|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
6-353 |
0e+00 |
|
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: 533.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 6 IGIDLGTTNSVAAHYGPEGIRFIPNETGELLTPSAVAFDERtGSYCVGRRAKNLIALDPRNGARKFKTTMGTDAQYTIRK 85
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVDED-GSILVGRAAKERLVTHPDRTAASFKRFMGTDKQYRLGN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 86 DRFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEMAGLTVERILNEPTAAAIAYGLQKQADV 165
Cdd:cd10235 80 HTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELAGLKVERLINEPTAAALAYGLHKREDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 166 HRFLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYVLKKEGQDFdrlLSRSPETAGLMMKRAELAKQ 245
Cdd:cd10235 160 TRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFLKKHRLDF---TSLSPSELAALRKRAEQAKR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 246 QLSTNDTVpLAISGSPLREKTIQITREEADEVFAPLIRRLATPCQTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDY 325
Cdd:cd10235 237 QLSSQDSA-EIRLTYRGEELEIELTREEFEELCAPLLERLRQPIERALRDAGLKPSDIDAVILVGGATRMPLVRQLIARL 315
|
330 340
....*....|....*....|....*...
gi 1759976916 326 FETEALAIVDPDLTVAQGAAIQAALYTN 353
Cdd:cd10235 316 FGRLPLSSLDPDEAVALGAAIQAALKAR 343
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
5-473 |
4.56e-169 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 488.18 E-value: 4.56e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 5 VIGIDLGTTNSVAAHYGPEGIRFIPNETGELLTPSAVAFDERtGSYCVGRRAKNLIALDPRNGARKFKTTMGT---DAQY 81
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPKD-GEVLVGEAAKRQAVTNPGRTIRSIKRLLGRslfDEAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 82 TIRKDRFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEMAGLTVERILNEPTAAAIAYGLQK 161
Cdd:COG0443 80 EVGGKRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARIAGLEVLRLLNEPTAAALAYGLDK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 162 QADVHRFLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYVLKKEGQDFDRLLSRSPETAGLMMKRAE 241
Cdd:COG0443 160 GKEEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPEFGKEEGIDLRLDPAALQRLREAAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 242 LAKQQLSTNDTVPLAISGSPLREKTIQITREEADEVFAPLIRRLATPCQTALRGASTKISNLDAVVLVGGATRMPCVRNF 321
Cdd:COG0443 240 KAKIELSSADEAEINLPFSGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADAGLSPSDIDAVLLVGGSTRMPAVRER 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 322 IEDYFETEALAIVDPDLTVAQGAAIQAALYTNDehvdeVTVTDVLSHSLGIEiskmignrYVPGFFSPIIHRNTVIPATR 401
Cdd:COG0443 320 VKELFGKEPLKGVDPDEAVALGAAIQAGVLAGD-----VKDLDVTPLSLGIE--------TLGGVFTKLIPRNTTIPTAK 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1759976916 402 AEIYKPLQVGQTVLNVEVYEGEGRHVKDNHKIGTVEVRGIPNRP--DNQVEVRFSYDLNGILEVEATILATNQK 473
Cdd:COG0443 387 SQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPrgVPQIEVTFDIDANGILSVSAKDLGTGKE 460
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
5-562 |
2.98e-135 |
|
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: 406.26 E-value: 2.98e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 5 VIGIDLGTTNSVAAHYGPEGIRFIPNETGELLTPSAVAF--DERTgsycVGRRAKNLIALDPRNGARKFKTTMGTDAQ-- 80
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFtpKERL----VGQAAKNQAVTNPKNTVFSVKRLIGRKFSdp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 81 ----------YTIRKDR--------------FNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAG 136
Cdd:pfam00012 77 vvqrdikhlpYKVVKLPngdagvevrylgetFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 137 EMAGLTVERILNEPTAAAIAYGLQKQADVHRFLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYVL- 215
Cdd:pfam00012 157 QIAGLNVLRIVNEPTAAALAYGLDKTDKERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAe 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 216 ---KKEGQDfdrlLSRSPETAGLMMKRAELAKQQLSTNDT-VPLAI-----SGSPLrekTIQITREEADEVFAPLIRRLA 286
Cdd:pfam00012 237 efkKKYGID----LSKDKRALQRLREAAEKAKIELSSNQTnINLPFitamaDGKDV---SGTLTRAKFEELVADLFERTL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 287 TPCQTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIVDPDLTVAQGAAIQAALYTNDEHVDEVTVTDVL 366
Cdd:pfam00012 310 EPVEKALKDAGLSKSEIDEVVLVGGSTRIPAVQELVKEFFGKEPSKGVNPDEAVAIGAAVQAGVLSGTFDVKDFLLLDVT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 367 SHSLGIEiskmignrYVPGFFSPIIHRNTVIPATRAEIYKPLQVGQTVLNVEVYEGEGRHVKDNHKIGTVEVRGIPNRPD 446
Cdd:pfam00012 390 PLSLGIE--------TLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPR 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 447 N--QVEVRFSYDLNGILEVEATILATNqKVLQLLTRDSRTLSAQDIKEATERMSLL-----KLDLREDRRIRA--LLVRA 517
Cdd:pfam00012 462 GvpQIEVTFDIDANGILTVSAKDKGTG-KEQEITIEASEGLSDDEIERMVKDAEEYaeedkKRKERIEAKNEAeeYVYSL 540
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1759976916 518 ELLIKD----LPPEQRNALEAELDRFESALDLHDREQIEALYNELKRIC 562
Cdd:pfam00012 541 EKSLEEegdkVPEAEKSKVESAIEWLKDELEGDDKEEIEAKTEELAQVS 589
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
5-559 |
3.80e-125 |
|
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE chaperone system. All members of the seed alignment were taken from completely sequenced bacterial or archaeal genomes and (except for Mycoplasma sequence) found clustered with other genes of this systems. This model excludes DnaK homologs that are not DnaK itself, such as the heat shock cognate protein HscA (TIGR01991). However, it is not designed to distinguish among DnaK paralogs in eukaryotes. Note that a number of dnaK genes have shadow ORFs in the same reverse (relative to dnaK) reading frame, a few of which have been assigned glutamate dehydrogenase activity. The significance of this observation is unclear; lengths of such shadow ORFs are highly variable as if the presumptive protein product is not conserved. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274091 [Multi-domain] Cd Length: 595 Bit Score: 380.12 E-value: 3.80e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 5 VIGIDLGTTNSVAAHYgpEGIR--FIPNETGELLTPSAVAFDErTGSYCVGRRAKNLIALDPRNGARKFKTTMGT----- 77
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVM--EGGEpvVIPNAEGARTTPSVVAFTK-NGERLVGQPAKRQAVTNPENTIYSIKRFMGRrfdev 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 78 ----------------DAQYTIRKDRFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEMAGL 141
Cdd:TIGR02350 79 teeakrvpykvvgdggDVRVKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 142 TVERILNEPTAAAIAYGLQKQADVHRFLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYVL----KK 217
Cdd:TIGR02350 159 EVLRIINEPTAAALAYGLDKSKKDEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLAdefkKE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 218 EGQDF--DRL-LSRSPETaglmmkrAELAKQQLS----TNDTVP-LAISGSPLREKTIQITREEADEVFAPLIRRLATPC 289
