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Conserved domains on  [gi|507085969|ref|WP_016156710|]
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MULTISPECIES: ATP-binding protein [Citrobacter]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 1-249 3.83e-160

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member PRK12377:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 248  Bit Score: 443.51  E-value: 3.83e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969   1 MKNIvNSGNALERLKKLIPPGVQPKFTSAAELLAWQREEGLKHCEELGKRNQKARTEKIFGRSGIQSLHRSCTFANYQVS 80
Cdd:PRK12377   1 MKNI-ATGGVLERIRRLAPQGVQPPFRTVDEWREWQLAEGRKRSEEINRQNQQLRVEKILNRSGIQPLHRKCSFANYQVQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969  81 GEGQRKAFTMAKSYAQNFGTGFASFVFSGGPGTGKNHLAAAIGNHLLSGGHSVLVVTIPDLMLRVRECYDGGQSEAALLD 160
Cdd:PRK12377  80 NDGQRYALSQAKSIADELMTGCTNFVFSGKPGTGKNHLAAAIGNRLLAKGRSVIVVTVPDVMSRLHESYDNGQSGEKFLQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969 161 DLCKVDLLVLDEVGIQRGSNGEKVILNQVIDRRLSSMRPVGILTNLNHEELLGALGARVIDRLQMDGGMWVNFDWGSYRK 240
Cdd:PRK12377 160 ELCKVDLLVLDEIGIQRETKNEQVVLNQIIDRRTASMRSVGMLTNLNHEAMSTLLGERVMDRMTMNGGRWVNFNWESWRP 239


                 ....*....
gi 507085969 241 NVSHLRIVK 249
Cdd:PRK12377 240 NVSHLRIVK 248
 
Name Accession Description Interval E-value
PRK12377 PRK12377
putative replication protein; Provisional
 1-249 3.83e-160

putative replication protein; Provisional


Pssm-ID: 183482 [Multi-domain]  Cd Length: 248  Bit Score: 443.51  E-value: 3.83e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969   1 MKNIvNSGNALERLKKLIPPGVQPKFTSAAELLAWQREEGLKHCEELGKRNQKARTEKIFGRSGIQSLHRSCTFANYQVS 80
Cdd:PRK12377   1 MKNI-ATGGVLERIRRLAPQGVQPPFRTVDEWREWQLAEGRKRSEEINRQNQQLRVEKILNRSGIQPLHRKCSFANYQVQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969  81 GEGQRKAFTMAKSYAQNFGTGFASFVFSGGPGTGKNHLAAAIGNHLLSGGHSVLVVTIPDLMLRVRECYDGGQSEAALLD 160
Cdd:PRK12377  80 NDGQRYALSQAKSIADELMTGCTNFVFSGKPGTGKNHLAAAIGNRLLAKGRSVIVVTVPDVMSRLHESYDNGQSGEKFLQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969 161 DLCKVDLLVLDEVGIQRGSNGEKVILNQVIDRRLSSMRPVGILTNLNHEELLGALGARVIDRLQMDGGMWVNFDWGSYRK 240
Cdd:PRK12377 160 ELCKVDLLVLDEIGIQRETKNEQVVLNQIIDRRTASMRSVGMLTNLNHEAMSTLLGERVMDRMTMNGGRWVNFNWESWRP 239


                 ....*....
gi 507085969 241 NVSHLRIVK 249
Cdd:PRK12377 240 NVSHLRIVK 248
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
106-240 5.10e-22

DNA replication protein DnaC [Replication, recombination and repair];


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 91.00  E-value: 5.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969 106 VFSGGPGTGKNHLAAAIGNHLLSGGHSVLVVTIPDLMLRVRECYDGGqSEAALLDDLCKVDLLVLDEVGIQRGSNGEKVI 185
Cdd:COG1484  103 ILLGPPGTGKTHLAIALGHEACRAGYRVRFTTAPDLVNELKEARADG-RLERLLKRLAKVDLLILDELGYLPLDAEGAEL 181

