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Conserved domains on  [gi|1890749784|ref|WP_183274391|]
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MULTISPECIES: plasmid segregation protein ParM domain-containing protein [Enterobacter cloacae complex]

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 ...
1-318 4.56e-124

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: 358.30  E-value: 4.56e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784   1 MNIYCDDGSTNVKLAWFEGNELQTRVSANSFRHGWKVAEFSAATFNYQVGTLKYTWDSVSRDAIPTTNVEYQYGDLNLLA 80
Cdd:pfam06406   1 MKIFIDDGSTNIKLAWLEDGEVKTLISPNSFKPEWSVSLGDKKPFNYEIDGEKYSFDPLSPDAVVTTDTSYQYSDVNVVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784  81 VHHALLNSGLEPQPVSLTVTLPLSEYYDGDCQRNEVNIRRKRENLMRELVLNKGRAFTVTDVKVMPESLPAAFSRLAELK 160
Cdd:pfam06406  81 IHHALLTSGLPPQDVDVVVTLPLSEYYDANNQPNMENIERKKANVMRPVELQGGETFTIRSVSVMPESIPAGFEVLKDLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784 161 pgPAETTLIIDLGGTTLDAGVIVGQFDDISAVHGNPSVGVSQVTRAAAGALRAADSETSALIADTVIRNRNDRQYLQRVI 240
Cdd:pfam06406 161 --ELESLLIIDLGGTTLDVAHVRGKLEGISKIYGDPSIGVSLITDAVKDALATASTRTSSYIADDLIIHRHDNNYLKQRI 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1890749784 241 NDAGKIDDVLNKITEAITSLGARVTSELTAFRNVNRVFLVGGGASLIEEAIRQAWPLAPDRIEVIGDPQLALAREIAL 318
Cdd:pfam06406 239 NNEDKRASVMEVINEAVKKLEQRVIRALSRFSGYTHVMVVGGGAELIATAIKKHTGVPDARFIKVDNPQFALVNGMYA 316
 
Name Accession Description Interval E-value
StbA pfam06406
StbA protein; This family consists of several bacterial StbA plasmid stability proteins.
1-318 4.56e-124

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


Pssm-ID: 310773 [Multi-domain]  Cd Length: 317  Bit Score: 358.30  E-value: 4.56e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784   1 MNIYCDDGSTNVKLAWFEGNELQTRVSANSFRHGWKVAEFSAATFNYQVGTLKYTWDSVSRDAIPTTNVEYQYGDLNLLA 80
Cdd:pfam06406   1 MKIFIDDGSTNIKLAWLEDGEVKTLISPNSFKPEWSVSLGDKKPFNYEIDGEKYSFDPLSPDAVVTTDTSYQYSDVNVVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784  81 VHHALLNSGLEPQPVSLTVTLPLSEYYDGDCQRNEVNIRRKRENLMRELVLNKGRAFTVTDVKVMPESLPAAFSRLAELK 160
Cdd:pfam06406  81 IHHALLTSGLPPQDVDVVVTLPLSEYYDANNQPNMENIERKKANVMRPVELQGGETFTIRSVSVMPESIPAGFEVLKDLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784 161 pgPAETTLIIDLGGTTLDAGVIVGQFDDISAVHGNPSVGVSQVTRAAAGALRAADSETSALIADTVIRNRNDRQYLQRVI 240
Cdd:pfam06406 161 --ELESLLIIDLGGTTLDVAHVRGKLEGISKIYGDPSIGVSLITDAVKDALATASTRTSSYIADDLIIHRHDNNYLKQRI 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1890749784 241 NDAGKIDDVLNKITEAITSLGARVTSELTAFRNVNRVFLVGGGASLIEEAIRQAWPLAPDRIEVIGDPQLALAREIAL 318
Cdd:pfam06406 239 NNEDKRASVMEVINEAVKKLEQRVIRALSRFSGYTHVMVVGGGAELIATAIKKHTGVPDARFIKVDNPQFALVNGMYA 316
ASKHA_NBD_ParM_R1-like cd24022
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and ...
3-319 1.36e-83

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: 255.27  E-value: 1.36e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784   3 IYCDDGSTNVKLAWFEGN-ELQTRVSANSFRHGWKV---AEFSAATFNYQVGTLKYTWDSVSRDAIPTTNVEYQYGDLNL 78
Cdd:cd24022     1 VGIDDGSANIKVAWGEDDgKIKTFKIPSRARRGAAVsgsLGGGSQVFNYEVDGERYTVGDVVSDPIDTRNDDYQTSDLNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784  79 LAVHHALLNSGLEPQPVSLTVTLPLSEYYDGDCQRNEVNIRRKRENLMRELVLNKGRA-FTVTDVKVMPESLPAAFSRLA 157
Cdd:cd24022    81 VLVHHALHQAGLGGRKVDIVTGLPVSQYYYKDGQKNTELIERKKKNLKKPVTLLGGKSpATIVSVKVMPEGVAAYFDYLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784 158 ELKPG------PAETTLIIDLGGTTLDAGVIVGQFDDISAVHGNPSVGVSQVTRAAAGA--LRAADSETSALIADTVIRN 229
Cdd:cd24022   161 DEDGNgtdeeeEEGPVAVIDIGGTTTDIAVVSGGLSIDHARSGTIELGVLDVRDALKDAlkKRFGLSSISDAELDRALRT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784 230 RNDRqylqrviNDAGKIDDVLNKITEAITSLGARVTSELTA----FRNVNRVFLVGGGASLIEEAIRQAWplaPDRIEVI 305
Cdd:cd24022   241 GKFR-------LNGGKEVDVSDLVNEAIAEVAERILNEIKRrlgdASDLDRVIFVGGGAELLEDELKEAL---GPNAIIV 310
                         330
                  ....*....|....
gi 1890749784 306 GDPQLALAREIALY 319
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.
1-318 4.56e-124

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


Pssm-ID: 310773 [Multi-domain]  Cd Length: 317  Bit Score: 358.30  E-value: 4.56e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784   1 MNIYCDDGSTNVKLAWFEGNELQTRVSANSFRHGWKVAEFSAATFNYQVGTLKYTWDSVSRDAIPTTNVEYQYGDLNLLA 80
Cdd:pfam06406   1 MKIFIDDGSTNIKLAWLEDGEVKTLISPNSFKPEWSVSLGDKKPFNYEIDGEKYSFDPLSPDAVVTTDTSYQYSDVNVVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784  81 VHHALLNSGLEPQPVSLTVTLPLSEYYDGDCQRNEVNIRRKRENLMRELVLNKGRAFTVTDVKVMPESLPAAFSRLAELK 160
Cdd:pfam06406  81 IHHALLTSGLPPQDVDVVVTLPLSEYYDANNQPNMENIERKKANVMRPVELQGGETFTIRSVSVMPESIPAGFEVLKDLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784 161 pgPAETTLIIDLGGTTLDAGVIVGQFDDISAVHGNPSVGVSQVTRAAAGALRAADSETSALIADTVIRNRNDRQYLQRVI 240
Cdd:pfam06406 161 --ELESLLIIDLGGTTLDVAHVRGKLEGISKIYGDPSIGVSLITDAVKDALATASTRTSSYIADDLIIHRHDNNYLKQRI 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1890749784 241 NDAGKIDDVLNKITEAITSLGARVTSELTAFRNVNRVFLVGGGASLIEEAIRQAWPLAPDRIEVIGDPQLALAREIAL 318
Cdd:pfam06406 239 NNEDKRASVMEVINEAVKKLEQRVIRALSRFSGYTHVMVVGGGAELIATAIKKHTGVPDARFIKVDNPQFALVNGMYA 316
ASKHA_NBD_ParM_R1-like cd24022
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and ...
3-319 1.36e-83

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: 255.27  E-value: 1.36e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784   3 IYCDDGSTNVKLAWFEGN-ELQTRVSANSFRHGWKV---AEFSAATFNYQVGTLKYTWDSVSRDAIPTTNVEYQYGDLNL 78
Cdd:cd24022     1 VGIDDGSANIKVAWGEDDgKIKTFKIPSRARRGAAVsgsLGGGSQVFNYEVDGERYTVGDVVSDPIDTRNDDYQTSDLNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784  79 LAVHHALLNSGLEPQPVSLTVTLPLSEYYDGDCQRNEVNIRRKRENLMRELVLNKGRA-FTVTDVKVMPESLPAAFSRLA 157
Cdd:cd24022    81 VLVHHALHQAGLGGRKVDIVTGLPVSQYYYKDGQKNTELIERKKKNLKKPVTLLGGKSpATIVSVKVMPEGVAAYFDYLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784 158 ELKPG------PAETTLIIDLGGTTLDAGVIVGQFDDISAVHGNPSVGVSQVTRAAAGA--LRAADSETSALIADTVIRN 229
Cdd:cd24022   161 DEDGNgtdeeeEEGPVAVIDIGGTTTDIAVVSGGLSIDHARSGTIELGVLDVRDALKDAlkKRFGLSSISDAELDRALRT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784 230 RNDRqylqrviNDAGKIDDVLNKITEAITSLGARVTSELTA----FRNVNRVFLVGGGASLIEEAIRQAWplaPDRIEVI 305
Cdd:cd24022   241 GKFR-------LNGGKEVDVSDLVNEAIAEVAERILNEIKRrlgdASDLDRVIFVGGGAELLEDELKEAL---GPNAIIV 310
                         330
                  ....*....|....
gi 1890749784 306 GDPQLALAREIALY 319
Cdd:cd24022   311 DEPEFANARGMLKY 324
ASKHA_NBD_ParM-like cd10227
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ...
3-314 6.15e-21

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: 90.27  E-value: 6.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784   3 IYCDDGSTNVKLAWFEGNELQT-----RVSANSFRHGWKVaEFSAATFN---YQVGTLKYTWDSVSRdaipTTNVEYQYG 74
Cdd:cd10227     1 IGIDIGNGNTKVVTGGGKEFKFpsavaEARESSLDDGLLE-DDIIVEYNgkrYLVGELALREGGGGR----STGDDKKKS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784  75 DLNLLAVHHAL-LNSGLEPQPVSLTVTLPLSEYYDgdcqRNEVNIRRKRENLMRELVLNKGRAFTVTDVKVMPESLPAAF 153
Cdd:cd10227    76 EDALLLLLAALaLLGDDEEVDVNLVVGLPISEYKE----EKKELKKKLLKGLHEFTFNGKERRITINDVKVLPEGAGAYL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784 154 SRLAELKPGPAETTLIIDLGGTTLDAGVIV-GQFDDISavhgnpsvgvsqvtraaagalraadSETSALiadtviRNRND 232
Cdd:cd10227   152 DYLLDDDELEDGNVLVIDIGGGTTDILTFEnGKPIEES-------------------------SDTLPG------GEEAL 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784 233 RQYLQRVINDAGKIDDvlnkiteaitslgarvtselTAFRNVNRVFLVGGGASLIEEAIRQAWplaPDRIEVIGDPQLAL 312
Cdd:cd10227   201 EKYADDILNELLKKLG--------------------DELDSADKILLTGGGAELLKDYLKEAY---FPNIIVLDDPQFAN 257

                  ..
gi 1890749784 313 AR 314
Cdd:cd10227   258 AR 259
ASKHA_NBD_ParM_pCBH-like cd24025
nucleotide-binding domain (NBD) of Clostridium botulinum plasmid segregation protein ParM and ...
84-314 4.23e-13

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: 68.85  E-value: 4.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784  84 ALLNSGLEpQPVSLTVTLPLSEYYDgdcQRNEvnIRRKRENLMRELVLNKG---RAFTVTDVKVMPESLPAAFSRLAELK 160
Cdd:cd24025    94 ALLAAEDD-EPVSLVTGLPLSYYKT---QKEA--LEEMLKGLHAVVVGVDGgteKRITIDRVRVFPQGAGALYDALLDDD 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784 161 PGPAETTL------IIDLGGTTLDAGVIVGQFDDISAVHGNPSVGVSQVTraaagalraadSETSALIADTVIRNRNDRQ 234
Cdd:cd24025   168 GQIIDKALakgrvgVIDIGYRTTDYVVFEDGEFLVPELSGSLETGMSTAY-----------RAIANALEEEYGIDLDLHE 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784 235 YLQRVIND----AGKIDDVLNKITEAITSLGARVTSELTA-----FRNVNRVFLVGGGASLIEEAIRQAWPlapdRIEVI 305
Cdd:cd24025   237 LDRALREGkirvRGKEIDLSDLIDEALKELARQIANEIRSlwgdgLGDLDAIILAGGGAELLAPYLKEMFP----NAEVV 312

                  ....*....
gi 1890749784 306 GDPQLALAR 314
Cdd:cd24025   313 PDPQFANAR 321
ASKHA_NBD_ParM_Psk41-like cd24021
nucleotide-binding domain (NBD) of Staphylococcus aureus pSK41 actin-like ParM protein and ...
72-314 5.42e-10

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: 59.22  E-value: 5.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784  72 QYGDLNLLAVHHALLNSGLEPQPVSLTVTLPlSEYYDGDCQrNEVnirrkRENLMRE---LVLNKGRAFTVTDVKVMPES 148
Cdd:cd24021    84 EFKLLSLIALAKLAKDYDEDVVEVVVVTGLP-SEDYDTEVE-EEL-----KKVLKGEhtvKINGKERTINVKDVYVIPQP 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784 149 LPAAFSRLA--ELKPGPAE----TTLIIDLGGTTLDaGVIVGQFDDISAVHGNPSvGVSQVTRAaagalraadsetsali 222
Cdd:cd24021   157 LGTLYNLLLdeNGEVKNEEledsKVLIIDIGGGTTD-VDVINGLKIDENRFQIET-GMKDVYDE---------------- 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784 223 adtvIRNRNDRQYLQRVINDAGkiDDVLNKITEAitslgarvtseLTAFRNVNRVFLVGGGASLIEEAIRQAwpLAPDRI 302
Cdd:cd24021   219 ----IAKEDITEIVEKAIEEYA--EEIVAEINNA-----------FKDLDSFDKVIFTGGGANILNKYLKEK--LEGDNF 279
                         250
                  ....*....|..
gi 1890749784 303 EVIGDPQLALAR 314
Cdd:cd24021   280 VFVENPQTANVR 291
ASKHA_NBD_ParM_Alp12-like cd24026
nucleotide-binding domain (NBD) of Clostridium tetani actin-like protein Alp12 and similar ...
78-309 6.00e-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: 47.28  E-value: 6.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784  78 LLAVHHALLNSGLEPqpVSLTVTLPLSEYYDGDcQRNEVnirrkRENLMRE-----LVLNKGRAFTVTDVKVMPESLPAA 152
Cdd:cd24026    80 YTAIAKLLENDKGNE--VNLVVGCPLNIYKNKE-LKEEY-----KEFIKGNgkiiiIVNGEKKSFKITDVTVKPEGSGVI 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784 153 FSRLAELKpgpAETTLIIDLGG------------------TTLDAGVIV---GQFDDISAVHGN--PSVGVSQVTRAAAG 209
Cdd:cd24026   152 YRNPEKFK---NKNVGVIDIGGlnvnfciydngipipesmFTDNLGGNVlenKIKEALNSYFGGniQDYDILNILINGYI 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784 210 ALRAADSETSALIADTVIRNrndrqYLQRVINDAGKiddvlNKITEaitslgarvtseltafrNVNRVFLVGGGASLIEE 289
Cdd:cd24026   229 KFNGEIEEESKEIIEEIKDE-----HLKEIINKIKS-----RKWNL-----------------ENMDIIFVGGTSLLLKD 281
                         250       260
                  ....*....|....*....|
gi 1890749784 290 AIRQAWPLApdriEVIGDPQ 309
Cdd:cd24026   282 YIKELFPNA----TISEDAQ 297
ASKHA_NBD_ParM_Alp7A-like cd24023
nucleotide-binding domain (NBD) of Bacillus subtilis actin-like protein Alp7A and similar ...
76-294 3.77e-04

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: 41.93  E-value: 3.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784  76 LNLLAVHHALLNSGLEPQP-----VSLTVTLPLSEYYDGdcqrnevNIRRKRENLMR---ELVLNKGRAFTVT------D 141
Cdd:cd24023   101 LTAIAYYAVKEAYEDDIKDeievkVDLSTGLPISEYKKE-------GAKEFFERFLKgehTVTFLDGPGKGVTvtikfeD 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784 142 VKVMPESLPAAFS-----------RLAELKPGPAETTLIIDLGGTTLDAGVIVGQFDDISAVHGNPsVGVSQVTRA--AA 208
Cdd:cd24023   174 VKVLPEGVAALFAliydedgnervEDTEDEDLKEKNILIIDIGGGTTDVAVFEGGKFDPDLSTGID-LGIGTALDEiiKE 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784 209 GALRAADSETSALIADTVIRNRNdrqylQRVINDAGKIDDVLNKITEAITSLGARVTSEL-----TAFRNVNRVFLVGGG 283
Cdd:cd24023   253 LKKEYGVEFDRRRLLFELIIKKK-----EYKDKNRGKKVDLTDIVEKALEELAEEILDEIekkwnKAGNDIEVIYVYGGG 327
                         250
                  ....*....|.
gi 1890749784 284 ASLIEEAIRQA 294
Cdd:cd24023   328 SILLKDYLKEL 338
ASKHA_NBD_HSP70 cd10170
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ...
124-314 1.14e-03

nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family chaperones assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some HSP70 family members are not chaperones but instead, function as NEFs to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle, some may function as both chaperones and NEFs. The HSP70 family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466811 [Multi-domain]  Cd Length: 329  Bit Score: 40.17  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784 124 NLMRELVLNKGRAFTVTDVKVMPESLpAAF-------SRLAELKPGpaETTLIIDLGGTTLDAGVI-----VGQFDDISA 191
Cdd:cd10170    91 EALREAARAAGFGSDSDNVRLVSEPE-AAAlyaledkGDLLPLKPG--DVVLVCDAGGGTVDLSLYevtsgSPLLLEEVA 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784 192 VHGNPSVGVSQVT-------------RAAAGALRAADSETSAL---------------------IADTVIRNRNDRQYLQ 237
Cdd:cd10170   168 PGGGALLGGTDIDeafekllreklgdKGKDLGRSDADALAKLLrefeeakkrfsggeederlvpSLLGGGLPELGLEKGT 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784 238 RVINDAGK---IDDVLNKITEAITSLGARvtselTAFRNVNRVFLVGGGAS--LIEEAIRQAWPLAPDRIEVIG-DPQLA 311
Cdd:cd10170   248 LLLTEEEIrdlFDPVIDKILELIEEQLEA-----KSGTPPDAVVLVGGFSRspYLRERLRERFGSAGIIIVLRSdDPDTA 322

                  ...
gi 1890749784 312 LAR 314
Cdd:cd10170   323 VAR 325
ASKHA_NBD_ParM_Ta0583-like cd24027
nucleotide-binding domain (NBD) of Thermoplasma acidophilum archaeal actin homolog and similar ...
84-308 4.77e-03

nucleotide-binding domain (NBD) of Thermoplasma acidophilum archaeal actin homolog and similar proteins from the ParM domain family; The family corresponds to a group of uncharacterized proteins similar to Thermoplasma acidophilum archaeal actin homolog Ta0583, which is the archaeal counterpart of the eukaryotic structural protein actin, such as MreB and ParM. Ta0583 could have a function in cellular organization. It polymerizes into bundles of filaments, forming a helix with a filament width of 5.5 nm and an axial repeating unit of 5.5 nm. Polymerization of Ta0583 requires NTP and is optimal with ATP, but GTP, UTP, CTP, and even the deoxy form of NTP can also support the polymerization reaction. Nucleoside diphosphate or AMP-PNP does not support polymerization.


Pssm-ID: 466877 [Multi-domain]  Cd Length: 323  Bit Score: 38.37  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784  84 ALLNSGLE---PQPVSLTVTLPLSEYYDgdcqrnEVNIRRKRENLMRELVLNKG---RAFTVTDVKVMPESLPAAFSRLA 157
Cdd:cd24027    87 ALWESGIHndsPVDLFLGTGLPLGTFDL------EVKAAKEALENKVLTVTGPEgevRKINITRLEIRPQGVGAALYLLN 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784 158 ELKPGPAETT----LIIDLGGTTLDAGVIvgQFDDISAVHGNPSVGVSQVTRAAAGALRAADSETSALI----ADTVIRN 229
Cdd:cd24027   161 QGIIEESEQQpgygVVIDVGSRTTDVLTI--RLGDVVELSFSLQIGVAVYGRAIKALSRKIAKETGFVVpfdlAQEALSH 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890749784 230 -----RNDRQYLQRVINDAgkIDDVLNKITEAItslgarvtseLTAFRN-VNRV---FLVGGGASLIEEAIRQawpLAPD 300
Cdd:cd24027   239 pvlfrQKEQVDGPEVSGPI--LEDLANRIIENI----------RLNLRGeVDRVtslLLVGGGSNLIGDRFEE---IAPG 303

                  ....*...
gi 1890749784 301 RIEVIGDP 308
Cdd:cd24027   304 TLVKIKPE 311
 
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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