NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|664517455|ref|WP_031034338|]
View 

AAA family ATPase [Streptomyces olivaceus]

Protein Classification

ATP-binding protein( domain architecture ID 1016174)

ATP-binding protein containing an AAA (ATPases Associated with various cellular Activities) domain, may function as an ATPase

CATH:  3.40.50.300
Gene Ontology:  GO:0005524|GO:0016887
PubMed:  18208389|16072036|11916378|15037234|15037233|17897320|18466635
SCOP:  2000039

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Kti12 super family cl29749
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 56-171 1.07e-16

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


The actual alignment was detected with superfamily member COG4088:

Pssm-ID: 443264 [Multi-domain]  Cd Length: 179  Bit Score: 74.76  E-value: 1.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664517455  56 LAVITGLPGSGKSTLMRRTVRGLR--------IDSQDTRDRWDRrmpRSVPYALYRPFVRLSHYAGLRRALRSGEGVVVH 127
Cdd:COG4088    6 LLILTGPPGSGKTTFAKALAQRLYaegiavalLHSDDFRRFLVN---ESFPKETYEEVVEDVRTTTADNALDNGYSVIVD 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 664517455 128 DCGTQAWVRAWLAREARRRgGTLHLLLLDVAPGEALAGQRERGR 171
Cdd:COG4088   83 GTFYYRSWQRDFRNLAKHK-APIHIIYLKAPLETALRRNRERGE 125
 
Name Accession Description Interval E-value
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 56-171 1.07e-16

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


Pssm-ID: 443264 [Multi-domain]  Cd Length: 179  Bit Score: 74.76  E-value: 1.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664517455  56 LAVITGLPGSGKSTLMRRTVRGLR--------IDSQDTRDRWDRrmpRSVPYALYRPFVRLSHYAGLRRALRSGEGVVVH 127
Cdd:COG4088    6 LLILTGPPGSGKTTFAKALAQRLYaegiavalLHSDDFRRFLVN---ESFPKETYEEVVEDVRTTTADNALDNGYSVIVD 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 664517455 128 DCGTQAWVRAWLAREARRRgGTLHLLLLDVAPGEALAGQRERGR 171
Cdd:COG4088   83 GTFYYRSWQRDFRNLAKHK-APIHIIYLKAPLETALRRNRERGE 125
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 56-171 6.03e-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: 44.61  E-value: 6.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664517455   56 LAVITGLPGSGKSTLMRRTVRGL---RIDSQDTRDR-WDRRMPRSVPYALYRPFVRLSHYAGLRRALRSGEGVVVHDCGT 131
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEELgavRLSSDDERKRlFGEGRPSISYYTDATDRTYERLHELARIALRAGRPVILDATNL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 664517455  132 QAWVRAWLAREARRRGGTLHLLLLDVAPGEALAGQRERGR 171
Cdd:pfam13671  81 RRDERARLLALAREYGVPVRIVVFEAPEEVLRERLAARAR 120
PNK-3'Pase TIGR01663
polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5 ...
 48-169 8.96e-04

polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5'-polynucleotide-kinase-3'-phosphatase, PNKP, which is believed to be involved in repair of oxidative DNA damage. Removal of 3' phosphates is essential for the further processing of the break by DNA polymerases. The central phosphatase domain is a member of the IIIA subfamily (TIGR01662) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. As is common in this superfamily, the enzyme is magnesium dependent. A difference between this enzyme and other HAD-superfamily phosphatases is in the third conserved catalytic motif which usually contains two conserved aspartate residues believed to be involved in binding the magnesium ion. Here, the second aspartate is replaced by a conserved arginine residue which may indicate an interaction with the phosphate backbone of the substrate. Very close relatives of this domain are also found separate from the N- and C-terminal domains seen here, as in the 3'-phosphatase found in plants. The larger family of these domains is described by TIGR01664. Outside of the phosphatase domain is a P-loop ATP-binding motif associated with the kinase activity. The entry for the mouse homolog appears to be missing a large piece of sequence corresponding to the first conserved catalytic motif of the phosphatase domain as well as the conserved threonine of the second motif. Either this is a sequencing artifact or this may represent a pseudo- or non-functional gene. Note that the EC number for the kinase function is: 2.7.1.78


Pssm-ID: 130724 [Multi-domain]  Cd Length: 526  Bit Score: 39.62  E-value: 8.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664517455   48 ALLFGPRDLAVITGLPGSGKSTLMRRTV--RGLRIDSQDTRDRWDRRMprsvpyalyrpfvrlshyAGLRRALRSGEGVV 125
Cdd:TIGR01663 363 ALDDAPCEMVIAVGFPGAGKSHFCKKFFqpAGYKHVNADTLGSTQNCL------------------TACERALDQGKRCA 424

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 664517455  126 VHDCGTQAWVRAWLAREARRRGGTLHLLLLDVAPGEALAGQRER 169
Cdd:TIGR01663 425 IDNTNPDAASRAKFLQCARAAGIPCRCFLFNAPLAQAKHNIAFR 468
uvrA PRK00349
excinuclease ABC subunit UvrA;
53-70 2.46e-03

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 38.52  E-value: 2.46e-03
                         10
                 ....*....|....*....
gi 664517455  53 PRD-LAVITGLPGSGKSTL 70
Cdd:PRK00349  24 PRDkLVVFTGLSGSGKSSL 42
 
Name Accession Description Interval E-value
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 56-171 1.07e-16

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


Pssm-ID: 443264 [Multi-domain]  Cd Length: 179  Bit Score: 74.76  E-value: 1.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664517455  56 LAVITGLPGSGKSTLMRRTVRGLR--------IDSQDTRDRWDRrmpRSVPYALYRPFVRLSHYAGLRRALRSGEGVVVH 127
Cdd:COG4088    6 LLILTGPPGSGKTTFAKALAQRLYaegiavalLHSDDFRRFLVN---ESFPKETYEEVVEDVRTTTADNALDNGYSVIVD 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 664517455 128 DCGTQAWVRAWLAREARRRgGTLHLLLLDVAPGEALAGQRERGR 171
Cdd:COG4088   83 GTFYYRSWQRDFRNLAKHK-APIHIIYLKAPLETALRRNRERGE 125
COG4639 COG4639
Predicted kinase [General function prediction only];
61-183 1.62e-10

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 57.15  E-value: 1.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664517455  61 GLPGSGKSTLMRRTVRGLRIDSQDT------RDRWDRRMPRSVpyalyrpfVRLSHYAgLRRALRSGEGVVVHDCGTQAW 134
Cdd:COG4639    9 GLPGSGKSTFARRLFAPTEVVSSDDirallgGDENDQSAWGDV--------FQLAHEI-ARARLRAGRLTVVDATNLQRE 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 664517455 135 VRAWLAREARRRGGTLHLLLLDVAPGEALAGQRERGRGVSRYAFLRHRR 183
Cdd:COG4639   80 ARRRLLALARAYGALVVAVVLDVPLEVCLARNAARDRQVPEEVIRRMLR 128
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
56-171 8.03e-09

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 52.99  E-value: 8.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664517455  56 LAVITGLPGSGKSTLMRRTVRGL---RIDSQDTRDRW-DRRMPRSVPYALYRPFVRLSHYAGLRRALRSGEGVVVHDCGT 131
Cdd:COG0645    1 LILVCGLPGSGKSTLARALAERLgavRLRSDVVRKRLfGAGLAPLERSPEATARTYARLLALARELLAAGRSVILDATFL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 664517455 132 QAWVRAWLAREARRRGGTLHLLLLDVAPGEALAGQRERGR 171
Cdd:COG0645   81 RRAQREAFRALAEEAGAPFVLIWLDAPEEVLRERLEARNA 120
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 56-171 6.03e-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: 44.61  E-value: 6.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664517455   56 LAVITGLPGSGKSTLMRRTVRGL---RIDSQDTRDR-WDRRMPRSVPYALYRPFVRLSHYAGLRRALRSGEGVVVHDCGT 131
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEELgavRLSSDDERKRlFGEGRPSISYYTDATDRTYERLHELARIALRAGRPVILDATNL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 664517455  132 QAWVRAWLAREARRRGGTLHLLLLDVAPGEALAGQRERGR 171
Cdd:pfam13671  81 RRDERARLLALAREYGVPVRIVVFEAPEEVLRERLAARAR 120
PNK-3'Pase TIGR01663
polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5 ...
 48-169 8.96e-04

polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5'-polynucleotide-kinase-3'-phosphatase, PNKP, which is believed to be involved in repair of oxidative DNA damage. Removal of 3' phosphates is essential for the further processing of the break by DNA polymerases. The central phosphatase domain is a member of the IIIA subfamily (TIGR01662) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. As is common in this superfamily, the enzyme is magnesium dependent. A difference between this enzyme and other HAD-superfamily phosphatases is in the third conserved catalytic motif which usually contains two conserved aspartate residues believed to be involved in binding the magnesium ion. Here, the second aspartate is replaced by a conserved arginine residue which may indicate an interaction with the phosphate backbone of the substrate. Very close relatives of this domain are also found separate from the N- and C-terminal domains seen here, as in the 3'-phosphatase found in plants. The larger family of these domains is described by TIGR01664. Outside of the phosphatase domain is a P-loop ATP-binding motif associated with the kinase activity. The entry for the mouse homolog appears to be missing a large piece of sequence corresponding to the first conserved catalytic motif of the phosphatase domain as well as the conserved threonine of the second motif. Either this is a sequencing artifact or this may represent a pseudo- or non-functional gene. Note that the EC number for the kinase function is: 2.7.1.78


Pssm-ID: 130724 [Multi-domain]  Cd Length: 526  Bit Score: 39.62  E-value: 8.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664517455   48 ALLFGPRDLAVITGLPGSGKSTLMRRTV--RGLRIDSQDTRDRWDRRMprsvpyalyrpfvrlshyAGLRRALRSGEGVV 125
Cdd:TIGR01663 363 ALDDAPCEMVIAVGFPGAGKSHFCKKFFqpAGYKHVNADTLGSTQNCL------------------TACERALDQGKRCA 424

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 664517455  126 VHDCGTQAWVRAWLAREARRRGGTLHLLLLDVAPGEALAGQRER 169
Cdd:TIGR01663 425 IDNTNPDAASRAKFLQCARAAGIPCRCFLFNAPLAQAKHNIAFR 468
uvrA PRK00349
excinuclease ABC subunit UvrA;
53-70 2.46e-03

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 38.52  E-value: 2.46e-03
                         10
                 ....*....|....*....
gi 664517455  53 PRD-LAVITGLPGSGKSTL 70
Cdd:PRK00349  24 PRDkLVVFTGLSGSGKSSL 42
PRK04040 PRK04040
adenylate kinase; Provisional
 58-81 3.11e-03

adenylate kinase; Provisional


Pssm-ID: 235210  Cd Length: 188  Bit Score: 37.18  E-value: 3.11e-03
                         10        20
                 ....*....|....*....|....
gi 664517455  58 VITGLPGSGKSTLMRRTVRGLRID 81
Cdd:PRK04040   6 VVTGVPGVGKTTVLNKALEKLKED 29
THEP1 COG1618
Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];
57-79 4.70e-03

Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];


Pssm-ID: 441225 [Multi-domain]  Cd Length: 175  Bit Score: 36.42  E-value: 4.70e-03
                         10        20
                 ....*....|....*....|...
gi 664517455  57 AVITGLPGSGKSTLMRRTVRGLR 79
Cdd:COG1618    3 IFITGRPGVGKTTLLLKVVEELR 25
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH