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Conserved domains on  [gi|1619373443|dbj|GCZ54813|]
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plasmid partition protein [Escherichia coli]

Protein Classification

acetate and sugar kinases/Hsc70/actin family protein( domain architecture ID 99298)

acetate and sugar kinases/Hsc70/actin (ASKHA) family protein catalyzes phosphoryl transfer from ATP to their respective substrates

CATH:  3.30.420.40
Gene Ontology:  GO:0000166
PubMed:  8800467|7781919
SCOP:  3000092

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
1-319 1.86e-125

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


The actual alignment was detected with superfamily member pfam06406:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 317  Bit Score: 361.76  E-value: 1.86e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443   1 MNVYCDDGSTTIKLAWNDNGKICKSLSQNSFRHGWKVdGLGIRQTFNYELDGKKYTYDEVSNQSILTTHIEYQYTDVNLL 80
Cdd:pfam06406   1 MKIFIDDGSTNIKLAWLEDGEVKTLISPNSFKPEWSV-SLGDKKPFNYEIDGEKYSFDPLSPDAVVTTDTSYQYSDVNVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443  81 AVHHALLNSGLAPQPVSLTVTLPISEFYTKECQKNELNIQRKIENLMRPIRLNKGDVFTIEHVDVMPESLPAVFSrlVVD 160
Cdd:pfam06406  80 AIHHALLTSGLPPQDVDVVVTLPLSEYYDANNQPNMENIERKKANVMRPVELQGGETFTIRSVSVMPESIPAGFE--VLK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443 161 KVGQFEKSLVVDIGGTTLDVGVIVGQFDSVSAIHGNSGIGVSSVTKAAMSALRMASSDTSFLVADELIKRRNDPDFVRQV 240
Cdd:pfam06406 158 DLDELESLLIIDLGGTTLDVAHVRGKLEGISKIYGDPSIGVSLITDAVKDALATASTRTSSYIADDLIIHRHDNNYLKQR 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1619373443 241 INDETKTDLVLNTIEGAIASLGEQVVNELGDFHHVNRVYVVGGGAPLIYDSIKTAWHHLGQKVVMMESPQTALVEAIAA 319
Cdd:pfam06406 238 INNEDKRASVMEVINEAVKKLEQRVIRALSRFSGYTHVMVVGGGAELIATAIKKHTGVPDARFIKVDNPQFALVNGMYA 316
 
Name Accession Description Interval E-value
StbA pfam06406
StbA protein; This family consists of several bacterial StbA plasmid stability proteins.
1-319 1.86e-125

StbA protein; This family consists of several bacterial StbA plasmid stability proteins.


Pssm-ID: 310773 [Multi-domain]  Cd Length: 317  Bit Score: 361.76  E-value: 1.86e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443   1 MNVYCDDGSTTIKLAWNDNGKICKSLSQNSFRHGWKVdGLGIRQTFNYELDGKKYTYDEVSNQSILTTHIEYQYTDVNLL 80
Cdd:pfam06406   1 MKIFIDDGSTNIKLAWLEDGEVKTLISPNSFKPEWSV-SLGDKKPFNYEIDGEKYSFDPLSPDAVVTTDTSYQYSDVNVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443  81 AVHHALLNSGLAPQPVSLTVTLPISEFYTKECQKNELNIQRKIENLMRPIRLNKGDVFTIEHVDVMPESLPAVFSrlVVD 160
Cdd:pfam06406  80 AIHHALLTSGLPPQDVDVVVTLPLSEYYDANNQPNMENIERKKANVMRPVELQGGETFTIRSVSVMPESIPAGFE--VLK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443 161 KVGQFEKSLVVDIGGTTLDVGVIVGQFDSVSAIHGNSGIGVSSVTKAAMSALRMASSDTSFLVADELIKRRNDPDFVRQV 240
Cdd:pfam06406 158 DLDELESLLIIDLGGTTLDVAHVRGKLEGISKIYGDPSIGVSLITDAVKDALATASTRTSSYIADDLIIHRHDNNYLKQR 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1619373443 241 INDETKTDLVLNTIEGAIASLGEQVVNELGDFHHVNRVYVVGGGAPLIYDSIKTAWHHLGQKVVMMESPQTALVEAIAA 319
Cdd:pfam06406 238 INNEDKRASVMEVINEAVKKLEQRVIRALSRFSGYTHVMVVGGGAELIATAIKKHTGVPDARFIKVDNPQFALVNGMYA 316
ASKHA_NBD_ParM_R1-like cd24022
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and ...
3-320 1.77e-88

nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and similar proteins from ParM domain family; Type II plasmid partition systems utilize ParM NTPases in coordination with a centromere-binding protein called ParR to mediate accurate DNA segregation, a process critical for plasmid retention. The family corresponds to a group of uncharacterized proteins similar to Escherichia coli ParM, also called ParA locus 36 kDa protein, or protein StbA. It is a plasmid-encoded protein involved in the control of plasmid partition and required for accurate segregation of low-copy-number plasmid R1.


Pssm-ID: 466872 [Multi-domain]  Cd Length: 324  Bit Score: 267.99  E-value: 1.77e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443   3 VYCDDGSTTIKLAW-NDNGKICKSLSQNSFRHGWKVDGL--GIRQTFNYELDGKKYTYDEVSNQSILTTHIEYQYTDVNL 79
Cdd:cd24022     1 VGIDDGSANIKVAWgEDDGKIKTFKIPSRARRGAAVSGSlgGGSQVFNYEVDGERYTVGDVVSDPIDTRNDDYQTSDLNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443  80 LAVHHALLNSGLAPQPVSLTVTLPISEFYTKECQKNELNIQRKIENLMRPI-RLNKGDVFTIEHVDVMPESLPAVFSRLV 158
Cdd:cd24022    81 VLVHHALHQAGLGGRKVDIVTGLPVSQYYYKDGQKNTELIERKKKNLKKPVtLLGGKSPATIVSVKVMPEGVAAYFDYLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443 159 VDKVG------QFEKSLVVDIGGTTLDVGVIVGQFDSVSAIHGNSGIGVSSVTKAAMSALRMA--SSDTSFLVADELIKR 230
Cdd:cd24022   161 DEDGNgtdeeeEEGPVAVIDIGGTTTDIAVVSGGLSIDHARSGTIELGVLDVRDALKDALKKRfgLSSISDAELDRALRT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443 231 RNDPDFVRQVINdetktdlVLNTIEGAIASLGEQVVNE----LGDFHHVNRVYVVGGGAPLIYDSIKTAWhhlGQKVVMM 306
Cdd:cd24022   241 GKFRLNGGKEVD-------VSDLVNEAIAEVAERILNEikrrLGDASDLDRVIFVGGGAELLEDELKEAL---GPNAIIV 310
                         330
                  ....*....|....
gi 1619373443 307 ESPQTALVEAIAAF 320
Cdd:cd24022   311 DEPEFANARGMLKY 324
 
Name Accession Description Interval E-value
StbA pfam06406
StbA protein; This family consists of several bacterial StbA plasmid stability proteins.
1-319 1.86e-125

StbA protein; This family consists of several bacterial StbA plasmid stability proteins.


Pssm-ID: 310773 [Multi-domain]  Cd Length: 317  Bit Score: 361.76  E-value: 1.86e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443   1 MNVYCDDGSTTIKLAWNDNGKICKSLSQNSFRHGWKVdGLGIRQTFNYELDGKKYTYDEVSNQSILTTHIEYQYTDVNLL 80
Cdd:pfam06406   1 MKIFIDDGSTNIKLAWLEDGEVKTLISPNSFKPEWSV-SLGDKKPFNYEIDGEKYSFDPLSPDAVVTTDTSYQYSDVNVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443  81 AVHHALLNSGLAPQPVSLTVTLPISEFYTKECQKNELNIQRKIENLMRPIRLNKGDVFTIEHVDVMPESLPAVFSrlVVD 160
Cdd:pfam06406  80 AIHHALLTSGLPPQDVDVVVTLPLSEYYDANNQPNMENIERKKANVMRPVELQGGETFTIRSVSVMPESIPAGFE--VLK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443 161 KVGQFEKSLVVDIGGTTLDVGVIVGQFDSVSAIHGNSGIGVSSVTKAAMSALRMASSDTSFLVADELIKRRNDPDFVRQV 240
Cdd:pfam06406 158 DLDELESLLIIDLGGTTLDVAHVRGKLEGISKIYGDPSIGVSLITDAVKDALATASTRTSSYIADDLIIHRHDNNYLKQR 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1619373443 241 INDETKTDLVLNTIEGAIASLGEQVVNELGDFHHVNRVYVVGGGAPLIYDSIKTAWHHLGQKVVMMESPQTALVEAIAA 319
Cdd:pfam06406 238 INNEDKRASVMEVINEAVKKLEQRVIRALSRFSGYTHVMVVGGGAELIATAIKKHTGVPDARFIKVDNPQFALVNGMYA 316
ASKHA_NBD_ParM_R1-like cd24022
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and ...
3-320 1.77e-88

nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and similar proteins from ParM domain family; Type II plasmid partition systems utilize ParM NTPases in coordination with a centromere-binding protein called ParR to mediate accurate DNA segregation, a process critical for plasmid retention. The family corresponds to a group of uncharacterized proteins similar to Escherichia coli ParM, also called ParA locus 36 kDa protein, or protein StbA. It is a plasmid-encoded protein involved in the control of plasmid partition and required for accurate segregation of low-copy-number plasmid R1.


Pssm-ID: 466872 [Multi-domain]  Cd Length: 324  Bit Score: 267.99  E-value: 1.77e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443   3 VYCDDGSTTIKLAW-NDNGKICKSLSQNSFRHGWKVDGL--GIRQTFNYELDGKKYTYDEVSNQSILTTHIEYQYTDVNL 79
Cdd:cd24022     1 VGIDDGSANIKVAWgEDDGKIKTFKIPSRARRGAAVSGSlgGGSQVFNYEVDGERYTVGDVVSDPIDTRNDDYQTSDLNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443  80 LAVHHALLNSGLAPQPVSLTVTLPISEFYTKECQKNELNIQRKIENLMRPI-RLNKGDVFTIEHVDVMPESLPAVFSRLV 158
Cdd:cd24022    81 VLVHHALHQAGLGGRKVDIVTGLPVSQYYYKDGQKNTELIERKKKNLKKPVtLLGGKSPATIVSVKVMPEGVAAYFDYLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443 159 VDKVG------QFEKSLVVDIGGTTLDVGVIVGQFDSVSAIHGNSGIGVSSVTKAAMSALRMA--SSDTSFLVADELIKR 230
Cdd:cd24022   161 DEDGNgtdeeeEEGPVAVIDIGGTTTDIAVVSGGLSIDHARSGTIELGVLDVRDALKDALKKRfgLSSISDAELDRALRT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443 231 RNDPDFVRQVINdetktdlVLNTIEGAIASLGEQVVNE----LGDFHHVNRVYVVGGGAPLIYDSIKTAWhhlGQKVVMM 306
Cdd:cd24022   241 GKFRLNGGKEVD-------VSDLVNEAIAEVAERILNEikrrLGDASDLDRVIFVGGGAELLEDELKEAL---GPNAIIV 310
                         330
                  ....*....|....
gi 1619373443 307 ESPQTALVEAIAAF 320
Cdd:cd24022   311 DEPEFANARGMLKY 324
ASKHA_NBD_ParM-like cd10227
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ...
3-312 1.68e-18

nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466825 [Multi-domain]  Cd Length: 263  Bit Score: 83.34  E-value: 1.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443   3 VYCDDGSTTIKLAWNDNGKIcKSLSQNSFRHGWKVDGLGIRQTFNYELDGKKYTYDEV---SNQSILTTHIEYQYTDVNL 79
Cdd:cd10227     1 IGIDIGNGNTKVVTGGGKEF-KFPSAVAEARESSLDDGLLEDDIIVEYNGKRYLVGELalrEGGGGRSTGDDKKKSEDAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443  80 LAVHHAL-LNSGLAPQPVSLTVTLPISEFYTKECQKNELNIQRKIENlmrpIRLNKGDVFTIEHVDVMPESLPAVFSRLV 158
Cdd:cd10227    80 LLLLAALaLLGDDEEVDVNLVVGLPISEYKEEKKELKKKLLKGLHEF----TFNGKERRITINDVKVLPEGAGAYLDYLL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443 159 VDKVGQFEKSLVVDIGGTTLDVGVIVGqfdsvsaihgnsgigvssvtkaamsalrmassdtsflvadelikrrndpdfvR 238
Cdd:cd10227   156 DDDELEDGNVLVIDIGGGTTDILTFEN----------------------------------------------------G 183
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1619373443 239 QVINDETKTdlvLNTIEGAIASLGEQVVNEL-----GDFHHVNRVYVVGGGAPLIYDSIKTAWHHlgqKVVMMESPQTA 312
Cdd:cd10227   184 KPIEESSDT---LPGGEEALEKYADDILNELlkklgDELDSADKILLTGGGAELLKDYLKEAYFP---NIIVLDDPQFA 256
ASKHA_NBD_ParM_pCBH-like cd24025
nucleotide-binding domain (NBD) of Clostridium botulinum plasmid segregation protein ParM and ...
83-312 4.33e-14

nucleotide-binding domain (NBD) of Clostridium botulinum plasmid segregation protein ParM and similar proteins from the ParM domain family; The family corresponds to a group of uncharacterized proteins similar to Clostridium botulinum pCBH plasmid segregation protein ParM, an actin-like polymerizing motor. pCBH ParM filament structure is far more complex in comparison to the known filament structures of actin, MreB, and other ParMs. It is bipolar and stiff and like microtubules. The 15 polymerizing strands are likely to exert greater combined force relative to typical two-stranded actin-like filaments.


Pssm-ID: 466875 [Multi-domain]  Cd Length: 326  Bit Score: 71.93  E-value: 4.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443  83 HHALLNSGLA------PQPVSLTVTLPISEFYTkecQKNELniQRKIENLMRPIRLNKGDV---FTIEHVDVMPESLPAV 153
Cdd:cd24025    85 TRVLLLTALAllaaedDEPVSLVTGLPLSYYKT---QKEAL--EEMLKGLHAVVVGVDGGTekrITIDRVRVFPQGAGAL 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443 154 FSRLVvDKVGQFEKSL-------VVDIGGTTLDVGVI-VGQFdsvsAIHGNSG---IGVSSVTKAAMSAL-RMASSDTSF 221
Cdd:cd24025   160 YDALL-DDDGQIIDKAlakgrvgVIDIGYRTTDYVVFeDGEF----LVPELSGsleTGMSTAYRAIANALeEEYGIDLDL 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443 222 LVADELIKRRndpdfvrQVINDETKTDLVlNTIEGAIASLGEQVVNEL----GDFHH-VNRVYVVGGGAPLIYDSIKTAW 296
Cdd:cd24025   235 HELDRALREG-------KIRVRGKEIDLS-DLIDEALKELARQIANEIrslwGDGLGdLDAIILAGGGAELLAPYLKEMF 306
                         250
                  ....*....|....*.
gi 1619373443 297 HHlgqkVVMMESPQTA 312
Cdd:cd24025   307 PN----AEVVPDPQFA 318
ASKHA_NBD_ParM_Psk41-like cd24021
nucleotide-binding domain (NBD) of Staphylococcus aureus pSK41 actin-like ParM protein and ...
96-315 1.75e-09

nucleotide-binding domain (NBD) of Staphylococcus aureus pSK41 actin-like ParM protein and similar proteins from the ParM domain family; Type II plasmid partition systems utilize ParM NTPases in coordination with a centromere-binding protein called ParR to mediate accurate DNA segregation, a process critical for plasmid retention. The family corresponds to a group of uncharacterized proteins similar to Staphylococcus aureus pSK41 actin-like ParM protein, which is functionally homologous to R1 ParM, a known actin homologue, suggesting that it may also form filaments to drive partition. However, pSK41 ParM shows the strongest structural homology to the archaeal actin-like protein Thermoplasma acidophilum Ta0583, but not R1 ParM.