Cdd:TIGR02350 239 EGIDLskDKMaLQRLKEA-------AEKAKIELSsvlsTEINLPfITADASGPKHLEMTLTRAKFEELTADLVERTKEPV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 290 QTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIVDPDLTVAQGAAIQAALYTNDehVDEVTVTDVLSHS 369
Cdd:TIGR02350 312 RQALKDAGLSASDIDEVILVGGSTRIPAVQELVKDFFGKEPNKSVNPDEVVAIGAAIQGGVLKGD--VKDVLLLDVTPLS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 370 LGIEIskmIGnryvpGFFSPIIHRNTVIPATRAEIYKPLQVGQTVLNVEVYEGEGRHVKDNHKIGTVEVRGIPNRPDN-- 447
Cdd:TIGR02350 390 LGIET---LG-----GVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGvp 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 448 QVEVRFSYDLNGILEVEATILATnQKVLQLLTRDSRTLSAQDI----KEAtermsllKLDLREDRRIR----------AL 513
Cdd:TIGR02350 462 QIEVTFDIDANGILHVSAKDKGT-GKEQSITITASSGLSEEEIermvKEA-------EANAEEDKKRKeeiearnnadSL 533
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1759976916 514 LVRAELLIKD----LPPEQRNALEAELDRFESALDLHDREQIEALYNELK 559
Cdd:TIGR02350 534 AYQAEKTLKEagdkLPAEEKEKIEKAVAELKEALKGEDVEEIKAKTEELQ 583
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
5-558 |
1.58e-122 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 374.44 E-value: 1.58e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 5 VIGIDLGTTNSVAAHYgpEG--IRFIPNETGELLTPSAVAFDErTGSYCVGRRAKNLIALDPRNGARKFKTTMGT----- 77
Cdd:PRK00290 4 IIGIDLGTTNSCVAVM--EGgePKVIENAEGARTTPSVVAFTK-DGERLVGQPAKRQAVTNPENTIFSIKRLMGRrdeev 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 78 -----------------DAQYTIRKDRFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEMAG 140
Cdd:PRK00290 81 qkdiklvpykivkadngDAWVEIDGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 141 LTVERILNEPTAAAIAYGLQKQADvHRFLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYVL---KK 217
Cdd:PRK00290 161 LEVLRIINEPTAAALAYGLDKKGD-EKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLAdefKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 218 EgQDFDrlLSRSPetagLMMKR----AELAKQQLS----TNDTVPL--AISGSPLrEKTIQITREEADEVFAPLIRRLAT 287
Cdd:PRK00290 240 E-NGID--LRKDK----MALQRlkeaAEKAKIELSsaqqTEINLPFitADASGPK-HLEIKLTRAKFEELTEDLVERTIE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 288 PCQTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIVDPDLTVAQGAAIQAALYTNDehVDEVTVTDVLS 367
Cdd:PRK00290 312 PCKQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLAGD--VKDVLLLDVTP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 368 HSLGIEIskmIGnryvpGFFSPIIHRNTVIPATRAEIYKPLQVGQTVLNVEVYEGEGRHVKDNHKIGTVEVRGIPNRPDN 447
Cdd:PRK00290 390 LSLGIET---LG-----GVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 448 --QVEVRFSYDLNGILEVEATILATNQKvlQLLT-RDSRTLSAQDI----KEATERMSllkldlrEDRRIR--------- 511
Cdd:PRK00290 462 vpQIEVTFDIDANGIVHVSAKDKGTGKE--QSITiTASSGLSDEEIermvKDAEANAE-------EDKKRKelvearnqa 532
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1759976916 512 -ALLVRAELLIKD----LPPEQRNALEAELDRFESALDLHDREQIEALYNEL 558
Cdd:PRK00290 533 dSLIYQTEKTLKElgdkVPADEKEKIEAAIKELKEALKGEDKEAIKAKTEEL 584
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
6-350 |
1.47e-121 |
|
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: 362.28 E-value: 1.47e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 6 IGIDLGTTNSVAAHYGPEG-IRFIPNETGELLTPSAVAFDERtGSYCVGRRAKNLIALDPRNGARKFKTTMGTD--AQYT 82
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGaEVIIENSEGKRTTPSVVYFDKD-GEVLVGEEAKNQALLDPENTIYSVKRLMGRDtkDKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 83 IRKDRFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEMAGLTVERILNEPTAAAIAYGLQKQ 162
Cdd:cd24029 80 IGGKEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAELAGLNVLRLINEPTAAALAYGLDKE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 163 ADVHRFLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYVLKKEGQDFDRLLSR-SPETAGLMMKRAE 241
Cdd:cd24029 160 GKDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEKIGIETGILDDKeDERARARLREAAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 242 LAKQQLSTNDTVPLAIsGSPLREKT--IQITREEADEVFAPLIRRLATPCQTALRGASTKISNLDAVVLVGGATRMPCVR 319
Cdd:cd24029 240 EAKIELSSSDSTDILI-LDDGKGGEleIEITREEFEELIAPLIERTIDLLEKALKDAKLSPEDIDRVLLVGGSSRIPLVR 318
|
330 340 350
....*....|....*....|....*....|.
gi 1759976916 320 NFIEDYFETEALAIVDPDLTVAQGAAIQAAL 350
Cdd:cd24029 319 EMLEEYFGREPISSVDPDEAVAKGAAIYAAS 349
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
5-567 |
1.83e-121 |
|
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act together as chaperones. HscA resembles DnaK but belongs in a separate clade. The apparent function is to aid assembly of iron-sulfur cluster proteins. Homologs from Buchnera and Wolbachia are clearly in the same clade but are highly derived and score lower than some examples of DnaK. [Protein fate, Protein folding and stabilization]
Pssm-ID: 273915 [Multi-domain] Cd Length: 599 Bit Score: 370.83 E-value: 1.83e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 5 VIGIDLGTTNSVAAHYGPEGIRFIPNETGELLTPSAVAFDERtGSYCVGRRAKNLIALDPRNGARKFKTTMG-------- 76
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYLKD-GGVEVGKEALAAAAEDPKNTISSVKRLMGrsiedikt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 77 -TDAQYTIRKD-----RFNS-------IELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEMAGLTV 143
Cdd:TIGR01991 80 fSILPYRFVDGpgemvRLRTvqgtvtpVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARLAGLNV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 144 ERILNEPTAAAIAYGLQKQADVHrFLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYVLKKEGQDFD 223
Cdd:TIGR01991 160 LRLLNEPTAAAVAYGLDKASEGI-YAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWILKQLGISAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 224 rllsRSPETAGLMMKRAELAKQQLSTNDTVPLAISGSPLREKTIqITREEADEVFAPLIRRLATPCQTALRGASTKISNL 303
Cdd:TIGR01991 239 ----LNPEDQRLLLQAARAAKEALTDAESVEVDFTLDGKDFKGK-LTRDEFEALIQPLVQKTLSICRRALRDAGLSVEEI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 304 DAVVLVGGATRMPCVRNFIEDYFETEALAIVDPDLTVAQGAAIQAALYTNDEHVDEVTVTDVLSHSLGIEiskMIGnryv 383
Cdd:TIGR01991 314 KGVVLVGGSTRMPLVRRAVAELFGQEPLTDIDPDQVVALGAAIQADLLAGNRIGNDLLLLDVTPLSLGIE---TMG---- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 384 pGFFSPIIHRNTVIPATRAEIYKPLQVGQTVLNVEVYEGEGRHVKDNHKIGTVEVRGIPNRPDNQ--VEVRFSYDLNGIL 461
Cdd:TIGR01991 387 -GLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAarIRVTFQVDADGLL 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 462 EVEATILATNQKVlQLLTRDSRTLSAQDI--------KEATERMS--LLKLDLREDRRIRALLVRAelLIKD---LPPEQ 528
Cdd:TIGR01991 466 TVSAQEQSTGVEQ-SIQVKPSYGLSDEEIermlkdsfKHAEEDMYarALAEQKVEAERILEALQAA--LAADgdlLSEDE 542
|
570 580 590
....*....|....*....|....*....|....*....
