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Conserved domains on  [gi|334188524|ref|NP_200842|]
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P-loop containing nucleoside triphosphate hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

adenylate kinase family protein( domain architecture ID 1904751)

adenylate kinase family protein such as adenylate kinase isoenzyme 6 that has ATPase activity and is a broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates

CATH:  3.40.50.300
EC:  2.7.4.-
Gene Ontology:  GO:0005524|GO:0016887|GO:0050145
SCOP:  4004025

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Fap7 super family cl42788
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
16-162 2.97e-32

Broad-specificity NMP kinase [Nucleotide transport and metabolism];


The actual alignment was detected with superfamily member COG1936:

Pssm-ID: 441539 [Multi-domain]  Cd Length: 173  Bit Score: 113.37  E-value: 2.97e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188524  16 LLITGTPGTGKSTTASALAEATNLRYICIGDLVKEKEFYHGWDNELECHFINEDSVIDELDDaMIEGGNIVDYHGCDFFP 95
Cdd:COG1936    3 IAITGTPGTGKTTVAKLLAERLGLEVIHLNDLVKEEGLYTEVDEERDSLVVDEDALAEELEE-LKEGDVIIEGHLAHLVD 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334188524  96 qrwFDRVVVLRTENSVLYDRLTNRGYSGTKLSNNLQCEMYQVLLEEAHDSYDEEIVTELQ--SNTIEDI 162
Cdd:COG1936   82 ---VDRVIVLRCNPEVLEERLEERGYSEEKIRENVEAEALDVILSEAVERFGEEKVYEIDttGRTPEEV 147
 
Name Accession Description Interval E-value
Fap7 COG1936
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
16-162 2.97e-32

Broad-specificity NMP kinase [Nucleotide transport and metabolism];


Pssm-ID: 441539 [Multi-domain]  Cd Length: 173  Bit Score: 113.37  E-value: 2.97e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188524  16 LLITGTPGTGKSTTASALAEATNLRYICIGDLVKEKEFYHGWDNELECHFINEDSVIDELDDaMIEGGNIVDYHGCDFFP 95
Cdd:COG1936    3 IAITGTPGTGKTTVAKLLAERLGLEVIHLNDLVKEEGLYTEVDEERDSLVVDEDALAEELEE-LKEGDVIIEGHLAHLVD 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334188524  96 qrwFDRVVVLRTENSVLYDRLTNRGYSGTKLSNNLQCEMYQVLLEEAHDSYDEEIVTELQ--SNTIEDI 162
Cdd:COG1936   82 ---VDRVIVLRCNPEVLEERLEERGYSEEKIRENVEAEALDVILSEAVERFGEEKVYEIDttGRTPEEV 147
AAA_18 pfam13238
AAA domain;
17-133 5.41e-27

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 98.65  E-value: 5.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188524   17 LITGTPGTGKSTTASALAEATNLRYIcIGDLVKEKEFYHGWDNEL-ECHFINED---SVIDELD--DAMIEGGN-IVDYH 89
Cdd:pfam13238   2 LITGTPGVGKTTLAKELSKRLGFGDN-VRDLALENGLVLGDDPETrESKRLDEDkldRLLDLLEenAALEEGGNlIIDGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 334188524   90 GCDFFPQRWFDRV-VVLRTENSVLYDRLTNRGYSGTKLSNNLQCE 133
Cdd:pfam13238  81 LAELEPERAKDLVgIVLRASPEELLERLEKRGYEEAKIKENEEAE 125
PRK03839 PRK03839
putative kinase; Provisional
 18-169 1.14e-19

putative kinase; Provisional


Pssm-ID: 179660  Cd Length: 180  Bit Score: 81.30  E-value: 1.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188524  18 ITGTPGTGKSTTASALAEATNLRYICIGDLVKEKEFYHGWDNELECHFINEDSVIDElddaMIEGGNIV-DYHGCDFFPQ 96
Cdd:PRK03839   5 ITGTPGVGKTTVSKLLAEKLGYEYVDLTEFALKKGIGEEKDDEMEIDFDKLAYFIEE----EFKEKNVVlDGHLSHLLPV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334188524  97 rwfDRVVVLRTENSVLYDRLTNRGYSGTKLSNNLQCEMYQVLLEEAHDSYDEEIVTELQSNTIEDISNNVSTL 169
Cdd:PRK03839  81 ---DYVIVLRAHPKIIKERLKERGYSKKKILENVEAELVDVCLCEALEEKEKVIEVDTTGKTPEEVVEEILEL 150
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 15-120 3.38e-07

Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine triphosphates (ATP) to adenosine monophosphates (AMP) and to yield adenosine diphosphates (ADP). This enzyme is required for the biosynthesis of ADP and is essential for homeostasis of adenosine phosphates.