Pssm-ID: 466871 [Multi-domain]  Cd Length: 298  Bit Score: 57.68  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443  96 VSLTVTLPISEFYTKEcqKNELniqrkIENLMRPIRLN---KGDVFTIEHVDVMPESLPAVFSrLVVDKVGQFEKS---- 168
Cdd:cd24021   107 VVVVTGLPSEDYDTEV--EEEL-----KKVLKGEHTVKingKERTINVKDVYVIPQPLGTLYN-LLLDENGEVKNEeled 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443 169 ---LVVDIGGTTLDVGVIVGqfdsvsaihGNSGIGVSSVTKAAMSALRMassdtsflvadelIKRRNDPDFVRQVINDet 245
Cdd:cd24021   179 skvLIIDIGGGTTDVDVING---------LKIDENRFQIETGMKDVYDE-------------IAKEDITEIVEKAIEE-- 234
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1619373443 246 KTDLVLNTIEgaiaslgeqvvNELGDFHHVNRVYVVGGGAPLIYDSIKtawHHL-GQKVVMMESPQTALVE 315
Cdd:cd24021   235 YAEEIVAEIN-----------NAFKDLDSFDKVIFTGGGANILNKYLK---EKLeGDNFVFVENPQTANVR 291
ASKHA_NBD_ParM_Alp7A-like cd24023
nucleotide-binding domain (NBD) of Bacillus subtilis actin-like protein Alp7A and similar ...
96-293 2.65e-09

nucleotide-binding domain (NBD) of Bacillus subtilis actin-like protein Alp7A and similar proteins from the ParM domain family; The family corresponds to a group of uncharacterized proteins similar to Bacillus subtilis actin-like protein Alp7A, a plasmid partitioning protein that functions in plasmid segregation. The subfamily also includes Bacillus thuringiensis ParM hybrid fusion protein.


Pssm-ID: 466873 [Multi-domain]  Cd Length: 368  Bit Score: 57.73  E-value: 2.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443  96 VSLTVTLPISEfYTKEcqknelNIQRKIENLM-------------RPIRLNkgdvFTIEHVDVMPESLPAVFSrLVVDKV 162
Cdd:cd24023   125 VDLSTGLPISE-YKKE------GAKEFFERFLkgehtvtfldgpgKGVTVT----IKFEDVKVLPEGVAALFA-LIYDED 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443 163 GQF------------EKSLVVDIGGTTLDVGVIV-GQFDSVSAihGNSGIGVSSVTKAAMSALR---MASSDTSFLVADE 226
Cdd:cd24023   193 GNErvedtededlkeKNILIIDIGGGTTDVAVFEgGKFDPDLS--TGIDLGIGTALDEIIKELKkeyGVEFDRRRLLFEL 270
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1619373443 227 LIKRRNDPDFVRQVINDetktdlVLNTIEGAIASLGEQVVNELGDF-----HHVNRVYVVGGGAPLIYDSIK 293
Cdd:cd24023   271 IIKKKEYKDKNRGKKVD------LTDIVEKALEELAEEILDEIEKKwnkagNDIEVIYVYGGGSILLKDYLK 336
ASKHA_NBD_ParM_Alp12-like cd24026
nucleotide-binding domain (NBD) of Clostridium tetani actin-like protein Alp12 and similar ...
38-293 7.80e-06

nucleotide-binding domain (NBD) of Clostridium tetani actin-like protein Alp12 and similar proteins from the ParM domain family; The family corresponds to a group of uncharacterized proteins similar to Clostridium tetani actin-like protein Alp12. It is a dynamically unstable force-generating motor involved in segregating the pE88 plasmid, which encodes the lethal tetanus toxin. Alp12 filaments have a unique polymer structure that is entirely different from F-actin and display dynamic behavior like microtubules. Alp12 can be repeatedly cycled between states of polymerization and dissociation, making it a novel candidate for incorporation into fuel-propelled nanobiopolymer machines.


Pssm-ID: 466876 [Multi-domain]  Cd Length: 308  Bit Score: 46.90  E-value: 7.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443  38 DGLGIRQTFNY--ELDGKKY-------TYDEVSNQSILTtHIEYQYTdvnllAVHHALLNSGLAPqpVSLTVTLPISEFY 108
Cdd:cd24026    36 DNLVEIGGNSYkvEYDGKEYligeqgeEYDYDTSKASLL-HKLCTYT-----AIAKLLENDKGNE--VNLVVGCPLNIYK 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443 109 TKEcQKNElniqrkIENLMRP---IRLNKGDV---FTIEHVDVMPESLPAVF---SRLVVDKVGqfekslVVDIGGTTLD 179
Cdd:cd24026   108 NKE-LKEE------YKEFIKGngkIIIIVNGEkksFKITDVTVKPEGSGVIYrnpEKFKNKNVG------VIDIGGLNVN 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443 180 VGVIV-GQFDSVSAIHGNSGIGV--SSVTKAAMSALRMASSDTS---FLVADELIKRRNDPDFVRQVINdETKTDLVLNT 253
Cdd:cd24026   175 FCIYDnGIPIPESMFTDNLGGNVleNKIKEALNSYFGGNIQDYDilnILINGYIKFNGEIEEESKEIIE-EIKDEHLKEI 253
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1619373443 254 IegaIASLGEQVVNELGDFHhvnrvyVVGGGAPLIYDSIK 293
Cdd:cd24026   254 I---NKIKSRKWNLENMDII------FVGGTSLLLKDYIK 284
ASKHA_NBD_PilM-like cd24004
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ...
138-285 8.11e-05

nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466854 [Multi-domain]  Cd Length: 282  Bit Score: 43.44  E-value: 8.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443 138 FTIEHVDVMPeslPAVFsRLVVDKVGQFEKSLVVDIGGTTLDVGVIvgQFDSVSAIhGNSGIGVSSVTKAAMSALrmass 217
Cdd:cd24004    90 LEPVGLTLEP---FAAA-NLLIPYDMRDLNIALVDIGAGTTDIALI--RNGGIEAY-RMVPLGGDDFTKAIAEGF----- 157
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1619373443 218 DTSFLVADELIKR--RNDPDFVRQVINDETKTDLVLNTIEGAIASLGEQVVNELGDFHHV----NRVYVVGGGA 285
Cdd:cd24004   158 LISFEEAEKIKRTygIFLLIEAKDQLGFTINKKEVYDIIKPVLEELASGIANAIEEYNGKfklpDAVYLVGGGS 231
ASKHA_NBD_PilM cd24049
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ...
138-285 2.24e-03

nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.


Pssm-ID: 466899 [Multi-domain]  Cd Length: 339  Bit Score: 39.18  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443 138 FTIEHVDVMPESLPAVFSRLVVDKVGqfEKSLVVDIGGTTLDVGVIV-GQFDSVSAIhgnsGIGVSSVTKAAMSALRMAS 216
Cdd:cd24049   150 LKPVAIDVESFALARALEYLLPDEEE--ETVALLDIGASSTTLVIVKnGKLLFTRSI----PVGGNDITEAIAKALGLSF 223
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1619373443 217 SDTsflvadELIKRRNDpdfvrqviNDETKTDLVLNTIEGAIASLGEQVVNELG---DFHH-------VNRVYVVGGGA 285
Cdd:cd24049   224 EEA------EELKREYG--------LLLEGEEGELKKVAEALRPVLERLVSEIRrslDYYRsqnggepIDKIYLTGGGS 288
FtsA pfam14450
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ...
170-287 3.79e-03

Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains. The FtsA protein contains two structurally related actin-like ATPase domains which are also structurally related to the ATPase domains of HSP70 (see PF00012). FtsA has a SHS2 domain PF02491 inserted in to the RnaseH fold PF02491.


Pssm-ID: 464177 [Multi-domain]  Cd Length: 167  Bit Score: 37.70  E-value: 3.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1619373443 170 VVDIGGTTLDVGVI-VGQFDSVSAIhgnsGIGVSSVTKAAMSALRmassdTSFLVAdELIKRR--------NDPDFVRQV 240
Cdd:pfam14450   2 LIDIGGGTTDIAVFeDGALRHTRVI----PVGGNGITKDIAIGLR-----TAVEEA-ERLKIKygsalaslADEDEVPGV 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1619373443 241 INDETKT---DLVLNTIEGAIASLGEQVVNELGDFH-----------HVNRVYVVGGGAPL 287
Cdd:pfam14450  72 GGREPREisrKELAEIIEARVEEILELVRAELEDREvlpgeyvrlevDVHGIVLTGGGSAL 132
 
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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