gi 1759976916 529 RNALEAELDRFESALDLHDREQIEALYNELKRICDSYGA 567
Cdd:TIGR01991 543 RAAIDAAMEALQKALQGDDADAIKAAIEALEEATDNFAA 581
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
5-560 |
2.57e-115 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 357.01 E-value: 2.57e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 5 VIGIDLGTTNSVAAHYgpEGIR--FIPNETGELLTPSAVAFDeRTGSYCVGRRAKNLIALDPRNGARKFKTTMGTDAQ-- 80
Cdd:PRK13410 4 IVGIDLGTTNSVVAVM--EGGKpvVIANAEGMRTTPSVVGFT-KDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 81 --------YTIRKDRFNSI--------------ELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEM 138
Cdd:PRK13410 81 dpeskrvpYTIRRNEQGNVrikcprlerefapeELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDAGRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 139 AGLTVERILNEPTAAAIAYGLQKQAdVHRFLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYV---- 214
Cdd:PRK13410 161 AGLEVERILNEPTAAALAYGLDRSS-SQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWLaeqf 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 215 LKKEGQDfdrlLSRSPETAGLMMKRAELAKQQLS----TNDTVPLAISGS--PLREKTiQITREEADEVFAPLIRRLATP 288
Cdd:PRK13410 240 LEKEGID----LRRDRQALQRLTEAAEKAKIELSgvsvTDISLPFITATEdgPKHIET-RLDRKQFESLCGDLLDRLLRP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 289 CQTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIVDPDLTVAQGAAIQAALYTNDehVDEVTVTDVLSH 368
Cdd:PRK13410 315 VKRALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLIPREPNQNVNPDEVVAVGAAIQAGILAGE--LKDLLLLDVTPL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 369 SLGIEiskMIGnryvpGFFSPIIHRNTVIPATRAEIYKPLQVGQTVLNVEVYEGEGRHVKDNHKIGTVEVRGIPNRPDN- 447
Cdd:PRK13410 393 SLGLE---TIG-----GVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGv 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 448 -QVEVRFSYDLNGILEVEATILATNQKvlQLLT-RDSRTLSAQD----IKEATERMSllkldlrEDRRIR---------- 511
Cdd:PRK13410 465 pQVQVAFDIDANGILQVSATDRTTGRE--QSVTiQGASTLSEQEvnrmIQEAEAKAD-------EDRRRReriekrnral 535
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1759976916 512 ALLVRAELLIKDLPPE--------QRNALEAELDRFESALDLHDREQI--------EALYnELKR 560
Cdd:PRK13410 536 TLIAQAERRLRDAALEfgpyfaerQRRAVESAMRDVQDSLEQDDDRELdlavadlqEALY-GLNR 599
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
6-553 |
6.60e-114 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 351.79 E-value: 6.60e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 6 IGIDLGTTNSVAAHYGPEGIRFIPNETGELLTPSAVAFDErtGSYCVGRRAKNLIALDPRNGARKFKTTMG---TDAQ-- 80
Cdd:PRK05183 22 VGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLE--DGIEVGYEARANAAQDPKNTISSVKRFMGrslADIQqr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 81 -----YTIRKD------------RFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEMAGLTV 143
Cdd:PRK05183 100 yphlpYQFVASengmplirtaqgLKSPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARLAGLNV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 144 ERILNEPTAAAIAYGLQKQADVHrFLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYVLKKEGQDfD 223
Cdd:PRK05183 180 LRLLNEPTAAAIAYGLDSGQEGV-IAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWILEQAGLS-P 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 224 RLlsrSPETAGLMMKRAELAKQQLSTNDTVPLAISGSplrekTIQITREEADEVFAPLIRRLATPCQTALRGASTKISNL 303
Cdd:PRK05183 258 RL---DPEDQRLLLDAARAAKEALSDADSVEVSVALW-----QGEITREQFNALIAPLVKRTLLACRRALRDAGVEADEV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 304 DAVVLVGGATRMPCVRNFIEDYFETEALAIVDPDLTVAQGAAIQAALYTNDEHVDEVTVTDVLSHSLGIEiskMIGnryv 383
Cdd:PRK05183 330 KEVVMVGGSTRVPLVREAVGEFFGRTPLTSIDPDKVVAIGAAIQADILAGNKPDSDMLLLDVIPLSLGLE---TMG---- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 384 pGFFSPIIHRNTVIPATRAEIYKPLQVGQTVLNVEVYEGEGRHVKDNHKIGTVEVRGIPNRPDNQ--VEVRFSYDLNGIL 461
Cdd:PRK05183 403 -GLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAarIRVTFQVDADGLL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 462 EV---------EATILA------TNQKVLQLLtRDSRTLSAQDIKeatERMsllkldLREDR----RIRALLVRAelLIK 522
Cdd:PRK05183 482 SVtamekstgvEASIQVkpsyglTDDEIARML-KDSMSHAEEDMQ---ARA------LAEQKveaeRVLEALQAA--LAA 549
|
570 580 590
....*....|....*....|....*....|....