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969 186 LNQVIDRRlSSMRPVGILTNLNHEELLGALG-----ARVIDRLqMDGGMWVNFDWGSYRK 240
Cdd:COG1484  182 LFELISDR-YERRSTIITSNLPFSEWGEVFGdptlaTAILDRL-VHHAHIIELKGESYRL 239
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 106-240 2.47e-17

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 78.28  E-value: 2.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969 106 VFSGGPGTGKNHLAAAIGNHLLSGGHSVLVVTIPDLMLRVRECYDGGQSEaALLDDLCKVDLLVLDEVGIQRGSNGEKVI 185
Cdd:NF038214  94 LLLGPPGTGKTHLAIALGYAACRQGYRVRFTTAADLVEQLAQARADGRLG-RLLRRLARYDLLIIDELGYLPFSREGANL 172

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507085969 186 LNQVIDRRL--SSMrpvgILT-NLNHEE---LLG--ALGARVIDRLqMDGGMWVNFDWGSYRK 240
Cdd:NF038214 173 LFELIADRYerGST----IITsNLPFSEwgeVFGdpTLAAAILDRL-VHHAHILELKGESYRL 230
IstB_IS21 pfam01695
IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is ...
 106-223 1.25e-13

IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is found associated with IS21 family insertion sequences. The function of this protein is unknown, but it may perform a transposase function.


Pssm-ID: 426385 [Multi-domain]  Cd Length: 238  Bit Score: 68.24  E-value: 1.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969  106 VFSGGPGTGKNHLAAAIGNHLLSGGHSVLVVTIPDLMLRVRECYDGGQSEAAlLDDLCKVDLLVLDEVGIQRGSNGEKVI 185
Cdd:pfam01695  96 VLLGPPGVGKTHLAIALGVEACRAGYSVRFTSAADLVNQLKRAHGDGKLTRK-LQQLLKPDVLILDEWGYLPLDQAEANL 174

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 507085969  186 LNQVIDRRLSSmRPVGILTNLNHEE---LLG--ALGARVIDRL 223
Cdd:pfam01695 175 LFQVISKRYEH-RSIILTSNLPFGEwgqVFGdaVLATAILDRL 216
DnaA TIGR00362
chromosomal replication initiator protein DnaA; DnaA is involved in DNA biosynthesis; ...
 1-127 5.46e-10

chromosomal replication initiator protein DnaA; DnaA is involved in DNA biosynthesis; initiation of chromosome replication and can also be transcription regulator. The C-terminal of the family hits the pfam bacterial DnaA (bac_dnaA) domain family. For a review, see Kaguni (2006). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273037 [Multi-domain]  Cd Length: 437  Bit Score: 58.70  E-value: 5.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969    1 MKNIVNSgNALERLKK----LIPPGVQPKFTSaaellaWQREEGLKHCEELGKRNQKARTEKIFGRSGIQSLHrscTFAN 76
Cdd:TIGR00362  43 VKEWIEK-NYLDLIEEllqeLFGAEIEIEFTV------GEDEEELEPNSKKPEPAPPEAPAPPSSASGLNPKY---TFDN 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 507085969   77 YqVSGEGQRKAFTMAKSYAQNFGTGFASFVFSGGPGTGKNHLAAAIGNHLL 127
Cdd:TIGR00362 113 F-VVGKSNRLAHAAALAVAENPGKAYNPLFIYGGVGLGKTHLLHAIGNEIL 162
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 83-226 2.40e-09

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: 54.46  E-value: 2.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969  83 GQRKAFTMAKSYAQNfgTGFASFVFSGGPGTGKNHLAAAIGNHLLSGGHSVLVVTIPDLMLRVRECYDGGQSEAALLDDL 162
Cdd:cd00009    2 GQEEAIEALREALEL--PPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFEL 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507085969 163 ---CKVDLLVLDEVG-IQRGSNGEKV-ILNQVIDRRLSS--MRPVGILTNLNHEELLGALGARVIDRLQMD 226
Cdd:cd00009   80 aekAKPGVLFIDEIDsLSRGAQNALLrVLETLNDLRIDRenVRVIGATNRPLLGDLDRALYDRLDIRIVIP 150
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 107-226 6.64e-06

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: 44.67  E-value: 6.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969   107 FSGGPGTGKNHLAAAIGNHLLSGGHSVLVVTIPDLMLRVREC------------YDGGQSEAALLDDL--CKVDLLVLDE 172
Cdd:smart00382   7 IVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQllliivggkkasGSGELRLRLALALArkLKPDVLILDE 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 507085969   173 VG---IQRGSNGEKVILNQVIDRRLSSMRPVGIL--TNLNHEELLGALGARVIDRLQMD 226
Cdd:smart00382  87 ITsllDAEQEALLLLLEELRLLLLLKSEKNLTVIltTNDEKDLGPALLRRRFDRRIVLL 145
 
Name Accession Description Interval E-value
PRK12377 PRK12377
putative replication protein; Provisional
 1-249 3.83e-160

putative replication protein; Provisional


Pssm-ID: 183482 [Multi-domain]  Cd Length: 248  Bit Score: 443.51  E-value: 3.83e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969   1 MKNIvNSGNALERLKKLIPPGVQPKFTSAAELLAWQREEGLKHCEELGKRNQKARTEKIFGRSGIQSLHRSCTFANYQVS 80
Cdd:PRK12377   1 MKNI-ATGGVLERIRRLAPQGVQPPFRTVDEWREWQLAEGRKRSEEINRQNQQLRVEKILNRSGIQPLHRKCSFANYQVQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969  81 GEGQRKAFTMAKSYAQNFGTGFASFVFSGGPGTGKNHLAAAIGNHLLSGGHSVLVVTIPDLMLRVRECYDGGQSEAALLD 160
Cdd:PRK12377  80 NDGQRYALSQAKSIADELMTGCTNFVFSGKPGTGKNHLAAAIGNRLLAKGRSVIVVTVPDVMSRLHESYDNGQSGEKFLQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969 161 DLCKVDLLVLDEVGIQRGSNGEKVILNQVIDRRLSSMRPVGILTNLNHEELLGALGARVIDRLQMDGGMWVNFDWGSYRK 240
Cdd:PRK12377 160 ELCKVDLLVLDEIGIQRETKNEQVVLNQIIDRRTASMRSVGMLTNLNHEAMSTLLGERVMDRMTMNGGRWVNFNWESWRP 239


                 ....*....
gi 507085969 241 NVSHLRIVK 249
Cdd:PRK12377 240 NVSHLRIVK 248
PRK07952 PRK07952
DNA replication protein DnaC; Validated
 1-243 9.85e-107

DNA replication protein DnaC; Validated


Pssm-ID: 181180 [Multi-domain]  Cd Length: 244  Bit Score: 308.24  E-value: 9.85e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969   1 MKNIvnsGNALERLKKLIPPGVQPKFTSAAELLAWQREEGLKHCEELGKRNQKARTEKIFGRSGIQSLHRSCTFANYQVS 80
Cdd:PRK07952   1 MKNV---GDLMQRLQKMMPAHIKPAFKTGEELLAWQKEQGRIRSAALERENRAMKMQRTFNRSGIRPLHQNCSFENYRVE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969  81 GEGQRKAFTMAKSYAQNFGTGFASFVFSGGPGTGKNHLAAAIGNHLLSGGHSVLVVTIPDLMLRVRECYDGGQ-SEAALL 159
Cdd:PRK07952  78 CEGQMNALSKARQYVEEFDGNIASFIFSGKPGTGKNHLAAAICNELLLRGKSVLIITVADIMSAMKDTFSNSEtSEEQLL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969 160 DDLCKVDLLVLDEVGIQRGSNGEKVILNQVIDRRLSSMRPVGILTNLNHEELLGALGARVIDRLQMDGGMWVNFDWGSYR 239
Cdd:PRK07952 158 NDLSNVDLLVIDEIGVQTESRYEKVIINQIVDRRSSSKRPTGMLTNSNMEEMTKLLGERVMDRMRLGNSLWVIFNWDSYR 237


