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Conserved domains on  [gi|41152277|ref|NP_957018|]
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guanylate kinase 1b [Danio rerio]

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 ...
 5-213 4.05e-88

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: 257.42  E-value: 4.05e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277     5 RPVVLSGPSGAGKSTLLKRLMKEYEGVFgFSVSHTTRNPRPGEEDGKglnclpmllgatllpvadvlssvtseDYHFVTK 84
Cdd:TIGR03263   1 LLIVISGPSGAGKSTLVKALLEEDPNLK-FSISATTRKPRPGEVDGV--------------------------DYFFVSK 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277    85 EKMQEGIDKDEFIENAEFSGNMYGTSKSSIEDVQAQNLICILDVDIQGVRNIKKTDLNPIYISIQPPSMEILEKRLRDRQ 164
Cdd:TIGR03263  54 EEFEEMIKAGEFLEWAEVHGNYYGTPKSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRG 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 41152277   165 TETEDSLQKRLEAARIDMELSKEpgvFDIVIVNDDLEEAYEKLKSVLIE 213
Cdd:TIGR03263 134 TDSEEVIERRLAKAKKEIAHADE---FDYVIVNDDLEKAVEELKSIILA 179
 
Name Accession Description Interval E-value
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
 5-213 4.05e-88

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: 257.42  E-value: 4.05e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277     5 RPVVLSGPSGAGKSTLLKRLMKEYEGVFgFSVSHTTRNPRPGEEDGKglnclpmllgatllpvadvlssvtseDYHFVTK 84
Cdd:TIGR03263   1 LLIVISGPSGAGKSTLVKALLEEDPNLK-FSISATTRKPRPGEVDGV--------------------------DYFFVSK 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277    85 EKMQEGIDKDEFIENAEFSGNMYGTSKSSIEDVQAQNLICILDVDIQGVRNIKKTDLNPIYISIQPPSMEILEKRLRDRQ 164
Cdd:TIGR03263  54 EEFEEMIKAGEFLEWAEVHGNYYGTPKSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRG 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 41152277   165 TETEDSLQKRLEAARIDMELSKEpgvFDIVIVNDDLEEAYEKLKSVLIE 213
Cdd:TIGR03263 134 TDSEEVIERRLAKAKKEIAHADE---FDYVIVNDDLEKAVEELKSIILA 179
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
7-219 3.18e-78

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 233.04  E-value: 3.18e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277   7 VVLSGPSGAGKSTLLKRLMKEYEGvFGFSVSHTTRNPRPGEEDGKglnclpmllgatllpvadvlssvtseDYHFVTKEK 86
Cdd:COG0194   5 IVLSGPSGAGKTTLVKALLERDPD-LRFSVSATTRPPRPGEVDGV--------------------------DYHFVSREE 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277  87 MQEGIDKDEFIENAEFSGNMYGTSKSSIEDVQAQNLICILDVDIQGVRNIKKTDLNPIYISIQPPSMEILEKRLRDRQTE 166
Cdd:COG0194  58 FERMIENGEFLEWAEVHGNYYGTPKAEVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRGRGTD 137

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 41152277 167 TEDSLQKRLEAARIDMELSKEpgvFDIVIVNDDLEEAYEKLKSVLIEEIEKVQ 219
Cdd:COG0194 138 SEEVIERRLAKAREELAHADE---FDYVVVNDDLDRAVEELKAIIRAERLRRE 187
gmk PRK00300
guanylate kinase; Provisional
 7-219 6.84e-78

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 232.67  E-value: 6.84e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277    7 VVLSGPSGAGKSTLLKRLMKEYEGVFgFSVSHTTRNPRPGEEDGKglnclpmllgatllpvadvlssvtseDYHFVTKEK 86
Cdd:PRK00300   8 IVLSGPSGAGKSTLVKALLERDPNLQ-LSVSATTRAPRPGEVDGV--------------------------DYFFVSKEE 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277   87 MQEGIDKDEFIENAEFSGNMYGTSKSSIEDVQAQNLICILDVDIQGVRNIKKTDLNPIYISIQPPSMEILEKRLRDRQTE 166
Cdd:PRK00300  61 FEEMIENGEFLEWAEVFGNYYGTPRSPVEEALAAGKDVLLEIDWQGARQVKKKMPDAVSIFILPPSLEELERRLRGRGTD 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 41152277  167 TEDSLQKRLEAARIDMELSKEpgvFDIVIVNDDLEEAYEKLKSVLIEEIEKVQ 219
Cdd:PRK00300 141 SEEVIARRLAKAREEIAHASE---YDYVIVNDDLDTALEELKAIIRAERLRRS 190
Guanylate_kin pfam00625
Guanylate kinase;
3-214 7.43e-76

