkrvleekgIETLDTQGNGYVNDLNFL 79
Cdd:PRK14489  11 LAGGLSRRMN--GRDKALILLGgKPLIERVVDRL------RPQFARIHLN------------INRDPARYQDLFPGLPVY 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530302  80 LQKIDGF------------------VFVVSGDLPLLDEEIIQKLVEFNSESVWT-SFLVSKEflnslGLESNLLVKHDS- 139
Cdd:PRK14489  71 PDILPGFqgplsgilaglehadseyLFVVACDTPFLPENLVKRLSKALAIEGADiAVPHDGE-----RAHPLFALYHRSc 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 663530302 140 ----TECVYTGISIINAdkikNLNLVNENYVILND-KRIAFNLNTNEDFELLNSP 189
Cdd:PRK14489 146 lpalRRYLAEGERRLFD----FFQRQRVRYVDLSTqKDAFFNVNTPEDLEQLRAI 196
 
Name Accession Description Interval E-value
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 1-187 3.79e-64

GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 195.49  E-value: 3.79e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530302   1 MAGGKGSRMEFPapEKLLLE-YEKPIIFHVIDSLNDShCFSKVFAATSLNSPDTKRVLEEKGIETLDTQGNGYVNDLNFL 79
Cdd:COG2266    1 MAGGKGTRLGGG--EKPLLEiCGKPMIDRVIDALEES-CIDKIYVAVSPNTPKTREYLKERGVEVIETPGEGYVEDLNEA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530302  80 LQKIDGFVFVVSGDLPLLDEEIIQKLVE--FNSESVWTSFLVSKEFLNSLGLESNLLVKHDStECVYTGISIINADKIKn 157
Cdd:COG2266   78 LESISGPVLVVPADLPLLTPEIIDDIIDayLESGKPSLTVVVPAALKRELGVSPDTTFEIDG-ELVPTGINIVDGSDGE- 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 663530302 158 lnlVNENYVILNDKRIAFNLNTNEDFELLN 187
Cdd:COG2266  156 ---QEETNLVLDDPRLALNVNTPEDLKLAE 182
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 1-107 2.36e-10

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 56.43  E-value: 2.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530302    1 MAGGKGSRMEFPapeKLLLEY-EKPIIFHVIDSLndSHCFSKVFAATslNSPDTKRVLEEKGIETL--DTQGNGYVNDLN 77
Cdd:pfam12804   4 LAGGRSSRMGGD---KALLPLgGKPLLERVLERL--RPAGDEVVVVA--NDEEVLAALAGLGVPVVpdPDPGQGPLAGLL 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 663530302   78 FLLQKIDG--FVFVVSGDLPLLDEEIIQKLVE 107
Cdd:pfam12804  77 AALRAAPGadAVLVLACDMPFLTPELLRRLLA 108
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 2-108 8.74e-10

MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 55.27  E-value: 8.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530302   2 AGGKGSRMEFPapeKLLLEYE-KPIIFHVIDSLndSHCFSKVFaatsLNSPDTKRVLEEKGIETL--DTQGNGYVNDLNF 78
Cdd:cd02503    7 AGGKSRRMGGD---KALLELGgKPLLEHVLERL--KPLVDEVV----ISANRDQERYALLGVPVIpdEPPGKGPLAGILA 77

                         90       100       110
                 ....*....|....*....|....*....|.
gi 663530302  79 LLQKIDG-FVFVVSGDLPLLDEEIIQKLVEF 108
Cdd:cd02503   78 ALRAAPAdWVLVLACDMPFLPPELLERLLAA 108
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 1-107 2.55e-09

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 54.10  E-value: 2.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530302   1 MAGGKGSRMEFPapeKLLLEYE-KPIIFHVIDSLNdSHCFSKVFAATSLNSPDTKRVLEEKGIETLdtqgngyVND---- 75
Cdd:cd04182    6 LAAGRSSRMGGN---KLLLPLDgKPLLRHALDAAL-AAGLSRVIVVLGAEADAVRAALAGLPVVVV-------INPdwee 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 663530302  76 ---------LNFLLQKIDGFVFVVsGDLPLLDEEIIQKLVE 107
Cdd:cd04182   75 gmssslaagLEALPADADAVLILL-ADQPLVTAETLRALID 114
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 23-134 4.47e-08

Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) 3-deoxy-manno-octulosonate cytidylyltransferase,, EC:2.7.7.38 catalysing the reaction:- CTP + 3-deoxy-D-manno-octulosonate <=> diphosphate + CMP-3-deoxy-D-manno-octulosonate, 2) acylneuraminate cytidylyltransferase EC:2.7.7.43,, catalysing the reaction:- CTP + N-acylneuraminate <=> diphosphate + CMP-N-acylneuraminate. NeuAc cytydilyltransferase of Mannheimia haemolytica has been characterized describing kinetics and regulation by substrate charge, energetic charge and amino-sugar demand.


Pssm-ID: 396773  Cd Length: 217  Bit Score: 51.18  E-value: 4.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530302   23 KPIIFHVIDSLNDSHCFSKVFAATSlnSPDTKRVLEEKGIETLDTQGN------GYVNDLNFLLQKIDGFVFVVSGDLPL 96
Cdd:pfam02348  24 KPLIHHVLEAALKSGAFEKVIVATD--SEEIADVAKEFGAGVVMTSGSlssgtdRFYEVVKAFLNDHDDIIVNIQGDNPL 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 663530302   97 LDEEIIQKLVE--FNSESVWTSFLVSKEFLNSLGLESNLL 134
Cdd:pfam02348 102 LQPEVILKAIEtlLNNGEPYMSTLVVPVGSAEEVLNANAL 141
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
 1-189 6.27e-05

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional


Pssm-ID: 237727 [Multi-domain]  Cd Length: 366  Bit Score: 42.43  E-value: 6.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530302   1 MAGGKGSRMEfpAPEKLLLEYE-KPIIFHVIDSLndshcfSKVFAATSLNspdtkrvleekgIETLDTQGNGYVNDLNFL 79
Cdd:PRK14489  11 LAGGLSRRMN--GRDKALILLGgKPLIERVVDRL------RPQFARIHLN------------INRDPARYQDLFPGLPVY 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530302  80 LQKIDGF------------------VFVVSGDLPLLDEEIIQKLVEFNSESVWT-SFLVSKEflnslGLESNLLVKHDS- 139
Cdd:PRK14489  71 PDILPGFqgplsgilaglehadseyLFVVACDTPFLPENLVKRLSKALAIEGADiAVPHDGE-----RAHPLFALYHRSc 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 663530302 140 ----TECVYTGISIINAdkikNLNLVNENYVILND-KRIAFNLNTNEDFELLNSP 189
Cdd:PRK14489 146 lpalRRYLAEGERRLFD----FFQRQRVRYVDLSTqKDAFFNVNTPEDLEQLRAI 196
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 1-107 7.89e-05

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 41.74  E-value: 7.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530302   1 MAGGKGSRMEFPAPeKLLLEY-EKPIIFHVIDSLNDSHCFSKV-----------FAATSLNSPDTKRVLEEKGIETLDTQ 68
Cdd:cd02516    6 LAAGSGSRMGADIP-KQFLELgGKPVLEHTLEAFLAHPAIDEIvvvvppddidlAKELAKYGLSKVVKIVEGGATRQDSV 84

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 663530302  69 GNGyvndLNFLLQKIDGFVFVVSGDLPLLDEEIIQKLVE 107
Cdd:cd02516   85 LNG----LKALPDADPDIVLIHDAARPFVSPELIDRLID 119
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-108 1.62e-04

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 41.36  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530302   1 MAGGKGSRMEFPAPEKLLLEYEKPIIFHVIDSLNDSHcFSKVFAATSLNSPDTKRVLEEKGIETLDTQ--GNGY-VNDLN 77
Cdd:PRK14354   8 LAAGKGTRMKSKLPKVLHKVCGKPMVEHVVDSVKKAG-IDKIVTVVGHGAEEVKEVLGDRSEFALQEEqlGTGHaVMQAE 86

                         90       100       110
                 ....*....|....*....|....*....|.
gi 663530302  78 FLLQKIDGFVFVVSGDLPLLDEEIIQKLVEF 108
Cdd:PRK14354  87 EFLADKEGTTLVICGDTPLITAETLKNLIDF 117
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1-108 1.70e-04

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 41.17  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530302   1 MAGGKGSRM--EFPapeKLLLEY-EKPIIFHVIDslndshcfskvfAATSLNSPDT-----------KRVLEEKGIETLD 66
Cdd:COG1207    8 LAAGKGTRMksKLP---KVLHPLaGKPMLEHVLD------------AARALGPDRIvvvvghgaeqvRAALADLDVEFVL 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 663530302  67 tQ----GNGY-VNDLNFLLQKIDGFVFVVSGDLPLLDEEIIQKLVEF 108
Cdd:COG1207   73 -QeeqlGTGHaVQQALPALPGDDGTVLVLYGDVPLIRAETLKALLAA 118
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-106 1.87e-04

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 41.25  E-value: 1.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530302   1 MAGGKGSRMEFPAPEKLLLEYEKPIIFHVIDSLnDSHCFSKVFAA---------TSLNSPDTKRVLEEKGIETldtqGNG 71
Cdd:PRK14356  11 LAAGKGTRMHSDKPKVLQTLLGEPMLRFVYRAL-RPLFGDNVWTVvghradmvrAAFPDEDARFVLQEQQLGT----GHA 85

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 663530302  72 YVNDLNFLLQKIDGFVFVVSGDLPLLDEEIIQKLV 106
Cdd:PRK14356  86 LQCAWPSLTAAGLDRVLVVNGDTPLVTTDTIDDFL 120
PRK13368 PRK13368
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 14-108 4.51e-04

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 184007  Cd Length: 238  Bit Score: 39.56  E-value: 4.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530302  14 PEKLLLE-YEKPIIFHVIDSLNDSHCFSKVFAATslNSPDTKRVLEEKGIETLDT--QGNGYVNDLNFLLQKIDG-FVFV 89
Cdd:PRK13368  17 PGKPLLDiLGKPMIQHVYERAAQAAGVEEVYVAT--DDQRIEDAVEAFGGKVVMTsdDHLSGTDRLAEVMLKIEAdIYIN 94

                         90
                 ....*....|....*....
gi 663530302  90 VSGDLPLLDEEIIQKLVEF 108
Cdd:PRK13368  95 VQGDEPMIRPRDIDTLIQP 113
 
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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