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Conserved domains on  [gi|45477098|sp|Q7VIA1|]
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RecName: Full=Guanylate kinase; AltName: Full=GMP kinase

Protein Classification

guanylate kinase( domain architecture ID 10799078)

guanylate kinase (GMP kinase) catalyzes the transfer of a phosphate group from ATP to guanosine monophosphate (GMP) to form guanosine diphosphate (GDP) and ADP

EC:  2.7.4.8
Gene Ontology:  GO:0004385|GO:0006163|GO:0005524

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
 6-184 6.13e-99

guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP kinase. This enzyme transfers a phosphate from ATP to GMP, yielding ADP and GDP. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


:

Pssm-ID: 213788  Cd Length: 179  Bit Score: 284.00  E-value: 6.13e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098     6 VLIISGPSGCGKSTLTKSLIESIPNVYFSISTTTRPMREGETDGVHYHFVSKEHFLQDIHNNVFLEWAEVHTNFYGTSLK 85
Cdd:TIGR03263   2 LIVISGPSGAGKSTLVKALLEEDPNLKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTPKS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098    86 PVQQALEQDKIVLFDVDVQGHHSIKEYFGDfAKSVFITTKNKDILRERLISRQTDDLQTIEFRLIQAHNEMQHIHNFDYL 165
Cdd:TIGR03263  82 PVEEALAAGKDVLLEIDVQGARQVKKKFPD-AVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADEFDYV 160

                         170
                  ....*....|....*....
gi 45477098   166 IINDDITTAKEAMVAIARS 184
Cdd:TIGR03263 161 IVNDDLEKAVEELKSIILA 179
 
Name Accession Description Interval E-value
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
 6-184 6.13e-99

guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP kinase. This enzyme transfers a phosphate from ATP to GMP, yielding ADP and GDP. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 213788  Cd Length: 179  Bit Score: 284.00  E-value: 6.13e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098     6 VLIISGPSGCGKSTLTKSLIESIPNVYFSISTTTRPMREGETDGVHYHFVSKEHFLQDIHNNVFLEWAEVHTNFYGTSLK 85
Cdd:TIGR03263   2 LIVISGPSGAGKSTLVKALLEEDPNLKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTPKS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098    86 PVQQALEQDKIVLFDVDVQGHHSIKEYFGDfAKSVFITTKNKDILRERLISRQTDDLQTIEFRLIQAHNEMQHIHNFDYL 165
Cdd:TIGR03263  82 PVEEALAAGKDVLLEIDVQGARQVKKKFPD-AVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADEFDYV 160

                         170
                  ....*....|....*....
gi 45477098   166 IINDDITTAKEAMVAIARS 184
Cdd:TIGR03263 161 IVNDDLEKAVEELKSIILA 179
gmk PRK00300
guanylate kinase; Provisional
 1-199 4.84e-95

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 275.04  E-value: 4.84e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098    1 MSKGAVLIISGPSGCGKSTLTKSLIESIPNVYFSISTTTRPMREGETDGVHYHFVSKEHFLQDIHNNVFLEWAEVHTNFY 80
Cdd:PRK00300   2 MRRGLLIVLSGPSGAGKSTLVKALLERDPNLQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGNYY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098   81 GTSLKPVQQALEQDKIVLFDVDVQGHHSIKEYFGDfAKSVFITTKNKDILRERLISRQTDDLQTIEFRLIQAHNEMQHIH 160
Cdd:PRK00300  82 GTPRSPVEEALAAGKDVLLEIDWQGARQVKKKMPD-AVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAHAS 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 45477098  161 NFDYLIINDDITTAKEAMVAIARS--LKY-QQIERLSKIIQK 199
Cdd:PRK00300 161 EYDYVIVNDDLDTALEELKAIIRAerLRRsRQQQRHAELIEE 202
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
3-184 1.11e-90

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 263.47  E-value: 1.11e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098   3 KGAVLIISGPSGCGKSTLTKSLIESIPNVYFSISTTTRPMREGETDGVHYHFVSKEHFLQDIHNNVFLEWAEVHTNFYGT 82
Cdd:COG0194   1 RGKLIVLSGPSGAGKTTLVKALLERDPDLRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYYGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098  83 SLKPVQQALEQDKIVLFDVDVQGHHSIKEYFGDfAKSVFITTKNKDILRERLISRQTDDLQTIEFRLIQAHNEMQHIHNF 162
Cdd:COG0194  81 PKAEVEEALAAGKDVLLEIDVQGARQVKKKFPD-AVSIFILPPSLEELERRLRGRGTDSEEVIERRLAKAREELAHADEF 159

                       170       180
                ....*....|....*....|..
gi 45477098 163 DYLIINDDITTAKEAMVAIARS 184
Cdd:COG0194 160 DYVVVNDDLDRAVEELKAIIRA 181
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 13-181 1.34e-54

Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions.


Pssm-ID: 214504 [Multi-domain]  Cd Length: 174  Bit Score: 171.32  E-value: 1.34e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098     13 SGCGKSTLTKSLIESIPNVY-FSISTTTRPMREGETDGVHYHFVSKEHFLQDIHNNVFLEWAEVHTNFYGTSLKPVQQAL 91
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFeRVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098     92 EQDKIVLFDVDVQGHHSIKE-YFgdFAKSVFITTKNKDILRERLISRQTDDLQTIEFRLIQAHNEMQHIHNFDYLIINDD 170
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKaQL--YPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEAQEYHLFDYVIVNDD 158

                          170
                   ....*....|.
gi 45477098    171 ITTAKEAMVAI 181
Cdd:smart00072 159 LEDAYEELKEI 169
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 6-174 1.72e-53

Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.


Pssm-ID: 238026  Cd Length: 137  Bit Score: 167.32  E-value: 1.72e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098   6 VLIISGPSGCGKSTLTKSLIES-IPNVYFSISTTTRPMREGETDGVHYHFVSKEHFLQDIHNNVFLEWAEVHTNFYGTSL 84
Cdd:cd00071   1 LIVLSGPSGVGKSTLLKRLLEEfDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098  85 KPVQQALEQDKIVLFDVDVQGHHSIKEYFGDfAKSVFITTKnkdilrerlisrqtddlqtiefrliqahnemqhihnfDY 164
Cdd:cd00071  81 AAVEEALAEGKIVILEIDVQGARQVKKSYPD-AVSIFILPP-------------------------------------DY 122

                       170
                ....*....|
gi 45477098 165 LIINDDITTA 174
Cdd:cd00071 123 VIVNDDLEKA 132
Guanylate_kin pfam00625
Guanylate kinase;
7-174 2.46e-48

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 156.00  E-value: 2.46e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098     7 LIISGPSGCGKSTLTKSLIESIPNVY-FSISTTTRPMREGETDGVHYHFVSKEHFLQDIHNNVFLEWAEVHTNFYGTSLK 85
Cdd:pfam00625   5 VVLSGPSGVGKSHIKKALLSEYPDKFgYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYGTSVE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098    86 PVQQALEQDKIVLFDVDVQGHHSIKEyfGDFA-KSVFITTKNKDILRERLISRQTDDLQTIEFRLIQAHNEMQHiHNFDY 164
Cdd:pfam00625  85 TIEQIHEQGKIVILDVDPQGVKQLRK--AELSpISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQH-YEFDV 161

                         170
                  ....*....|
gi 45477098   165 LIINDDITTA 174
Cdd:pfam00625 162 IIVNDDLEEA 171
 
