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Conserved domains on  [gi|2225490735|ref|WP_245522074|]
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UMP kinase [Thermosphaera aggregans]

Protein Classification

amino acid kinase family protein( domain architecture ID 663)

amino acid kinase (AAK) family protein catalyzes the phosphorylation of a variety of substrates including amino acids, using ATP as the source of the phosphoryl group

CATH:  3.40.1160.10
EC:  2.7.-.-
Gene Ontology:  GO:0005524|GO:0016310|GO:0016301
PubMed:  12005432

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAK super family cl00452
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 5-223 1.58e-54

Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like N-acetylglutamate kinase (NAGK), carbamate kinase (CK), aspartokinase (AK), glutamate-5-kinase (G5K) and UMP kinase (UMPK). The AAK superfamily includes kinases that phosphorylate a variety of amino acid substrates. These kinases catalyze the formation of phosphoric anhydrides, generally with a carboxylate, and use ATP as the source of the phosphoryl group; are involved in amino acid biosynthesis. Some of these kinases control the process via allosteric feed-back inhibition.


The actual alignment was detected with superfamily member cd04253:

Pssm-ID: 444912 [Multi-domain]  Cd Length: 221  Bit Score: 173.97  E-value: 1.58e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735   5 TLVLKITGKAFDEGPWL--LEKYVSILKTLSEKYKLVVITGGGRLARHYIDMARNIGVvSNYWLDLIGIDVSRLNALLLI 82
Cdd:cd04253     1 RIVISLGGSVLAPEKDAdfIKEYANVLRKISDGHKVAVVVGGGRLAREYISVARKLGA-SEAFLDEIGIMATRLNARLLI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735  83 ASMEGrAYPKPYESLSELLSALPYSNVLVAGGLIPGQSTASVAVQSAEAVGARVLYYFSAIGYVYDKDPVKHVDAQPFKE 162
Cdd:cd04253    80 AALGD-AYPPVPTSYEEALEAMFTGKIVVMGGTEPGQSTDAVAALLAERLGADLLINATNVDGVYSKDPRKDPDAKKFDR 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2225490735 163 ITATRLKEILAQ-KQLPGEYALIDDKALDMAVRSGIEIRLIFFKHPEKIFESLNGLNPGTRI 223
Cdd:cd04253   159 LSADELIDIVGKsSWKAGSNEPFDPLAAKIIERSGIKTIVVDGRDPENLERALKGEFVGTII 220
 
Name Accession Description Interval E-value
AAK_UMPK-PyrH-Pf cd04253
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ...
 5-223 1.58e-54

AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase (uridylate kinase) enzymes that catalyze UMP phosphorylation and play a key role in pyrimidine nucleotide biosynthesis; regulation of this process is via feed-back control and via gene repression of carbamoyl phosphate synthetase (the first enzyme of the pyrimidine biosynthesis pathway). The UMP kinase of Pyrococcus furiosus (Pf) is known to function as a homohexamer, with GTP and UTP being allosteric effectors. Like other related enzymes (carbamate kinase, aspartokinase, and N-acetylglutamate kinase) the E. coli and most bacterial UMPKs have a conserved, N-terminal, lysine residue proposed to function in the catalysis of the phosphoryl group transfer, whereas most archaeal UMPKs (this CD) appear to lack this residue and the Pyrococcus furiosus structure has an additional Mg ion bound to the ATP molecule which is proposed to function as the catalysis instead. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239786 [Multi-domain]  Cd Length: 221  Bit Score: 173.97  E-value: 1.58e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735   5 TLVLKITGKAFDEGPWL--LEKYVSILKTLSEKYKLVVITGGGRLARHYIDMARNIGVvSNYWLDLIGIDVSRLNALLLI 82
Cdd:cd04253     1 RIVISLGGSVLAPEKDAdfIKEYANVLRKISDGHKVAVVVGGGRLAREYISVARKLGA-SEAFLDEIGIMATRLNARLLI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735  83 ASMEGrAYPKPYESLSELLSALPYSNVLVAGGLIPGQSTASVAVQSAEAVGARVLYYFSAIGYVYDKDPVKHVDAQPFKE 162
Cdd:cd04253    80 AALGD-AYPPVPTSYEEALEAMFTGKIVVMGGTEPGQSTDAVAALLAERLGADLLINATNVDGVYSKDPRKDPDAKKFDR 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2225490735 163 ITATRLKEILAQ-KQLPGEYALIDDKALDMAVRSGIEIRLIFFKHPEKIFESLNGLNPGTRI 223
Cdd:cd04253   159 LSADELIDIVGKsSWKAGSNEPFDPLAAKIIERSGIKTIVVDGRDPENLERALKGEFVGTII 220
pyrH_arch TIGR02076
uridylate kinase, putative; This family consists of the archaeal and spirochete proteins most ...
 6-223 4.68e-54

uridylate kinase, putative; This family consists of the archaeal and spirochete proteins most closely related to bacterial uridylate kinases (TIGR02075), an enzyme involved in pyrimidine biosynthesis. Members are likely, but not known, to be functionally equivalent to their bacterial counterparts. However, substantial sequence differences suggest that regulatory mechanisms may be different; the bacterial form is allosterically regulated by GTP. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 273956 [Multi-domain]  Cd Length: 221  Bit Score: 172.88  E-value: 4.68e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735   6 LVLKITGKAFDEG--PWLLEKYVSILKTLSEKYKLVVITGGGRLARHYIDMARNIGVvSNYWLDLIGIDVSRLNALLLIA 83
Cdd:TIGR02076   1 IVISLGGSVLSPEidAEFIKEFANILRKLSDEHKVGVVVGGGKTARRYIGVARELGA-SETFLDEIGIDATRLNAMLLIA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735  84 SMEGRAYPKPYESLSELLSALPYSNVLVAGGLIPGQSTASVAVQSAEAVGARVLYYFSAIGYVYDKDPVKHVDAQPFKEI 163
Cdd:TIGR02076  80 ALGDDAYPKVPENFEEALEAMSLGKIVVMGGTHPGHTTDAVAALLAEFSKADLLINATNVDGVYDKDPKKDPDAKKFDKL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2225490735 164 TATRLKEILAQKQL-PGEYALIDDKALDMAVRSGIEIRLIFFKHPEKIFESLNGLNPGTRI 223
Cdd:TIGR02076 160 TPEELVEIVGSSSVkAGSNEVVDPLAAKIIERSKIRTIVVNGRDPENLEKVLKGEHVGTII 220
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 4-202 2.39e-19

Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino acid substrates, as well as uridylate kinase and carbamate kinase. This family includes: Aspartokinase EC:2.7.2.4. Acetylglutamate kinase EC:2.7.2.8. Glutamate 5-kinase EC:2.7.2.11. Uridylate kinase EC:2.7.4.-. Carbamate kinase EC:2.7.2.2.


Pssm-ID: 395565 [Multi-domain]  Cd Length: 232  Bit Score: 83.18  E-value: 2.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735   4 NTLVLKITGKAFDEGPwLLEKYVSILKTLSEK-YKLVVITGGGRLARHYI-------DMARNIGVVSNYWL--DLIGIDV 73
Cdd:pfam00696   1 KRVVIKLGGSSLTDKE-RLKRLADEIAALLEEgRKLVVVHGGGAFADGLLallglspRFARLTDAETLEVAtmDALGSLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735  74 SRLNALLLIASMEGRAYP--------------KPYESLSELLSALPYSNVL-VAGGLI----PGQ----STASVAVQSAE 130
Cdd:pfam00696  80 ERLNAALLAAGLPAVGLPaaqllateagfiddVVTRIDTEALEELLEAGVVpVITGFIgidpEGElgrgSSDTLAALLAE 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2225490735 131 AVGARVLYYFSAIGYVYDKDPVKHVDAQPFKEITATRLKEILAQKQLPGEYALIDDKALDMAVRSGIEIRLI 202
Cdd:pfam00696 160 ALGADKLIILTDVDGVYTADPRKVPDAKLIPEISYDELLELLASGLATGGMKVKLPAALEAARRGGIPVVIV 231
 
Name Accession Description Interval E-value
AAK_UMPK-PyrH-Pf cd04253
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ...
 5-223 1.58e-54

AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase (uridylate kinase) enzymes that catalyze UMP phosphorylation and play a key role in pyrimidine nucleotide biosynthesis; regulation of this process is via feed-back control and via gene repression of carbamoyl phosphate synthetase (the first enzyme of the pyrimidine biosynthesis pathway). The UMP kinase of Pyrococcus furiosus (Pf) is known to function as a homohexamer, with GTP and UTP being allosteric effectors. Like other related enzymes (carbamate kinase, aspartokinase, and N-acetylglutamate kinase) the E. coli and most bacterial UMPKs have a conserved, N-terminal, lysine residue proposed to function in the catalysis of the phosphoryl group transfer, whereas most archaeal UMPKs (this CD) appear to lack this residue and the Pyrococcus furiosus structure has an additional Mg ion bound to the ATP molecule which is proposed to function as the catalysis instead. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239786 [Multi-domain]  Cd Length: 221  Bit Score: 173.97  E-value: 1.58e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735   5 TLVLKITGKAFDEGPWL--LEKYVSILKTLSEKYKLVVITGGGRLARHYIDMARNIGVvSNYWLDLIGIDVSRLNALLLI 82
Cdd:cd04253     1 RIVISLGGSVLAPEKDAdfIKEYANVLRKISDGHKVAVVVGGGRLAREYISVARKLGA-SEAFLDEIGIMATRLNARLLI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735  83 ASMEGrAYPKPYESLSELLSALPYSNVLVAGGLIPGQSTASVAVQSAEAVGARVLYYFSAIGYVYDKDPVKHVDAQPFKE 162
Cdd:cd04253    80 AALGD-AYPPVPTSYEEALEAMFTGKIVVMGGTEPGQSTDAVAALLAERLGADLLINATNVDGVYSKDPRKDPDAKKFDR 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2225490735 163 ITATRLKEILAQ-KQLPGEYALIDDKALDMAVRSGIEIRLIFFKHPEKIFESLNGLNPGTRI 223
Cdd:cd04253   159 LSADELIDIVGKsSWKAGSNEPFDPLAAKIIERSGIKTIVVDGRDPENLERALKGEFVGTII 220
pyrH_arch TIGR02076
uridylate kinase, putative; This family consists of the archaeal and spirochete proteins most ...
 6-223 4.68e-54

uridylate kinase, putative; This family consists of the archaeal and spirochete proteins most closely related to bacterial uridylate kinases (TIGR02075), an enzyme involved in pyrimidine biosynthesis. Members are likely, but not known, to be functionally equivalent to their bacterial counterparts. However, substantial sequence differences suggest that regulatory mechanisms may be different; the bacterial form is allosterically regulated by GTP. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 273956 [Multi-domain]  Cd Length: 221  Bit Score: 172.88  E-value: 4.68e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735   6 LVLKITGKAFDEG--PWLLEKYVSILKTLSEKYKLVVITGGGRLARHYIDMARNIGVvSNYWLDLIGIDVSRLNALLLIA 83
Cdd:TIGR02076   1 IVISLGGSVLSPEidAEFIKEFANILRKLSDEHKVGVVVGGGKTARRYIGVARELGA-SETFLDEIGIDATRLNAMLLIA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735  84 SMEGRAYPKPYESLSELLSALPYSNVLVAGGLIPGQSTASVAVQSAEAVGARVLYYFSAIGYVYDKDPVKHVDAQPFKEI 163
Cdd:TIGR02076  80 ALGDDAYPKVPENFEEALEAMSLGKIVVMGGTHPGHTTDAVAALLAEFSKADLLINATNVDGVYDKDPKKDPDAKKFDKL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2225490735 164 TATRLKEILAQKQL-PGEYALIDDKALDMAVRSGIEIRLIFFKHPEKIFESLNGLNPGTRI 223
Cdd:TIGR02076 160 TPEELVEIVGSSSVkAGSNEVVDPLAAKIIERSKIRTIVVNGRDPENLEKVLKGEHVGTII 220
AAK_UMPK-like cd04239
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ...
 7-223 3.99e-37

AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) enzyme that catalyzes UMP phosphorylation and plays a key role in pyrimidine nucleotide biosynthesis. Regulation of this process is via feed-back control and via gene repression of carbamoyl phosphate synthetase (the first enzyme of the pyrimidine biosynthesis pathway). The UMP kinases of E. coli (Ec) and Pyrococcus furiosus (Pf) are known to function as homohexamers, with GTP and UTP being allosteric effectors. Like other related enzymes (carbamate kinase, aspartokinase, and N-acetylglutamate kinase) the E. coli and most bacterial UMPKs have a conserved, N-terminal, lysine residue proposed to function in the catalysis of the phosphoryl group transfer, whereas most archaeal UMPKs appear to lack this residue and the Pyrococcus furiosus structure has an additional Mg ion bound to the ATP molecule which is proposed to function as the catalysis instead. Also included in this CD are the alpha and beta subunits of the Mo storage protein (MosA and MosB) characterized as an alpha4-beta4 octamer containing an ATP-dependent, polynuclear molybdenum-oxide cluster. These and related sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239772 [Multi-domain]  Cd Length: 229  Bit Score: 129.58  E-value: 3.99e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735   7 VLKITGKAF-DEGPW----LLEKYVSILKTL-SEKYKLVVITGGGRLARHYIDMARNIGVVSnywLDLIGIDVSRLNALL 80
Cdd:cd04239     3 VLKLSGEALaGEGGGidpeVLKEIAREIKEVvDLGVEVAIVVGGGNIARGYIAAARGMPRAT---ADYIGMLATVMNALA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735  81 LIASME---GRAYPK----------PYeSLSELLSALPYSNVLVAGG--LIPGQSTASVAVQSAEAVGARVLYYFSAIGY 145
Cdd:cd04239    80 LQDALEklgVKTRVMsaipmqgvaePY-IRRRAIRHLEKGRIVIFGGgtGNPGFTTDTAAALRAEEIGADVLLKATNVDG 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2225490735 146 VYDKDPVKHVDAQPFKEITAtrlKEILAQKQLPgeyalIDDKALDMAVRSGIEIRLIFFKHPEKIFESLNGLNPGTRI 223
Cdd:cd04239   159 VYDADPKKNPDAKKYDRISY---DELLKKGLKV-----MDATALTLCRRNKIPIIVFNGLKPGNLLRALKGEHVGTLI 228
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 4-202 2.39e-19

Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino acid substrates, as well as uridylate kinase and carbamate kinase. This family includes: Aspartokinase EC:2.7.2.4. Acetylglutamate kinase EC:2.7.2.8. Glutamate 5-kinase EC:2.7.2.11. Uridylate kinase EC:2.7.4.-. Carbamate kinase EC:2.7.2.2.


Pssm-ID: 395565 [Multi-domain]  Cd Length: 232  Bit Score: 83.18  E-value: 2.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735   4 NTLVLKITGKAFDEGPwLLEKYVSILKTLSEK-YKLVVITGGGRLARHYI-------DMARNIGVVSNYWL--DLIGIDV 73
Cdd:pfam00696   1 KRVVIKLGGSSLTDKE-RLKRLADEIAALLEEgRKLVVVHGGGAFADGLLallglspRFARLTDAETLEVAtmDALGSLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735  74 SRLNALLLIASMEGRAYP--------------KPYESLSELLSALPYSNVL-VAGGLI----PGQ----STASVAVQSAE 130
Cdd:pfam00696  80 ERLNAALLAAGLPAVGLPaaqllateagfiddVVTRIDTEALEELLEAGVVpVITGFIgidpEGElgrgSSDTLAALLAE 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2225490735 131 AVGARVLYYFSAIGYVYDKDPVKHVDAQPFKEITATRLKEILAQKQLPGEYALIDDKALDMAVRSGIEIRLI 202
Cdd:pfam00696 160 ALGADKLIILTDVDGVYTADPRKVPDAKLIPEISYDELLELLASGLATGGMKVKLPAALEAARRGGIPVVIV 231
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 7-223 3.39e-10

Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like N-acetylglutamate kinase (NAGK), carbamate kinase (CK), aspartokinase (AK), glutamate-5-kinase (G5K) and UMP kinase (UMPK). The AAK superfamily includes kinases that phosphorylate a variety of amino acid substrates. These kinases catalyze the formation of phosphoric anhydrides, generally with a carboxylate, and use ATP as the source of the phosphoryl group; are involved in amino acid biosynthesis. Some of these kinases control the process via allosteric feed-back inhibition.


Pssm-ID: 239033 [Multi-domain]  Cd Length: 248  Bit Score: 58.22  E-value: 3.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735   7 VLKITGKAFDEGPwLLEKYVSILKTL-SEKYKLVVITGGGRLARHYI-DMARNIGVVSNY-----WLDLIGIDVSRLNAL 79
Cdd:cd02115     1 VIKFGGSSVSSEE-RLRNLARILVKLaSEGGRVVVVHGAGPQITDELlAHGELLGYARGLritdrETDALAAMGEGMSNL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735  80 LLIASME------------------------GRAYPKPYESLSELL--------SALPYSNVLVAGGLIPGqSTASVAVQ 127
Cdd:cd02115    80 LIAAALEqhgikavpldltqagfaspnqghvGKITKVSTDRLKSLLengilpilSGFGGTDEKETGTLGRG-GSDSTAAL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735 128 SAEAVGARVLYYFSAIGYVYDKDPVKHVDAQPFKEITATRLKEILAQKQLPgeyalIDDKALDMAVRSGIEIRLIFFKHP 207
Cdd:cd02115   159 LAAALKADRLVILTDVDGVYTADPRKVPDAKLLSELTYEEAAELAYAGAMV-----LKPKAADPAARAGIPVRIANTENP 233

                         250
                  ....*....|....*.
gi 2225490735 208 EKIfESLNGLNPGTRI 223
Cdd:cd02115   234 GAL-ALFTPDGGGTLI 248
AAK_UMPK-MosAB cd04255
AAK_UMPK-MosAB: This CD includes the alpha and beta subunits of the Mo storage protein (MosA ...
 7-223 4.40e-10

AAK_UMPK-MosAB: This CD includes the alpha and beta subunits of the Mo storage protein (MosA and MosB) which are related to uridine monophosphate kinase (UMPK) enzymes that catalyze the phosphorylation of UMP by ATP, yielding UDP, and playing a key role in pyrimidine nucleotide biosynthesis. The Mo storage protein from the nitrogen-fixing bacterium, Azotobacter vinelandii, is characterized as an alpha4-beta4 octamer containing a polynuclear molybdenum-oxide cluster which is ATP-dependent to bind Mo and pH-dependent to release Mo. These and related bacterial sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239788 [Multi-domain]  Cd Length: 262  Bit Score: 57.79  E-value: 4.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735   7 VLKITGKAF-DEGPWLLEKYVSILKTLSEKYKLVVITGGGRLARHY----IDMARNIGVVSNywldlIGIDVSRLNALLL 81
Cdd:cd04255    34 VVKIGGQSIiDRGAEAVLPLVEEIVALRPEHKLLILTGGGTRARHVysigLDLGMPTGVLAK-----LGASVSEQNAEML 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735  82 --IASMEGRAYPKP----------YESLSELLSALP---YSNVLVAGGLIPGQSTASVAVQSAEAVGARVLYYFSAIGYV 146
Cdd:cd04255   109 atLLAKHGGSKVGHgdllqlptflKAGRAPVISGMPpygLWEHPAEEGRIPPHRTDVGAFLLAEVIGARNLIFVKDEDGL 188

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2225490735 147 YDKDPVKHVDAQPFKEITATRLKEiLAQKQLPGEYALIDDKALDMAVRsgiEIRLIFFKHPEKIFESLNGLNPGTRI 223
Cdd:cd04255   189 YTADPKKNKKAEFIPEISAAELLK-KDLDDLVLERPVLDLLQNARHVK---EVQIVNGLVPGNLTRALRGEHVGTII 261
AAK_UC cd04240
AAK_UC: Uncharacterized (UC) amino acid kinase-like proteins found mainly in archaea and a few ...
 7-223 1.71e-04

AAK_UC: Uncharacterized (UC) amino acid kinase-like proteins found mainly in archaea and a few bacteria. Sequences in this CD are members of the Amino Acid Kinase (AAK) superfamily.


Pssm-ID: 239773 [Multi-domain]  Cd Length: 203  Bit Score: 41.19  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735   7 VLKITGKAFDEGPWLLEKyvsiLKTLSeKYKLVVITGGGRLA---RHYiDMARNIGVVSNYWL-----DLIGIDVSRLNA 78
Cdd:cd04240     1 VVKIGGSLIREAVRLLRW----LKTLS-GGGVVIVPGGGPFAdvvRRY-QERKGLSDAAAHWMailamEQYGYLLADLEP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735  79 LLLIASM-EGRAYPKPyeSLSELLsaLPYSNVLVAGGLIPGQSTAS--VAVQSAEAVGARVLYYFSAIGYVYDKDpvkhv 155
Cdd:cd04240    75 RLVARTLaELTDVLER--GKIAIL--LPYRLLLDTDPLPHSWEVTSdsIAAWLAKKLGAKRLVIVTDVDGIYEKD----- 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2225490735 156 daqpfkeitATRLKEIlAQKQLPGEYAlIDDKALDMAVRSGIEIRLIFFKHPEKIFESLNGL-NPGTRI 223
Cdd:cd04240   146 ---------GKLVNEI-AAAELLGETS-VDPAFPRLLTKYGIRCYVVNGDDPERVLAALRGReGVGTRI 203
AAK_UMPK-PyrH-Ec cd04254
UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) ...
 7-223 1.87e-03

UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) enzyme that catalyzes UMP phosphorylation and plays a key role in pyrimidine nucleotide biosynthesis; regulation of this process is via feed-back control and via gene repression of carbamoyl phosphate synthetase (the first enzyme of the pyrimidine biosynthesis pathway). The UMP kinase of E. coli (Ec) is known to function as a homohexamer, with GTP and UTP being allosteric effectors. Like other related enzymes (carbamate kinase, aspartokinase, and N-acetylglutamate kinase) the E. coli and most bacterial and chloroplast UMPKs (this CD) have a conserved, N-terminal, lysine residue proposed to function in the catalysis of the phosphoryl group transfer, whereas most archaeal UMPKs appear to lack this residue and the Pyrococcus furiosus structure has an additional Mg ion bound to the ATP molecule which is proposed to function as the catalysis instead. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239787 [Multi-domain]  Cd Length: 231  Bit Score: 38.24  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735   7 VLKITGKAF-DEG-----PWLLEKYVSILKTLSE-KYKLVVITGGGRLARHY----IDMARNIGvvsnywlDLIGIDVSR 75
Cdd:cd04254     4 LLKLSGEALaGENgfgidPEVLNRIAREIKEVVDlGVEVAIVVGGGNIFRGAsaaeAGMDRATA-------DYMGMLATV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735  76 LNALLLIASMEgRAYPKpyeslSELLSALPYSNV--------------------LVAGGLIPGQSTASVAVQSAEAVGAR 135
Cdd:cd04254    77 INALALQDALE-SLGVK-----TRVMSAIPMQGVaepyirrrairhlekgrvviFAGGTGNPFFTTDTAAALRAIEINAD 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735 136 VLYYFSAIGYVYDKDPVKHVDAQPFKEITatrLKEILaQKQLpgeyALIDDKALDMAVRSGIEIRLIFFKHPEKIFESLN 215
Cdd:cd04254   151 VILKATKVDGVYDADPKKNPNAKRYDHLT---YDEVL-SKGL----KVMDATAFTLCRDNNLPIVVFNINEPGNLLKAVK 222


                  ....*...
gi 2225490735 216 GLNPGTRI 223
Cdd:cd04254   223 GEGVGTLI 230
AAK_FomA-like cd04241
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ...
 9-223 8.89e-03

AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar proteins found in a wide range of organisms. Together, the fomA and fomB genes in the fosfomycin biosynthetic gene cluster of Streptomyces wedmorensis confer high-level fosfomycin resistance. FomA and FomB proteins converted fosfomycin to fosfomycin monophosphate and fosfomycin diphosphate in the presence of ATP and a magnesium ion, indicating that FomA and FomB catalyzed phosphorylations of fosfomycin and fosfomycin monophosphate, respectively. FomA and related sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239774 [Multi-domain]  Cd Length: 252  Bit Score: 36.47  E-value: 8.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735   9 KITGKAFDEGpwLLEKYVSILKTLSEKyKLVVITGGGRLARHYI---DMARNIGVVSNYWLDLIGIDVSRLN-----ALL 80
Cdd:cd04241    14 KDRPETIREE--NLERIARELAEAIDE-KLVLVHGGGSFGHPKAkeyGLPDGDGSFSAEGVAETHEAMLELNsivvdALL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735  81 -------------LIASMEGRAYPKPYESLSELLSA--LP--YSNVLVAGGLIPG-QSTASVAVQSAEAVGARVLYYFSA 142
Cdd:cd04241    91 eagvpavsvppssFFVTENGRIVSFDLEVIKELLDRgfVPvlHGDVVLDEGGGITiLSGDDIVVELAKALKPERVIFLTD 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225490735 143 IGYVYDKDPVkhvDAQPFKEITATRLKEILAQKQLPGeyalID---------DKALDMAvRSGIEIRLIFFKHPEKIFES 213
Cdd:cd04241   171 VDGVYDKPPP---DAKLIPEIDVGSLEDILAALGSAG----TDvtggmagkiEELLELA-RRGIEVYIFNGDKPENLYRA 242

                         250
                  ....*....|
gi 2225490735 214 LNGLNPGTRI 223
Cdd:cd04241   243 LLGNFIGTRI 252
 
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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