NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2727058535|ref|WP_343032239|]
View 

Hsp70 family protein [Allochromatium palmeri]

Protein Classification

Hsp70 family protein( domain architecture ID 10178379)

Hsp70 (heat shock protein 70) family protein is a molecular chaperone involved in DNA replication, protein folding and the stress response; similar to Beet yellows virus movement protein Hsp70h, which transports viral genomes to neighboring plant cells directly through the plasmodesmata

CATH:  3.30.420.40
Gene Ontology:  GO:0005524|GO:0140662
PubMed:  8800467|15770419|7781919
SCOP:  3000092

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ASKHA_NBD_HSP70 cd10170
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ...
 20-407 9.47e-32

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: 126.07  E-value: 9.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  20 LAIDFGTSNTYVTKCPGDKEDPVGVDFGDGRDGIATAilyrDGKEPLIGHVAleefgdagaehddyriraqfkpdlvssa 99
Cdd:cd10170     1 VGIDFGTTYSGVAYALLGPGEPPLVVLQLPWPGGDGG----SSKVPSVLEVV---------------------------- 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 100 eartyaRDFLVGLLTLARRQHKDIAPLQ----RQVIFGVPSEASETYRDALRAIAEEAGFGA----VKTVDEPKGALYFH 171
Cdd:cd10170    49 ------ADFLRALLEHAKAELGDRIWELekapIEVVITVPAGWSDAAREALREAARAAGFGSdsdnVRLVSEPEAAALYA 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 172 LQRKDI-TPIEALRGALVVDFGGGTCDFALLVRGEILHS-------WGDMHLGGRLFDDLFYQWFIEQNPEAVVAMRRER 243
Cdd:cd10170   123 LEDKGDlLPLKPGDVVLVCDAGGGTVDLSLYEVTSGSPLlleevapGGGALLGGTDIDEAFEKLLREKLGDKGKDLGRSD 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 244 AEFFVLAVR-CREVKEKFSLAMALDPTTvyrktlgaYGRLNDVTWDSFLARARRYRPSETFAqylramnpqagahldtfp 322
Cdd:cd10170   203 ADALAKLLReFEEAKKRFSGGEEDERLV--------PSLLGGGLPELGLEKGTLLLTEEEIR------------------ 256

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 323 qgiDLLDWFRQTLRQGL--AHEQMRHQDLACVILTGGSSAWPFVADIVTDELKQIQPKPIepsqiersprlVHSDRPYVT 400
Cdd:cd10170   257 ---DLFDPVIDKILELIeeQLEAKSGTPPDAVVLVGGFSRSPYLRERLRERFGSAGIIIV-----------LRSDDPDTA 322


                  ....*..
gi 2727058535 401 VSQGLAI 407
Cdd:cd10170   323 VARGAAL 329
AraH super family cl42655
Ribose/xylose/arabinose/galactoside ABC-type transport system, permease component ...
 558-610 6.57e-03

Ribose/xylose/arabinose/galactoside ABC-type transport system, permease component [Carbohydrate transport and metabolism];


The actual alignment was detected with superfamily member COG1172:

Pssm-ID: 440785  Cd Length: 322  Bit Score: 39.32  E-value: 6.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2727058535 558 GVVLALSAtiisVLAATISGGAGTAIIMSGPIGLLIGALVGLIAGALAMRYGL 610
Cdd:COG1172    76 GSVVALSG----VVAALLLVALGLPILLAILLALLVGALLGLLNGLLVAKLRI 124
 
Name Accession Description Interval E-value
ASKHA_NBD_HSP70 cd10170
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ...
 20-407 9.47e-32

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: 126.07  E-value: 9.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  20 LAIDFGTSNTYVTKCPGDKEDPVGVDFGDGRDGIATAilyrDGKEPLIGHVAleefgdagaehddyriraqfkpdlvssa 99
Cdd:cd10170     1 VGIDFGTTYSGVAYALLGPGEPPLVVLQLPWPGGDGG----SSKVPSVLEVV---------------------------- 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 100 eartyaRDFLVGLLTLARRQHKDIAPLQ----RQVIFGVPSEASETYRDALRAIAEEAGFGA----VKTVDEPKGALYFH 171
Cdd:cd10170    49 ------ADFLRALLEHAKAELGDRIWELekapIEVVITVPAGWSDAAREALREAARAAGFGSdsdnVRLVSEPEAAALYA 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 172 LQRKDI-TPIEALRGALVVDFGGGTCDFALLVRGEILHS-------WGDMHLGGRLFDDLFYQWFIEQNPEAVVAMRRER 243
Cdd:cd10170   123 LEDKGDlLPLKPGDVVLVCDAGGGTVDLSLYEVTSGSPLlleevapGGGALLGGTDIDEAFEKLLREKLGDKGKDLGRSD 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 244 AEFFVLAVR-CREVKEKFSLAMALDPTTvyrktlgaYGRLNDVTWDSFLARARRYRPSETFAqylramnpqagahldtfp 322
Cdd:cd10170   203 ADALAKLLReFEEAKKRFSGGEEDERLV--------PSLLGGGLPELGLEKGTLLLTEEEIR------------------ 256

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 323 qgiDLLDWFRQTLRQGL--AHEQMRHQDLACVILTGGSSAWPFVADIVTDELKQIQPKPIepsqiersprlVHSDRPYVT 400
Cdd:cd10170   257 ---DLFDPVIDKILELIeeQLEAKSGTPPDAVVLVGGFSRSPYLRERLRERFGSAGIIIV-----------LRSDDPDTA 322


                  ....*..
gi 2727058535 401 VSQGLAI 407
Cdd:cd10170   323 VARGAAL 329
DnaK COG0443
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ...
 19-407 3.26e-24

Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440212 [Multi-domain]  Cd Length: 473  Bit Score: 106.45  E-value: 3.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  19 VLAIDFGTSNTYVTKCPGDKedPVGVDFGDGRDGIATAILYRDGKEPLIGHVALEefgdAGAEHDDYRIRAqFK------ 92
Cdd:COG0443     1 AIGIDLGTTNSVVAVVEGGE--PQVIPNAEGRRTLPSVVAFPKDGEVLVGEAAKR----QAVTNPGRTIRS-IKrllgrs 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  93 -PDLVSSAEARTY-----ARDFLVGLLTLARRQHKDiaPLQRQVIfGVPSEASETYRDALRAIAEEAGFGAVKTVDEPKG 166
Cdd:COG0443    74 lFDEATEVGGKRYspeeiSALILRKLKADAEAYLGE--PVTRAVI-TVPAYFDDAQRQATKDAARIAGLEVLRLLNEPTA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 167 ALYFHLQRKDitPIEALrgALVVDFGGGTCDFALLVRG----EILHSWGDMHLGGRLFDDLFYQWFIEQNPEAV-VAMRR 241
Cdd:COG0443   151 AALAYGLDKG--KEEET--ILVYDLGGGTFDVSILRLGdgvfEVLATGGDTHLGGDDFDQALADYVAPEFGKEEgIDLRL 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 242 ERAEFFVLAVRCREVKEKFSLAMAldpTTVyrkTLGAYGrlnDVTWDSFLARArryrpseTFAQYLRamnpqagahldtf 321
Cdd:COG0443   227 DPAALQRLREAAEKAKIELSSADE---AEI---NLPFSG---GKHLDVELTRA-------EFEELIA------------- 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 322 pqgiDLLDWFRQTLRQGLAHEQMRHQDLACVILTGGSSAWPFVADIVTDELKQiqpkpiEPsqiersprlVHSDRPYVTV 401
Cdd:COG0443   278 ----PLVERTLDPVRQALADAGLSPSDIDAVLLVGGSTRMPAVRERVKELFGK------EP---------LKGVDPDEAV 338


                  ....*.
gi 2727058535 402 SQGLAI 407
Cdd:COG0443   339 ALGAAI 344
dnaK CHL00094
heat shock protein 70
 129-231 4.88e-08

heat shock protein 70


Pssm-ID: 214360 [Multi-domain]  Cd Length: 621  Bit Score: 56.28  E-value: 4.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 129 QVIFGVPSEASETYRDALRAIAEEAGFGAVKTVDEPKGA-LYFHLQRKDITPIealrgaLVVDFGGGTCDFALLVRG--- 204
Cdd:CHL00094  137 QAVITVPAYFNDSQRQATKDAGKIAGLEVLRIINEPTAAsLAYGLDKKNNETI------LVFDLGGGTFDVSILEVGdgv 210

                          90       100
                  ....*....|....*....|....*...
gi 2727058535 205 -EILHSWGDMHLGGRLFDDLFYQWFIEQ 231
Cdd:CHL00094  211 fEVLSTSGDTHLGGDDFDKKIVNWLIKE 238
MreB_Mbl pfam06723
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ...
 130-209 2.13e-06

MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.


Pssm-ID: 399596 [Multi-domain]  Cd Length: 327  Bit Score: 50.25  E-value: 2.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 130 VIFGVPSEASETYRDALRAIAEEAGFGAVKTVDEPK----GAlyfhlqrkDItPIEALRGALVVDFGGGTCDFALLVRGE 205
Cdd:pfam06723  96 VVICVPSGITEVERRAVKEAAKNAGAREVFLIEEPMaaaiGA--------GL-PVEEPTGNMVVDIGGGTTEVAVISLGG 166


                  ....
gi 2727058535 206 ILHS 209
Cdd:pfam06723 167 IVTS 170
AraH COG1172
Ribose/xylose/arabinose/galactoside ABC-type transport system, permease component ...
 558-610 6.57e-03

Ribose/xylose/arabinose/galactoside ABC-type transport system, permease component [Carbohydrate transport and metabolism];


Pssm-ID: 440785  Cd Length: 322  Bit Score: 39.32  E-value: 6.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2727058535 558 GVVLALSAtiisVLAATISGGAGTAIIMSGPIGLLIGALVGLIAGALAMRYGL 610
Cdd:COG1172    76 GSVVALSG----VVAALLLVALGLPILLAILLALLVGALLGLLNGLLVAKLRI 124
 
Name Accession Description Interval E-value
ASKHA_NBD_HSP70 cd10170
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ...
 20-407 9.47e-32

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: 126.07  E-value: 9.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  20 LAIDFGTSNTYVTKCPGDKEDPVGVDFGDGRDGIATAilyrDGKEPLIGHVAleefgdagaehddyriraqfkpdlvssa 99
Cdd:cd10170     1 VGIDFGTTYSGVAYALLGPGEPPLVVLQLPWPGGDGG----SSKVPSVLEVV---------------------------- 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 100 eartyaRDFLVGLLTLARRQHKDIAPLQ----RQVIFGVPSEASETYRDALRAIAEEAGFGA----VKTVDEPKGALYFH 171
Cdd:cd10170    49 ------ADFLRALLEHAKAELGDRIWELekapIEVVITVPAGWSDAAREALREAARAAGFGSdsdnVRLVSEPEAAALYA 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 172 LQRKDI-TPIEALRGALVVDFGGGTCDFALLVRGEILHS-------WGDMHLGGRLFDDLFYQWFIEQNPEAVVAMRRER 243
Cdd:cd10170   123 LEDKGDlLPLKPGDVVLVCDAGGGTVDLSLYEVTSGSPLlleevapGGGALLGGTDIDEAFEKLLREKLGDKGKDLGRSD 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 244 AEFFVLAVR-CREVKEKFSLAMALDPTTvyrktlgaYGRLNDVTWDSFLARARRYRPSETFAqylramnpqagahldtfp 322
Cdd:cd10170   203 ADALAKLLReFEEAKKRFSGGEEDERLV--------PSLLGGGLPELGLEKGTLLLTEEEIR------------------ 256

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 323 qgiDLLDWFRQTLRQGL--AHEQMRHQDLACVILTGGSSAWPFVADIVTDELKQIQPKPIepsqiersprlVHSDRPYVT 400
Cdd:cd10170   257 ---DLFDPVIDKILELIeeQLEAKSGTPPDAVVLVGGFSRSPYLRERLRERFGSAGIIIV-----------LRSDDPDTA 322


                  ....*..
gi 2727058535 401 VSQGLAI 407
Cdd:cd10170   323 VARGAAL 329
DnaK COG0443
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ...
 19-407 3.26e-24

Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440212 [Multi-domain]  Cd Length: 473  Bit Score: 106.45  E-value: 3.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  19 VLAIDFGTSNTYVTKCPGDKedPVGVDFGDGRDGIATAILYRDGKEPLIGHVALEefgdAGAEHDDYRIRAqFK------ 92
Cdd:COG0443     1 AIGIDLGTTNSVVAVVEGGE--PQVIPNAEGRRTLPSVVAFPKDGEVLVGEAAKR----QAVTNPGRTIRS-IKrllgrs 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  93 -PDLVSSAEARTY-----ARDFLVGLLTLARRQHKDiaPLQRQVIfGVPSEASETYRDALRAIAEEAGFGAVKTVDEPKG 166
Cdd:COG0443    74 lFDEATEVGGKRYspeeiSALILRKLKADAEAYLGE--PVTRAVI-TVPAYFDDAQRQATKDAARIAGLEVLRLLNEPTA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 167 ALYFHLQRKDitPIEALrgALVVDFGGGTCDFALLVRG----EILHSWGDMHLGGRLFDDLFYQWFIEQNPEAV-VAMRR 241
Cdd:COG0443   151 AALAYGLDKG--KEEET--ILVYDLGGGTFDVSILRLGdgvfEVLATGGDTHLGGDDFDQALADYVAPEFGKEEgIDLRL 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 242 ERAEFFVLAVRCREVKEKFSLAMAldpTTVyrkTLGAYGrlnDVTWDSFLARArryrpseTFAQYLRamnpqagahldtf 321
Cdd:COG0443   227 DPAALQRLREAAEKAKIELSSADE---AEI---NLPFSG---GKHLDVELTRA-------EFEELIA------------- 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 322 pqgiDLLDWFRQTLRQGLAHEQMRHQDLACVILTGGSSAWPFVADIVTDELKQiqpkpiEPsqiersprlVHSDRPYVTV 401
Cdd:COG0443   278 ----PLVERTLDPVRQALADAGLSPSDIDAVLLVGGSTRMPAVRERVKELFGK------EP---------LKGVDPDEAV 338


                  ....*.
gi 2727058535 402 SQGLAI 407
Cdd:COG0443   339 ALGAAI 344
ASKHA_NBD_HSP70_DnaK_HscA_HscC cd24029
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ...
 22-385 5.95e-20

nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and similar proteins; Escherichia coli DnaK, also called heat shock 70 kDa protein/HSP70, plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Moreover, DnaK participates actively in the response to hyperosmotic shock. Escherichia coli HscA, also called Hsc66, acts as a chaperone involved in the maturation of iron-sulfur cluster-containing proteins. It has a low intrinsic ATPase activity which is markedly stimulated by HscB. It is involved in the maturation of IscU. Escherichia coli HscC, also called Hsc62, or YbeW, may act as the chaperone. It has ATPase activity. It cannot be stimulated by DnaJ. The family also includes Saccharomyces cerevisiae stress-seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and Ssc3p (also called extracellular mutant protein 10/Ecm10), and Saccharomyces cerevisiae Stress-seventy subfamily Q protein 1/Ssq1p (also called Ssc2p; Ssh1p; mtHSP70 homolog). They all belong to the heat shock protein 70 (HSP70) family of chaperones that 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); for Escherichia coli DnaK, these are the DnaJ and GrpE, respectively.


Pssm-ID: 466879 [Multi-domain]  Cd Length: 351  Bit Score: 91.87  E-value: 5.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  22 IDFGTSNTYVTKCPGDKEDPVGVDFGdGRDGIATAILYRDGKEPLIGHVALEEfgdagAEHDDYRIRAQFK------PDL 95
Cdd:cd24029     3 IDLGTTNSAVAYWDGNGAEVIIENSE-GKRTTPSVVYFDKDGEVLVGEEAKNQ-----ALLDPENTIYSVKrlmgrdTKD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  96 VSSAEARTY-----ARDFLVGLLTLARRQHKDiaPLQRQVIfGVPSEASETYRDALRAIAEEAGFGAVKTVDEPKGAL-- 168
Cdd:cd24029    77 KEEIGGKEYtpeeiSAEILKKLKEDAEEQLGG--EVKGAVI-TVPAYFNDKQRKATKKAAELAGLNVLRLINEPTAAAla 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 169 --YFHLQRKDItpiealrgALVVDFGGGTCDFALL-VRG---EILHSWGDMHLGGRLFDDLFYQWFIEQNPEAVVAMRRE 242
Cdd:cd24029   154 ygLDKEGKDGT--------ILVYDLGGGTFDVSILeIENgkfEVLATGGDNFLGGDDFDEAIAELILEKIGIETGILDDK 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 243 RAEFFV--LAVRCREVKEKFSlamaldptTVYRKTLGAYGRLNDVTWDSFLararryrpseTFAQYLRAMNPqagahldt 320
Cdd:cd24029   226 EDERARarLREAAEEAKIELS--------SSDSTDILILDDGKGGELEIEI----------TREEFEELIAP-------- 279

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2727058535 321 fpqgidLLDWFRQTLRQGLAHEQMRHQDLACVILTGGSSAWPFVADIVTDELKQIQPKPIEPSQI 385
Cdd:cd24029   280 ------LIERTIDLLEKALKDAKLSPEDIDRVLLVGGSSRIPLVREMLEEYFGREPISSVDPDEA 338
ASKHA_NBD_HSP70_YegD-like cd10231
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ...
 20-406 3.56e-13

nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar proteins; The family includes a group of uncharacterized proteins similar to Escherichia coli chaperone protein YegD that belongs to the heat shock protein 70 family of chaperones that 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. YegD lacks the SBD. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some family members are not chaperones but instead, function as NEFs for their Hsp70 partners, other family members function as both chaperones and NEFs.