Name Accession Description Interval E-value
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
 6-184 6.13e-99

guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP kinase. This enzyme transfers a phosphate from ATP to GMP, yielding ADP and GDP. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 213788  Cd Length: 179  Bit Score: 284.00  E-value: 6.13e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098     6 VLIISGPSGCGKSTLTKSLIESIPNVYFSISTTTRPMREGETDGVHYHFVSKEHFLQDIHNNVFLEWAEVHTNFYGTSLK 85
Cdd:TIGR03263   2 LIVISGPSGAGKSTLVKALLEEDPNLKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTPKS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098    86 PVQQALEQDKIVLFDVDVQGHHSIKEYFGDfAKSVFITTKNKDILRERLISRQTDDLQTIEFRLIQAHNEMQHIHNFDYL 165
Cdd:TIGR03263  82 PVEEALAAGKDVLLEIDVQGARQVKKKFPD-AVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADEFDYV 160

                         170
                  ....*....|....*....
gi 45477098   166 IINDDITTAKEAMVAIARS 184
Cdd:TIGR03263 161 IVNDDLEKAVEELKSIILA 179
gmk PRK00300
guanylate kinase; Provisional
 1-199 4.84e-95

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 275.04  E-value: 4.84e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098    1 MSKGAVLIISGPSGCGKSTLTKSLIESIPNVYFSISTTTRPMREGETDGVHYHFVSKEHFLQDIHNNVFLEWAEVHTNFY 80
Cdd:PRK00300   2 MRRGLLIVLSGPSGAGKSTLVKALLERDPNLQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGNYY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098   81 GTSLKPVQQALEQDKIVLFDVDVQGHHSIKEYFGDfAKSVFITTKNKDILRERLISRQTDDLQTIEFRLIQAHNEMQHIH 160
Cdd:PRK00300  82 GTPRSPVEEALAAGKDVLLEIDWQGARQVKKKMPD-AVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAHAS 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 45477098  161 NFDYLIINDDITTAKEAMVAIARS--LKY-QQIERLSKIIQK 199
Cdd:PRK00300 161 EYDYVIVNDDLDTALEELKAIIRAerLRRsRQQQRHAELIEE 202
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
3-184 1.11e-90

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 263.47  E-value: 1.11e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098   3 KGAVLIISGPSGCGKSTLTKSLIESIPNVYFSISTTTRPMREGETDGVHYHFVSKEHFLQDIHNNVFLEWAEVHTNFYGT 82
Cdd:COG0194   1 RGKLIVLSGPSGAGKTTLVKALLERDPDLRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYYGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098  83 SLKPVQQALEQDKIVLFDVDVQGHHSIKEYFGDfAKSVFITTKNKDILRERLISRQTDDLQTIEFRLIQAHNEMQHIHNF 162
Cdd:COG0194  81 PKAEVEEALAAGKDVLLEIDVQGARQVKKKFPD-AVSIFILPPSLEELERRLRGRGTDSEEVIERRLAKAREELAHADEF 159

                       170       180
                ....*....|....*....|..
gi 45477098 163 DYLIINDDITTAKEAMVAIARS 184
Cdd:COG0194 160 DYVVVNDDLDRAVEELKAIIRA 181
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 13-181 1.34e-54

Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions.


Pssm-ID: 214504 [Multi-domain]  Cd Length: 174  Bit Score: 171.32  E-value: 1.34e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098     13 SGCGKSTLTKSLIESIPNVY-FSISTTTRPMREGETDGVHYHFVSKEHFLQDIHNNVFLEWAEVHTNFYGTSLKPVQQAL 91
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFeRVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098     92 EQDKIVLFDVDVQGHHSIKE-YFgdFAKSVFITTKNKDILRERLISRQTDDLQTIEFRLIQAHNEMQHIHNFDYLIINDD 170
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKaQL--YPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEAQEYHLFDYVIVNDD 158

                          170
                   ....*....|.
gi 45477098    171 ITTAKEAMVAI 181
Cdd:smart00072 159 LEDAYEELKEI 169
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 6-174 1.72e-53

Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.


Pssm-ID: 238026  Cd Length: 137  Bit Score: 167.32  E-value: 1.72e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098   6 VLIISGPSGCGKSTLTKSLIES-IPNVYFSISTTTRPMREGETDGVHYHFVSKEHFLQDIHNNVFLEWAEVHTNFYGTSL 84
Cdd:cd00071   1 LIVLSGPSGVGKSTLLKRLLEEfDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098  85 KPVQQALEQDKIVLFDVDVQGHHSIKEYFGDfAKSVFITTKnkdilrerlisrqtddlqtiefrliqahnemqhihnfDY 164
Cdd:cd00071  81 AAVEEALAEGKIVILEIDVQGARQVKKSYPD-AVSIFILPP-------------------------------------DY 122

                       170
                ....*....|
gi 45477098 165 LIINDDITTA 174
Cdd:cd00071 123 VIVNDDLEKA 132
gmk PRK14738
guanylate kinase; Provisional
 7-168 4.16e-50

guanylate kinase; Provisional


Pssm-ID: 237809  Cd Length: 206  Bit Score: 161.05  E-value: 4.16e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098    7 LIISGPSGCGKSTLTKSLIESIPNVYFSISTTTRPMREGETDGVHYHFVSKEHFLQDIHNNVFLEWAEVHTNFYGTSLKP 86
Cdd:PRK14738  16 VVISGPSGVGKDAVLARMRERKLPFHFVVTATTRPKRPGEIDGVDYHFVTPEEFREMISQNELLEWAEVYGNYYGVPKAP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098   87 VQQALEQDKIVLFDVDVQGHHSIKEYFGDfAKSVFITTKNKDILRERLISRQTDDLQTIEFRLIQAHNEMQHIHNFDYLI 166
Cdd:PRK14738  96 VRQALASGRDVIVKVDVQGAASIKRLVPE-AVFIFLAPPSMDELTRRLELRRTESPEELERRLATAPLELEQLPEFDYVV 174


                 ..
gi 45477098  167 IN 168
Cdd:PRK14738 175 VN 176
gmk PRK14737
guanylate kinase; Provisional
 1-181 1.32e-48

guanylate kinase; Provisional


Pssm-ID: 173199  Cd Length: 186  Bit Score: 156.69  E-value: 1.32e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098    1 MSKGAVLIISGPSGCGKSTLTKSLIESIPNVYFSISTTTRPMREGETDGVHYHFVSKEHFLQDIHNNVFLEWAEVHTNFY 80
Cdd:PRK14737   1 KASPKLFIISSVAGGGKSTIIQALLEEHPDFLFSISCTTRAPRPGDEEGKTYFFLTIEEFKKGIADGEFLEWAEVHDNYY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098   81 GTSLKPVQQALEQDKIVLFDVDVQGHHSIKEYFGDFAKSVFITTKNKDILRERLISRQTDDLQTIEFRLIQAHNEMQHIH 160
Cdd:PRK14737  81 GTPKAFIEDAFKEGRSAIMDIDVQGAKIIKEKFPERIVTIFIEPPSEEEWEERLIHRGTDSEESIEKRIENGIIELDEAN 160

                        170       180
                 ....*....|....*....|.
gi 45477098  161 NFDYLIINDDITTAKEAMVAI 181
Cdd:PRK14737 161 EFDYKIINDDLEDAIADLEAI 181
Guanylate_kin pfam00625
Guanylate kinase;
7-174 2.46e-48

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 156.00  E-value: 2.46e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098     7 LIISGPSGCGKSTLTKSLIESIPNVY-FSISTTTRPMREGETDGVHYHFVSKEHFLQDIHNNVFLEWAEVHTNFYGTSLK 85
Cdd:pfam00625   5 VVLSGPSGVGKSHIKKALLSEYPDKFgYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYGTSVE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098    86 PVQQALEQDKIVLFDVDVQGHHSIKEyfGDFA-KSVFITTKNKDILRERLISRQTDDLQTIEFRLIQAHNEMQHiHNFDY 164
Cdd:pfam00625  85 TIEQIHEQGKIVILDVDPQGVKQLRK--AELSpISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQH-YEFDV 161

                         170
                  ....*....|
gi 45477098   165 LIINDDITTA 174
Cdd:pfam00625 162 IIVNDDLEEA 171
PLN02772 PLN02772
guanylate kinase
 7-171 7.78e-35

guanylate kinase


Pssm-ID: 215414 [Multi-domain]  Cd Length: 398  Bit Score: 126.88  E-value: 7.78e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098    7 LIISGPSGCGKSTLTKSLIESIPNVY-FSISTTTRPMREGETDGVHYHFVSKEHFLQDIHNNVFLEWAEVHTNFYGTSLK 85
Cdd:PLN02772 138 IVISGPSGVGKGTLISMLMKEFPSMFgFSVSHTTRAPREMEKDGVHYHFTERSVMEKEIKDGKFLEFASVHGNLYGTSIE 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098   86 PVQQALEQDKIVLFDVDVQGHHSIKEYFGDfAKSVFITTKNKDILRERLISRQTDDLQTIEFRLIQAHNEMQHIHN---F 162
Cdd:PLN02772 218 AVEVVTDSGKRCILDIDVQGARSVRASSLE-AIFIFICPPSMEELEKRLRARGTETEEQIQKRLRNAEAELEQGKSsgiF 296


                 ....*....
gi 45477098  163 DYLIINDDI 171
Cdd:PLN02772 297 DHILYNDNL 305
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 3-25 4.69e-04

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 39.58  E-value: 4.69e-04
                        10        20
                ....*....|....*....|...
gi 45477098   3 KGAVLIISGPSGCGKSTLTKSLI 25
Cdd:COG1127  30 RGEILAIIGGSGSGKSVLLKLII 52
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 3-31 5.13e-04

ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 39.63  E-value: 5.13e-04
                        10        20        30
                ....*....|....*....|....*....|..
gi 45477098   3 KGAVLIISGPSGCGKSTLTKSL---IESIPNV 31
Cdd:COG1117  36 ENKVTALIGPSGCGKSTLLRCLnrmNDLIPGA 67
AAA_18 pfam13238
AAA domain;
8-152 5.21e-04

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 38.56  E-value: 5.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098     8 IISGPSGCGKSTLTKSLIESIPNVYFSIST-TTRPMREGETDGVHYHFVSKEHFLQDIHNNvFLEWAevhtnfygtslkp 86
Cdd:pfam13238   2 LITGTPGVGKTTLAKELSKRLGFGDNVRDLaLENGLVLGDDPETRESKRLDEDKLDRLLDL-LEENA------------- 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45477098    87 vqqALEQDKIVLFDvdvqGHHSIKEYFGDF-AKSVFITTkNKDILRERLISRQTDDLQTIEFRLIQA 152
Cdd:pfam13238  68 ---ALEEGGNLIID----GHLAELEPERAKdLVGIVLRA-SPEELLERLEKRGYEEAKIKENEEAEI 126
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 1-30 1.11e-03

Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 38.28  E-value: 1.11e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 45477098   1 MSKGAVLI-ISGPSGCGKSTLTKSLIESIPN 30
Cdd:COG0572   3 RSGKPRIIgIAGPSGSGKTTFARRLAEQLGA 33
PRK10078 PRK10078
ribose 1,5-bisphosphokinase; Provisional
 11-170 1.36e-03