gi 1759976916 523 D---LPPEQRNALEAELDRFESALDLHDREQIEA 553
Cdd:PRK05183 550 DgdlLSAAERAAIDAAMAALREVAQGDDADAIEA 583
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
5-568 |
5.29e-110 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 342.89 E-value: 5.29e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 5 VIGIDLGTTNS-VAAHYGPEGIrFIPNETGELLTPSAVAFDeRTGSYCVGRRAK--------NLIALDPRNGARKFKTT- 74
Cdd:PRK13411 4 VIGIDLGTTNScVAVLEGGKPI-VIPNSEGGRTTPSIVGFG-KSGDRLVGQLAKrqavtnaeNTVYSIKRFIGRRWDDTe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 75 -----------MGTD--AQYTIRKDRFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEMAGL 141
Cdd:PRK13411 82 eersrvpytcvKGRDdtVNVQIRGRNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAGTIAGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 142 TVERILNEPTAAAIAYGLQKQADVHRFLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYVL----KK 217
Cdd:PRK13411 162 EVLRIINEPTAAALAYGLDKQDQEQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWLVenfqQQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 218 EGQDfdrlLSRSPETAGLMMKRAELAKQQLS----TNDTVPLAISG-SPLREKTIQITREEADEVFAPLIRRLATPCQTA 292
Cdd:PRK13411 242 EGID----LSQDKMALQRLREAAEKAKIELSsmltTSINLPFITADeTGPKHLEMELTRAKFEELTKDLVEATIEPMQQA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 293 LRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFETEAL-AIVDPDLTVAQGAAIQAALYTNDehVDEVTVTDVLSHSLG 371
Cdd:PRK13411 318 LKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFGGKQPdRSVNPDEAVALGAAIQAGVLGGE--VKDLLLLDVTPLSLG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 372 IEIskmignryVPGFFSPIIHRNTVIPATRAEIYKPLQVGQTVLNVEVYEGEGRHVKDNHKIGTVEVRGIPNRPDN--QV 449
Cdd:PRK13411 396 IET--------LGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGvpQI 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 450 EVRFSYDLNGILEVEATILATNQKVLQLLTrDSRTLSAQDIkeatERMSLLKLDLREDRRIR-----------ALLVRAE 518
Cdd:PRK13411 468 EVSFEIDVNGILKVSAQDQGTGREQSIRIT-NTGGLSSNEI----ERMRQEAEKYAEEDRRRkqlielknqadSLLYSYE 542
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1759976916 519 LLIKD----LPPEQRNALEAELDRFESALDLHD--REQIEALYNELKRICDSYGAE 568
Cdd:PRK13411 543 STLKEngelISEELKQRAEQKVEQLEAALTDPNisLEELKQQLEEFQQALLAIGAE 598
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
5-559 |
1.70e-108 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 337.86 E-value: 1.70e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 5 VIGIDLGTTNSVAAHYgpEGIR--FIPNETGELLTPSAVAFdERTGSYCVGRRAKNLIALDPRNGARKFKTTMGTDAQ-- 80
Cdd:CHL00094 4 VVGIDLGTTNSVVAVM--EGGKptVIPNAEGFRTTPSIVAY-TKKGDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSei 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 81 --------YTIRKDRFNSI--------------ELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEM 138
Cdd:CHL00094 81 seeakqvsYKVKTDSNGNIkiecpalnkdfspeEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAGKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 139 AGLTVERILNEPTAAAIAYGLQKQADvHRFLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYVLK-- 216
Cdd:CHL00094 161 AGLEVLRIINEPTAASLAYGLDKKNN-ETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLIKef 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 217 --KEGQDfdrlLSRSPETAGLMMKRAELAKQQLS----TNDTVPLaISGSPLREKTIQ--ITREEADEVFAPLIRRLATP 288
Cdd:CHL00094 240 kkKEGID----LSKDRQALQRLTEAAEKAKIELSnltqTEINLPF-ITATQTGPKHIEktLTRAKFEELCSDLINRCRIP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 289 CQTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIVDPDLTVAQGAAIQAALYTNDehVDEVTVTDVLSH 368
Cdd:CHL00094 315 VENALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLLGKKPNQSVNPDEVVAIGAAVQAGVLAGE--VKDILLLDVTPL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 369 SLGIEIskmignryVPGFFSPIIHRNTVIPATRAEIYKPLQVGQTVLNVEVYEGEGRHVKDNHKIGTVEVRGIPNRPDN- 447
Cdd:CHL00094 393 SLGVET--------LGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGv 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 448 -QVEVRFSYDLNGILEVEATILATNQKvlQLLT-RDSRTLSAQDI----KEATERMSLLKLDlREDRRIR----ALLVRA 517
Cdd:CHL00094 465 pQIEVTFDIDANGILSVTAKDKGTGKE--QSITiQGASTLPKDEVermvKEAEKNAAEDKEK-REKIDLKnqaeSLCYQA 541
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1759976916 518 ELLIKDL----PPEQRNALEAELDRFESALDLHDREQIEALYNELK 559
Cdd:CHL00094 542 EKQLKELkdkiSEEKKEKIENLIKKLRQALQNDNYESIKSLLEELQ 587
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
2-348 |
2.27e-108 |
|
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: 329.18 E-value: 2.27e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 2 SEVVIGIDLGTTNSVAAHYGPEGIRFIPNETGELLTPSAVAFDERtGSYCVGRRAKNLIALDPRNGARKFKTTMGTDAQ- 80
Cdd:cd10236 1 HRLAVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGED-GKITVGEKAKENAITDPENTISSVKRLMGRSLAd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 81 ---------YTIRKD------------RFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEMA 139
Cdd:cd10236 80 vkeelpllpYRLVGDenelprfrtgagNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 140 GLTVERILNEPTAAAIAYGLQKQADvHRFLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYVLKKEG 219
Cdd:cd10236 160 GLNVLRLLNEPTAAALAYGLDQKKE-GTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWILKQIG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 220 QDFDrllsRSPETAGLMMKRAELAKQQLSTNDTVPLAISGSPLREKTiQITREEADEVFAPLIRRLATPCQTALRGASTK 299
Cdd:cd10236 239 IDAR----LDPAVQQALLQAARRAKEALSDADSASIEVEVEGKDWER-EITREEFEELIQPLVKRTLEPCRRALKDAGLE 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1759976916 300 ISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIVDPDLTVAQGAAIQA 348
Cdd:cd10236 314 PADIDEVVLVGGSTRIPLVRQRVAEFFGREPLTSINPDEVVALGAAIQA 362
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
5-350 |
2.68e-102 |
|
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: 313.68 E-value: 2.68e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 5 VIGIDLGTTNSVAAHYGPEGIRFIPNETGELLTPSAVAFDErtGSYCVGRRAKNLIALDPRNGARKFKTTMG---TDAQy 81
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTD--GERLVGEAAKNQAASNPENTIFDVKRLIGrkfDDPS- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 82 tIRKDR---------------------------FNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRK 134
Cdd:cd24028 78 -VQSDIkhwpfkvvededgkpkievtykgeektFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 135 AGEMAGLTVERILNEPTAAAIAYGLQKQADVHR-FLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNY 213
Cdd:cd24028 157 AATIAGLNVLRIINEPTAAALAYGLDKKSSGERnVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 214 VLKKEGQDFDRLLSRSPETAGLMMKRAELAKQQLSTNDTVPLAIS----GSPLrekTIQITREEADEVFAPLIRRLATPC 289
Cdd:cd24028 237 LVEEFKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDslydGIDF---ETTITRAKFEELCEDLFKKCLEPV 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1759976916 290 QTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYF-ETEALAIVDPDLTVAQGAAIQAAL 350
Cdd:cd24028 314 EKVLKDAKLSKDDIDEVVLVGGSTRIPKIQELLSEFFgGKELCKSINPDEAVAYGAAIQAAI 375
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
1-497 |
1.92e-101 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 320.59 E-value: 1.92e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 1 MSEVVIGIDLGTTNSVAAHYGPEGIRFIPNETGELLTPSAVAF--DERTgsycVGRRAKNLIALDPRNG--------ARK 70
