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Conserved domains on  [gi|21356141|ref|NP_648408|]
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uncharacterized protein Dmel_CG11811 [Drosophila melanogaster]

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

 Zoom to residue level

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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 ...
 36-216 2.10e-78

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: 233.54  E-value: 2.10e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141    36 RPLVLCGPSGSGKSTLLKRLFAEFPStFGFSISHTTRKPREGEEHGVHYYFVERPEMEAAIAGDEFIETAEFTGNLYGTS 115
Cdd:TIGR03263   1 LLIVISGPSGAGKSTLVKALLEEDPN-LKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141   116 KAAVREIQAQGRVCILDIEQKGVEQIKRTDLNPILIFNNPPSIKELERRLRKRGSETEESLSKRLNAAQVELDYGltpGN 195
Cdd:TIGR03263  80 KSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHA---DE 156

                         170       180
                  ....*....|....*....|.
gi 21356141   196 FHKIINNVDIDVAYEEFRNFV 216
Cdd:TIGR03263 157 FDYVIVNDDLEKAVEELKSII 177
 
Name Accession Description Interval E-value
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
 36-216 2.10e-78

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: 233.54  E-value: 2.10e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141    36 RPLVLCGPSGSGKSTLLKRLFAEFPStFGFSISHTTRKPREGEEHGVHYYFVERPEMEAAIAGDEFIETAEFTGNLYGTS 115
Cdd:TIGR03263   1 LLIVISGPSGAGKSTLVKALLEEDPN-LKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141   116 KAAVREIQAQGRVCILDIEQKGVEQIKRTDLNPILIFNNPPSIKELERRLRKRGSETEESLSKRLNAAQVELDYGltpGN 195
Cdd:TIGR03263  80 KSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHA---DE 156

                         170       180
                  ....*....|....*....|.
gi 21356141   196 FHKIINNVDIDVAYEEFRNFV 216
Cdd:TIGR03263 157 FDYVIVNDDLEKAVEELKSII 177
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
38-226 1.80e-73

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 221.10  E-value: 1.80e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141  38 LVLCGPSGSGKSTLLKRLFAEFPStFGFSISHTTRKPREGEEHGVHYYFVERPEMEAAIAGDEFIETAEFTGNLYGTSKA 117
Cdd:COG0194   5 IVLSGPSGAGKTTLVKALLERDPD-LRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYYGTPKA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141 118 AVREIQAQGRVCILDIEQKGVEQIKRTDLNPILIFNNPPSIKELERRLRKRGSETEESLSKRLNAAQVELDYgltPGNFH 197
Cdd:COG0194  84 EVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRGRGTDSEEVIERRLAKAREELAH---ADEFD 160

                       170       180
                ....*....|....*....|....*....
gi 21356141 198 KIINNVDIDVAYEEFRNFVVQELKEQQKQ 226
Cdd:COG0194 161 YVVVNDDLDRAVEELKAIIRAERLRRERQ 189
gmk PRK00300
guanylate kinase; Provisional
 38-226 3.33e-71

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 216.11  E-value: 3.33e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141   38 LVLCGPSGSGKSTLLKRLFAEFPStFGFSISHTTRKPREGEEHGVHYYFVERPEMEAAIAGDEFIETAEFTGNLYGTSKA 117
Cdd:PRK00300   8 IVLSGPSGAGKSTLVKALLERDPN-LQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGNYYGTPRS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141  118 AVREIQAQGRVCILDIEQKGVEQIKRTDLNPILIFNNPPSIKELERRLRKRGSETEESLSKRLNAAQVEL------DYgl 191
Cdd:PRK00300  87 PVEEALAAGKDVLLEIDWQGARQVKKKMPDAVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIahaseyDY-- 164

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 21356141  192 tpgnfhkIINNVDIDVAYEEFRNFVVQELKEQQKQ 226
Cdd:PRK00300 165 -------VIVNDDLDTALEELKAIIRAERLRRSRQ 192
Guanylate_kin pfam00625
Guanylate kinase;
34-219 1.48e-70

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 213.78  E-value: 1.48e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141    34 GPRPLVLCGPSGSGKSTLLKRLFAEFPSTFGFSISHTTRKPREGEEHGVHYYFVERPEMEAAIAGDEFIETAEFTGNLYG 113
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141   114 TSKAAVREIQAQGRVCILDIEQKGVEQIKRTDLNPILIFNNPPSIKELERRLRKRGSETEESLSKRLNAAQVELDYgltp 193
Cdd:pfam00625  81 TSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQH---- 156