Pssm-ID: 466829 [Multi-domain]  Cd Length: 409  Bit Score: 71.92  E-value: 3.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  20 LAIDFGTSNTYVTKCPGDKedPVGVDFGDGRDGIATAILYRDGKEPLIGHValeEFGDAGAEH-----DDYRIRAQFKPD 94
Cdd:cd10231     1 IGLDFGTSNSSLAVADDGK--TDLVPFEGDSPTLPSLLYFPRREEEGAESI---YFGNDAIDAylndpEEGRLIKSVKSF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  95 LVSSAEARTYA---RDFLVGLLTLARRQHKDIAPLQ-----RQVIFGVPSEASETYRDA-------LRAIAEEAGFGAVK 159
Cdd:cd10231    76 LGSSLFDETTIfgrRYPFEDLVAAILRHLKRRAERQlgeeiDSVVVGRPVHFSGVGAEDdaqaesrLRDAARRAGFRNVE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 160 TVDEPKGA-LYFHLQRKDitpiEALrgALVVDFGGGTCDFALL--------VRGEILHSWGDmHLGG-----RLFDDLFY 225
Cdd:cd10231   156 FQYEPIAAaLDYEQRLDR----EEL--VLVVDFGGGTSDFSVLrlgpnrtdRRADILATSGV-GIGGddfdrELALKKVM 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 226 QWFIEQNPEAVV-AMRRERAEFFVLAVR---CREVKEKFSLAMALDPTTVYRKTlGAYGRLNDVtwdsfLARARRYR--- 298
Cdd:cd10231   229 PHLGRGSTYVSGdKGLPVPAWLYADLSNwhaISLLYTKKTLRLLLDLRRDAADP-EKIERLLSL-----VEDQLGHRlfr 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 299 ------------PSETFAqyLRAMNPQAGAHL--DTFPQGI-DLLDWFRQTLRQGLAHEQMRHQDLACVILTGGSSAWPF 363
Cdd:cd10231   303 aveqakialssaDEATLS--FDFIEISIKVTItrDEFETAIaFPLARILEALERTLNDAGVKPSDVDRVFLTGGSSQSPA 380

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 2727058535 364 VADIVTDELKQIqpkpiepsqierspRLVHSDrPYVTVSQGLA 406
Cdd:cd10231   381 VRQALASLFGQA--------------RLVEGD-EFGSVAAGLA 408
ASKHA_NBD_HSP70_HSPA1-like cd24028
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ...
 134-370 7.38e-13

nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The HSPA1-like family includes human HSPA1A (70-kDa heat shock protein 1A, also known as HSP72; HSPA1; HSP70I; HSPA1B; HSP70-1; HSP70-1A), HSPA1B (70-kDa heat shock protein 1B, also known as HSPA1A; HSP70-2; HSP70-1B), and HSPA1L (70-kDa heat shock protein 1-like, also known as HSP70T; hum70t; HSP70-1L; HSP70-HOM), HSPA2 (70-kDa heat shock protein 2, also known as HSP70-2; HSP70-3), BiP (also known as HSP70 family protein 5 /HSPA5; 70-kDa heat shock protein 5; glucose-regulated protein 78/GRP78; immunoglobulin heavy chain-binding protein), HSPA6 (also known as heat shock 70kDa protein 6; HSP70B'), HSPA7 (heat shock 70kDa protein 7 , also known as HSP70B), HSPA8 (heat shock 70kDa protein 8, also known as Lipopolysaccharide-associated protein 1/LAP1; HSC70; HSP73; HSPA10), HSPA13 (also known as 70-kDa heat shock protein 13; STCH; microsomal stress-70 protein ATPase core; stress-70 protein chaperone microsome-associated 60 kDa protein), as well as Saccharmoyces cerevisiae Hsp70 chaperone Ssb1-2 and heat shock protein Ssa1-4. HSPA1A/1B, HSPA1L, HSPA2 and HSPA6-8 are molecular chaperones implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. They play pivotal roles in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. BiP plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. It plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). HSPA13 has peptide-independent ATPase activity. All family members belong to the heat shock protein 70 (HSP70) family of chaperones that 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).


Pssm-ID: 466878 [Multi-domain]  Cd Length: 376  Bit Score: 70.62  E-value: 7.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 134 VPSEASETYRDALRAIAEEAGFGAVKTVDEPK-GALYFHLQRKDITpieaLRGALVVDFGGGTCDFALL-VRG---EILH 208
Cdd:cd24028   142 VPAYFNDAQRQATKDAATIAGLNVLRIINEPTaAALAYGLDKKSSG----ERNVLVFDLGGGTFDVSLLsIDNgvfEVKA 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 209 SWGDMHLGGRLFDDLFYQWFIE-----------QNPEAVVAMRREraeffvlavrCREVKEKFSLAMAldpTTVYRKTLG 277
Cdd:cd24028   218 TAGDTHLGGEDFDNRLVEYLVEefkkkhgkdlrENPRAMRRLRSA----------CERAKRTLSTSTS---ATIEIDSLY 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 278 aygrlNDVTWDSFLARARryrpsetfaqyLRAMNpqagahLDTFPQGIDLLDwfrQTLRQGlaheQMRHQDLACVILTGG 357
Cdd:cd24028   285 -----DGIDFETTITRAK-----------FEELC------EDLFKKCLEPVE---KVLKDA----KLSKDDIDEVVLVGG 335

                         250
                  ....*....|...
gi 2727058535 358 SSAWPFVADIVTD 370
Cdd:cd24028   336 STRIPKIQELLSE 348
ASKHA_NBD_HSP70_HscC cd10235
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ...
 125-414 1.10e-12

nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar proteins; Escherichia coli HscC, also called Hsc62, or YbeW, may act as the chaperone. It has ATPase activity. It cannot be stimulated by DnaJ. Members in this subfamily belong to the heat shock protein 70 (Hsp70) family of chaperones that 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). Two genes in the vicinity of the HscC gene code for potential cochaperones: J-domain containing proteins, DjlB/YbeS and DjlC/YbeV. HscC and its co-chaperone partners may play a role in the SOS DNA damage response. HscC does not appear to require a NEF.


Pssm-ID: 466833 [Multi-domain]  Cd Length: 343  Bit Score: 69.97  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 125 PLQRQVIfGVPSEASETYRDALRAIAEEAGFGAVKTVDEPKGA-LYFHLQRKDitpiEALRgALVVDFGGGTCDFALL-- 201
Cdd:cd10235   106 PVTEAVI-SVPAYFNDEQRKATKDAGELAGLKVERLINEPTAAaLAYGLHKRE----DETR-FLVFDLGGGTFDVSVLel 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 202 VRG--EILHSWGDMHLGGRLFDDLFYQWFIEQNPEAVVAMRRERAEffVLAVRCREVKEKFSLAMALDPTTVYRKTLGAY 279
Cdd:cd10235   180 FEGviEVHASAGDNFLGGEDFTHALADYFLKKHRLDFTSLSPSELA--ALRKRAEQAKRQLSSQDSAEIRLTYRGEELEI 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 280 grlnDVTwdsflararryrpSETFAQylrAMNPqagahldtfpqgidLLDWFRQTLRQGLAHEQMRHQDLACVILTGGSS 359
Cdd:cd10235   258 ----ELT-------------REEFEE---LCAP--------------LLERLRQPIERALRDAGLKPSDIDAVILVGGAT 303

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2727058535 360 AWPFVADIVTDELKQIQPKPIEPSQiersprlvhsdrpyvTVSQGLAIVPALQQR 414
Cdd:cd10235   304 RMPLVRQLIARLFGRLPLSSLDPDE---------------AVALGAAIQAALKAR 343
ASKHA_NBD_MreB-like cd10225
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ...
 20-209 8.95e-11

nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins; MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like 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: 466824 [Multi-domain]  Cd Length: 317  Bit Score: 63.65  E-value: 8.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  20 LAIDFGTSNTYVtkcpgdkedpvgvdFGDGRdGIataILyrdgKEPLIghVALEE-------FGDA-----GAEHDDYRI 87
Cdd:cd10225     2 IGIDLGTANTLV--------------YVKGK-GI---VL----NEPSV--VAVDKntgkvlaVGEEakkmlGRTPGNIVA 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  88 RAQFKPDLVSSAEArtyARDFLVGLLTLARRQHKDIAPlqrQVIFGVPSEASETYRDALRAIAEEAGFGAVKTVDEPK-G 166
Cdd:cd10225    58 IRPLRDGVIADFEA---TEAMLRYFIRKAHRRRGFLRP---RVVIGVPSGITEVERRAVKEAAEHAGAREVYLIEEPMaA 131

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2727058535 167 ALYFHLqrkditPIEALRGALVVDFGGGTCDFALLVRGEILHS 209
Cdd:cd10225   132 AIGAGL------PIEEPRGSMVVDIGGGTTEIAVISLGGIVTS 168
ASKHA_NBD_HSP70_HSPA12 cd10229
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ...
 19-227 9.47e-10

nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar proteins; The family includes heat shock 70 kDa proteins HSPA12A and HSPA12B. HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. Both HSPA12A and HSPA12B belong to the heat shock protein 70 (HSP70) family of chaperones that 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). No co-chaperones have yet been identified for HSPA12A and HSPA12B.