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 226.49  E-value: 7.43e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277     3 GPRPVVLSGPSGAGKSTLLKRLMKEYEGVFGFSVSHTTRNPRPGEEDGKglnclpmllgatllpvadvlssvtseDYHFV 82
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGK--------------------------DYYFV 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277    83 TKEKMQEGIDKDEFIENAEFSGNMYGTSKSSIEDVQAQNLICILDVDIQGVRNIKKTDLNPIYISIQPPSMEILEKRLRD 162
Cdd:pfam00625  55 SKEEMERDISANEFLEYAQFSGNMYGTSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKG 134

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 41152277   163 RQTETEDSLQKRLEAARIDMELSKepgvFDIVIVNDDLEEAYEKLKSVLIEE 214
Cdd:pfam00625 135 RGKEQEEKINKRMAAAEQEFQHYE----FDVIIVNDDLEEAYKKLKEALEAE 182
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 13-215 4.57e-72

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: 216.78  E-value: 4.57e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277     13 SGAGKSTLLKRLMKEYEGVFGFSVSHTTRNPRPGEEDGKglnclpmllgatllpvadvlssvtseDYHFVTKEKMQEGID 92
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGV--------------------------DYHFVSKEEFEDDIK 54

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277     93 KDEFIENAEFSGNMYGTSKSSIEDVQAQNLICILDVDIQGVRNIKKTDLNPIYISIQPPSMEILEKRLRDRQTETEDSLQ 172
Cdd:smart00072  55 SGLFLEWGEYEGNYYGTSKETIRQVAEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQ 134

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 41152277    173 KRLEAARIDMelsKEPGVFDIVIVNDDLEEAYEKLKSVLIEEI 215
Cdd:smart00072 135 KRLAAAQKEA---QEYHLFDYVIVNDDLEDAYEELKEILEAEQ 174
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 6-208 1.06e-70

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: 212.01  E-value: 1.06e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277   6 PVVLSGPSGAGKSTLLKRLMKEYEGVFGFSVSHTTRNPRPGEEDGKglnclpmllgatllpvadvlssvtseDYHFVTKE 85
Cdd:cd00071   1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGV--------------------------DYHFVSKE 54

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277  86 KMQEGIDKDEFIENAEFSGNMYGTSKSSIEDVQAQNLICILDVDIQGVRNIKKTDLNPIYISIQPPsmeilekrlrdrqt 165
Cdd:cd00071  55 EFERLIENGEFLEWAEFHGNYYGTSKAAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP-------------- 120

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 41152277 166 etedslqkrleaaridmelskepgvfDIVIVNDDLEEAYEKLK 208
Cdd:cd00071 121 --------------------------DYVIVNDDLEKAYEELK 137
 
Name Accession Description Interval E-value
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
 5-213 4.05e-88

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: 257.42  E-value: 4.05e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277     5 RPVVLSGPSGAGKSTLLKRLMKEYEGVFgFSVSHTTRNPRPGEEDGKglnclpmllgatllpvadvlssvtseDYHFVTK 84
Cdd:TIGR03263   1 LLIVISGPSGAGKSTLVKALLEEDPNLK-FSISATTRKPRPGEVDGV--------------------------DYFFVSK 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277    85 EKMQEGIDKDEFIENAEFSGNMYGTSKSSIEDVQAQNLICILDVDIQGVRNIKKTDLNPIYISIQPPSMEILEKRLRDRQ 164
Cdd:TIGR03263  54 EEFEEMIKAGEFLEWAEVHGNYYGTPKSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRG 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 41152277   165 TETEDSLQKRLEAARIDMELSKEpgvFDIVIVNDDLEEAYEKLKSVLIE 213
Cdd:TIGR03263 134 TDSEEVIERRLAKAKKEIAHADE---FDYVIVNDDLEKAVEELKSIILA 179
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
7-219 3.18e-78