ribose 1,5-bisphosphokinase; Provisional


Pssm-ID: 236648  Cd Length: 186  Bit Score: 38.19  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098   11 GPSGCGKSTLTKSL-IESIPNVYFSISTTTRPMREGETDGVHyhfVSKEHFLQDIHNNVF-LEWaEVHTNFYGTSLKpVQ 88
Cdd:PRK10078   9 GPSGSGKDSLLAALrQREQTQLLVAHRYITRPASAGSENHIA---LSEQEFFTRAGQNLFaLSW-HANGLYYGVGIE-ID 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098   89 QALEQDkivlFDVDVQGHHS----IKEYFGDFAKSVFITTkNKDILRERLISRQTDDLQTIEFRLIQAhnemQHIHNFDY 164
Cdd:PRK10078  84 LWLHAG----FDVLVNGSRAhlpqARARYQSALLPVCLQV-SPEILRQRLENRGRENASEINARLARA----ARYQPQDC 154


                 ....*.
gi 45477098  165 LIINDD 170
Cdd:PRK10078 155 HTLNND 160
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 3-25 1.61e-03

ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 38.25  E-value: 1.61e-03
                        10        20
                ....*....|....*....|...
gi 45477098   3 KGAVLIISGPSGCGKSTLTKSLI 25
Cdd:cd03261  25 RGEILAIIGPSGSGKSTLLRLIV 47
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 3-150 1.68e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 37.35  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45477098      3 KGAVLIISGPSGCGKSTLTKSLIESIP---NVYFSISTTTRPMREGETDGVHYHFVSKEHFLQDIHNNVFLEWAEVHTNF 79
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGppgGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45477098     80 ------YGTSLKPVQQALEQDKIVLFDVDVQGHHSikeyfgdfAKSVFITTKNKDILRERLISRQTDDLqtIEFRLI 150
Cdd:smart00382  81 vlildeITSLLDAEQEALLLLLEELRLLLLLKSEK--------NLTVILTTNDEKDLGPALLRRRFDRR--IVLLLI 147
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 2-20 1.88e-03

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 37.85  E-value: 1.88e-03
                        10
                ....*....|....*....
gi 45477098   2 SKGAVLIISGPSGCGKSTL 20
Cdd:COG4136  25 APGEILTLMGPSGSGKSTL 43
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
3-24 2.17e-03

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 37.49  E-value: 2.17e-03
                        10        20
                ....*....|....*....|..
gi 45477098   3 KGAVLIISGPSGCGKSTLTKSL 24
Cdd:COG4619  25 AGECVAITGPSGSGKSTLLRAL 46
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 7-28 2.25e-03

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


Pssm-ID: 459992  Cd Length: 102  Bit Score: 36.04  E-value: 2.25e-03
                          10        20
                  ....*....|....*....|..
gi 45477098     7 LIISGPSGCGKSTLTKSLIESI 28
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARAL 22
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 1-20 3.00e-03

ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 37.08  E-value: 3.00e-03
                        10        20
                ....*....|....*....|
gi 45477098   1 MSKGAVLIISGPSGCGKSTL 20
Cdd:cd03255  27 IEKGEFVAIVGPSGSGKSTL 46
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 3-25 3.18e-03

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 37.10  E-value: 3.18e-03
                        10        20
                ....*....|....*....|...
gi 45477098   3 KGAVLIISGPSGCGKSTLTKSLI 25
Cdd:cd03257  30 KGETLGLVGESGSGKSTLARAIL 52
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
6-35 3.23e-03

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 36.81  E-value: 3.23e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 45477098   6 VLIISGPSGCGKSTLTKSLIESIPNVYFSI 35
Cdd:COG0645   1 LILVCGLPGSGKSTLARALAERLGAVRLRS 30
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
3-20 3.39e-03

ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 36.95  E-value: 3.39e-03
                        10
                ....*....|....*...
gi 45477098   3 KGAVLIISGPSGCGKSTL 20
Cdd:COG1136  33 AGEFVAIVGPSGSGKSTL 50
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 1-66 3.41e-03

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 37.07  E-value: 3.41e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45477098   1 MSKGAVLIISGPSGCGKSTLTKSLIESIP--NVYFSISTTTRPMRE-----GETDGVHYHFVSKEHFLQDIHN 66
Cdd:COG3267  40 AQGGGFVVLTGEVGTGKTTLLRRLLERLPddVKVAYIPNPQLSPAEllraiADELGLEPKGASKADLLRQLQE 112
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 3-31 4.13e-03

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).


Pssm-ID: 213227 [Multi-domain]  Cd Length: 227  Bit Score: 36.78  E-value: 4.13e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 45477098   3 KGAVLIISGPSGCGKSTLTKS---LIESIPNV 31
Cdd:cd03260  25 KGEITALIGPSGCGKSTLLRLlnrLNDLIPGA 56
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 4-25 5.62e-03

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 36.04  E-value: 5.62e-03
                        10        20
                ....*....|....*....|..
gi 45477098   4 GAVLIISGPSGCGKSTLTKSLI 25
Cdd:cd03246  28 GESLAIIGPSGSGKSTLARLIL 49
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 1-24 6.04e-03

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 35.70  E-value: 6.04e-03
                          10        20
                  ....*....|....*....|....
gi 45477098     1 MSKGAVLIISGPSGCGKSTLTKSL 24
Cdd:pfam00005   8 LNPGEILALVGPNGAGKSTLLKLI 31
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
 6-30 7.60e-03

Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide adenine dinucleotide (NAD+). This enzyme catalyzes the phosphorylation of nicotinamide riboside (NR) to form nicotinamide mononucleotide (NMN). It defines the NR salvage pathway of NAD+ biosynthesis in addition to the pathways through nicotinic acid mononucleotide (NaMN). This enzyme can also phosphorylate the anticancer drug tiazofurin, which is an analog of nicotinamide riboside.


Pssm-ID: 238982 [Multi-domain]  Cd Length: 187  Bit Score: 35.76  E-value: 7.60e-03
                        10        20
                ....*....|....*....|....*
gi 45477098   6 VLIISGPSGCGKSTLTKSLIESIPN 30
Cdd:cd02024   1 IVGISGVTNSGKTTLAKLLQRILPN 25
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 1-26 8.10e-03

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 35.85  E-value: 8.10e-03
                         10        20
                 ....*....|....*....|....*....
gi 45477098    1 MSKGAVLIISGPSGCGKSTLTK---SLIE 26
Cdd:PRK10247  30 LRAGEFKLITGPSGCGKSTLLKivaSLIS 58
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 3-20 8.54e-03

ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 36.20  E-value: 8.54e-03
                        10
                ....*....|....*...
gi 45477098   3 KGAVLIISGPSGCGKSTL 20
Cdd:COG3839  28 DGEFLVLLGPSGCGKSTL 45
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 7-58 9.35e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 35.20  E-value: 9.35e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 45477098   7 LIISGPSGCGKSTLTKSLIESI-----PNVYFSISTTTRPMREGETDGVHYHFVSKE 58
Cdd:cd00009  22 LLLYGPPGTGKTTLARAIANELfrpgaPFLYLNASDLLEGLVVAELFGHFLVRLLFE 78
PTZ00202 PTZ00202
tuzin; Provisional
 6-43 9.68e-03

tuzin; Provisional


Pssm-ID: 240312  Cd Length: 550  Bit Score: 36.30  E-value: 9.68e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 45477098    6 VLIISGPSGCGKSTLTKSLI--ESIPNVYFSISTTTRPMR 43
Cdd:PTZ00202 288 IVVFTGFRGCGKSSLCRSAVrkEGMPAVFVDVRGTEDTLR 327
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 3-24 9.86e-03

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 35.30  E-value: 9.86e-03
                        10        20
                ....*....|....*....|..
gi 45477098   3 KGAVLIISGPSGCGKSTLTKSL 24
Cdd:cd00267  24 AGEIVALVGPNGSGKSTLLRAI 45
 
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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