Pssm-ID: 466827 [Multi-domain]  Cd Length: 372  Bit Score: 61.14  E-value: 9.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  19 VLAIDFGTSNT-----YVTKCPGD--KEDPVGVDFGDGRDGIATAILYRDGKEPL-IGHVALEEFGDAGA--EHDDYRiR 88
Cdd:cd10229     2 VVAIDFGTTYSgyaysFITDPGDIhtMYNWWGAPTGVSSPKTPTCLLLNPDGEFHsFGYEAREKYSDLAEdeEHQWLY-F 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  89 AQFKPDLVSSAEART-----------------------YARDFLvgLLTLARRQHKDIAPLQRQVIFGVPSEASETYRDA 145
Cdd:cd10229    81 FKFKMMLLSEKELTRdtkvkavngksmpalevfaealrYLKDHA--LKELRDRSGSSLDEDDIRWVLTVPAIWSDAAKQF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 146 LRAIAEEAGFgaVKTVD--------EPKGALYF---HLQRKDITPIEALRGALVVDFGGGTCDFALL-----VRGEILHS 209
Cdd:cd10229   159 MREAAVKAGL--ISEENseqliialEPEAAALYcqkLLAEGEEKELKPGDKYLVVDCGGGTVDITVHevledGKLEELLK 236

                         250
                  ....*....|....*...
gi 2727058535 210 WGDMHLGGRLFDDLFYQW 227
Cdd:cd10229   237 ASGGPWGSTSVDEEFEEL 254
ASKHA_NBD_HSP70_HSPA13 cd10237
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ...
 19-242 4.01e-09

nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; HSPA13, also called 70-kDa heat shock protein 13, STCH, microsomal stress-70 protein ATPase core, or stress-70 protein chaperone microsome-associated 60 kDa protein, has peptide-independent ATPase activity. It belongs to the heat shock protein 70 (HSP70) family of chaperones that 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). HSPA13 contains an NBD but lacks an SBD. It may function to regulate cell proliferation and survival and modulate the TRAIL-mediated cell death pathway. The HSPA13 gene is a candidate stomach cancer susceptibility gene; a mutation in the NBD coding region of HSPA13 has been identified in stomach cancer cells. The NBD of HSPA13 interacts with the ubiquitin-like proteins Chap1 and Chap2, implicating HSPA13 in regulating cell cycle and cell death events. HSPA13 is induced by the Ca2+ ionophore A23187.


Pssm-ID: 466835 [Multi-domain]  Cd Length: 409  Bit Score: 59.28  E-value: 4.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  19 VLAIDFGTsnTYvtKC-----PGDKEDPVGVDfGDGRDGIATAILYRDGKEPLIGHVALEEfgdagAEH-------DDYR 86
Cdd:cd10237    24 IVGIDLGT--TY--SCvgvyhAVTGEVEVIPD-DDGHKSIPSVVAFTPDGGVLVGYDALAQ-----AEHnpsntiyDAKR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  87 I---------------RAQFK--PDLVSSA--------EARTYARDFLVGLLTLARRQHKDI---APLQRQVIfGVPSEA 138
Cdd:cd10237    94 FigktftkeeleeeakRYPFKvvNDNIGSAffevplngSTLVVSPEDIGSLILLKLKKAAEAylgVPVAKAVI-SVPAEF 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 139 SETYRDALRAIAEEAGFGAVKTVDEPKGA-LYFHLQRKditpiEALRGALVVDFGGGTCDFALL-VRG---EILHSWGDM 213
Cdd:cd10237   173 DEKQRNATRKAANLAGLEVLRVINEPTAAaMAYGLHKK-----SDVNNVLVVDLGGGTLDVSLLnVQGgmfLTRAMAGNN 247

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2727058535 214 HLGGRLFDDLFYQWFIEQ----------NPEAVVAMRRE 242
Cdd:cd10237   248 HLGGQDFNQRLFQYLIDRiakkfgktltDKEDIQRLRQA 286
MreB COG1077
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ...
 130-209 7.87e-09

Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 440695 [Multi-domain]  Cd Length: 339  Bit Score: 57.78  E-value: 7.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 130 VIFGVPSEASETYRDALRAIAEEAGFGAVKTVDEPK----GAlyfhlqrkDItPIEALRGALVVDFGGGTCDFALLVRGE 205
Cdd:COG1077   102 VVICVPSGITEVERRAVRDAAEQAGAREVYLIEEPMaaaiGA--------GL-PIEEPTGNMVVDIGGGTTEVAVISLGG 172


                  ....
gi 2727058535 206 ILHS 209
Cdd:COG1077   173 IVVS 176
dnaK CHL00094
heat shock protein 70
 129-231 4.88e-08

heat shock protein 70


Pssm-ID: 214360 [Multi-domain]  Cd Length: 621  Bit Score: 56.28  E-value: 4.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 129 QVIFGVPSEASETYRDALRAIAEEAGFGAVKTVDEPKGA-LYFHLQRKDITPIealrgaLVVDFGGGTCDFALLVRG--- 204
Cdd:CHL00094  137 QAVITVPAYFNDSQRQATKDAGKIAGLEVLRIINEPTAAsLAYGLDKKNNETI------LVFDLGGGTFDVSILEVGdgv 210

                          90       100
                  ....*....|....*....|....*...
gi 2727058535 205 -EILHSWGDMHLGGRLFDDLFYQWFIEQ 231
Cdd:CHL00094  211 fEVLSTSGDTHLGGDDFDKKIVNWLIKE 238
ASKHA_NBD_MamK cd24009
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ...
 20-201 5.13e-08

nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called magnetosome cytoskeleton protein MamK, is a protein with ATPase activity which forms dynamic cytoplasmic filaments (probably with paralog MamK-like) that may organize magnetosomes into long chains running parallel to the long axis of the cell. Turnover of MamK filaments is probably promoted by MamK-like (e.g.. MamJ and/or LimJ), which provides a monomer pool. MamK forms twisted filaments in the presence of ATP or GTP. It serves to close gaps between magnetosomes in the chain. Interaction with MCP10 is involved in controlling the response to magnetic fields, possibly by controlling flagellar rotation. The MamK 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: 466859 [Multi-domain]  Cd Length: 328  Bit Score: 55.29  E-value: 5.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  20 LAIDFGTSNTYVTKCPGDKEDPVGVdFGDGRDGIATAILyrdGKEPLIGHVALEeFGDAGAEhddyriraqFKP--DLV- 96
Cdd:cd24009     4 IGIDLGTSRSAVVTSRGKRFSFRSV-VGYPKDIIARKLL---GKEVLFGDEALE-NRLALDL---------RRPleDGVi 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  97 --SSAEARTYARDFLVGLLTLARRQHKDiaplQRQVIFGVPSEASETYRDALRAIAEEAgFGAVKTVDEPKGALYfHLQR 174
Cdd:cd24009    70 keGDDRDLEAARELLQHLIELALPGPDD----EIYAVIGVPARASAENKQALLEIAREL-VDGVMVVSEPFAVAY-GLDR 143

                         170       180
                  ....*....|....*....|....*..
gi 2727058535 175 kditpieaLRGALVVDFGGGTCDFALL 201
Cdd:cd24009   144 --------LDNSLIVDIGAGTTDLCRM 162
ASKHA_NBD_HSP70_ScSsz1p-like cd10232
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ...
 18-228 7.11e-08

nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex subunit Ssz1 and similar proteins; Ssz1, also called DnaK-related protein Ssz1, heat shock protein 70 homolog Ssz1, or pleiotropic drug resistance protein 13 (PDR13), is a component of the ribosome-associated complex (RAC), a heterodimeric chaperone complex involved in regulation of accurate translation termination and in folding or maintaining nascent polypeptides in a folding-competent state. RAC stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones Ssb1/Ssb2 that bind to the nascent polypeptide chain. Ssz1 is required for Zuo1 to function efficiently as a J-protein for Ssb1/Ssb2. It is also involved in pleiotropic drug resistance by post-translational activation of transcription factor PDR1. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that 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.