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 233.04  E-value: 3.18e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277   7 VVLSGPSGAGKSTLLKRLMKEYEGvFGFSVSHTTRNPRPGEEDGKglnclpmllgatllpvadvlssvtseDYHFVTKEK 86
Cdd:COG0194   5 IVLSGPSGAGKTTLVKALLERDPD-LRFSVSATTRPPRPGEVDGV--------------------------DYHFVSREE 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277  87 MQEGIDKDEFIENAEFSGNMYGTSKSSIEDVQAQNLICILDVDIQGVRNIKKTDLNPIYISIQPPSMEILEKRLRDRQTE 166
Cdd:COG0194  58 FERMIENGEFLEWAEVHGNYYGTPKAEVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRGRGTD 137

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 41152277 167 TEDSLQKRLEAARIDMELSKEpgvFDIVIVNDDLEEAYEKLKSVLIEEIEKVQ 219
Cdd:COG0194 138 SEEVIERRLAKAREELAHADE---FDYVVVNDDLDRAVEELKAIIRAERLRRE 187
gmk PRK00300
guanylate kinase; Provisional
 7-219 6.84e-78

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 232.67  E-value: 6.84e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277    7 VVLSGPSGAGKSTLLKRLMKEYEGVFgFSVSHTTRNPRPGEEDGKglnclpmllgatllpvadvlssvtseDYHFVTKEK 86
Cdd:PRK00300   8 IVLSGPSGAGKSTLVKALLERDPNLQ-LSVSATTRAPRPGEVDGV--------------------------DYFFVSKEE 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277   87 MQEGIDKDEFIENAEFSGNMYGTSKSSIEDVQAQNLICILDVDIQGVRNIKKTDLNPIYISIQPPSMEILEKRLRDRQTE 166
Cdd:PRK00300  61 FEEMIENGEFLEWAEVFGNYYGTPRSPVEEALAAGKDVLLEIDWQGARQVKKKMPDAVSIFILPPSLEELERRLRGRGTD 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 41152277  167 TEDSLQKRLEAARIDMELSKEpgvFDIVIVNDDLEEAYEKLKSVLIEEIEKVQ 219
Cdd:PRK00300 141 SEEVIARRLAKAREEIAHASE---YDYVIVNDDLDTALEELKAIIRAERLRRS 190
Guanylate_kin pfam00625
Guanylate kinase;
3-214 7.43e-76

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 226.49  E-value: 7.43e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277     3 GPRPVVLSGPSGAGKSTLLKRLMKEYEGVFGFSVSHTTRNPRPGEEDGKglnclpmllgatllpvadvlssvtseDYHFV 82
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGK--------------------------DYYFV 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277    83 TKEKMQEGIDKDEFIENAEFSGNMYGTSKSSIEDVQAQNLICILDVDIQGVRNIKKTDLNPIYISIQPPSMEILEKRLRD 162
Cdd:pfam00625  55 SKEEMERDISANEFLEYAQFSGNMYGTSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKG 134

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 41152277   163 RQTETEDSLQKRLEAARIDMELSKepgvFDIVIVNDDLEEAYEKLKSVLIEE 214
Cdd:pfam00625 135 RGKEQEEKINKRMAAAEQEFQHYE----FDVIIVNDDLEEAYKKLKEALEAE 182
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 13-215 4.57e-72

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: 216.78  E-value: 4.57e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277     13 SGAGKSTLLKRLMKEYEGVFGFSVSHTTRNPRPGEEDGKglnclpmllgatllpvadvlssvtseDYHFVTKEKMQEGID 92
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGV--------------------------DYHFVSKEEFEDDIK 54

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277     93 KDEFIENAEFSGNMYGTSKSSIEDVQAQNLICILDVDIQGVRNIKKTDLNPIYISIQPPSMEILEKRLRDRQTETEDSLQ 172
Cdd:smart00072  55 SGLFLEWGEYEGNYYGTSKETIRQVAEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQ 134

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 41152277    173 KRLEAARIDMelsKEPGVFDIVIVNDDLEEAYEKLKSVLIEEI 215
Cdd:smart00072 135 KRLAAAQKEA---QEYHLFDYVIVNDDLEDAYEELKEILEAEQ 174
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 6-208 1.06e-70

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: 212.01  E-value: 1.06e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277   6 PVVLSGPSGAGKSTLLKRLMKEYEGVFGFSVSHTTRNPRPGEEDGKglnclpmllgatllpvadvlssvtseDYHFVTKE 85
Cdd:cd00071   1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGV--------------------------DYHFVSKE 54

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277  86 KMQEGIDKDEFIENAEFSGNMYGTSKSSIEDVQAQNLICILDVDIQGVRNIKKTDLNPIYISIQPPsmeilekrlrdrqt 165
Cdd:cd00071  55 EFERLIENGEFLEWAEFHGNYYGTSKAAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP-------------- 120

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 41152277 166 etedslqkrleaaridmelskepgvfDIVIVNDDLEEAYEKLK 208
Cdd:cd00071 121 --------------------------DYVIVNDDLEKAYEELK 137
PLN02772 PLN02772
guanylate kinase
 3-211 3.46e-67

guanylate kinase


Pssm-ID: 215414 [Multi-domain]  Cd Length: 398  Bit Score: 212.01  E-value: 3.46e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277    3 GPRPVVLSGPSGAGKSTLLKRLMKEYEGVFGFSVSHTTRNPRPGEEDGKglnclpmllgatllpvadvlssvtseDYHFV 82
Cdd:PLN02772 134 AEKPIVISGPSGVGKGTLISMLMKEFPSMFGFSVSHTTRAPREMEKDGV--------------------------HYHFT 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277   83 TKEKMQEGIDKDEFIENAEFSGNMYGTSKSSIEDVQAQNLICILDVDIQGVRNIKKTDLNPIYISIQPPSMEILEKRLRD 162
Cdd:PLN02772 188 ERSVMEKEIKDGKFLEFASVHGNLYGTSIEAVEVVTDSGKRCILDIDVQGARSVRASSLEAIFIFICPPSMEELEKRLRA 267

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 41152277  163 RQTETEDSLQKRLEAARIDMELSKEPGVFDIVIVNDDLEEAYEKLKSVL 211
Cdd:PLN02772 268 RGTETEEQIQKRLRNAEAELEQGKSSGIFDHILYNDNLEECYKNLKKLL 316
gmk PRK14738
guanylate kinase; Provisional
 4-222 1.07e-44

guanylate kinase; Provisional


Pssm-ID: 237809  Cd Length: 206  Bit Score: 148.34  E-value: 1.07e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277    4 PRPVVLSGPSGAGKSTLLKRlMKEYEGVFGFSVSHTTRNPRPGEEDGKglnclpmllgatllpvadvlssvtseDYHFVT 83
Cdd:PRK14738  13 PLLVVISGPSGVGKDAVLAR-MRERKLPFHFVVTATTRPKRPGEIDGV--------------------------DYHFVT 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277   84 KEKMQEGIDKDEFIENAEFSGNMYGTSKSSIEDVQAQNLICILDVDIQGVRNIKKTDLNPIYISIQPPSMEILEKRLRDR 163
Cdd:PRK14738  66 PEEFREMISQNELLEWAEVYGNYYGVPKAPVRQALASGRDVIVKVDVQGAASIKRLVPEAVFIFLAPPSMDELTRRLELR 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41152277  164 QTETEDSLQKRLEAARIDMELSKEpgvFDIVIVN--DDLEEAYEKLKSVLIEEIEKVQDAQ 222
Cdd:PRK14738 146 RTESPEELERRLATAPLELEQLPE---FDYVVVNpeDRLDEAVAQIMAIISAEKSRVHPRR 203
gmk PRK14737
guanylate kinase; Provisional
 1-212 7.83e-42