Pssm-ID: 238713 [Multi-domain]  Cd Length: 194  Bit Score: 48.00  E-value: 3.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188524  15 NLLITGTPGTGKSTTASALAEATNLRYICIGDLVKEKefyhgwdnelechfINEDSVIDELDDAMIEGGNIVD------- 87
Cdd:cd01428    1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREE--------------IASGTELGKKAKEYIDSGKLVPdeivikl 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188524  88 ----------YHGC--DFFP------QRWF---------DRVVVLRTENSVLYDRLTNRG 120
Cdd:cd01428   67 lkerlkkpdcKKGFilDGFPrtvdqaEALDelldegikpDKVIELDVPDEVLIERILGRR 126
cyt_kin_arch TIGR02173
cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. ...
 18-119 5.67e-06

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: 44.34  E-value: 5.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188524   18 ITGTPGTGKSTTASALAEATNLRYICIGDLVKEKEFYHGWDNELECHFINEDSVIDELDD------AMIEGGNIVDYHGC 91
Cdd:TIGR02173   5 ISGPPGSGKTTVAKILAEKLSLKLISAGDIFRELAAKMGLDLIEFLNYAEENPEIDKKIDrriheiALKEKNVVLESRLA 84

                          90       100
                  ....*....|....*....|....*...
gi 334188524   92 DFFPQRWFDRVVVLRTENSVLYDRLTNR 119
Cdd:TIGR02173  85 GWIVREYADVKIWLKAPLEVRARRIAKR 112
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 13-34 2.15e-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: 36.97  E-value: 2.15e-03
                           10        20
                   ....*....|....*....|..
gi 334188524    13 RPNLLITGTPGTGKSTTASALA 34
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALA 23
 
Name Accession Description Interval E-value
Fap7 COG1936
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
16-162 2.97e-32

Broad-specificity NMP kinase [Nucleotide transport and metabolism];


Pssm-ID: 441539 [Multi-domain]  Cd Length: 173  Bit Score: 113.37  E-value: 2.97e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188524  16 LLITGTPGTGKSTTASALAEATNLRYICIGDLVKEKEFYHGWDNELECHFINEDSVIDELDDaMIEGGNIVDYHGCDFFP 95
Cdd:COG1936    3 IAITGTPGTGKTTVAKLLAERLGLEVIHLNDLVKEEGLYTEVDEERDSLVVDEDALAEELEE-LKEGDVIIEGHLAHLVD 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334188524  96 qrwFDRVVVLRTENSVLYDRLTNRGYSGTKLSNNLQCEMYQVLLEEAHDSYDEEIVTELQ--SNTIEDI 162
Cdd:COG1936   82 ---VDRVIVLRCNPEVLEERLEERGYSEEKIRENVEAEALDVILSEAVERFGEEKVYEIDttGRTPEEV 147
AAA_18 pfam13238
AAA domain;
17-133 5.41e-27

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 98.65  E-value: 5.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188524   17 LITGTPGTGKSTTASALAEATNLRYIcIGDLVKEKEFYHGWDNEL-ECHFINED---SVIDELD--DAMIEGGN-IVDYH 89
Cdd:pfam13238   2 LITGTPGVGKTTLAKELSKRLGFGDN-VRDLALENGLVLGDDPETrESKRLDEDkldRLLDLLEenAALEEGGNlIIDGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 334188524   90 GCDFFPQRWFDRV-VVLRTENSVLYDRLTNRGYSGTKLSNNLQCE 133
Cdd:pfam13238  81 LAELEPERAKDLVgIVLRASPEELLERLEKRGYEEAKIKENEEAE 125
PRK03839 PRK03839
putative kinase; Provisional
 18-169 1.14e-19

putative kinase; Provisional


Pssm-ID: 179660  Cd Length: 180  Bit Score: 81.30  E-value: 1.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188524  18 ITGTPGTGKSTTASALAEATNLRYICIGDLVKEKEFYHGWDNELECHFINEDSVIDElddaMIEGGNIV-DYHGCDFFPQ 96
Cdd:PRK03839   5 ITGTPGVGKTTVSKLLAEKLGYEYVDLTEFALKKGIGEEKDDEMEIDFDKLAYFIEE----EFKEKNVVlDGHLSHLLPV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334188524  97 rwfDRVVVLRTENSVLYDRLTNRGYSGTKLSNNLQCEMYQVLLEEAHDSYDEEIVTELQSNTIEDISNNVSTL 169
Cdd:PRK03839  81 ---DYVIVLRAHPKIIKERLKERGYSKKKILENVEAELVDVCLCEALEEKEKVIEVDTTGKTPEEVVEEILEL 150
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 15-120 3.38e-07

Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine triphosphates (ATP) to adenosine monophosphates (AMP) and to yield adenosine diphosphates (ADP). This enzyme is required for the biosynthesis of ADP and is essential for homeostasis of adenosine phosphates.


Pssm-ID: 238713 [Multi-domain]  Cd Length: 194  Bit Score: 48.00  E-value: 3.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188524  15 NLLITGTPGTGKSTTASALAEATNLRYICIGDLVKEKefyhgwdnelechfINEDSVIDELDDAMIEGGNIVD------- 87
Cdd:cd01428    1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREE--------------IASGTELGKKAKEYIDSGKLVPdeivikl 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188524  88 ----------YHGC--DFFP------QRWF---------DRVVVLRTENSVLYDRLTNRG 120
Cdd:cd01428   67 lkerlkkpdcKKGFilDGFPrtvdqaEALDelldegikpDKVIELDVPDEVLIERILGRR 126
cyt_kin_arch TIGR02173
cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. ...
 18-119 5.67e-06

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: 44.34  E-value: 5.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188524   18 ITGTPGTGKSTTASALAEATNLRYICIGDLVKEKEFYHGWDNELECHFINEDSVIDELDD------AMIEGGNIVDYHGC 91
Cdd:TIGR02173   5 ISGPPGSGKTTVAKILAEKLSLKLISAGDIFRELAAKMGLDLIEFLNYAEENPEIDKKIDrriheiALKEKNVVLESRLA 84

                          90       100
                  ....*....|....*....|....*...
gi 334188524   92 DFFPQRWFDRVVVLRTENSVLYDRLTNR 119
Cdd:TIGR02173  85 GWIVREYADVKIWLKAPLEVRARRIAKR 112
PRK04182 PRK04182
cytidylate kinase; Provisional
 18-50 1.13e-05

cytidylate kinase; Provisional


Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 43.64  E-value: 1.13e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 334188524  18 ITGTPGTGKSTTASALAEATNLRYICIGDLVKE 50
Cdd:PRK04182   5 ISGPPGSGKTTVARLLAEKLGLKHVSAGEIFRE 37
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
13-42 5.75e-05

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 42.18  E-value: 5.75e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 334188524  13 RPNLLITGTPGTGKSTTASALAEATNLRYI 42
Cdd:COG1223   35 PRKILFYGPPGTGKTMLAEALAGELKLPLL 64
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 10-77 7.66e-05

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 40.98  E-value: 7.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188524  10 RRERPNLLITGTPGTGKSTTASALAEAT---NLRYICI-------GDLVKEKEFYHGWDNELEchfINEDS-----VIDE 74
Cdd:cd00009   16 LPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLnasdlleGLVVAELFGHFLVRLLFE---LAEKAkpgvlFIDE 92


                 ...
gi 334188524  75 LDD 77
Cdd:cd00009   93 IDS 95
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 16-42 7.70e-05

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: 40.65  E-value: 7.70e-05
                          10        20
                  ....*....|....*....|....*..
gi 334188524   16 LLITGTPGTGKSTTASALAEATNLRYI 42
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFI 27
PRK06217 PRK06217
hypothetical protein; Validated
 15-119 9.62e-05

hypothetical protein; Validated


Pssm-ID: 168472  Cd Length: 183  Bit Score: 41.19  E-value: 9.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188524  15 NLLITGTPGTGKSTTASALAEATNLRYICIGD---LVKEKEFYHGWDNELECHFINEDSVIDElddAMIEGGNIVDYhGC 91
Cdd:PRK06217   3 RIHITGASGSGTTTLGAALAERLDIPHLDTDDyfwLPTDPPFTTKRPPEERLRLLLEDLRPRE---GWVLSGSALGW-GD 78

                         90       100
                 ....*....|....*....|....*...
gi 334188524  92 DFFPQrwFDRVVVLRTENSVLYDRLTNR 119
Cdd:PRK06217  79 PLEPL--FDLVVFLTIPPELRLERLRLR 104
AAA_17 pfam13207
AAA domain;
19-89 9.82e-05

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 40.30  E-value: 9.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188524   19 TGTPGTGKSTTASALAEATNLRYICIGDLVKE--KEfyHGWDNELEcHFINEDSVIDELDDAMI---------EGGNIVD 87
Cdd:pfam13207   1 TGVPGSGKTTQLKKLAEKLGFPHISAGDLLREeaKE--RGLVEDRD-EMRKLPLEPQKELQKLAaeriaeeagEGGVIVD 77


                  ..
gi 334188524   88 YH 89
Cdd:pfam13207  78 GH 79
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 16-42 1.46e-04

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: 39.93  E-value: 1.46e-04
                         10        20
                 ....*....|....*....|....*..
gi 334188524  16 LLITGTPGTGKSTTASALAEATNLRYI 42
Cdd:cd02021    2 IVVMGVSGSGKSTVGKALAERLGAPFI 28
rfc PRK00440
replication factor C small subunit; Reviewed
 8-34 1.82e-04

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 40.63  E-value: 1.82e-04
                         10        20
                 ....*....|....*....|....*..
gi 334188524   8 VTRRERPNLLITGTPGTGKSTTASALA 34
Cdd:PRK00440  33 VKEKNMPHLLFAGPPGTGKTTAALALA 59
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 16-44 1.97e-04

MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 40.54  E-value: 1.97e-04
                         10        20
                 ....*....|....*....|....*....
gi 334188524  16 LLITGTPGTGKSTTASALAEATNLRYICI 44
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRI 62
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
16-44 3.33e-04

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 39.13  E-value: 3.33e-04
                         10        20
                 ....*....|....*....|....*....
gi 334188524  16 LLITGTPGTGKSTTASALAEATNLRYICI 44
Cdd:COG0645    2 ILVCGLPGSGKSTLARALAERLGAVRLRS 30
CmkB COG1102
Cytidylate kinase [Nucleotide transport and metabolism];
18-86 5.52e-04

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440719 [Multi-domain]  Cd Length: 188  Bit Score: 39.04  E-value: 5.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188524  18 ITGTPGTGKSTTASALAEATNLRYIcIGDLVKE------------KEFYHGWDNELECHFINEDSVIDELDDAMIE---G 82
Cdd:COG1102    5 ISREPGSGGTTIAKRLAEKLGLPLY-DGEILREaakerglseeefEKLDEKAPSLLYRDTAEEDEIDRALDKVIRElarK 83


                 ....
gi 334188524  83 GNIV 86
Cdd:COG1102   84 GNCV 87
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 2-42 7.70e-04

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 39.12  E-value: 7.70e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 334188524   2 ARRNRGVTRRERpnLLITGTPGTGKSTTASALAEATNLRYI 42
Cdd:COG0464  182 LREEYGLPPPRG--LLLYGPPGTGKTLLARALAGELGLPLI 220
PRK14531 PRK14531
adenylate kinase; Provisional
 16-120 1.20e-03

adenylate kinase; Provisional


Pssm-ID: 172997 [Multi-domain]  Cd Length: 183  Bit Score: 37.87  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188524  16 LLITGTPGTGKSTTASALAEATNLRYICIGDLVKeKEFYHGWD--NELECHFINEDSVIDELDDAMIEgGNIVDYHG--- 90
Cdd:PRK14531   5 LLFLGPPGAGKGTQAARLCAAHGLRHLSTGDLLR-SEVAAGSAlgQEAEAVMNRGELVSDALVLAIVE-SQLKALNSggw 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 334188524  91 -CDFFP----------------QRWFDRVVVLRTENSVLYDRLTNRG 120
Cdd:PRK14531  83 lLDGFPrtvaqaealeplleelKQPIEAVVLLELDDAVLIERLLARG 129
AAA_28 pfam13521
AAA domain;
18-42 1.40e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 37.63  E-value: 1.40e-03
                          10        20
                  ....*....|....*....|....*
gi 334188524   18 ITGTPGTGKSTTASALAEATNLRYI 42
Cdd:pfam13521   4 ITGGPSTGKTTLAEALAARFGYPVV 28
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 14-42 1.56e-03

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 38.14  E-value: 1.56e-03
                         10        20
                 ....*....|....*....|....*....
gi 334188524  14 PNLLITGTPGTGKSTTASALAEATNLRYI 42
Cdd:PRK13342  37 SSMILWGPPGTGKTTLARIIAGATDAPFE 65
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 13-36 1.70e-03

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 38.03  E-value: 1.70e-03
                         10        20
                 ....*....|....*....|....
gi 334188524  13 RPNLLITGTPGTGKSTTASALAEA 36
Cdd:COG0507  140 RRVSVLTGGAGTGKTTTLRALLAA 163
aroK PRK00131
shikimate kinase; Reviewed
 10-51 2.08e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 37.09  E-value: 2.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 334188524  10 RRERPNLLITGTPGTGKSTTASALAEATNLRYICIGDLVKEK 51
Cdd:PRK00131   1 MLKGPNIVLIGFMGAGKSTIGRLLAKRLGYDFIDTDHLIEAR 42
Pgk2 COG2074
2-phosphoglycerate kinase/Mevalonate-3-phosphate 5-kinase [Carbohydrate transport and ...
 16-50 2.14e-03

2-phosphoglycerate kinase/Mevalonate-3-phosphate 5-kinase [Carbohydrate transport and metabolism, Lipid transport and metabolism];


Pssm-ID: 441677  Cd Length: 207  Bit Score: 37.24  E-value: 2.14e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 334188524  16 LLITGTPGTGKSTTASALAEATNLRYICIGDLVKE 50
Cdd:COG2074    9 ILIGGASGVGKSTIAAELARRLGIPRVISTDSIRE 43
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 13-34 2.15e-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: 36.97  E-value: 2.15e-03
                           10        20
                   ....*....|....*....|..
gi 334188524    13 RPNLLITGTPGTGKSTTASALA 34
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALA 23
PRK13764 PRK13764
ATPase; Provisional
 17-35 2.41e-03

ATPase; Provisional


Pssm-ID: 184311 [Multi-domain]  Cd Length: 602  Bit Score: 37.51  E-value: 2.41e-03
                         10
                 ....*....|....*....
gi 334188524  17 LITGTPGTGKSTTASALAE 35
Cdd:PRK13764 261 LIAGAPGAGKSTFAQALAE 279
PilT cd01131
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein ...
 1-55 2.82e-03

Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein responsible for the retraction of type IV pili, likely by pili disassembly. This retraction provides the force required for travel of bacteria in low water environments by a mechanism known as twitching motility.


Pssm-ID: 410875 [Multi-domain]  Cd Length: 223  Bit Score: 37.13  E-value: 2.82e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 334188524   1 MARRNRGVtrrerpnLLITGTPGTGKSTTASALAEATNLRY----ICIGDLVkekEFYH 55
Cdd:cd01131   16 LALKPRGL-------VLVTGPTGSGKSTTLAAMIDYINETRskhiITIEDPI---EFVH 64
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 8-36 2.85e-03

Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440295 [Multi-domain]  Cd Length: 189  Bit Score: 36.61  E-value: 2.85e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 334188524   8 VTRRERPNLL--------ITGTPGTGKSTTASALAEA 36
Cdd:COG0529    3 VTREERAALKgqkgfvvwFTGLSGSGKSTLANALERR 39
PTZ00088 PTZ00088
adenylate kinase 1; Provisional
 16-51 3.28e-03

adenylate kinase 1; Provisional


Pssm-ID: 240262 [Multi-domain]  Cd Length: 229  Bit Score: 36.70  E-value: 3.28e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 334188524  16 LLITGTPGTGKSTTASALAEATNLRYICIGDLVKEK 51
Cdd:PTZ00088   9 IVLFGAPGVGKGTFAEILSKKENLKHINMGNILREE 44
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
6-35 5.38e-03

Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 36.36  E-value: 5.38e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 334188524   6 RGVTRRERP-NLLITGTPGTGKSTTASALAE 35
Cdd:COG1474   43 RPALRGERPsNVLIYGPTGTGKTAVAKYVLE 73
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
11-36 7.10e-03

DNA polymerase III, delta prime subunit [Replication, recombination and repair];


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 36.11  E-value: 7.10e-03
                         10        20
                 ....*....|....*....|....*.
gi 334188524  11 RERPNLLITGTPGTGKSTTASALAEA 36
Cdd:COG0470   16 RLPHALLLHGPPGIGKTTLALALARD 41
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 4-36 8.12e-03

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 35.68  E-value: 8.12e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 334188524   4 RNRGVTRRERPNLLITGTPGTGKSTTASALAEA 36
Cdd:PRK09270  24 AALQAEPQRRTIVGIAGPPGAGKSTLAEFLEAL 56
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 3-44 8.20e-03

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_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: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 35.23  E-value: 8.20e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 334188524   3 RRNR-GVTRRERP--NLLITGTPGTGKSTTASALAEA---TNLRYICI 44
Cdd:cd19499   28 RRARaGLSDPNRPigSFLFLGPTGVGKTELAKALAELlfgDEDNLIRI 75
44 PHA02544
clamp loader, small subunit; Provisional
 8-44 9.56e-03

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 35.74  E-value: 9.56e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 334188524   8 VTRRERPN-LLITGTPGTGKSTTASALAEATNLRYICI 44
Cdd:PHA02544  37 VKKGRIPNmLLHSPSPGTGKTTVAKALCNEVGAEVLFV 74
 
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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