Pssm-ID: 466830 [Multi-domain]  Cd Length: 349  Bit Score: 55.06  E-value: 7.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  18 PVLAIDFGTSNTYVTKCPGDKEDPVgVDFGDGRDGIATAILYRDGkeplighvalEEFGDAGAEHDDYR----IRAQFKP 93
Cdd:cd10232     1 VVIGISFGNSNSSIAIINKDGRAEV-IANEDGDRQIPSILAYHGD----------EEYHGSQAKAQLVRnpknTVANFRD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  94 DLvssAEARTYARDFLVGLLTLARRQHKDI--APLQRQVIfGVPSEASETYRDALRAIAEEAGFGAVKTVDEPKGALYFH 171
Cdd:cd10232    70 LL---GTTTLTVSEVTTRYLRRLKESAEDYlgKKVTGAVL-SVPTDFTEKQKAALVAAAAAAGLEVLQLIPEPAAAALAY 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2727058535 172 LQRKDITPIEAL-RGALVVDFGGGTCDFALL-VRG---EILHSWGDMHLGGRLFDDLFYQWF 228
Cdd:cd10232   146 DLRAETSGDTIKdKTVVVADLGGTRSDVTVVaVRGglyTILATVHDYELGGVALDDVLVGHF 207
PTZ00186 PTZ00186
heat shock 70 kDa precursor protein; Provisional
 19-259 1.67e-07

heat shock 70 kDa precursor protein; Provisional


Pssm-ID: 140213 [Multi-domain]  Cd Length: 657  Bit Score: 54.69  E-value: 1.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  19 VLAIDFGTSNTYVTKCPGDKedPVGVDFGDGRDGIATAILYRdGKEPLIGHVALEE-------------------FGDAG 79
Cdd:PTZ00186   29 VIGVDLGTTYSCVATMDGDK--ARVLENSEGFRTTPSVVAFK-GSEKLVGLAAKRQaitnpqstfyavkrligrrFEDEH 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  80 AEHD----DYRI-RAQFKPDLVSSAEARTYARDfLVGLLTLARRQHKDIAPLQRQV---IFGVPSEASETYRDALRAIAE 151
Cdd:PTZ00186  106 IQKDiknvPYKIvRAGNGDAWVQDGNGKQYSPS-QIGAFVLEKMKETAENFLGHKVsnaVVTCPAYFNDAQRQATKDAGT 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 152 EAGFGAVKTVDEPKGA-LYFHLQRKDITPIEalrgalVVDFGGGTCDFALL-VRG---EILHSWGDMHLGGRLFDDLFYQ 226
Cdd:PTZ00186  185 IAGLNVIRVVNEPTAAaLAYGMDKTKDSLIA------VYDLGGGTFDISVLeIAGgvfEVKATNGDTHLGGEDFDLALSD 258

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2727058535 227 WFIEQ-NPEAVVAMRRERAEFfvlaVRCREVKEK 259
Cdd:PTZ00186  259 YILEEfRKTSGIDLSKERMAL----QRVREAAEK 288
ASKHA_NBD_HSP70_HSPA14 cd10238
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ...
 85-223 3.84e-07

nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; HSPA14, also called HSP70-like protein 1 (Hsp70L1), or heat shock protein HSP60, is a component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, HSPA14 binds to the nascent polypeptide chain, while DNAJC2 stimulates its ATPase activity. It belongs to the heat shock protein 70 (HSP70) family of chaperones that 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.


Pssm-ID: 466836 [Multi-domain]  Cd Length: 377  Bit Score: 52.63  E-value: 3.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  85 YRIRAQFKPDLVSSAEartyardflvgLLTLARRQHKDIAPLQRQ-----VIFGVPSEASETYRDALRAIAEEAGFGAVK 159
Cdd:cd10238    99 YEIELEEKKKLVSPKE-----------VAKLIFKKMKEIAQSHGGsdvidVVLTVPLDFDEDQRNALKEAAEKAGFNVLR 167

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2727058535 160 TVDEPKGA-LYFHLQRKDITPIEALrgaLVVDFGGGTCDFALL-VRG---EILHSWGDMHLGGRLFDDL 223
Cdd:cd10238   168 VISEPSAAaLAYGIGQDDPTENSNV---LVYRLGGTSLDVTVLsVNNgmyRVLATRTDDNLGGDDFTEA 233
PLN03184 PLN03184
chloroplast Hsp70; Provisional
 16-368 1.30e-06

chloroplast Hsp70; Provisional


Pssm-ID: 215618 [Multi-domain]  Cd Length: 673  Bit Score: 51.77  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  16 AQPVLAIDFGTSNTYVTKCPGDKedPVGVDFGDGRDGIATAILYRDGKEPLIGHVALEE---------------FGDAGA 80
Cdd:PLN03184   38 AEKVVGIDLGTTNSAVAAMEGGK--PTIVTNAEGQRTTPSVVAYTKNGDRLVGQIAKRQavvnpentffsvkrfIGRKMS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  81 EHDD------YR---------------IRAQFKPDLVSSAEARTYARD---FLVGLLTLArrqhkdiaplqrqvIFGVPS 136
Cdd:PLN03184  116 EVDEeskqvsYRvvrdengnvkldcpaIGKQFAAEEISAQVLRKLVDDaskFLNDKVTKA--------------VITVPA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 137 EASETYRDALRAIAEEAGFGAVKTVDEPKGA-LYFHLQRKDITPIealrgaLVVDFGGGTCDFALLVRG----EILHSWG 211
Cdd:PLN03184  182 YFNDSQRTATKDAGRIAGLEVLRIINEPTAAsLAYGFEKKSNETI------LVFDLGGGTFDVSVLEVGdgvfEVLSTSG 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 212 DMHLGGRLFDDLFYQWFIE--QNPEAVVAMRRERAeffvlAVRCREVKEKFSLAMaldpttvyrktlgaygrlndvtwdS 289
Cdd:PLN03184  256 DTHLGGDDFDKRIVDWLASnfKKDEGIDLLKDKQA-----LQRLTEAAEKAKIEL------------------------S 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 290 FLARARRYRPSETFAqylrAMNPQagaHLDT------FPQGI-DLLDWFRQTLRQGLAHEQMRHQDLACVILTGGSSAWP 362
Cdd:PLN03184  307 SLTQTSISLPFITAT----ADGPK---HIDTtltrakFEELCsDLLDRCKTPVENALRDAKLSFKDIDEVILVGGSTRIP 379


                  ....*.
gi 2727058535 363 FVADIV 368
Cdd:PLN03184  380 AVQELV 385
MreB_Mbl pfam06723
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ...
 130-209 2.13e-06

MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.


Pssm-ID: 399596 [Multi-domain]  Cd Length: 327  Bit Score: 50.25  E-value: 2.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 130 VIFGVPSEASETYRDALRAIAEEAGFGAVKTVDEPK----GAlyfhlqrkDItPIEALRGALVVDFGGGTCDFALLVRGE 205
Cdd:pfam06723  96 VVICVPSGITEVERRAVKEAAKNAGAREVFLIEEPMaaaiGA--------GL-PVEEPTGNMVVDIGGGTTEVAVISLGG 166


                  ....
gi 2727058535 206 ILHS 209
Cdd:pfam06723 167 IVTS 170
ASKHA_NBD_HSP70_Ssb cd24093
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ...
 129-384 2.56e-06

nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar proteins; Ssb is ribosome-bound, Hsp70-type chaperone that assists in the co-translational folding of newly synthesized proteins in the cytosol. It stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Saccharmoyces cerevisiae Ssb are encoded by two genes, SSB1 and SSB2. Ssb1p is also known as cold-inducible protein YG101. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that 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).


Pssm-ID: 466943 [Multi-domain]  Cd Length: 375  Bit Score: 50.37  E-value: 2.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 129 QVIFGVPSEASETYRDALRAIAEEAGFGAVKTVDEPKGA-LYFHLQRKDItpiEALRGALVVDFGGGTCDFALL-VRG-- 204
Cdd:cd24093   135 KAVITVPAYFNDAQRQATKDAGAIAGLNVLRIINEPTAAaIAYGLGAGKS---EKERHVLIFDLGGGTFDVSLLhIAGgv 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 205 -EILHSWGDMHLGGRLFDDLFYQWFIEQNPEAV--------VAMRRERAEffvlavrCREVKEKFSlamALDPTTVYRKT 275
Cdd:cd24093   212 yTVKSTSGNTHLGGQDFDTNLLEHFKAEFKKKTgldisddaRALRRLRTA-------AERAKRTLS---SVTQTTVEVDS 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 276 LgaygrLNDVTWDSFLARARryrpsetfaqyLRAMNPQAgahldtfpqgidlldwFRQTLR---QGLAHEQMRHQDLACV 352
Cdd:cd24093   282 L-----FDGEDFESSITRAR-----------FEDLNAAL----------------FKSTLEpveQVLKDAKISKSQIDEV 329

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2727058535 353 ILTGGSSAWPFVADIVTD--ELKQIQpKPIEPSQ 384
Cdd:cd24093   330 VLVGGSTRIPKVQKLLSDffDGKQLE-KSINPDE 362
PRK13930 PRK13930
rod shape-determining protein MreB; Provisional
 130-209 3.19e-06

rod shape-determining protein MreB; Provisional


Pssm-ID: 237564 [Multi-domain]  Cd Length: 335  Bit Score: 49.75  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 130 VIFGVPSEASETYRDALRAIAEEAGFGAVKTVDEPK----GAlyfhlqrkDItPIEALRGALVVDFGGGTCDFALLVRGE 205
Cdd:PRK13930  103 IVICVPSGITEVERRAVREAAEHAGAREVYLIEEPMaaaiGA--------GL-PVTEPVGNMVVDIGGGTTEVAVISLGG 173


                  ....
gi 2727058535 206 ILHS 209
Cdd:PRK13930  174 IVYS 177
ASKHA_NBD_HSP70_HscA cd10236
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ...
 125-263 4.44e-06

nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar proteins; Escherichia coli HscA, also called Hsc66, acts as a chaperone involved in the maturation of iron-sulfur cluster-containing proteins. It has a low intrinsic ATPase activity which is markedly stimulated by HscB. It is involved in the maturation of IscU. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that 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). HscA's partner J-domain protein is HscB; it does not appear to require a NEF and has been shown to be induced by cold-shock. The HscA-HscB chaperone/co-chaperone pair is involved in [Fe-S] cluster assembly.