                 ....
gi 507085969 240 KNVS 243
Cdd:PRK07952 238 SRVT 241
PRK08116 PRK08116
hypothetical protein; Validated
 36-223 3.32e-34

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 123.98  E-value: 3.32e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969  36 QREEGLKHCEELGKRNQKARTEKIFGRSGIQSLHRSCTFANYQVSGeGQRKAFTMAKSYAQNFGTGFAS---FVFSGGPG 112
Cdd:PRK08116  46 EREAEEAKEREEENREKQRRIERLKSNSLLDEKFRNSTFENFLFDK-GSEKAYKIARKYVKKFEEMKKEnvgLLLWGSVG 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969 113 TGKNHLAAAIGNHLLSGGHSVLVVTIPDLMLRVRECYDGGQSEA--ALLDDLCKVDLLVLDEVGIQRGSNGEKVILNQVI 190
Cdd:PRK08116 125 TGKTYLAACIANELIEKGVPVIFVNFPQLLNRIKSTYKSSGKEDenEIIRSLVNADLLILDDLGAERDTEWAREKVYNII 204

                        170       180       190
                 ....*....|....*....|....*....|...
gi 507085969 191 DRRLSSMRPVGILTNLNHEELLGALGARVIDRL 223
Cdd:PRK08116 205 DSRYRKGLPTIVTTNLSLEELKNQYGKRIYDRI 237
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
106-240 5.10e-22

DNA replication protein DnaC [Replication, recombination and repair];


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 91.00  E-value: 5.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969 106 VFSGGPGTGKNHLAAAIGNHLLSGGHSVLVVTIPDLMLRVRECYDGGqSEAALLDDLCKVDLLVLDEVGIQRGSNGEKVI 185
Cdd:COG1484  103 ILLGPPGTGKTHLAIALGHEACRAGYRVRFTTAPDLVNELKEARADG-RLERLLKRLAKVDLLILDELGYLPLDAEGAEL 181

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969 186 LNQVIDRRlSSMRPVGILTNLNHEELLGALG-----ARVIDRLqMDGGMWVNFDWGSYRK 240
Cdd:COG1484  182 LFELISDR-YERRSTIITSNLPFSEWGEVFGdptlaTAILDRL-VHHAHIIELKGESYRL 239
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 106-240 2.47e-17

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 78.28  E-value: 2.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969 106 VFSGGPGTGKNHLAAAIGNHLLSGGHSVLVVTIPDLMLRVRECYDGGQSEaALLDDLCKVDLLVLDEVGIQRGSNGEKVI 185
Cdd:NF038214  94 LLLGPPGTGKTHLAIALGYAACRQGYRVRFTTAADLVEQLAQARADGRLG-RLLRRLARYDLLIIDELGYLPFSREGANL 172

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507085969 186 LNQVIDRRL--SSMrpvgILT-NLNHEE---LLG--ALGARVIDRLqMDGGMWVNFDWGSYRK 240
Cdd:NF038214 173 LFELIADRYerGST----IITsNLPFSEwgeVFGdpTLAAAILDRL-VHHAHILELKGESYRL 230
PRK06835 PRK06835
DNA replication protein DnaC; Validated
 74-226 3.06e-16