Cdd:PTZ00009 2 TKGPAIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFtdTERL----IGDAAKNQVARNPENTvfdakrliGRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 71 --------------FKTTMGTD------AQYTIRKDRFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQ 130
Cdd:PTZ00009 78 fddsvvqsdmkhwpFKVTTGGDdkpmieVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 131 ATRKAGEMAGLTVERILNEPTAAAIAYGLQKQADVHR-FLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHA 209
Cdd:PTZ00009 158 ATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGDGEKnVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 210 LLNYVLkkegQDFDRL-LSRSPETAGLMMKR----AELAKQQLSTNDTVPLAISGspLREK---TIQITREEADEVFAPL 281
Cdd:PTZ00009 238 LVEFCV----QDFKRKnRGKDLSSNQRALRRlrtqCERAKRTLSSSTQATIEIDS--LFEGidyNVTISRARFEELCGDY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 282 IRRLATPCQTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFE-TEALAIVDPDLTVAQGAAIQAALYTND--EHVD 358
Cdd:PTZ00009 312 FRNTLQPVEKVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNgKEPCKSINPDEAVAYGAAVQAAILTGEqsSQVQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 359 EVTVTDVLSHSLGIEISKmignryvpGFFSPIIHRNTVIPATRAEIYKPLQVGQTVLNVEVYEGEGRHVKDNHKIGTVEV 438
Cdd:PTZ00009 392 DLLLLDVTPLSLGLETAG--------GVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHL 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1759976916 439 RGIPNRPDN--QVEVRFSYDLNGILEVEATILATNQKVLQLLTRDSRTLSAQDIkeatERM 497
Cdd:PTZ00009 464 DGIPPAPRGvpQIEVTFDIDANGILNVSAEDKSTGKSNKITITNDKGRLSKADI----DRM 520
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
5-349 |
4.51e-100 |
|
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: 307.87 E-value: 4.51e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 5 VIGIDLGTTNSVAAHYgpEG--IRFIPNETGELLTPSAVAFDErTGSYCVGRRAKNLIALDPRNGARKFKTTMGTD---- 78
Cdd:cd10234 1 IIGIDLGTTNSCVAVM--EGgkPTVIPNAEGGRTTPSVVAFTK-DGERLVGQPAKRQAVTNPENTIFSIKRFMGRRykev 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 79 ------AQYTIRKDRFNSI------------ELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEMAG 140
Cdd:cd10234 78 everkqVPYPVVSAGNGDAwveiggkeytpeEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 141 LTVERILNEPTAAAIAYGLQKQADvHRFLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYVL----K 216
Cdd:cd10234 158 LEVLRIINEPTAAALAYGLDKKKD-EKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLAdefkK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 217 KEGQDfdrlLSRSPETaglmMKR----AELAKQQLST-------------NDTVPLAISgsplrektIQITREEADEVFA 279
Cdd:cd10234 237 EEGID----LSKDKMA----LQRlkeaAEKAKIELSSvleteinlpfitaDASGPKHLE--------MKLTRAKFEELTE 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 280 PLIRRLATPCQTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIVDPDLTVAQGAAIQAA 349
Cdd:cd10234 301 DLVERTIEPVEQALKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGG 370
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
2-560 |
1.13e-99 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 316.41 E-value: 1.13e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 2 SEVVIGIDLGTTNS-VAAHYGPEGIrFIPNETGELLTPSAVAFdERTGSYCVGRRAKNLIALDPRNGARKFKTTMG---- 76
Cdd:PLN03184 38 AEKVVGIDLGTTNSaVAAMEGGKPT-IVTNAEGQRTTPSVVAY-TKNGDRLVGQIAKRQAVVNPENTFFSVKRFIGrkms 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 77 ------TDAQYTIRKD--------------RFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAG 136
Cdd:PLN03184 116 evdeesKQVSYRVVRDengnvkldcpaigkQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 137 EMAGLTVERILNEPTAAAIAYGLQKQADvHRFLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYVL- 215
Cdd:PLN03184 196 RIAGLEVLRIINEPTAASLAYGFEKKSN-ETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLAs 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 216 ---KKEGQDF---DRLLSRSPETaglmmkrAELAKQQLS----TNDTVPL--AISGSPLREKTiQITREEADEVFAPLIR 283
Cdd:PLN03184 275 nfkKDEGIDLlkdKQALQRLTEA-------AEKAKIELSsltqTSISLPFitATADGPKHIDT-TLTRAKFEELCSDLLD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 284 RLATPCQTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIVDPDLTVAQGAAIQAALYTNDehVDEVTVT 363
Cdd:PLN03184 347 RCKTPVENALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKLTGKDPNVTVNPDEVVALGAAVQAGVLAGE--VSDIVLL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 364 DVLSHSLGIEIskmignryVPGFFSPIIHRNTVIPATRAEIYKPLQVGQTVLNVEVYEGEGRHVKDNHKIGTVEVRGIPN 443
Cdd:PLN03184 425 DVTPLSLGLET--------LGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPP 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 444 RPDN--QVEVRFSYDLNGILEVEATILATNQKVLQLLTRDSrTLSAQD----IKEAtERMSLLKLDLREDRRIR----AL 513
Cdd:PLN03184 497 APRGvpQIEVKFDIDANGILSVSATDKGTGKKQDITITGAS-TLPKDEvermVQEA-EKFAKEDKEKRDAVDTKnqadSV 574
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1759976916 514 LVRAELLIKDL----PPEQRNALEAELDRFESALDLHDREQIEALYNELKR 560
Cdd:PLN03184 575 VYQTEKQLKELgdkvPADVKEKVEAKLKELKDAIASGSTQKMKDAMAALNQ 625
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
5-559 |
1.68e-93 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 300.20 E-value: 1.68e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 5 VIGIDLGTTNS-VAAHYGPEGiRFIPNETGELLTPSAVAFDErTGSYCVGRRAKNLIALDPRNG--------ARKF---- 71
Cdd:PTZ00400 43 IVGIDLGTTNScVAIMEGSQP-KVIENSEGMRTTPSVVAFTE-DGQRLVGIVAKRQAVTNPENTvfatkrliGRRYdeda 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 72 -KTTMGT-----------DAQYTIRKDRFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEMA 139
Cdd:PTZ00400 121 tKKEQKIlpykivrasngDAWIEAQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAGKIA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 140 GLTVERILNEPTAAAIAYGLQKqADVHRFLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYVL---- 215
Cdd:PTZ00400 201 GLDVLRIINEPTAAALAFGMDK-NDGKTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYLIaefk 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 216 KKEGQDF--DRL-LSRSPETaglmmkrAELAKQQLSTNDTVPL------AISGSPlREKTIQITREEADEVFAPLIRRLA 286
Cdd:PTZ00400 280 KQQGIDLkkDKLaLQRLREA-------AETAKIELSSKTQTEInlpfitADQSGP-KHLQIKLSRAKLEELTHDLLKKTI 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 287 TPCQTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIVDPDLTVAQGAAIQAALYTNDehVDEVTVTDVL 366
Cdd:PTZ00400 352 EPCEKCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIFGKEPSKGVNPDEAVAMGAAIQAGVLKGE--IKDLLLLDVT 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 367 SHSLGIEIskmignryVPGFFSPIIHRNTVIPATRAEIYKPLQVGQTVLNVEVYEGEGRHVKDNHKIGTVEVRGIPNRPD 446
Cdd:PTZ00400 430 PLSLGIET--------LGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPR 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 447 N--QVEVRFSYDLNGILEVEATILATNQKvLQLLTRDSRTLSAQDIkeatERMSLLKLDLREDRRIRALLV----RAELL 520
Cdd:PTZ00400 502 GvpQIEVTFDVDANGIMNISAVDKSTGKK-QEITIQSSGGLSDEEI----EKMVKEAEEYKEQDEKKKELVdaknEAETL 576
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1759976916 521 I----------KD-LPPEQRNALEAELDRFESALDLHDREQIEALYNELK 559
Cdd:PTZ00400 577 IysvekqlsdlKDkISDADKDELKQKITKLRSTLSSEDVDSIKDKTKQLQ 626
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
4-350 |
1.92e-88 |
|
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: 277.94 E-value: 1.92e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 4 VVIGIDLGTTNSVAAHYGPEGIRFIPNETGELLTPSAVAFDErtGSYCVGRRAKNLIALDPRNG--------ARKFK-TT 74
Cdd:cd10241 2 TVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTD--GERLIGDAAKNQATSNPENTvfdvkrliGRKFDdKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 75 MGTDAQY----TIRKD--------------RFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAG 136
Cdd:cd10241 80 VQKDIKLlpfkIVNKNgkpyiqvevkgekkTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 137 EMAGLTVERILNEPTAAAIAYGLQKQADVHRFLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYVL- 215
Cdd:cd10241 160 TIAGLNVLRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFIk 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 216 ---KKEGQDfdrlLSRSPETAGLMMKRAELAKQQLSTNDTVPLAI----SGSPLREKtiqITREEADEVFAPLIRRLATP 288
Cdd:cd10241 240 lfkKKTGKD----ISKDKRAVQKLRREVEKAKRALSSQHQARIEIeslfDGEDFSET---LTRAKFEELNMDLFRKTLKP 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1759976916 289 CQTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAI-VDPDLTVAQGAAIQAAL 350
Cdd:cd10241 313 VQKVLEDAGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFNGKEPSRgINPDEAVAYGAAVQAGI 375
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
5-564 |
5.04e-88 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 285.81 E-value: 5.04e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 5 VIGIDLGTTNSVAAHYGPEGIRFIPNETGELLTPSAVAFdeRTGSYCVGRRAKNLIALDPRNGARKFKTTMG-----TDA 79
Cdd:PTZ00186 29 VIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAF--KGSEKLVGLAAKRQAITNPQSTFYAVKRLIGrrfedEHI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 80 QYTIRK--------------------DRFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEMA 139
Cdd:PTZ00186 107 QKDIKNvpykivragngdawvqdgngKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTIA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 140 GLTVERILNEPTAAAIAYGLQKQADvHRFLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYVL---- 215
Cdd:PTZ00186 187 GLNVIRVVNEPTAAALAYGMDKTKD-SLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYILeefr 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 216 KKEGQDFdrllsrSPETAGLMMKR--AELAKQQLS----TNDTVPLaISGSPLREKTIQ--ITREEADEVFAPLIRRLAT 287
Cdd:PTZ00186 266 KTSGIDL------SKERMALQRVReaAEKAKCELSsameTEVNLPF-ITANADGAQHIQmhISRSKFEGITQRLIERSIA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 288 PCQTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIVDPDLTVAQGAAIQAALYTNDehVDEVTVTDVLS 367
Cdd:PTZ00186 339 PCKQCMKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFFQKDPFRGVNPDEAVALGAATLGGVLRGD--VKGLVLLDVTP 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 368 HSLGIEIskmignryVPGFFSPIIHRNTVIPATRAEIYKPLQVGQTVLNVEVYEGEGRHVKDNHKIGTVEVRGIPNRPDN 447
Cdd:PTZ00186 417 LSLGIET--------LGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRG 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 448 --QVEVRFSYDLNGILEVEATILATNQKVLQLLTRDSrTLSAQDIkeatERMSLLKLDLREDRRIRALLVRaellIKDLP 525
Cdd:PTZ00186 489 vpQIEVTFDIDANGICHVTAKDKATGKTQNITITANG-GLSKEQI----EQMIRDSEQHAEADRVKRELVE----VRNNA 559
|
570 580 590
....*....|....*....|....*....|....*....
gi 1759976916 526 PEQRNALEAELDRFESALDLhDREQIEALYNELKRICDS 564
Cdd:PTZ00186 560 ETQLTTAERQLGEWKYVSDA-EKENVKTLVAELRKAMEN 597
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
5-350 |
8.27e-85 |
|
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: 269.59 E-value: 8.27e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 5 VIGIDLGTT-NSVAA-HYGPEGIRFIPNETGELLTPSAVAFDErTGSYCVGRRAKNLIALDPRN---GARKF------KT 73
Cdd:cd10237 24 IVGIDLGTTySCVGVyHAVTGEVEVIPDDDGHKSIPSVVAFTP-DGGVLVGYDALAQAEHNPSNtiyDAKRFigktftKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 74 TMGTDA---QYTIRKDRFNSIELS----------------SMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRK 134
Cdd:cd10237 103 ELEEEAkryPFKVVNDNIGSAFFEvplngstlvvspedigSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 135 AGEMAGLTVERILNEPTAAAIAYGLQKQADVHRFLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYV 214
Cdd:cd10237 183 AANLAGLEVLRVINEPTAAAMAYGLHKKSDVNNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQYL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 215 LKKEGQDFDRLLSRSPETAGLMMKrAELAKQQLSTNDTVPLAISGSPLREK------TIQITREEADEVFAPLIRRLATP 288
Cdd:cd10237 263 IDRIAKKFGKTLTDKEDIQRLRQA-VEEVKLNLTNHNSASLSLPLQISLPSafkvkfKEEITRDLFETLNEDLFQRVLEP 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1759976916 289 CQTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIVDPDLTVAQGAAIQAAL 350
Cdd:cd10237 342 IRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFFGKDPNTSVDPELAVVTGVAIQAGI 403
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
6-350 |
3.55e-83 |
|
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: 264.49 E-value: 3.55e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 6 IGIDLGTTNSVAAHYGPEGIRFIPNETGELLTPSAVAF--DERTgsycVGRRAKNLIALDPRNG--------ARK----- 70
Cdd:cd10233 2 IGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFtdTERL----IGDAAKNQVAMNPTNTvfdakrliGRKfddpv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 71 ---------FKTTMGTD-----AQYTIRKDRFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAG 136
Cdd:cd10233 78 vqsdmkhwpFKVVSGGDkpkiqVEYKGETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 137 EMAGLTVERILNEPTAAAIAYGLQKQADVHR-FLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYVL 215
Cdd:cd10233 158 TIAGLNVLRIINEPTAAAIAYGLDKKGKGERnVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 216 kkegQDFDRL----LSRSPETAGLMMKRAELAKQQLSTNDTVPLAISGspLREKT---IQITREEADEVFAPLIRRLATP 288
Cdd:cd10233 238 ----QEFKRKhkkdISGNPRALRRLRTACERAKRTLSSSTQASIEIDS--LFEGIdfyTSITRARFEELCADLFRSTLEP 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1759976916 289 CQTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFE-TEALAIVDPDLTVAQGAAIQAAL 350
Cdd:cd10233 312 VEKVLRDAKLDKSQIHEIVLVGGSTRIPKVQKLLQDFFNgKELNKSINPDEAVAYGAAVQAAI 374
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
5-348 |
6.65e-80 |
|
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and similar proteins; This subgroup includes human mitochondrial HSPA9 (also known as mitochondrial stress-70 protein; mortalin; 75 kDa glucose-regulated protein/GRP-75; HSPA9B; MOT; peptide-binding protein 74/PBP74). It acts as a chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. It interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU. HSPA9 regulates erythropoiesis via stabilization of ISC assembly. It may play a role in the control of cell proliferation and cellular aging. Members in this subgroup 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: 466839 [Multi-domain] Cd Length: 377 Bit Score: 256.04 E-value: 6.65e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 5 VIGIDLGTTNS-VAAHYGPEGiRFIPNETGELLTPSAVAFDERtGSYCVGRRAKNLIALDPRNG--------ARKF---- 71
Cdd:cd11733 3 VIGIDLGTTNScVAVMEGKTP-KVIENAEGARTTPSVVAFTAD-GERLVGMPAKRQAVTNPENTlyatkrliGRRFddpe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 72 -------------KTTMGtDAQYTIRKDRFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEM 138
Cdd:cd11733 81 vqkdikmvpykivKASNG-DAWVEAHGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDAGQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 139 AGLTVERILNEPTAAAIAYGLQKQADvHRFLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYVLK-- 216
Cdd:cd11733 160 AGLNVLRIINEPTAAALAYGLDKKDD-KIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNYLVAef 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 217 KEGQDFDrlLSRSPetagLMMKR----AELAKQQLS----TNDTVP-LAISGSPLREKTIQITREEADEVFAPLIRRLAT 287
Cdd:cd11733 239 KKEQGID--LSKDN----LALQRlreaAEKAKIELSsslqTDINLPfITADASGPKHLNMKLTRAKFESLVGDLIKRTVE 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1759976916 288 PCQTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIVDPDLTVAQGAAIQA 348
Cdd:cd11733 313 PCKKCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIFGKAPSKGVNPDEAVAMGAAIQG 373
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
6-350 |
4.09e-76 |
|
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: 246.05 E-value: 4.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 6 IGIDLGTTNSVAAHYgPEGIRFIPNETGELLTPSAVAFDERtgSYCVGRRAKNLIALDPRNG--------ARKF-----K 72
Cdd:cd24093 2 IGIDLGTTYSCVATY-ESSVEIIANEQGNRVTPSFVAFTPE--ERLIGDAAKNQAALNPRNTvfdakrliGRRFddesvQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 73 TTMGT--------------DAQYTIRKDRFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEM 138
Cdd:cd24093 79 KDMKTwpfkvidvngnpviEVQYLGETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 139 AGLTVERILNEPTAAAIAYGL-QKQADVHR-FLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYVL- 215
Cdd:cd24093 159 AGLNVLRIINEPTAAAIAYGLgAGKSEKERhVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKa 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 216 ---KKEGQDfdrlLSRSPETAGLMMKRAELAKQQLSTNDTVPLAI-SGSPLREKTIQITREEADEVFAPLIRRLATPCQT 291
Cdd:cd24093 239 efkKKTGLD----ISDDARALRRLRTAAERAKRTLSSVTQTTVEVdSLFDGEDFESSITRARFEDLNAALFKSTLEPVEQ 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 292 ALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFETEAL-AIVDPDLTVAQGAAIQAAL 350
Cdd:cd24093 315 VLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLeKSINPDEAVAYGAAVQGAI 374
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
5-350 |
3.63e-73 |
|
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: 238.50 E-value: 3.63e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 5 VIGIDLGTTNSVAAHYGPEGIRFIPNETGELLTPSAVAFdERTGSYCVGRRAKNLIALDPRNG--------ARKF----- 71
Cdd:cd11734 3 VIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAF-TKDGERLVGVPAKRQAVVNPENTlfatkrliGRKFddaev 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 72 ------------KTTMGtDAQYTIRKDRFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEMA 139
Cdd:cd11734 82 qrdikevpykivKHSNG-DAWVEARGQKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAGQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 140 GLTVERILNEPTAAAIAYGLQKQADvHRFLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYVL---- 215
Cdd:cd11734 161 GLNVLRVINEPTAAALAYGLDKSGD-KVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHIVsefk 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 216 KKEGQDF--DRL-LSRSPETaglmmkrAELAKQQLS----TNDTVP-LAISGSPLREKTIQITREEADEVFAPLIRRLAT 287
Cdd:cd11734 240 KESGIDLskDRMaIQRIREA-------AEKAKIELSstlqTDINLPfITADASGPKHINMKLTRAQFESLVKPLVDRTVE 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1759976916 288 PCQTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIVDPDLTVAQGAAIQAAL 350
Cdd:cd11734 313 PCKKALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIFGREPSKGVNPDEAVAIGAAIQGGV 375
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
3-465 |
9.55e-64 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 219.34 E-value: 9.55e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 3 EVVIGIDLGTTNSVAAHYGPEGIRFIPNETGELLTPSAVAFDErtGSYCVGrrAKNLIALDPRNGARKFKTTMGTDAQYT 82
Cdd:PRK01433 19 QIAVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTS--NNFTIG--NNKGLRSIKRLFGKTLKEILNTPALFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 83 IRKD----------------RFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEMAGLTVERI 146
Cdd:PRK01433 95 LVKDyldvnsselklnfankQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLAAKIAGFEVLRL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 147 LNEPTAAAIAYGLQKQADvHRFLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYVLKKegqdFDrlL 226
Cdd:PRK01433 175 IAEPTAAAYAYGLNKNQK-GCYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQYLCNK----FD--L 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 227 SRSPETAGLmmkrAELAKQQLSTNDTvplaisgspLREKTIQITREEADEVFAPLIRRLATPCQTALRGASTKisNLDAV 306
Cdd:PRK01433 248 PNSIDTLQL----AKKAKETLTYKDS---------FNNDNISINKQTLEQLILPLVERTINIAQECLEQAGNP--NIDGV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 307 VLVGGATRMPCVRNFIEDYFETEALAIVDPDLTVAQGAAIQAALYTNdEHVDEVTVtDVLSHSLGIEIskmignryVPGF 386
Cdd:PRK01433 313 ILVGGATRIPLIKDELYKAFKVDILSDIDPDKAVVWGAALQAENLIA-PHTNSLLI-DVVPLSLGMEL--------YGGI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 387 FSPIIHRNTVIPATRAEIYKPLQVGQTVLNVEVYEGEGRHVKDNHKIGTVEVRGIPNRP--DNQVEVRFSYDLNGILEVE 464
Cdd:PRK01433 383 VEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKagSIRAEVTFAIDADGILSVS 462
|
.
gi 1759976916 465 A 465
Cdd:PRK01433 463 A 463
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
6-349 |
1.47e-60 |
|
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: 205.10 E-value: 1.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 6 IGIDLGTTNSVAAHYGPEGIRFIPNETGELLTPSAVAFD--ERTgsycVGRRAKNLIALDPRNGARKFKTTMGT-----D 78
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTekERL----IGEAAKSQQKSNYKNTIRNFKRLIGLkfddpE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 79 AQYTIRKDRFNSIELS-----------------------SMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKA 135
Cdd:cd11732 77 VQKEIKLLPFKLVELEdgkvgievsyngeevvfspeqvlAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 136 GEMAGLTVERILNEPTAAAIAYGLQKQ-----ADVHRFLIF-DLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHA 209
Cdd:cd11732 157 AEIAGLNCLRLINETTAAALDYGIYKSdllesEEKPRIVAFvDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 210 LLNYVL----KKEGQDfdrlLSRSPETAGLMMKRAELAKQQLSTNDTVPLAISgSPLREK--TIQITREEADEVFAPLIR 283
Cdd:cd11732 237 LVEHFAeefkKKYKID----PLENPKARLRLLDACEKLKKVLSANGEAPLNVE-CLMEDIdfSGQIKREEFEELIQPLLA 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1759976916 284 RLATPCQTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIVDPDLTVAQGAAIQAA 349
Cdd:cd11732 312 RLEAPIKKALAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVFGKDLSTTLNADEAVARGCALQAA 377
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
5-350 |
1.11e-55 |
|
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and similar proteins; The subgroup includes Arabidopsis thaliana Hsp70-14, also known as heat shock 70 kDa protein 14; heat shock protein 91), Hsp70-15 (also known as heat shock 70 kDa protein 15), and Hsp70-16 (also known as heat shock 70 kDa protein 16). In cooperation with other chaperones, they are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions. Members in this subgroup 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: 466945 [Multi-domain] Cd Length: 389 Bit Score: 192.53 E-value: 1.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 5 VIGIDLGTTNSVAAHYGPEGIRFIPNETGELLTPSAVAFDERTGSycVGRRAKNLIALDPRNGA--------RK------ 70