                         170       180
                  ....*....|....*....|....*.
gi 21356141   194 GNFHKIINNVDIDVAYEEFRNFVVQE 219
Cdd:pfam00625 157 YEFDVIIVNDDLEEAYKKLKEALEAE 182
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 37-213 9.23e-66

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: 199.68  E-value: 9.23e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141  37 PLVLCGPSGSGKSTLLKRLFAEFPSTFGFSISHTTRKPREGEEHGVHYYFVERPEMEAAIAGDEFIETAEFTGNLYGTSK 116
Cdd:cd00071   1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141 117 AAVREIQAQGRVCILDIEQKGVEQIKRTDLNPILIFNNPPsikelerrlrkrgseteeslskrlnaaqvelDYgltpgnf 196
Cdd:cd00071  81 AAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP-------------------------------DY------- 122

                       170
                ....*....|....*..
gi 21356141 197 hkIINNVDIDVAYEEFR 213
Cdd:cd00071 123 --VIVNDDLEKAYEELK 137
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 44-219 5.84e-65

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: 199.06  E-value: 5.84e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141     44 SGSGKSTLLKRLFAEFPSTFGFSISHTTRKPREGEEHGVHYYFVERPEMEAAIAGDEFIETAEFTGNLYGTSKAAVREIQ 123
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141    124 AQGRVCILDIEQKGVEQIKRTDLNPILIFNNPPSIKELERRLRKRGSETEESLSKRLNAAQVELDYgltPGNFHKIINNV 203
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEAQE---YHLFDYVIVND 157

                          170
                   ....*....|....*.
gi 21356141    204 DIDVAYEEFRNFVVQE 219
Cdd:smart00072 158 DLEDAYEELKEILEAE 173
 
Name Accession Description Interval E-value
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
 36-216 2.10e-78

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: 233.54  E-value: 2.10e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141    36 RPLVLCGPSGSGKSTLLKRLFAEFPStFGFSISHTTRKPREGEEHGVHYYFVERPEMEAAIAGDEFIETAEFTGNLYGTS 115
Cdd:TIGR03263   1 LLIVISGPSGAGKSTLVKALLEEDPN-LKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141   116 KAAVREIQAQGRVCILDIEQKGVEQIKRTDLNPILIFNNPPSIKELERRLRKRGSETEESLSKRLNAAQVELDYGltpGN 195
Cdd:TIGR03263  80 KSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHA---DE 156

                         170       180
                  ....*....|....*....|.
gi 21356141   196 FHKIINNVDIDVAYEEFRNFV 216
Cdd:TIGR03263 157 FDYVIVNDDLEKAVEELKSII 177
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
38-226 1.80e-73

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 221.10  E-value: 1.80e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141  38 LVLCGPSGSGKSTLLKRLFAEFPStFGFSISHTTRKPREGEEHGVHYYFVERPEMEAAIAGDEFIETAEFTGNLYGTSKA 117
Cdd:COG0194   5 IVLSGPSGAGKTTLVKALLERDPD-LRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYYGTPKA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141 118 AVREIQAQGRVCILDIEQKGVEQIKRTDLNPILIFNNPPSIKELERRLRKRGSETEESLSKRLNAAQVELDYgltPGNFH 197
Cdd:COG0194  84 EVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRGRGTDSEEVIERRLAKAREELAH---ADEFD 160

                       170       180
                ....*....|....*....|....*....
gi 21356141 198 KIINNVDIDVAYEEFRNFVVQELKEQQKQ 226
Cdd:COG0194 161 YVVVNDDLDRAVEELKAIIRAERLRRERQ 189
gmk PRK00300
guanylate kinase; Provisional
 38-226 3.33e-71

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 216.11  E-value: 3.33e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141   38 LVLCGPSGSGKSTLLKRLFAEFPStFGFSISHTTRKPREGEEHGVHYYFVERPEMEAAIAGDEFIETAEFTGNLYGTSKA 117
Cdd:PRK00300   8 IVLSGPSGAGKSTLVKALLERDPN-LQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGNYYGTPRS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141  118 AVREIQAQGRVCILDIEQKGVEQIKRTDLNPILIFNNPPSIKELERRLRKRGSETEESLSKRLNAAQVEL------DYgl 191
Cdd:PRK00300  87 PVEEALAAGKDVLLEIDWQGARQVKKKMPDAVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIahaseyDY-- 164