DNA replication protein DnaC; Validated


Pssm-ID: 235871 [Multi-domain]  Cd Length: 329  Bit Score: 76.48  E-value: 3.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969  74 FANYQVSGEGQ------RKAFTMAKSYAQNFGTGFASFVFSGGPGTGKNHLAAAIGNHLLSGGHSVLVVTIPDLM----- 142
Cdd:PRK06835 149 YSDEKDDDEPLsprknmEKILEKCKNFIENFDKNNENLLFYGNTGTGKTFLSNCIAKELLDRGKSVIYRTADELIeilre 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969 143 LRVRECYDGGQSEAALLDdlckVDLLVLDEVGIQRGSNGEKVILNQVIDRRLSSMRPVGILTNLNHEELLGALGARVIDR 222
Cdd:PRK06835 229 IRFNNDKELEEVYDLLIN----CDLLIIDDLGTEKITEFSKSELFNLINKRLLRQKKMIISTNLSLEELLKTYSERISSR 304


                 ....
gi 507085969 223 LQMD 226
Cdd:PRK06835 305 LLGN 308
IstB_IS21 pfam01695
IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is ...
 106-223 1.25e-13

IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is found associated with IS21 family insertion sequences. The function of this protein is unknown, but it may perform a transposase function.


Pssm-ID: 426385 [Multi-domain]  Cd Length: 238  Bit Score: 68.24  E-value: 1.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969  106 VFSGGPGTGKNHLAAAIGNHLLSGGHSVLVVTIPDLMLRVRECYDGGQSEAAlLDDLCKVDLLVLDEVGIQRGSNGEKVI 185
Cdd:pfam01695  96 VLLGPPGVGKTHLAIALGVEACRAGYSVRFTSAADLVNQLKRAHGDGKLTRK-LQQLLKPDVLILDEWGYLPLDQAEANL 174

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 507085969  186 LNQVIDRRLSSmRPVGILTNLNHEE---LLG--ALGARVIDRL 223
Cdd:pfam01695 175 LFQVISKRYEH-RSIILTSNLPFGEwgqVFGdaVLATAILDRL 216
PRK06921 PRK06921
hypothetical protein; Provisional
 55-222 6.59e-13

hypothetical protein; Provisional


Pssm-ID: 180750 [Multi-domain]  Cd Length: 266  Bit Score: 66.34  E-value: 6.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969  55 RTEKIFGRSGIQSLHRSCTFANYQVSGEGQ--RKAFTMAKSYAQNF----GTGFASFVFSGGPGTGKNHLAAAIGNHLLS 128
Cdd:PRK06921  64 KIERLLKASEITEAFRKLTFKNFKTEGKPQaiKDAYECAVEYVKDFekiqESRKNSIALLGQPGSGKTHLLTAAANELMR 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969 129 GGHsvlvvtIPDLMLRVRECYDGGQSE----AALLDDLCKVDLLVLDEV-----GIQRGSNGEKVILNQVIDRRLSSMRP 199
Cdd:PRK06921 144 KKG------VPVLYFPFVEGFGDLKDDfdllEAKLNRMKKVEVLFIDDLfkpvnGKPRATEWQIEQMYSVLNYRYLNHKP 217

                        170       180
                 ....*....|....*....|....*.
gi 507085969 200 VGILTNLNHEELLG---ALGARVIDR 222
Cdd:PRK06921 218 ILISSELTIDELLDideALGSRIVEM 243
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
68-225 2.02e-10

Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 59.82  E-value: 2.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969  68 LHRSCTFANYqVSGEGQRKAFTMAKSYAQNFGTGFASFVFSGGPGTGKNHLAAAIGNHLLS--GGHSVLVVTIPDLMLRV 145
Cdd:COG0593    1 LNPRYTFDNF-VVGPSNRLAHAAALAVAEWPGKAYNPLFLYGGVGLGKTHLLHAIGNEALEnnPGARVVYLTAEEFTNDF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969 146 RECYDGGQSEaALLDDLCKVDLLVLDEvgIQRGSNGEKV------ILNQVIDRR----LSSMRPVGILTNLnhEEllgal 215
Cdd:COG0593   80 INAIRNNTIE-EFKEKYRSVDVLLIDD--IQFLAGKEATqeeffhTFNALREAGkqivLTSDRPPKELPGL--EE----- 149

                        170
                 ....*....|
gi 507085969 216 gaRVIDRLQM 225
Cdd:COG0593  150 --RLRSRLEW 157
DnaA TIGR00362
chromosomal replication initiator protein DnaA; DnaA is involved in DNA biosynthesis; ...
 1-127 5.46e-10

chromosomal replication initiator protein DnaA; DnaA is involved in DNA biosynthesis; initiation of chromosome replication and can also be transcription regulator. The C-terminal of the family hits the pfam bacterial DnaA (bac_dnaA) domain family. For a review, see Kaguni (2006). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273037 [Multi-domain]  Cd Length: 437  Bit Score: 58.70  E-value: 5.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969    1 MKNIVNSgNALERLKK----LIPPGVQPKFTSaaellaWQREEGLKHCEELGKRNQKARTEKIFGRSGIQSLHrscTFAN 76
Cdd:TIGR00362  43 VKEWIEK-NYLDLIEEllqeLFGAEIEIEFTV------GEDEEELEPNSKKPEPAPPEAPAPPSSASGLNPKY---TFDN 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 507085969   77 YqVSGEGQRKAFTMAKSYAQNFGTGFASFVFSGGPGTGKNHLAAAIGNHLL 127
Cdd:TIGR00362 113 F-VVGKSNRLAHAAALAVAENPGKAYNPLFIYGGVGLGKTHLLHAIGNEIL 162
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 83-226 2.40e-09

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: 54.46  E-value: 2.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969  83 GQRKAFTMAKSYAQNfgTGFASFVFSGGPGTGKNHLAAAIGNHLLSGGHSVLVVTIPDLMLRVRECYDGGQSEAALLDDL 162
Cdd:cd00009    2 GQEEAIEALREALEL--PPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFEL 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507085969 163 ---CKVDLLVLDEVG-IQRGSNGEKV-ILNQVIDRRLSS--MRPVGILTNLNHEELLGALGARVIDRLQMD 226
Cdd:cd00009   80 aekAKPGVLFIDEIDsLSRGAQNALLrVLETLNDLRIDRenVRVIGATNRPLLGDLDRALYDRLDIRIVIP 150
PRK08181 PRK08181
transposase; Validated
 86-193 4.09e-09

transposase; Validated


Pssm-ID: 136670 [Multi-domain]  Cd Length: 269  Bit Score: 55.71  E-value: 4.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969  86 KAFTMAKSYAQNFGTGFASFVFSGGPGTGKNHLAAAIGNHLLSGGHSVLVVTIPDLMLRVRECYDGGQSEAAlLDDLCKV 165
Cdd:PRK08181  90 KAQVMAIAAGDSWLAKGANLLLFGPPGGGKSHLAAAIGLALIENGWRVLFTRTTDLVQKLQVARRELQLESA-IAKLDKF 168

                         90       100
                 ....*....|....*....|....*...
gi 507085969 166 DLLVLDEVGIQRGSNGEKVILNQVIDRR 193
Cdd:PRK08181 169 DLLILDDLAYVTKDQAETSVLFELISAR 196
PRK06526 PRK06526
transposase; Provisional
 97-174 2.03e-08

transposase; Provisional


Pssm-ID: 180607  Cd Length: 254  Bit Score: 53.33  E-value: 2.03e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507085969  97 NFGTGFASFVFSGGPGTGKNHLAAAIGNHLLSGGHSVLVVTIPDLMLRVRECYDGGQSEAALLdDLCKVDLLVLDEVG 174
Cdd:PRK06526  93 DFVTGKENVVFLGPPGTGKTHLAIGLGIRACQAGHRVLFATAAQWVARLAAAHHAGRLQAELV-KLGRYPLLIVDEVG 169
Bac_DnaA pfam00308
Bacterial dnaA protein;
68-225 5.52e-08