guanylate kinase; Provisional


Pssm-ID: 173199  Cd Length: 186  Bit Score: 140.13  E-value: 7.83e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277    1 MSGPRPVVLSGPSGAGKSTLLKRLMKEYEGVFgFSVSHTTRNPRPGEEDGKglnclpmllgatllpvadvlssvtseDYH 80
Cdd:PRK14737   1 KASPKLFIISSVAGGGKSTIIQALLEEHPDFL-FSISCTTRAPRPGDEEGK--------------------------TYF 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277   81 FVTKEKMQEGIDKDEFIENAEFSGNMYGTSKSSIEDVQAQNLICILDVDIQGVRNIK-KTDLNPIYISIQPPSMEILEKR 159
Cdd:PRK14737  54 FLTIEEFKKGIADGEFLEWAEVHDNYYGTPKAFIEDAFKEGRSAIMDIDVQGAKIIKeKFPERIVTIFIEPPSEEEWEER 133

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 41152277  160 LRDRQTETEDSLQKRLEAARIDMELSKEpgvFDIVIVNDDLEEAYEKLKSVLI 212
Cdd:PRK14737 134 LIHRGTDSEESIEKRIENGIIELDEANE---FDYKIINDDLEDAIADLEAIIC 183
PhnN COG3709
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
1-211 5.26e-07

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


Pssm-ID: 442923  Cd Length: 188  Bit Score: 48.27  E-value: 5.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277   1 MSGP-RPVVLSGPSGAGKSTLLKRLMKEYEGVFGFSVSH--TTRNPRPGEEDgkglnclpmllgatllpvadvlssvtse 77
Cdd:COG3709   1 MSGPgRLIYVVGPSGAGKDSLLAAARARLAADPRLVFARryITRPADAGGED---------------------------- 52

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277  78 dyHfvtkekmqEGIDKDEFI---ENAEFS------GNMYGTSkSSIEDVQAQNliciLDVDIQGVRNI------KKTDLN 142
Cdd:COG3709  53 --H--------DALSEAEFArraAAGAFAlhwqahGLRYGIP-AEIDAWLAAG----RDVVVNGSRAVlpqaraRYPRLL 117

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152277 143 PIYISIqppSMEILEKRLRDRQTETEDSLQKRLeaARIDMELSKEPGVfdIVIVND-DLEEAYEKLKSVL 211
Cdd:COG3709 118 VVLITA---SPEVLAQRLAARGRESAEEIEARL--ARAAEFLPDGPDV--LVIDNDgPLEDAGARLLALL 180
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
7-45 5.64e-06

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 45.43  E-value: 5.64e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 41152277   7 VVLSGPSGAGKSTLLKRLMKEY---EG---VFGFSVSHTTRNPRP 45
Cdd:COG2884  31 VFLTGPSGAGKSTLLKLLYGEErptSGqvlVNGQDLSRLKRREIP 75
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 7-42 7.80e-05

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: 42.00  E-value: 7.80e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 41152277   7 VVLSGPSGAGKSTLLKRLMKEYEGVFGfSVS-------HTTRN 42
Cdd:cd01854  88 SVLVGQSGVGKSTLLNALLPELVLATG-EISeklgrgrHTTTH 129
COG4639 COG4639
Predicted kinase [General function prediction only];
7-29 1.41e-04

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 40.58  E-value: 1.41e-04
                        10        20
                ....*....|....*....|...
gi 41152277   7 VVLSGPSGAGKSTLLKRLMKEYE 29
Cdd:COG4639   5 VVLIGLPGSGKSTFARRLFAPTE 27
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 7-22 1.80e-04

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: 41.27  E-value: 1.80e-04
                        10
                ....*....|....*.
gi 41152277   7 VVLSGPSGAGKSTLLK 22
Cdd:COG4778  40 VALTGPSGAGKSTLLK 55
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
7-30 5.53e-04

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 39.80  E-value: 5.53e-04
                        10        20
                ....*....|....*....|....*..
gi 41152277   7 VVLSGPSGAGKSTLLK---RLMKEYEG 30
Cdd:COG4619  29 VAITGPSGSGKSTLLRalaDLDPPTSG 55
PRK01889 PRK01889
GTPase RsgA; Reviewed
 2-65 6.83e-04