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 21356141  192 tpgnfhkIINNVDIDVAYEEFRNFVVQELKEQQKQ 226
Cdd:PRK00300 165 -------VIVNDDLDTALEELKAIIRAERLRRSRQ 192
Guanylate_kin pfam00625
Guanylate kinase;
34-219 1.48e-70

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 213.78  E-value: 1.48e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141    34 GPRPLVLCGPSGSGKSTLLKRLFAEFPSTFGFSISHTTRKPREGEEHGVHYYFVERPEMEAAIAGDEFIETAEFTGNLYG 113
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141   114 TSKAAVREIQAQGRVCILDIEQKGVEQIKRTDLNPILIFNNPPSIKELERRLRKRGSETEESLSKRLNAAQVELDYgltp 193
Cdd:pfam00625  81 TSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQH---- 156

                         170       180
                  ....*....|....*....|....*.
gi 21356141   194 GNFHKIINNVDIDVAYEEFRNFVVQE 219
Cdd:pfam00625 157 YEFDVIIVNDDLEEAYKKLKEALEAE 182
PLN02772 PLN02772
guanylate kinase
 27-214 5.85e-66

guanylate kinase


Pssm-ID: 215414 [Multi-domain]  Cd Length: 398  Bit Score: 208.92  E-value: 5.85e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141   27 SKKMTAPGPRPLVLCGPSGSGKSTLLKRLFAEFPSTFGFSISHTTRKPREGEEHGVHYYFVERPEMEAAIAGDEFIETAE 106
Cdd:PLN02772 127 SKGVRGNAEKPIVISGPSGVGKGTLISMLMKEFPSMFGFSVSHTTRAPREMEKDGVHYHFTERSVMEKEIKDGKFLEFAS 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141  107 FTGNLYGTSKAAVREIQAQGRVCILDIEQKGVEQIKRTDLNPILIFNNPPSIKELERRLRKRGSETEESLSKRLNAAQVE 186
Cdd:PLN02772 207 VHGNLYGTSIEAVEVVTDSGKRCILDIDVQGARSVRASSLEAIFIFICPPSMEELEKRLRARGTETEEQIQKRLRNAEAE 286

                        170       180
                 ....*....|....*....|....*...
gi 21356141  187 LDYGLTPGNFHKIINNVDIDVAYEEFRN 214
Cdd:PLN02772 287 LEQGKSSGIFDHILYNDNLEECYKNLKK 314
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 37-213 9.23e-66

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: 199.68  E-value: 9.23e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141  37 PLVLCGPSGSGKSTLLKRLFAEFPSTFGFSISHTTRKPREGEEHGVHYYFVERPEMEAAIAGDEFIETAEFTGNLYGTSK 116
Cdd:cd00071   1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141 117 AAVREIQAQGRVCILDIEQKGVEQIKRTDLNPILIFNNPPsikelerrlrkrgseteeslskrlnaaqvelDYgltpgnf 196
Cdd:cd00071  81 AAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP-------------------------------DY------- 122

                       170
                ....*....|....*..
gi 21356141 197 hkIINNVDIDVAYEEFR 213
Cdd:cd00071 123 --VIVNDDLEKAYEELK 137
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 44-219 5.84e-65

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: 199.06  E-value: 5.84e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141     44 SGSGKSTLLKRLFAEFPSTFGFSISHTTRKPREGEEHGVHYYFVERPEMEAAIAGDEFIETAEFTGNLYGTSKAAVREIQ 123
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141    124 AQGRVCILDIEQKGVEQIKRTDLNPILIFNNPPSIKELERRLRKRGSETEESLSKRLNAAQVELDYgltPGNFHKIINNV 203
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEAQE---YHLFDYVIVND 157

                          170
                   ....*....|....*.
gi 21356141    204 DIDVAYEEFRNFVVQE 219
Cdd:smart00072 158 DLEDAYEELKEILEAE 173
gmk PRK14738
guanylate kinase; Provisional
 31-187 8.66e-42

guanylate kinase; Provisional


Pssm-ID: 237809  Cd Length: 206  Bit Score: 141.02  E-value: 8.66e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141   31 TAPGPRPLVLCGPSGSGKSTLLKRLfAEFPSTFGFSISHTTRKPREGEEHGVHYYFVERPEMEAAIAGDEFIETAEFTGN 110
Cdd:PRK14738   9 KPAKPLLVVISGPSGVGKDAVLARM-RERKLPFHFVVTATTRPKRPGEIDGVDYHFVTPEEFREMISQNELLEWAEVYGN 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21356141  111 LYGTSKAAVREIQAQGRVCILDIEQKGVEQIKRTDLNPILIFNNPPSIKELERRLRKRGSETEESLSKRLNAAQVEL 187
Cdd:PRK14738  88 YYGVPKAPVRQALASGRDVIVKVDVQGAASIKRLVPEAVFIFLAPPSMDELTRRLELRRTESPEELERRLATAPLEL 164
gmk PRK14737
guanylate kinase; Provisional
 35-202 1.67e-38

guanylate kinase; Provisional


Pssm-ID: 173199  Cd Length: 186  Bit Score: 132.04  E-value: 1.67e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141   35 PRPLVLCGPSGSGKSTLLKRLFAEFPStFGFSISHTTRKPREGEEHGVHYYFVERPEMEAAIAGDEFIETAEFTGNLYGT 114
Cdd:PRK14737   4 PKLFIISSVAGGGKSTIIQALLEEHPD-FLFSISCTTRAPRPGDEEGKTYFFLTIEEFKKGIADGEFLEWAEVHDNYYGT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141  115 SKAAVREIQAQGRVCILDIEQKGVEQIKrtDLNP---ILIFNNPPSIKELERRLRKRGSETEESLSKRLNAAQVELDYgl 191
Cdd:PRK14737  83 PKAFIEDAFKEGRSAIMDIDVQGAKIIK--EKFPeriVTIFIEPPSEEEWEERLIHRGTDSEESIEKRIENGIIELDE-- 158

                        170
                 ....*....|.
gi 21356141  192 TPGNFHKIINN 202
Cdd:PRK14737 159 ANEFDYKIIND 169
PhnN COG3709
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
30-213 1.21e-10

Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];


Pssm-ID: 442923  Cd Length: 188  Bit Score: 58.67  E-value: 1.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141  30 MTAPGPrpLV-LCGPSGSGKSTLLKRLFAEFPSTFGFSISH--TTRKPR-EGEEHgvhyYFVERPEMEAAIAGDEFIETA 105
Cdd:COG3709   1 MSGPGR--LIyVVGPSGAGKDSLLAAARARLAADPRLVFARryITRPADaGGEDH----DALSEAEFARRAAAGAFALHW 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141 106 EFTGNLYGTSkAAVREIQAQGRVCILDIEQKGVEQIKR--TDLNPILIfNNPPSIkeLERRLRKRGSETEESLSKRLNAA 183
Cdd:COG3709  75 QAHGLRYGIP-AEIDAWLAAGRDVVVNGSRAVLPQARAryPRLLVVLI-TASPEV--LAQRLAARGRESAEEIEARLARA 150

                       170       180       190
                ....*....|....*....|....*....|
gi 21356141 184 QvelDYGLTPGNFHKIINNVDIDVAYEEFR 213
Cdd:COG3709 151 A---EFLPDGPDVLVIDNDGPLEDAGARLL 177
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 38-169 3.53e-07

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 48.07  E-value: 3.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141    38 LVLCGPSGSGKSTLLKRLFAEFPstfgfsishttrkpregeehgvhYYFVERPEMEAAIAGDEFI---ETAEFTGNLYGT 114
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELG-----------------------AVRLSSDDERKRLFGEGRPsisYYTDATDRTYER 58

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21356141   115 SKAAVREIQAQGRVCILDI------EQKGVEQIKRTDLNPILIFNNPPSIKELERRLRKRG 169
Cdd:pfam13671  59 LHELARIALRAGRPVILDAtnlrrdERARLLALAREYGVPVRIVVFEAPEEVLRERLAARA 119
COG4639 COG4639
Predicted kinase [General function prediction only];
39-60 1.18e-05

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 43.66  E-value: 1.18e-05
                        10        20
                ....*....|....*....|..
gi 21356141  39 VLCGPSGSGKSTLLKRLFAEFP 60
Cdd:COG4639   6 VLIGLPGSGKSTFARRLFAPTE 27
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
40-73 4.28e-05

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 43.12  E-value: 4.28e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 21356141  40 LCGPSGSGKSTLLKRLFAEFPST------FGFSISHTTRK 73
Cdd:COG2884  33 LTGPSGAGKSTLLKLLYGEERPTsgqvlvNGQDLSRLKRR 72
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
38-175 5.33e-05

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 42.21  E-value: 5.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141  38 LVLCGPSGSGKSTLLKRLfaefpstfgfsishttrkpreGEEHGVHYYfveRP-EMEAAIAGDEFIE---TAEFTGNLYG 113
Cdd:COG0645   2 ILVCGLPGSGKSTLARAL---------------------AERLGAVRL---RSdVVRKRLFGAGLAPlerSPEATARTYA 57

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141 114 TSKAAVREIQAQGRVCILD-------IEQKGVEQIKRTDLNPILIF-NNPPSikELERRLRKRGSETEES 175
Cdd:COG0645  58 RLLALARELLAAGRSVILDatflrraQREAFRALAEEAGAPFVLIWlDAPEE--VLRERLEARNAEGGDS 125
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 38-53 2.52e-04

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 41.13  E-value: 2.52e-04
                        10
                ....*....|....*.
gi 21356141  38 LVLCGPSGSGKSTLLK 53
Cdd:COG1126  30 VVIIGPSGSGKSTLLR 45
AAA_22 pfam13401
AAA domain;
34-60 2.61e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 39.63  E-value: 2.61e-04
                          10        20
                  ....*....|....*....|....*..
gi 21356141    34 GPRPLVLCGPSGSGKSTLLKRLFAEFP 60
Cdd:pfam13401   4 GAGILVLTGESGTGKTTLLRRLLEQLP 30
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 39-167 3.27e-04

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 40.13  E-value: 3.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141  39 VLCGPSGSGKSTLLKRLFAEFPSTFGfSISHTTRKPREG----EEHGVHYYFVERPEMEAAIAGDEFIETAEFtgnlYGT 114
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVGEVS-DVPGTTRDPDVYvkelDKGKVKLVLVDTPGLDEFGGLGREELARLL----LRG 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21356141 115 SKAAVREIQAQGRVCILDIEQKGVEQIKRTDLNPILIFN-----NPPSIKELERRLRK 167
Cdd:cd00882  76 ADLILLVVDSTDRESEEDAKLLILRRLRKEGIPIILVGNkidllEEREVEELLRLEEL 133
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 35-93 4.04e-04

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: 39.66  E-value: 4.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 21356141     35 PRPLVLCGPSGSGKSTLLKRLFAEFPSTFGFSISHTTRKPREGEEHGVHYYFVERPEME 93
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS 60
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
36-131 4.26e-04

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 40.94  E-value: 4.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141  36 RPLVLCGPSGSGKSTLLKRLFAEFPSTfgfSISHTTRKPregeehgvhyYFVERPEMEAAIAGDEFIEtaEFTGNLYGTS 115
Cdd:COG5635 181 KRLLILGEPGSGKTTLLRYLALELAER---YLDAEDPIP----------ILIELRDLAEEASLEDLLA--EALEKRGGEP 245

                        90
                ....*....|....*.
gi 21356141 116 KAAVREIQAQGRVCIL 131
Cdd:COG5635 246 EDALERLLRNGRLLLL 261
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
38-53 7.98e-04

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 39.41  E-value: 7.98e-04
                        10
                ....*....|....*.
gi 21356141  38 LVLCGPSGSGKSTLLK 53
Cdd:COG4619  29 VAITGPSGSGKSTLLR 44
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 30-60 1.26e-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: 38.67  E-value: 1.26e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 21356141  30 MTAPGPRPLVL-CGPSGSGKSTLLKRLFAEFP 60
Cdd:COG0572   1 AARSGKPRIIGiAGPSGSGKTTFARRLAEQLG 32
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 35-59 1.44e-03

tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];


Pssm-ID: 443264 [Multi-domain]  Cd Length: 179  Bit Score: 38.17  E-value: 1.44e-03
                        10        20
                ....*....|....*....|....*
gi 21356141  35 PRPLVLCGPSGSGKSTLLKRLFAEF 59
Cdd:COG4088   4 PMLLILTGPPGSGKTTFAKALAQRL 28
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 38-57 1.54e-03

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 38.57  E-value: 1.54e-03
                        10        20
                ....*....|....*....|
gi 21356141  38 LVLCGPSGSGKSTLLKRLFA 57
Cdd:COG4778  40 VALTGPSGAGKSTLLKCIYG 59
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 38-64 1.80e-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: 37.61  E-value: 1.80e-03
                        10        20
                ....*....|....*....|....*..
gi 21356141  38 LVLCGPSGSGKSTLLKRLFAEFPSTFG 64
Cdd:cd00267  28 VALVGPNGSGKSTLLRAIAGLLKPTSG 54
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 31-53 2.32e-03

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 443319 [Multi-domain]  Cd Length: 358  Bit Score: 38.54  E-value: 2.32e-03
                        10        20
                ....*....|....*....|...
gi 21356141  31 TAPGPRPLVLCGPSGSGKSTLLK 53
Cdd:COG4148  21 TLPGRGVTALFGPSGSGKTTLLR 43
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 38-53 2.64e-03

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 38.13  E-value: 2.64e-03
                        10
                ....*....|....*.
gi 21356141  38 LVLCGPSGSGKSTLLK 53
Cdd:COG3839  32 LVLLGPSGCGKSTLLR 47
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
33-167 3.11e-03

Predicted ATP-binding protein involved in virulence [General function prediction only];


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 38.06  E-value: 3.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356141  33 PGPRPLVLCGPSGSGKSTLLK-------RLFAEFPSTFGFSISHTTRKPrEGEEHGVHYYFVER--PEMEAAIAGDEFIE 103
Cdd:COG3950  23 NPPRLTVLVGENGSGKTTLLEaialalsGLLSRLDDVKFRKLLIRNGEF-GDSAKLILYYGTSRllLDGPLKKLERLKEE 101

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21356141 104 TAEFTGNLYGT--SKAAVREIQAQGRVCILDIEQKGVEQIKRTdLNPIL-IFNNP-PSIKELERRLRK 167
Cdd:COG3950 102 YFSRLDGYDSLldEDSNLREFLEWLREYLEDLENKLSDELDEK-LEAVReALNKLlPDFKDIRIDRDP 168
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 38-53 3.22e-03

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 37.51  E-value: 3.22e-03
                        10
                ....*....|....*.
gi 21356141  38 LVLCGPSGSGKSTLLK 53
Cdd:cd03262  29 VVIIGPSGSGKSTLLR 44
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 39-55 3.59e-03

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 37.38  E-value: 3.59e-03
                        10
                ....*....|....*..
gi 21356141  39 VLCGPSGSGKSTLLKRL 55
Cdd:cd01854  89 VLVGQSGVGKSTLLNAL 105
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 38-64 3.98e-03

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 37.44  E-value: 3.98e-03
                         10        20
                 ....*....|....*....|....*..
gi 21356141   38 LVLCGPSGSGKSTLLKRLFAEFPSTFG 64
Cdd:PRK13548  31 VAILGPNGAGKSTLLRALSGELSPDSG 57
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 38-76 4.60e-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: 37.46  E-value: 4.60e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 21356141  38 LVLCGPSGSGKSTLLKRLFAEFPSTFGF-SISHTTRKPRE 76
Cdd:COG3267  46 VVLTGEVGTGKTTLLRRLLERLPDDVKVaYIPNPQLSPAE 85
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 32-53 6.17e-03

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 37.44  E-value: 6.17e-03
                        10        20
                ....*....|....*....|..
gi 21356141  32 APGPRpLVLCGPSGSGKSTLLK 53
Cdd:COG4987 359 PPGER-VAIVGPSGSGKSTLLA 379
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 33-89 6.85e-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: 35.97  E-value: 6.85e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21356141  33 PGPRPLVLCGPSGSGKSTLLKR----LFAEFPSTFGFSISHTTRKPREGEEHGVHYYFVER 89
Cdd:cd00009  17 PPPKNLLLYGPPGTGKTTLARAianeLFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLF 77
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 35-86 7.29e-03

ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 36.18  E-value: 7.29e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 21356141  35 PRPLVLCGPSGSGKSTLLKRLFAEFPSTFgFSISHT--TRKPREGEEHGVHYYF 86
Cdd:cd19509  32 PRGILLYGPPGTGKTLLARAVASESGSTF-FSISASslVSKWVGESEKIVRALF 84
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 38-53 7.39e-03

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). 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: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 36.21  E-value: 7.39e-03
                        10
                ....*....|....*.
gi 21356141  38 LVLCGPSGSGKSTLLK 53
Cdd:cd03228  31 VAIVGPSGSGKSTLLK 46
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 39-68 7.75e-03

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 36.60  E-value: 7.75e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 21356141  39 VLCGPSGSGKSTLLKRLFAEFPSTFGFSIS 68
Cdd:COG1119  33 AILGPNGAGKSTLLSLITGDLPPTYGNDVR 62
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 38-53 9.13e-03

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 36.29  E-value: 9.13e-03
                        10
                ....*....|....*.
gi 21356141  38 LVLCGPSGSGKSTLLK 53
Cdd:cd03225  30 VLIVGPNGSGKSTLLR 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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