Pssm-ID: 466834 [Multi-domain]  Cd Length: 367  Bit Score: 49.52  E-value: 4.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 125 PLQRQVIfGVPSEASETYRDALRAIAEEAGFGAVKTVDEPKGA-LYFHLQRKDitpiealRGALVV-DFGGGTCDFALL- 201
Cdd:cd10236   132 ELTGAVI-TVPAYFDDAQRQATKDAARLAGLNVLRLLNEPTAAaLAYGLDQKK-------EGTIAVyDLGGGTFDISILr 203

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2727058535 202 -VRG--EILHSWGDMHLGGRLFDDLFYQWFIEQNPEAVVAMRRERAEFFVLAvrcREVKEKFSLA 263
Cdd:cd10236   204 lSDGvfEVLATGGDTALGGDDFDHLLADWILKQIGIDARLDPAVQQALLQAA---RRAKEALSDA 265
PTZ00009 PTZ00009
heat shock 70 kDa protein; Provisional
 134-384 8.25e-06

heat shock 70 kDa protein; Provisional


Pssm-ID: 240227 [Multi-domain]  Cd Length: 653  Bit Score: 49.02  E-value: 8.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 134 VPSEASETYRDALRAIAEEAGFGAVKTVDEPKGA-LYFHLQRKDitpiEALRGALVVDFGGGTCDFALL-VRG---EILH 208
Cdd:PTZ00009  147 VPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAaIAYGLDKKG----DGEKNVLIFDLGGGTFDVSLLtIEDgifEVKA 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 209 SWGDMHLGGRLFDDLFYQWFIEQnpeavvAMRRERAEffvlavrcrevkekfslamalDPTTVYRktlgAYGRLNdvtwd 288
Cdd:PTZ00009  223 TAGDTHLGGEDFDNRLVEFCVQD------FKRKNRGK---------------------DLSSNQR----ALRRLR----- 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 289 SFLARARRYRPSETfaqylramnpQAGAHLDTFPQGIDL-------------LDWFRQTL---RQGLAHEQMRHQDLACV 352
Cdd:PTZ00009  267 TQCERAKRTLSSST----------QATIEIDSLFEGIDYnvtisrarfeelcGDYFRNTLqpvEKVLKDAGMDKRSVHEV 336

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2727058535 353 ILTGGSSAWPFVADIVTDELKQIQP-KPIEPSQ 384
Cdd:PTZ00009  337 VLVGGSTRIPKVQSLIKDFFNGKEPcKSINPDE 369
PRK13411 PRK13411
molecular chaperone DnaK; Provisional
 129-231 8.56e-06

molecular chaperone DnaK; Provisional


Pssm-ID: 184039 [Multi-domain]  Cd Length: 653  Bit Score: 48.98  E-value: 8.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 129 QVIFGVPSEASETYRDALRAIAEEAGFGAVKTVDEPKGA-LYFHLQRKDitpiEALRgALVVDFGGGTCDFALLVRG--- 204
Cdd:PRK13411  135 QAVITVPAYFTDAQRQATKDAGTIAGLEVLRIINEPTAAaLAYGLDKQD----QEQL-ILVFDLGGGTFDVSILQLGdgv 209

                          90       100
                  ....*....|....*....|....*...
gi 2727058535 205 -EILHSWGDMHLGGRLFDDLFYQWFIEQ 231
Cdd:PRK13411  210 fEVKATAGNNHLGGDDFDNCIVDWLVEN 237
ASKHA_NBD_HSP70_Ssc1_3 cd11734
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ...
 18-259 1.68e-05

nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein Ssc1p and Ssc3p and similar proteins; This subgroup includes Saccharomyces cerevisiae Stress-Seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and sc3p (also called extracellular mutant protein 10/Ecm10). Ssc1p is an essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. It constitutes the ATP-driven core of the motor and binds the precursor preprotein. It is required for the import of the processed frataxin homolog YFH1 into the mitochondrion. Ssc1p also acts as a non-catalytic component of endonuclease SceI (endo.SceI), which cleaves specifically at multiple sites on mitochondrial DNA and produces double-stranded breaks. Ssc1p confers broader sequence specificity, greater stability, and higher activity on the catalytic subunit. Ssc3p plays a role in facilitating the assembly of some protein complexes inside the mitochondria. It may initiate the events that lead to refolding of imported precursors in the matrix space.


Pssm-ID: 466840 [Multi-domain]  Cd Length: 378  Bit Score: 47.44  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  18 PVLAIDFGTSNTYVT----KCPGDKEDPVGvdfgdGRDGIATAILYRDGkEPLIGHVALEE------------------- 74
Cdd:cd11734     2 PVIGIDLGTTNSCVAvmegKTPRVIENAEG-----ARTTPSVVAFTKDG-ERLVGVPAKRQavvnpentlfatkrligrk 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  75 FGDAGAEHD----DYRIRAQFKPDLVSSAEARTYARDfLVGLLTLARRQHKDIAPLQRQV---IFGVPSEASETYRDALR 147
Cdd:cd11734    76 FDDAEVQRDikevPYKIVKHSNGDAWVEARGQKYSPS-QIGAFVLGKMKETAEGYLGKPVknaVVTVPAYFNDSQRQATK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 148 AIAEEAGFGAVKTVDEPKGA-LYFHLQRKDITPIEalrgalVVDFGGGTCDFALL--VRG--EILHSWGDMHLGGRLFDD 222
Cdd:cd11734   155 DAGQIAGLNVLRVINEPTAAaLAYGLDKSGDKVIA------VYDLGGGTFDISILeiQKGvfEVKSTNGDTHLGGEDFDI 228

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2727058535 223 LFYQWFIEQ-NPEAVVAMRRERaeffvLAV-RCREVKEK 259
Cdd:cd11734   229 ALVRHIVSEfKKESGIDLSKDR-----MAIqRIREAAEK 262
hscA PRK01433
chaperone protein HscA; Provisional
 7-228 3.20e-05

chaperone protein HscA; Provisional


Pssm-ID: 234955 [Multi-domain]  Cd Length: 595  Bit Score: 47.16  E-value: 3.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535   7 PSTARPSAEAQPVLAIDFGTSNT----------YVTKCPGDKED-PVGVDFGDGRDGIATAILYRDGKEpLIGHvALEEF 75
Cdd:PRK01433    9 PEQADFKQERQIAVGIDFGTTNSliaiatnrkvKVIKSIDDKELiPTTIDFTSNNFTIGNNKGLRSIKR-LFGK-TLKEI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  76 GDA---GAEHDDY------RIRAQFKPDLVSSAEArtyARDFLVGLLTLARRQHKDiaPLQRQVIfGVPSEASETYRDAL 146
Cdd:PRK01433   87 LNTpalFSLVKDYldvnssELKLNFANKQLRIPEI---AAEIFIYLKNQAEEQLKT--NITKAVI-TVPAHFNDAARGEV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 147 RAIAEEAGFGAVKTVDEPKGALYFHLQRKDITPIealrgALVVDFGGGTCDFALLVRGE----ILHSWGDMHLGGRLFDD 222
Cdd:PRK01433  161 MLAAKIAGFEVLRLIAEPTAAAYAYGLNKNQKGC-----YLVYDLGGGTFDVSILNIQEgifqVIATNGDNMLGGNDIDV 235


                  ....*.
gi 2727058535 223 LFYQWF 228
Cdd:PRK01433  236 VITQYL 241
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
 134-231 7.06e-05

Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region.