Bacterial dnaA protein;


Pssm-ID: 278724 [Multi-domain]  Cd Length: 219  Bit Score: 51.94  E-value: 5.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969   68 LHRSCTFANYqVSGEGQRKAFTMAKSYAQNFGTGFASFVFSGGPGTGKNHLAAAIGNHLLSGGHS--VLVVTIPDLMLR- 144
Cdd:pfam00308   1 LNPRYTFENF-VIGPSNRFAHAAALTVAKAPGKAYNPLFIYGGVGLGKTHLLHAIGNYALQNAPNlrVVYLTAEEFLNDf 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969  145 VRECYDGgqSEAALLDDLCKVDLLVLDEvgIQRGSNGEKV------ILNQVIDRR----LSSMRPVGILTNLNheellga 214
Cdd:pfam00308  80 VDAIRDN--KTNQFKEKYRNVDVLLIDD--IQFLAGKEGTqeeffhTFNALHESGkqivFSSDRPPKELEELE------- 148

                         170
                  ....*....|.
gi 507085969  215 lgARVIDRLQM 225
Cdd:pfam00308 149 --DRLRSRFQW 157
dnaA PRK00149
chromosomal replication initiator protein DnaA;
73-225 2.28e-07

chromosomal replication initiator protein DnaA;


Pssm-ID: 234667 [Multi-domain]  Cd Length: 401  Bit Score: 50.90  E-value: 2.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969  73 TFANYqVSGEGQRKAFTMAKSYAQNFGTGFASFVFSGGPGTGKNHLAAAIGNHLL--SGGHSVLVVTIPDLMLRVRECYD 150
Cdd:PRK00149  71 TFDNF-VVGKSNRLAHAAALAVAENPGKAYNPLFIYGGVGLGKTHLLHAIGNYILekNPNAKVVYVTSEKFTNDFVNALR 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969 151 GGQSEaALLDDLCKVDLLVLDEvgIQRGSNGEKV------ILN-------QVIdrrLSSMRPVGILTNLnhEEllgalga 217
Cdd:PRK00149 150 NNTME-EFKEKYRSVDVLLIDD--IQFLAGKERTqeeffhTFNalheagkQIV---LTSDRPPKELPGL--EE------- 214


                 ....*...
gi 507085969 218 RVIDRLQM 225
Cdd:PRK00149 215 RLRSRFEW 222
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 107-226 6.64e-06

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: 44.67  E-value: 6.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969   107 FSGGPGTGKNHLAAAIGNHLLSGGHSVLVVTIPDLMLRVREC------------YDGGQSEAALLDDL--CKVDLLVLDE 172
Cdd:smart00382   7 IVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQllliivggkkasGSGELRLRLALALArkLKPDVLILDE 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 507085969   173 VG---IQRGSNGEKVILNQVIDRRLSSMRPVGIL--TNLNHEELLGALGARVIDRLQMD 226
Cdd:smart00382  87 ITsllDAEQEALLLLLEELRLLLLLKSEKNLTVIltTNDEKDLGPALLRRRFDRRIVLL 145
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 104-212 2.98e-05

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: 43.04  E-value: 2.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969 104 SFVFSGGPGTGKNHLAAAIGNHLlsgGHSVLVVTIPDLMLRVRecydgGQSEAAL------LDDLCKVdLLVLDEV---G 174
Cdd:cd19481   28 GILLYGPPGTGKTLLAKALAGEL---GLPLIVVKLSSLLSKYV-----GESEKNLrkiferARRLAPC-ILFIDEIdaiG 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 507085969 175 IQRGSNGEKVILNQVIDRRLSSMRPVGILTNL------NHEELL 212
Cdd:cd19481   99 RKRDSSGESGELRRVLNQLLTELDGVNSRSKVlviaatNRPDLL 142
PRK09183 PRK09183
transposase/IS protein; Provisional
 106-223 5.46e-05

transposase/IS protein; Provisional


Pssm-ID: 181681  Cd Length: 259  Bit Score: 43.16  E-value: 5.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969 106 VFSGGPGTGKNHLAAAIGNHLLSGGHSVLVVTIPDLMLRVRECYDGGQSEAALLDDLCKVDLLVLDEVGIQRGSNGEKVI 185
Cdd:PRK09183 106 VLLGPSGVGKTHLAIALGYEAVRAGIKVRFTTAADLLLQLSTAQRQGRYKTTLQRGVMAPRLLIIDEIGYLPFSQEEANL 185

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 507085969 186 LNQVIDRRL--SSMrpvgILT-NLN----HEELLG--ALGARVIDRL 223
Cdd:PRK09183 186 FFQVIAKRYekGSM----ILTsNLPfgqwDQTFAGdaALTSAMLDRL 228
PRK08939 PRK08939
primosomal protein DnaI; Reviewed
 44-174 2.53e-04

primosomal protein DnaI; Reviewed


Pssm-ID: 236353 [Multi-domain]  Cd Length: 306  Bit Score: 41.39  E-value: 2.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969  44 CEELGKRNQKARTEKIfgrsgIQSLH-----RSCTFANYQVSGEGQRKAFTMAKSYAQNFGTGfaSFV----FSGGPGTG 114
Cdd:PRK08939  96 TPEKIEADEEKAIKKR-----IQSIYmpkdlLQASLADIDLDDRDRLDALMAALDFLEAYPPG--EKVkglyLYGDFGVG 168

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969 115 KNHLAAAIGNHLLSGGHSVLVVTIPDLMLRVRECYDGGQSEaALLDDLCKVDLLVLDEVG 174
Cdd:PRK08939 169 KSYLLAAIANELAKKGVSSTLLHFPEFIRELKNSISDGSVK-EKIDAVKEAPVLMLDDIG 227
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
 83-174 3.93e-04

DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 39.85  E-value: 3.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507085969  83 GQRKAFTMAksyaqnFGTGFasFVFSGGPGTGKNHLAAAIGNHLLSGGHSVLV-------------------VTIPDLmL 143
Cdd:cd17933    1 EQKAAVRLV------LRNRV--SVLTGGAGTGKTTTLKALLAALEAEGKRVVLaaptgkaakrlsestgieaSTIHRL-L 71

                         90       100       110
                 ....*....|....*....|....*....|.
gi 507085969 144 RVREcydGGQSEAALLDDLCKVDLLVLDEVG 174
Cdd:cd17933   72 GINP---GGGGFYYNEENPLDADLLIVDEAS 99
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
 104-136 2.75e-03

DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are nucleic acid motor proteins that couple ATP hydrolysis to translocation along with the concomitant unwinding of DNA or RNA. This is central to many aspects of cellular DNA and RNA metabolism and accordingly, they are implicated in a wide range of nucleic acid processing events including DNA replication, recombination, and repair as well as many aspects of RNA metabolism. Superfamily 1 helicases are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350801 [Multi-domain]  Cd Length: 127  Bit Score: 36.79  E-value: 2.75e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 507085969 104 SFVFSGGPGTGKNHLAAAIGNHLLSGGHSVLVV 136
Cdd:cd18043   16 NVVIQGPPGTGKSQTIANIIANALARGKRVLFV 48
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 106-158 2.94e-03

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: 38.35  E-value: 2.94e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 507085969 106 VFSGGPGTGKNHLAAAIGNHLlsGGHsVLVVTIPDLMlrvrecyDG--GQSEAAL 158
Cdd:COG0464  195 LLYGPPGTGKTLLARALAGEL--GLP-LIEVDLSDLV-------SKyvGETEKNL 239
 
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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