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 39.92  E-value: 6.83e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41152277    2 SGPRPVVLSGPSGAGKSTLLKRLMkeyegvfGFSVSHT--TRnprpgEEDGKG--------LNCLPMllGATLL 65
Cdd:PRK01889 193 SGGKTVALLGSSGVGKSTLVNALL-------GEEVQKTgaVR-----EDDSKGrhttthreLHPLPS--GGLLI 252
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 7-27 7.45e-04

Cell division ATP-binding protein FtsE; 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


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 39.31  E-value: 7.45e-04
                        10        20
                ....*....|....*....|.
gi 41152277   7 VVLSGPSGAGKSTLLKRLMKE 27
Cdd:cd03292  30 VFLVGPSGAGKSTLLKLIYKE 50
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 7-29 8.62e-04

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: 38.52  E-value: 8.62e-04
                        10        20
                ....*....|....*....|...
gi 41152277   7 VVLSGPSGAGKSTLLKRLMKEYE 29
Cdd:cd03228  31 VAIVGPSGSGKSTLLKLLLRLYD 53
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 2-30 8.63e-04

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 38.64  E-value: 8.63e-04
                          10        20
                  ....*....|....*....|....*....
gi 41152277     2 SGPRPVVLSGPSGAGKSTLLKRLMKEYEG 30
Cdd:pfam13191  22 GRPPSVLLTGEAGTGKTTLLRELLRALER 50
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 4-49 1.27e-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: 38.12  E-value: 1.27e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 41152277      4 PRPVVLSGPSGAGKSTLLKRLMKEYEGVFGFSVSHTTRNPRPGEED 49
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLD 47
AAA_22 pfam13401
AAA domain;
1-31 1.48e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 37.32  E-value: 1.48e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 41152277     1 MSGPRPVVLSGPSGAGKSTLLKRLMKEYEGV 31
Cdd:pfam13401   2 RFGAGILVLTGESGTGKTTLLRRLLEQLPEV 32
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 7-29 2.13e-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: 38.59  E-value: 2.13e-03
                        10        20
                ....*....|....*....|...
gi 41152277   7 VVLSGPSGAGKSTLLKRLMKEYE 29
Cdd:COG4987 364 VAIVGPSGSGKSTLLALLLRFLD 386
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 7-45 2.34e-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: 36.43  E-value: 2.34e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 41152277     7 VVLSGPSGAGKSTLLKRLMKEYEGVFGFSVSHT-TRNPRP 45
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARALLKKLGLPKDSVySRNPDD 40
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 7-39 2.81e-03

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


Pssm-ID: 238977 [Multi-domain]  Cd Length: 69  Bit Score: 35.39  E-value: 2.81e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 41152277   7 VVLSGPSGAGKSTLLKRLMKEYEGvFGFSVSHT 39
Cdd:cd02019   2 IAITGGSGSGKSTVAKKLAEQLGG-RSVVVLDE 33
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 7-30 3.69e-03

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


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 37.82  E-value: 3.69e-03
                        10        20
                ....*....|....*....|....*..
gi 41152277   7 VVLSGPSGAGKSTLLK---RLMKEYEG 30
Cdd:COG4988 366 VALVGPSGAGKSTLLNlllGFLPPYSG 392
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 7-24 4.70e-03

RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 36.75  E-value: 4.70e-03
                          10
                  ....*....|....*...
gi 41152277     7 VVLSGPSGAGKSTLLKRL 24
Cdd:pfam03193 109 TVLAGQSGVGKSTLLNAL 126
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 7-40 4.74e-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: 37.06  E-value: 4.74e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 41152277   7 VVLSGPSGAGKSTLLK---RLMKEYEG---VFGFSVSHTT 40
Cdd:cd03225  30 VLIVGPNGSGKSTLLRllnGLLGPTSGevlVDGKDLTKLS 69
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 1-27 4.75e-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: 36.74  E-value: 4.75e-03
                        10        20
                ....*....|....*....|....*...
gi 41152277   1 MSGPRPVVL-SGPSGAGKSTLLKRLMKE 27
Cdd:COG0572   3 RSGKPRIIGiAGPSGSGKTTFARRLAEQ 30
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
1-32 5.03e-03

Predicted ATPase, AAA+ superfamily [General function prediction only];


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 37.23  E-value: 5.03e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 41152277   1 MSGPRPVVLSGPSGAGKSTLLKRLMKEYEGVF 32
Cdd:COG1373  17 LDNRKAVVITGPRQVGKTTLLKQLAKELENIL 48
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 7-29 5.15e-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: 36.09  E-value: 5.15e-03
                          10        20
                  ....*....|....*....|...
gi 41152277     7 VVLSGPSGAGKSTLLKRLMKEYE 29
Cdd:pfam00005  14 LALVGPNGAGKSTLLKLIAGLLS 36
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 7-25 5.62e-03

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 36.97  E-value: 5.62e-03
                        10
                ....*....|....*....
gi 41152277   7 VVLSGPSGAGKSTLLkRLM 25
Cdd:COG3839  32 LVLLGPSGCGKSTLL-RMI 49
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 7-24 5.63e-03

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 36.92  E-value: 5.63e-03
                         10
                 ....*....|....*...
gi 41152277    7 VVLSGPSGAGKSTLLKRL 24
Cdd:PRK11124  31 LVLLGPSGAGKSSLLRVL 48
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 7-31 7.37e-03

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 36.88  E-value: 7.37e-03
                          10        20
                  ....*....|....*....|....*...
gi 41152277     7 VVLSGPSGAGKSTLLK---RLMKEYEGV 31
Cdd:TIGR02857 351 VALVGPSGAGKSTLLNlllGFVDPTEGS 378
AAA_14 pfam13173
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 4-28 7.75e-03

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 463799 [Multi-domain]  Cd Length: 128  Bit Score: 35.26  E-value: 7.75e-03
                          10        20
                  ....*....|....*....|....*
gi 41152277     4 PRPVVLSGPSGAGKSTLLKRLMKEY 28
Cdd:pfam13173   2 RKILVITGPRQVGKTTLLLQLIKEL 26
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 1-29 8.06e-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: 36.30  E-value: 8.06e-03
                        10        20
                ....*....|....*....|....*....
gi 41152277   1 MSGPRPVVLSGPSGAGKSTLLKRLMKEYE 29
Cdd:COG3267  40 AQGGGFVVLTGEVGTGKTTLLRRLLERLP 68
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 7-29 8.75e-03

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 36.74  E-value: 8.75e-03
                        10        20
                ....*....|....*....|...
gi 41152277   7 VVLSGPSGAGKSTLLKRLMKEYE 29
Cdd:COG2274 504 VAIVGRSGSGKSTLLKLLLGLYE 526
PRK12289 PRK12289
small ribosomal subunit biogenesis GTPase RsgA;
8-41 8.79e-03

small ribosomal subunit biogenesis GTPase RsgA;


Pssm-ID: 237040 [Multi-domain]  Cd Length: 352  Bit Score: 36.53  E-value: 8.79e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 41152277    8 VLSGPSGAGKSTLLKRLMKEYEGVFGfSVS-------HTTR 41
Cdd:PRK12289 176 VVAGPSGVGKSSLINRLIPDVELRVG-KVSgklgrgrHTTR 215
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 7-30 9.02e-03

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 36.09  E-value: 9.02e-03
                        10        20
                ....*....|....*....|....
gi 41152277   7 VVLSGPSGAGKSTLLKRLMKEYEG 30
Cdd:COG2401  59 VLIVGASGSGKSTLLRLLAGALKG 82
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
7-24 9.17e-03

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 36.14  E-value: 9.17e-03
                        10
                ....*....|....*...
gi 41152277   7 VVLSGPSGAGKSTLLKRL 24
Cdd:COG4161  31 LVLLGPSGAGKSSLLRVL 48
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
7-27 9.50e-03

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 35.66  E-value: 9.50e-03
                        10        20
                ....*....|....*....|.
gi 41152277   7 VVLSGPSGAGKSTLLKRLMKE 27
Cdd:COG0645   2 ILVCGLPGSGKSTLARALAER 22
 
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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