Pssm-ID: 394970 [Multi-domain]  Cd Length: 598  Bit Score: 46.10  E-value: 7.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 134 VPSEASETYRDALRAIAEEAGFGAVKTVDEPKGA-LYFHLQRKDITpiealRGALVVDFGGGTCDFALLV--RG--EILH 208
Cdd:pfam00012 140 VPAYFNDAQRQATKDAGQIAGLNVLRIVNEPTAAaLAYGLDKTDKE-----RNIAVYDLGGGTFDVSILEigRGvfEVKA 214

                          90       100
                  ....*....|....*....|...
gi 2727058535 209 SWGDMHLGGRLFDDLFYQWFIEQ 231
Cdd:pfam00012 215 TNGDTHLGGEDFDLRLVDHLAEE 237
ASKHA_NBD_HSP70_ScSse cd24094
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ...
 130-370 1.32e-04

nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and similar proteins; The subgroup includes two Saccharomyces cerevisiae heat shock protein homologs, Sse1 and Sse2. They may have calcium-dependent calmodulin-binding activities. Both Sse1 and Sse2 belong to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family, and includes proteins believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, 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 also regulated by J-domain proteins.


Pssm-ID: 466944 [Multi-domain]  Cd Length: 385  Bit Score: 44.67  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 130 VIFGVPSEASETYRDALRAIAEEAGFGAVKTVDEPKG-ALYFHLQRKDI-TPIEALRGALVVDFGGG--TCDFALLVRGE 205
Cdd:cd24094   136 VVISVPGWFTDEQRRAILDAAEIAGLNPLRLMNDTTAaALGYGITKTDLpEPEEKPRIVAFVDIGHSsyTVSIVAFKKGQ 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 206 --ILHSWGDMHLGGRLFDDLFYQWFIEQ-----------NPEAVvamrreraefFVLAVRCREVKEKFSlAMALDPTTVy 272
Cdd:cd24094   216 ltVKGTAYDRHFGGRDFDKALTDHFADEfkekykidvrsNPKAY----------FRLLAAAEKLKKVLS-ANAQAPLNV- 283

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 273 rKTLgaygrLNDVTWDSFLARarryrpsETFAQYLRamnpqagahldtfpqgiDLLDWFRQTLRQGLAHEQMRHQDLACV 352
Cdd:cd24094   284 -ESL-----MNDIDVSSMLKR-------EEFEELIA-----------------PLLERVTAPLEKALAQAGLTKDEIDFV 333

                         250
                  ....*....|....*...
gi 2727058535 353 ILTGGSSAWPFVADIVTD 370
Cdd:cd24094   334 ELVGGTTRVPALKESISA 351
ASKHA_NBD_HSP70_HSPA4L cd11738
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ...
 100-369 2.07e-04

nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; HSPA4L, also called heat shock 70-related protein APG-1, heat-shock protein family A member 4-like protein, HSPA4-like protein, osmotic stress protein 94, or HSPH3, possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase. It is expressed ubiquitously and predominantly in the testis. It is required for normal spermatogenesis and plays a role in osmotolerance. HSPA4L belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, 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 also regulated by J-domain proteins.


Pssm-ID: 466844 [Multi-domain]  Cd Length: 383  Bit Score: 44.14  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 100 EARTYARDFLVGLLtLARRQHKDIAPLQRQV---IFGVPSEASETYRDALRAIAEEAGFGAVKTVDEPKG-ALYFHLQRK 175
Cdd:cd11738   107 EERVFAIEQVTGML-LTKLKETSENALKKPVadcVISVPSFFTDAERRSVMDAAQIAGLNCLRLMNETTAvALAYGIYKQ 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 176 DI-TPIEALRGALVVDFGGGTCDFALLV----RGEILHSWGDMHLGGRLFDDLFYQWFIEQ-----------NPEAVVAM 239
Cdd:cd11738   186 DLpALEEKPRNVVFVDMGHSAYQVSICAfnkgKLKVLATTFDPYLGGRNFDEVLVDYFCEEfktkyklnvkeNIRALLRL 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 240 RREraeffvlavrCREVKEKFSLAMALDPttvyrktLGAYGRLNDVTWDSFLARARRyrpSETFAQYLRAMNPqagahld 319
Cdd:cd11738   266 YQE----------CEKLKKLMSANASDLP-------LNIECFMNDIDVSSKMNRAQF---EELCASLLARVEP------- 318

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2727058535 320 tfpqgidlldwfrqTLRQGLAHEQMRHQDLACVILTGGSSAWPFVADIVT 369
Cdd:cd11738   319 --------------PLKAVMEQAKLQREDIYSIEIVGGATRIPAVKERIA 354
PRK13928 PRK13928
rod shape-determining protein Mbl; Provisional
 130-222 3.04e-04

rod shape-determining protein Mbl; Provisional


Pssm-ID: 237563 [Multi-domain]  Cd Length: 336  Bit Score: 43.35  E-value: 3.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 130 VIFGVPSEASETYRDALRAIAEEAGFGAVKTVDEPKGA-----LyfhlqrkDITpiEAlRGALVVDFGGGTCDFALLVRG 204
Cdd:PRK13928   98 IMICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAaigagL-------DIS--QP-SGNMVVDIGGGTTDIAVLSLG 167

                          90
                  ....*....|....*...
gi 2727058535 205 EILHSwGDMHLGGRLFDD 222
Cdd:PRK13928  168 GIVTS-SSIKVAGDKFDE 184
hscA PRK05183
chaperone protein HscA; Provisional
 187-261 7.45e-04

chaperone protein HscA; Provisional


Pssm-ID: 235360 [Multi-domain]  Cd Length: 616  Bit Score: 42.86  E-value: 7.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 187 LVVDFGGGTCDFALL--VRG--EILHSWGDMHLGGRLFDDLFYQWFIEQ---NPEAVVAMRREraeffvLAVRCREVKEK 259
Cdd:PRK05183  204 AVYDLGGGTFDISILrlSKGvfEVLATGGDSALGGDDFDHLLADWILEQaglSPRLDPEDQRL------LLDAARAAKEA 277


                  ..
gi 2727058535 260 FS 261
Cdd:PRK05183  278 LS 279
ASKHA_NBD_HSP70_BiP cd10241
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ...
 153-242 8.96e-04

nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; This subfamily includes human BiP (also known as HSP70 family protein 5 /HSPA5; 70-kDa heat shock protein 5; glucose-regulated protein 78/GRP78; immunoglobulin heavy chain-binding protein), Sacchaormyces cerevisiae BiP (also known as Grp78p), Arabidopsis thaliana BiP1-3 (also known as luminal-binding protein 1-3) and related proteins. BiP plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. It plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). BiP may function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. It appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. BiP may also play a role in apoptosis and cell proliferation. Plant BiP may be required for pollen development and pollen tube growth. This subfamily belongs to the heat shock protein 70 (HSP70) family of chaperones that 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).


Pssm-ID: 466837 [Multi-domain]  Cd Length: 376  Bit Score: 42.20  E-value: 8.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 153 AGFGAVKTVDEPKGA-LYFHLQRKDitpieALRGALVVDFGGGTCDFALLV--RG--EILHSWGDMHLGGRLFDDLFYQW 227
Cdd:cd10241   162 AGLNVLRIINEPTAAaIAYGLDKKG-----GEKNILVFDLGGGTFDVSLLTidNGvfEVLATNGDTHLGGEDFDQRVMDH 236

                          90       100
                  ....*....|....*....|....*.
gi 2727058535 228 FIE-----------QNPEAVVAMRRE 242
Cdd:cd10241   237 FIKlfkkktgkdisKDKRAVQKLRRE 262
ASKHA_NBD_ParM-like cd10227
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ...
 20-218 1.35e-03

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: 40.97  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  20 LAIDFGTSNT-YVTKCPGD--------KEDPVGVDFGDGRDGIATAIlyrDGKEPLIGHVALEEFGDAGAEHDDYRiraq 90
Cdd:cd10227     1 IGIDIGNGNTkVVTGGGKEfkfpsavaEARESSLDDGLLEDDIIVEY---NGKRYLVGELALREGGGGRSTGDDKK---- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  91 fkpdLVSSAEARtyardFLVGLLTLARRQHKDIAplqrqVIFGVPSE--ASETYRDALRAIAEEAGFGA----------- 157
Cdd:cd10227    74 ----KSEDALLL-----LLAALALLGDDEEVDVN-----LVVGLPISeyKEEKKELKKKLLKGLHEFTFngkerritind 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2727058535 158 VKTVDEPKGALYFHLQRKDITPIEALrgaLVVDFGGGTCDFALLVRGEILHSWGDMHLGGR 218
Cdd:cd10227   140 VKVLPEGAGAYLDYLLDDDELEDGNV---LVIDIGGGTTDILTFENGKPIEESSDTLPGGE 197
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 125-632 1.39e-03

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 42.17  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  125 PLQRQV--IFGVPSEASETYRDALRAIAEEAGFGAVKTVDEPKGALYFHLQRKDITPIEALRGALVVDFGGGTCDFALLV 202
Cdd:COG3321    867 PFQREDaaAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALA 946

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  203 RGEILHSWGDMHLGGRLFDDLFYQWFIEQNPEAVVAMRRERAEFFVLAVRCREVKEKFSLAMALDPTTVYRKTLGAYGRL 282
Cdd:COG3321    947 AAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAA 1026

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  283 NDVTWDSFLARARRYRPSETFAQYLRAMNPQAGAHLDTFPQGIDLLDWFRQTLRQGLAHEQMRHQDLACVILTGGSSAWP 362
Cdd:COG3321   1027 LLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAAL 1106

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  363 FVADIVTDELKQIQPKPIEPSQIERSPRLVHSDRPYVTVSQGLAIVPALQQRLAATQVDLRRELPAFIATRIAPLIERRM 442
Cdd:COG3321   1107 LLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALA 1186

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  443 DEAAHRIAERVAVGLFDERIEPILRHFRQEGGSVADLKARLAE---DAAAFRPQLEAIVTTQLAKVLTGVAADTTELMQD 519
Cdd:COG3321   1187 AALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAaaaLALLALAAAAAAVAALAAAAAALLAALAALALLA 1266

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535  520 WYRQHRLTVDQSLSHAGTPVDMAEGLRLADLDVYGEISGVVLALSATIISVLAATISGGAGTAIIMSGPIGLLIGALVGL 599
Cdd:COG3321   1267 AAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAA 1346

                          490       500       510
                   ....*....|....*....|....*....|...
gi 2727058535  600 IAGALAMRYGLDEAKRRAEHWEGAPRWILARAL 632
Cdd:COG3321   1347 AAAAAAAAAAAAAAAALAAAAGAAAAAAALALA 1379
PTZ00400 PTZ00400
DnaK-type molecular chaperone; Provisional
 128-231 1.79e-03

DnaK-type molecular chaperone; Provisional


Pssm-ID: 240403 [Multi-domain]  Cd Length: 663  Bit Score: 41.73  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 128 RQVIFGVPSEASETYRDALRAIAEEAGFGAVKTVDEPKGA-LYFHLQRKDITPIEalrgalVVDFGGGTCDFALLvrgEI 206
Cdd:PTZ00400  175 KQAVITVPAYFNDSQRQATKDAGKIAGLDVLRIINEPTAAaLAFGMDKNDGKTIA------VYDLGGGTFDISIL---EI 245

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2727058535 207 L-------HSWGDMHLGGRLFDDLFYQWFIEQ 231
Cdd:PTZ00400  246 LggvfevkATNGNTSLGGEDFDQRILNYLIAE 277
ASKHA_NBD_HSP70_HSPA1 cd10233
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ...
 134-244 2.28e-03

nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; This subfamily includes human HSPA1A (70-kDa heat shock protein 1A, also known as HSP72; HSPA1; HSP70I; HSPA1B; HSP70-1; HSP70-1A), HSPA1B (70-kDa heat shock protein 1B, also known as HSPA1A; HSP70-2; HSP70-1B), and HSPA1L (70-kDa heat shock protein 1-like, also known as HSP70T; hum70t; HSP70-1L; HSP70-HOM), HSPA2 (70-kDa heat shock protein 2, also known as HSP70-2; HSP70-3), HSPA6 (also known as heat shock 70kDa protein 6; HSP70B'), HSPA7 (heat shock 70kDa protein 7 , also known as HSP70B), and HSPA8 (heat shock 70kDa protein 8, also known as Lipopolysaccharide-associated protein 1/LAP1; HSC70; HSP73; HSPA10). They are molecular chaperones implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. They play pivotal roles in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The subfamily also includes Saccharomyces cerevisiae heat shock protein Ssa1-4, which may play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. This subfamily belongs to the heat shock protein 70 (HSP70) family of chaperones that 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).


Pssm-ID: 466831 [Multi-domain]  Cd Length: 375  Bit Score: 40.69  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 134 VPSEASETYRDALRAIAEEAGFGAVKTVDEPK-GALYFHLQRKDitpiEALRGALVVDFGGGTCDFALLV--RG--EILH 208
Cdd:cd10233   141 VPAYFNDSQRQATKDAGTIAGLNVLRIINEPTaAAIAYGLDKKG----KGERNVLIFDLGGGTFDVSLLTieDGifEVKA 216

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2727058535 209 SWGDMHLGGRLFDDLFYQWFIE-----------QNPEavvAMRR-----ERA 244
Cdd:cd10233   217 TAGDTHLGGEDFDNRLVNHFVQefkrkhkkdisGNPR---ALRRlrtacERA 265
ASKHA_NBD_PilM-like cd24004
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ...
 144-220 2.80e-03

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: 40.35  E-value: 2.80e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2727058535 144 DALRAIAEEAGFGAVKTVDEPKGALYFHlqrkdITPIEALRGALVVDFGGGTCDFALLVRGEILHSwGDMHLGGRLF 220
Cdd:cd24004    79 ESLLNVLEKAGLEPVGLTLEPFAAANLL-----IPYDMRDLNIALVDIGAGTTDIALIRNGGIEAY-RMVPLGGDDF 149
AraH COG1172
Ribose/xylose/arabinose/galactoside ABC-type transport system, permease component ...
 558-610 6.57e-03

Ribose/xylose/arabinose/galactoside ABC-type transport system, permease component [Carbohydrate transport and metabolism];


Pssm-ID: 440785  Cd Length: 322  Bit Score: 39.32  E-value: 6.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2727058535 558 GVVLALSAtiisVLAATISGGAGTAIIMSGPIGLLIGALVGLIAGALAMRYGL 610
Cdd:COG1172    76 GSVVALSG----VVAALLLVALGLPILLAILLALLVGALLGLLNGLLVAKLRI 124
ASKHA_NBD_HSP70_HSP105-110-like cd11732
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ...
 121-231 6.93e-03

nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa heat shock proteins family includes the human proteins, HSPA4 (also known as 70-kDa heat shock protein 4; APG-2; HS24/P52; hsp70 RY; HSPH2), HSPA4L (also known as 70-kDa heat shock protein 4-like; APG-1; HSPH3; OSP94), and HSPH1 (also known as heat shock 105kDa/110kDa protein 1; HSP105; HSP105A; HSP105B; NY-CO-25), Saccharomyces cerevisiae Sse1p, Sse2p and a sea urchin sperm receptor. They all belong to the heat shock protein 70 (HSP70) family of chaperones that 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).


Pssm-ID: 466838 [Multi-domain]  Cd Length: 377  Bit Score: 39.47  E-value: 6.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 121 KDIAPLQ-----RQVIFGVPSEASETYRDALRAIAEEAGFGAVKTVDEPKG-ALYFHLQRKDITPIEAlRGALV--VDFG 192
Cdd:cd11732   123 KEIAEAAnkgevKDCVISVPGYYTDAQRRALLDAAEIAGLNCLRLINETTAaALDYGIYKSDLLESEE-KPRIVafVDMG 201

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2727058535 193 GGTCDFAL--LVRG--EILHSWGDMHLGGRLFDDLFYQWFIEQ 231
Cdd:cd11732   202 HSSTQVSIaaFTKGklKVLSTAFDRNLGGRDFDRALVEHFAEE 244
PRK13927 PRK13927
rod shape-determining protein MreB; Provisional
 117-195 7.73e-03

rod shape-determining protein MreB; Provisional


Pssm-ID: 237562 [Multi-domain]  Cd Length: 334  Bit Score: 38.92  E-value: 7.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2727058535 117 RRQHKDIAPLQRQVIfGVPSEASETYRDALRAIAEEAGFGAVKTVDEP----KGAlyfhlqrkDItPIEALRGALVVDFG 192
Cdd:PRK13927   87 KKVHKNFRPSPRVVI-CVPSGITEVERRAVRESALGAGAREVYLIEEPmaaaIGA--------GL-PVTEPTGSMVVDIG 156


                  ...
gi 2727058535 193 GGT 195
Cdd:PRK13927  157 GGT 159
ASKHA_NBD_HSP70_DnaK-like cd10234
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ...
 187-231 7.96e-03

nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar proteins; This subfamily includes Escherichia coli chaperone protein DnaK (also known as heat shock 70 kDa protein/HSP70), human mitochondrial heat shock 70 kDa protein HSPA9 (also known as mitochondrial stress-70 protein; mortalin; 75 kDa glucose-regulated protein/GRP-75; HSPA9B; MOT; peptide-binding protein 74/PBP74), Saccharomyces cerevisiae stress-seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and Ssc3p (also called extracellular mutant protein 10/Ecm10), and Saccharomyces cerevisiae Stress-seventy subfamily Q protein 1/Ssq1p (also called Ssc2p; Ssh1p; mtHSP70 homolog). They all belong to the heat shock protein 70 (HSP70) family of chaperones that 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); for Escherichia coli DnaK, these are the DnaJ and GrpE, respectively.


Pssm-ID: 466832 [Multi-domain]  Cd Length: 373  Bit Score: 39.00  E-value: 7.96e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2727058535 187 LVVDFGGGTCDFALLVRG----EILHSWGDMHLGGRLFDDLFYQWFIEQ 231
Cdd:cd10234   185 LVYDLGGGTFDVSILEIGdgvfEVLSTNGDTHLGGDDFDQRIIDYLADE 233
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH