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Conserved domains on  [gi|1958181278|ref|WP_201289174|]
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(d)CMP kinase [Halovenus carboxidivorans]

Protein Classification

AAA family ATPase( domain architecture ID 11480180)

AAA family ATPase similar to (d)CMP kinase, which catalyzes the phosphorylation of cytidine monophosphate (CMP) or dCMP to produce cytidine diphosphate (CDP) or dCDP, using ATP as the preferred phosphoryl donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK04182 PRK04182
cytidylate kinase; Provisional
 1-179 4.14e-86

cytidylate kinase; Provisional


:

Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 251.26  E-value: 4.14e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278   1 MFVTVSGPPGCGATSLCTRLAEALDCPYVSGGEIFRDIAEERGMGLTELSAKAQESDEIDRELDRRLRSIAEKwgasNKP 80
Cdd:PRK04182    1 MIITISGPPGSGKTTVARLLAEKLGLKHVSAGEIFRELAKERGMSLEEFNKYAEEDPEIDKEIDRRQLEIAEK----EDN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278  81 FVLESRLAGWLAGERADLRIYLNAPEEVRKDRISDRE----ETA-AEMSVREVNEAGRYQAYYDIDLDDRTFYDMHVNTA 155
Cdd:PRK04182   77 VVLEGRLAGWMAKDYADLKIWLKAPLEVRAERIAEREgisvEEAlEETIEREESEAKRYKEYYGIDIDDLSIYDLVINTS 156

                         170       180
                  ....*....|....*....|....
gi 1958181278 156 RWSQEGVFRIVSAAIEGYDPESDE 179
Cdd:PRK04182  157 RWDPEGVFDIILTAIDKLLKAKDE 180
 
Name Accession Description Interval E-value
PRK04182 PRK04182
cytidylate kinase; Provisional
 1-179 4.14e-86

cytidylate kinase; Provisional


Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 251.26  E-value: 4.14e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278   1 MFVTVSGPPGCGATSLCTRLAEALDCPYVSGGEIFRDIAEERGMGLTELSAKAQESDEIDRELDRRLRSIAEKwgasNKP 80
Cdd:PRK04182    1 MIITISGPPGSGKTTVARLLAEKLGLKHVSAGEIFRELAKERGMSLEEFNKYAEEDPEIDKEIDRRQLEIAEK----EDN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278  81 FVLESRLAGWLAGERADLRIYLNAPEEVRKDRISDRE----ETA-AEMSVREVNEAGRYQAYYDIDLDDRTFYDMHVNTA 155
Cdd:PRK04182   77 VVLEGRLAGWMAKDYADLKIWLKAPLEVRAERIAEREgisvEEAlEETIEREESEAKRYKEYYGIDIDDLSIYDLVINTS 156

                         170       180
                  ....*....|....*....|....
gi 1958181278 156 RWSQEGVFRIVSAAIEGYDPESDE 179
Cdd:PRK04182  157 RWDPEGVFDIILTAIDKLLKAKDE 180
cyt_kin_arch TIGR02173
cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. ...
 1-171 2.76e-57

cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. Members of this family are found in the archaea and in spirochaetes, and differ considerably from the common bacterial form of cytidylate kinase described by TIGR00017.


Pssm-ID: 274012 [Multi-domain]  Cd Length: 171  Bit Score: 178.00  E-value: 2.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278   1 MFVTVSGPPGCGATSLCTRLAEALDCPYVSGGEIFRDIAEERGMGLTELSAKAQESDEIDRELDRRLRSIAEKwgasNKP 80
Cdd:TIGR02173   1 MIITISGPPGSGKTTVAKILAEKLSLKLISAGDIFRELAAKMGLDLIEFLNYAEENPEIDKKIDRRIHEIALK----EKN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278  81 FVLESRLAGWLAGERADLRIYLNAPEEVRKDRISDRE-----ETAAEMSVREVNEAGRYQAYYDIDLDDRTFYDMHVNTA 155
Cdd:TIGR02173  77 VVLESRLAGWIVREYADVKIWLKAPLEVRARRIAKREgksltVARSETIEREESEKRRYLKFYGIDIDDLSIYDLVINTS 156

                         170
                  ....*....|....*.
gi 1958181278 156 RWSQEGVfRIVSAAIE 171
Cdd:TIGR02173 157 NWDPNNV-DIILDALD 171
CmkB COG1102
Cytidylate kinase [Nucleotide transport and metabolism];
1-176 6.64e-53

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440719 [Multi-domain]  Cd Length: 188  Bit Score: 167.31  E-value: 6.64e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278   1 MFVTVSGPPGCGATSLCTRLAEALDCPYVsGGEIFRDIAEERGMGLTELSAKAQ-----------ESDEIDRELDRRLRS 69
Cdd:COG1102     1 MVITISREPGSGGTTIAKRLAEKLGLPLY-DGEILREAAKERGLSEEEFEKLDEkapsllyrdtaEEDEIDRALDKVIRE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278  70 IAEKwgasnKPFVLESRLAGW-LAGERADLRIYLNAPEEVRKDRISDR-----EETAAEMSVREVNEAGRYQAYYDIDLD 143
Cdd:COG1102    80 LARK-----GNCVIVGRLADWiLRDRPNVLKVFLTAPLEVRVKRIAERegiseEEAEKEIKKRDKSRAKYYKYYYGIDWG 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1958181278 144 DRTFYDMHVNTARWSQEGVFRIVSAAIEGYDPE 176
Cdd:COG1102   155 DPSNYDLVINTSRLGIEEAVDLILAAIEAREKK 187
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
 3-144 7.08e-26

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 96.79  E-value: 7.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278   3 VTVSGPPGCGATSLCTRLAEALDCPYVSGGEIfrdiaeeRGMGLTELSAKAQESDEIDRELDRRLRSIAEKwgasnKPFV 82
Cdd:cd02020     2 IAIDGPAGSGKSTVAKLLAKKLGLPYLDTGGI-------RTEEVGKLASEVAAIPEVRKALDERQRELAKK-----PGIV 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958181278  83 LESRLAGWLAGERADLRIYLNAPEEVRKDRIS----------DREETAAEMSVREVNEAGRYQAYYDIDLDD 144
Cdd:cd02020    70 LEGRDIGTVVFPDADLKIFLTASPEVRAKRRAkqlqakgegvDLEEILAEIIERDERDSTRYVAPLKLAEDA 141
AAA_18 pfam13238
AAA domain;
3-135 1.92e-17

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 74.39  E-value: 1.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278   3 VTVSGPPGCGATSLCTRLAEALDCpyvsgGEIFRDIAEERGMgLTELSAKAQESDEIDRELDRRLRSIAEKWGA--SNKP 80
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGF-----GDNVRDLALENGL-VLGDDPETRESKRLDEDKLDRLLDLLEENAAleEGGN 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958181278  81 FVLESRLAGWLAGERADL-RIYLNAPEEVRKDRISDREETAAEMsvREVNEAGRYQ 135
Cdd:pfam13238  75 LIIDGHLAELEPERAKDLvGIVLRASPEELLERLEKRGYEEAKI--KENEEAEILG 128
 
Name Accession Description Interval E-value
PRK04182 PRK04182
cytidylate kinase; Provisional
 1-179 4.14e-86

cytidylate kinase; Provisional


Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 251.26  E-value: 4.14e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278   1 MFVTVSGPPGCGATSLCTRLAEALDCPYVSGGEIFRDIAEERGMGLTELSAKAQESDEIDRELDRRLRSIAEKwgasNKP 80
Cdd:PRK04182    1 MIITISGPPGSGKTTVARLLAEKLGLKHVSAGEIFRELAKERGMSLEEFNKYAEEDPEIDKEIDRRQLEIAEK----EDN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278  81 FVLESRLAGWLAGERADLRIYLNAPEEVRKDRISDRE----ETA-AEMSVREVNEAGRYQAYYDIDLDDRTFYDMHVNTA 155
Cdd:PRK04182   77 VVLEGRLAGWMAKDYADLKIWLKAPLEVRAERIAEREgisvEEAlEETIEREESEAKRYKEYYGIDIDDLSIYDLVINTS 156

                         170       180
                  ....*....|....*....|....
gi 1958181278 156 RWSQEGVFRIVSAAIEGYDPESDE 179
Cdd:PRK04182  157 RWDPEGVFDIILTAIDKLLKAKDE 180
cyt_kin_arch TIGR02173
cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. ...
 1-171 2.76e-57

cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. Members of this family are found in the archaea and in spirochaetes, and differ considerably from the common bacterial form of cytidylate kinase described by TIGR00017.


Pssm-ID: 274012 [Multi-domain]  Cd Length: 171  Bit Score: 178.00  E-value: 2.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278   1 MFVTVSGPPGCGATSLCTRLAEALDCPYVSGGEIFRDIAEERGMGLTELSAKAQESDEIDRELDRRLRSIAEKwgasNKP 80
Cdd:TIGR02173   1 MIITISGPPGSGKTTVAKILAEKLSLKLISAGDIFRELAAKMGLDLIEFLNYAEENPEIDKKIDRRIHEIALK----EKN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278  81 FVLESRLAGWLAGERADLRIYLNAPEEVRKDRISDRE-----ETAAEMSVREVNEAGRYQAYYDIDLDDRTFYDMHVNTA 155
Cdd:TIGR02173  77 VVLESRLAGWIVREYADVKIWLKAPLEVRARRIAKREgksltVARSETIEREESEKRRYLKFYGIDIDDLSIYDLVINTS 156

                         170
                  ....*....|....*.
gi 1958181278 156 RWSQEGVfRIVSAAIE 171
Cdd:TIGR02173 157 NWDPNNV-DIILDALD 171
CmkB COG1102
Cytidylate kinase [Nucleotide transport and metabolism];
1-176 6.64e-53

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440719 [Multi-domain]  Cd Length: 188  Bit Score: 167.31  E-value: 6.64e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278   1 MFVTVSGPPGCGATSLCTRLAEALDCPYVsGGEIFRDIAEERGMGLTELSAKAQ-----------ESDEIDRELDRRLRS 69
Cdd:COG1102     1 MVITISREPGSGGTTIAKRLAEKLGLPLY-DGEILREAAKERGLSEEEFEKLDEkapsllyrdtaEEDEIDRALDKVIRE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278  70 IAEKwgasnKPFVLESRLAGW-LAGERADLRIYLNAPEEVRKDRISDR-----EETAAEMSVREVNEAGRYQAYYDIDLD 143
Cdd:COG1102    80 LARK-----GNCVIVGRLADWiLRDRPNVLKVFLTAPLEVRVKRIAERegiseEEAEKEIKKRDKSRAKYYKYYYGIDWG 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1958181278 144 DRTFYDMHVNTARWSQEGVFRIVSAAIEGYDPE 176
Cdd:COG1102   155 DPSNYDLVINTSRLGIEEAVDLILAAIEAREKK 187
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
 3-144 7.08e-26

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 96.79  E-value: 7.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278   3 VTVSGPPGCGATSLCTRLAEALDCPYVSGGEIfrdiaeeRGMGLTELSAKAQESDEIDRELDRRLRSIAEKwgasnKPFV 82
Cdd:cd02020     2 IAIDGPAGSGKSTVAKLLAKKLGLPYLDTGGI-------RTEEVGKLASEVAAIPEVRKALDERQRELAKK-----PGIV 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958181278  83 LESRLAGWLAGERADLRIYLNAPEEVRKDRIS----------DREETAAEMSVREVNEAGRYQAYYDIDLDD 144
Cdd:cd02020    70 LEGRDIGTVVFPDADLKIFLTASPEVRAKRRAkqlqakgegvDLEEILAEIIERDERDSTRYVAPLKLAEDA 141
AAA_18 pfam13238
AAA domain;
3-135 1.92e-17

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 74.39  E-value: 1.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278   3 VTVSGPPGCGATSLCTRLAEALDCpyvsgGEIFRDIAEERGMgLTELSAKAQESDEIDRELDRRLRSIAEKWGA--SNKP 80
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGF-----GDNVRDLALENGL-VLGDDPETRESKRLDEDKLDRLLDLLEENAAleEGGN 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958181278  81 FVLESRLAGWLAGERADL-RIYLNAPEEVRKDRISDREETAAEMsvREVNEAGRYQ 135
Cdd:pfam13238  75 LIIDGHLAELEPERAKDLvGIVLRASPEELLERLEKRGYEEAKI--KENEEAEILG 128
Cytidylate_kin2 pfam13189
Cytidylate kinase-like family; This family includes enzymes related to cytidylate kinase.
 3-156 2.93e-17

Cytidylate kinase-like family; This family includes enzymes related to cytidylate kinase.


Pssm-ID: 433023 [Multi-domain]  Cd Length: 176  Bit Score: 75.36  E-value: 2.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278   3 VTVSGPPGCGATSLCTRLAEALDCPYVSGgEIFRDIAEERGMGLTEL-----------------SAKAQESDEIDRELDR 65
Cdd:pfam13189   2 ITISRQYGSGGTTIAKKLAEKLGYPFYDR-EILDEIAKELGISEEEFelfdeksrlssflyslaGGRVRGDALSDDRLFD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278  66 RLRSIAEKWgASNKPFVLESRLAGW-LAGERADLRIYLNAPEEVRKDRISDRE---ETAAEMSVREVN--EAGRYQAYYD 139
Cdd:pfam13189  81 AQSKVIREL-AAEDNCVIVGRGADYiLKDIPNVLRVFLTAPLEDRVKRVMEREglsEEEARELIKETDkrRAKYYKYYTG 159

                         170
                  ....*....|....*..
gi 1958181278 140 IDLDDRTFYDMHVNTAR 156
Cdd:pfam13189 160 KDWGDAENYDLVINTSK 176
AAA_17 pfam13207
AAA domain;
6-117 1.47e-15

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 69.58  E-value: 1.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278   6 SGPPGCGATSLCTRLAEALDCPYVSGGEIFRDIAEERGMGLTeLSAKAQESDEIDRELDRRL-RSIAEKwgASNKPFVLE 84
Cdd:pfam13207   1 TGVPGSGKTTQLKKLAEKLGFPHISAGDLLREEAKERGLVED-RDEMRKLPLEPQKELQKLAaERIAEE--AGEGGVIVD 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958181278  85 SRLAG-WLAGERA------------DLRIYLNA-PEEVRKDRISDRE 117
Cdd:pfam13207  78 GHPRIkTPAGYLPglpvevlrelkpDAIILLEAdPEEILERRLKDRT 124
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 7-116 2.89e-06

Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or related kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440329 [Multi-domain]  Cd Length: 212  Bit Score: 45.89  E-value: 2.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278   7 GPPGCGATSLCTRLAEALDCPYVSGGEIFRD-IAEErgmglTELSAKAQE--------SDEIDREL-DRRL--------- 67
Cdd:COG0563     7 GPPGAGKGTQAKRLAEKYGIPHISTGDMLRAaVKAG-----TELGKKAKEymdagelvPDEIVIGLvKERLaqpdcangf 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958181278  68 ------RSI--AEkwgasnkpfVLESRLAGwlAGERADLRIYLNAPEEVRKDRISDR 116
Cdd:COG0563    82 ildgfpRTVaqAE---------ALDELLAE--LGIKLDAVIELDVDDEELVERLSGR 127
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 1-131 7.63e-06

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: 43.84  E-value: 7.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278   1 MFVTVsGPPGCGATSLCTRLAEALDCPYVSGGEIFRDIAEERGMGLTELsakaqeSDEIDReLDRRLRSIAEKWGASNKP 80
Cdd:pfam13671   1 LILLV-GLPGSGKSTLARRLLEELGAVRLSSDDERKRLFGEGRPSISYY------TDATDR-TYERLHELARIALRAGRP 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958181278  81 FVLEsrlAGWL-AGERADLR------------IYLNAPEEVRKDRISDREETAAEMSvrEVNEA 131
Cdd:pfam13671  73 VILD---ATNLrRDERARLLalareygvpvriVVFEAPEEVLRERLAARARAGGDPS--DVPEE 131
ADK pfam00406
Adenylate kinase;
5-122 9.15e-06

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 44.22  E-value: 9.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278   5 VSGPPGCGATSLCTRLAEALDCPYVSGGEIFRD-IAEErgmglTELSAKAQE--------SDEIDRELDR-RLRSiaekw 74
Cdd:pfam00406   1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAeIKSG-----TELGKEAKEymdkgelvPDEVVVGLVKeRLEQ----- 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958181278  75 GASNKPFVL----------ESRLAGWLAGERADLRIYLNAPEEVRKDRISDREETAAE 122
Cdd:pfam00406  71 NDCKNGFLLdgfprtvpqaEALEELLERGIKLDYVIEFDVPDEVLVERLTGRRIHPNS 128
PRK03839 PRK03839
putative kinase; Provisional
 1-116 5.73e-05

putative kinase; Provisional


Pssm-ID: 179660  Cd Length: 180  Bit Score: 42.01  E-value: 5.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278   1 MFVTVSGPPGCGATSLCTRLAEALDCPYVSggeiFRDIAEERGMGltelsakAQESDEIDRELDRRLRSIAEKWgaSNKP 80
Cdd:PRK03839    1 MIIAITGTPGVGKTTVSKLLAEKLGYEYVD----LTEFALKKGIG-------EEKDDEMEIDFDKLAYFIEEEF--KEKN 67

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958181278  81 FVLESRLAGWLageRADLRIYLNAPEEVRKDRISDR 116
Cdd:PRK03839   68 VVLDGHLSHLL---PVDYVIVLRAHPKIIKERLKER 100
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 5-117 6.62e-05

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 41.08  E-value: 6.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278   5 VSGPPGCGATSLCTRLAEALDCPYVSgGEIFRDIAEERGMgltelsAKAQESDEIDRELD-RRLRSIAEKWGASNKPFV- 82
Cdd:cd02021     4 VMGVSGSGKSTVGKALAERLGAPFID-GDDLHPPANIAKM------AAGIPLNDEDRWPWlQALTDALLAKLASAGEGVv 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958181278  83 -----LESRLAGWLAGERADLR---IYLNAPEEVRKDRISDRE 117
Cdd:cd02021    77 vacsaLKRIYRDILRGGAANPRvrfVHLDGPREVLAERLAARK 119
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 5-61 4.17e-04

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 38.73  E-value: 4.17e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958181278   5 VSGPPGCGATSLCTRLAEALDCPY--VSGGEIFRDIAEERGMGLTELSAKAQES-------DEIDR 61
Cdd:pfam00004   3 LYGPPGTGKTTLAKAVAKELGAPFieISGSELVSKYVGESEKRLRELFEAAKKLapcvifiDEIDA 68
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
5-118 8.23e-04

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 38.36  E-value: 8.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278   5 VSGPPGCGATSLCTRLAEALDCPYVSggeifRDIAEERGMGltELSAKAQESDEIDRELDRRLRSIAEKWGASNKPFVLE 84
Cdd:COG0645     4 VCGLPGSGKSTLARALAERLGAVRLR-----SDVVRKRLFG--AGLAPLERSPEATARTYARLLALARELLAAGRSVILD 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958181278  85 SrlAGWLAGERADLR------------IYLNAPEEVRKDRISDREE 118
Cdd:COG0645    77 A--TFLRRAQREAFRalaeeagapfvlIWLDAPEEVLRERLEARNA 120
adk PRK02496
adenylate kinase; Provisional
 7-54 8.79e-04

adenylate kinase; Provisional


Pssm-ID: 179433 [Multi-domain]  Cd Length: 184  Bit Score: 38.58  E-value: 8.79e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958181278   7 GPPGCGATSLCTRLAEALDCPYVSGGEIFRDIAEERgmglTELSAKAQ 54
Cdd:PRK02496    8 GPPGAGKGTQAVVLAEHLHIPHISTGDILRQAIKEQ----TPLGIKAQ 51
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 7-43 9.86e-04

lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain 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: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 38.31  E-value: 9.86e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958181278   7 GPPGCGATSLCTRLAEALDCPYVS---GGeiFRDIAEERG 43
Cdd:cd19500    44 GPPGVGKTSLGKSIARALGRKFVRislGG--VRDEAEIRG 81
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 3-69 4.95e-03

first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like 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: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 36.23  E-value: 4.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278   3 VTVSGPPGCGATSLCTRLAEALDCPY--VSGGEIFRDIAEERGMGLTELSAKAQES-------DEID----------REL 63
Cdd:cd19518    37 VLLHGPPGCGKTMLANAIAGELKVPFlkISATEIVSGVSGESEEKIRELFDQAISNapcivfiDEIDaitpkresaqREM 116


                  ....*.
gi 1958181278  64 DRRLRS 69
Cdd:cd19518   117 ERRIVS 122
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 3-67 5.09e-03

first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. 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: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 36.12  E-value: 5.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958181278   3 VTVSGPPGCGATSLCTRLAEALDCPY--VSGGEIFRDIAEERGMGLTELSAKAQES-------DEID----------REL 63
Cdd:cd19503    37 VLLHGPPGTGKTLLARAVANEAGANFlsISGPSIVSKYLGESEKNLREIFEEARSHapsiifiDEIDalapkreedqREV 116


                  ....
gi 1958181278  64 DRRL 67
Cdd:cd19503   117 ERRV 120
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 7-60 7.94e-03

proteases similar to RecA; RecA-like NTPases. This family 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. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 35.34  E-value: 7.94e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958181278   7 GPPGCGATSLCTRLAEALDCP--YVSGGEIFRDIAEERGMGLTELSAKAQES-------DEID 60
Cdd:cd19481    33 GPPGTGKTLLAKALAGELGLPliVVKLSSLLSKYVGESEKNLRKIFERARRLapcilfiDEID 95
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 7-66 9.51e-03

second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). 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: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 35.34  E-value: 9.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958181278   7 GPPGCGATSLCTRLAEALDCPY--VSGGEIFRDIAEERGMGLTELSAKAQES-------DEIDRELDRR 66
Cdd:cd19511    34 GPPGCGKTLLAKALASEAGLNFisVKGPELFSKYVGESERAVREIFQKARQAapciiffDEIDSLAPRR 102
 
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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