Cdd:cd24095 3 VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQRF--LGEAAAASILMNPKNTIsqlkrligRKfddpev 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 71 --------FKTTMGTD------AQYTIRKDRFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAG 136
Cdd:cd24095 81 qrdlklfpFKVTEGPDgeiginVNYLGEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 137 EMAGLTVERILNEPTAAAIAYGLQK----QADVHRFLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLN 212
Cdd:cd24095 161 QIAGLNCLRLMNETTATALAYGIYKtdlpETDPTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 213 YVlKKEGQDFDRLLSRSPETAGLMMKRA-ELAKQQLSTNDTVPLAISgSPLREKTIQ--ITREEADEVFAPLIRRLATPC 289
Cdd:cd24095 241 HF-AAEFKEKYKIDVKSNKKASLRLRAAcEKVKKILSANPEAPLNIE-CLMEDKDVKgmITREEFEELAAPLLERLLEPL 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1759976916 290 QTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIVDPDLTVAQGAAIQAAL 350
Cdd:cd24095 319 EKALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFFGKEPSRTMNASECVARGCALQCAM 379
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
5-350 |
2.63e-54 |
|
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: 188.60 E-value: 2.63e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 5 VIGIDLGTTNSVAAHYGPEGIRFIPNETGELLTPSAVAFDERTgsYCVGRRAKNLIALDPRNGARKFKTTMG-----TDA 79
Cdd:cd10238 2 AFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDNE--KIVGLAAKQGLIRNASNTVVRVKQLLGrsfddPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 80 QYTIRK----------------------DRFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGE 137
Cdd:cd10238 80 QELKKEskckiiekdgkpgyeieleekkKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 138 MAGLTVERILNEPTAAAIAYGL--QKQADVHRFLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYvL 215
Cdd:cd10238 160 KAGFNVLRVISEPSAAALAYGIgqDDPTENSNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEH-L 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 216 KKEGQDFDRLLSRSPETAglMMK---RAELAKQQLSTNDTVPLAIS----GSPLRektIQITREEADEVFAPLIRRLATP 288
Cdd:cd10238 239 ASEFKRQWKQDVRENKRA--MAKlmnAAEVCKHVLSTLNTATCSVEslydGMDFQ---CNVSRARFESLCSSLFQQCLEP 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1759976916 289 CQTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYF-ETEALAIVDPDLTVAQGAAIQAAL 350
Cdd:cd10238 314 IQEVLNSAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFpSAEVLSSIPPDEVIAIGAAKQAGL 376
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
5-349 |
9.99e-52 |
|
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; This subgroup includes human HYOU1 (also known as human hypoxia up-regulated 1, 170 kDa glucose-regulated protein/GRP170; HSP12A; 150 kDa oxygen-regulated protein/ORP150; GRP-170; ORP-150) and Saccharomyces cerevisiae Lhs1p (also known as Cer1p, SsI1). Mammalian HYOU1 has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. It may play a role as a molecular chaperone and participate in protein folding. HYOU1 functions as a nucleotide exchange factor (NEF) for HSPA5 (also known as BiP, Grp78 or HspA5) and may also act as a HSPA5-independent chaperone. S. cerevisiae Lhs1p, does not have a detectable endogenous ATPase activity like canonical HSP70s, but functions as a NEF for Kar2p; it's interaction with Kar2p is stimulated by nucleotide-binding. In addition, Lhs1p has a nucleotide-independent holdase activity that prevents heat-induced aggregation of proteins in vitro. Members in this subgroup 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: 466828 [Multi-domain] Cd Length: 353 Bit Score: 180.77 E-value: 9.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 5 VIGIDLGTTNSVAAHYGPeGIRF--IPNETGELLTPSAVAF--DERTgsycVGRRAKNLIALDPRNGARKFKTTMGtdaq 80
Cdd:cd10230 2 VLGIDLGSEFIKVALVKP-GVPFeiVLNEESKRKTPSAVAFrnGERL----FGDDALALATRFPENTFSYLKDLLG---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 81 YTIRkdrfnsiELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEMAGLTVERILNEPTAAAIAYGLQ 160
Cdd:cd10230 73 YSVE-------ELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIAGLNVLSLINDNTAAALNYGID 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 161 K---QADVHRFLIFDLGGGTFDVCVME------------HDEGILETLSVAGISQLGGEDFSHALLNYVLKK--EGQDFD 223
Cdd:cd10230 146 RrfeNNEPQNVLFYDMGASSTSATVVEfssvkekdkgknKTVPQVEVLGVGWDRTLGGLEFDLRLADHLADEfnEKHKKD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 224 RLLSRSPETAGLMMKRAELAKQQLSTNDTVPLAISG----SPLREKtiqITREEADEVFAPLIRRLATPCQTALRGASTK 299
Cdd:cd10230 226 KDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESlyddIDFRTK---ITREEFEELCADLFERVVAPIEEALEKAGLT 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1759976916 300 ISNLDAVVLVGGATRMPCVRNFIEDYFETEALA-IVDPDLTVAQGAAIQAA 349
Cdd:cd10230 303 LDDIDSVELIGGGTRVPKVQEALKEALGRKELGkHLNADEAAALGAAFYAA 353
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
6-350 |
5.51e-49 |
|
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: 174.49 E-value: 5.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 6 IGIDLGTTNSVAAHYGPEGIRFIPNETGELLTPSAVAFDERtgSYCVGRRAKNLIALDPRNGA--------RKF------ 71
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPK--SRYLGEAAKTQETSNFKNTVgslkrligRTFsdpeva 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 72 -------------KTTMGTDAQYTIRKDRFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEM 138
Cdd:cd24094 79 eeekyftaklvdaNGEVGAEVNYLGEKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 139 AGLTVERILNEPTAAAIAYGLQK-----QADVHRFLIF-DLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLN 212
Cdd:cd24094 159 AGLNPLRLMNDTTAAALGYGITKtdlpePEEKPRIVAFvDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 213 YVLK--KEGQDFDrlLSRSPETAGLMMKRAELAKQQLSTNDTVPLAISgSPLREK--TIQITREEADEVFAPLIRRLATP 288
Cdd:cd24094 239 HFADefKEKYKID--VRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVE-SLMNDIdvSSMLKREEFEELIAPLLERVTAP 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1759976916 289 CQTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIVDPDLTVAQGAAIQAAL 350
Cdd:cd24094 316 LEKALAQAGLTKDEIDFVELVGGTTRVPALKESISAFFGKPLSTTLNQDEAVARGAAFACAI 377
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
6-346 |
1.74e-48 |
|
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: 171.52 E-value: 1.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 6 IGIDLGTTNSVAAHYGPEGIRFIPNETGelltpsavafdertgsycvgrraknLIALDPRNGARKFKTTmgtdaqytirk 85
Cdd:cd10170 1 VGIDFGTTYSGVAYALLGPGEPPLVVLQ-------------------------LPWPGGDGGSSKVPSV----------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 86 drfnsIELSSMVLKSLKADAERLFGFEVN-------RAVITVPAYFSEAQRQATRKAGEMAGLTVE----RILNEPTAAA 154
Cdd:cd10170 45 -----LEVVADFLRALLEHAKAELGDRIWelekapiEVVITVPAGWSDAAREALREAARAAGFGSDsdnvRLVSEPEAAA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 155 IAYGLQKQADVH-----RFLIFDLGGGTFDVCVMEHDEG---ILETLSVAGISQLGGEDFSHALLNYVLKKEGQDFDRLL 226
Cdd:cd10170 120 LYALEDKGDLLPlkpgdVVLVCDAGGGTVDLSLYEVTSGsplLLEEVAPGGGALLGGTDIDEAFEKLLREKLGDKGKDLG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 227 SRSPETAGLMMKRAELAKQQLSTNDTVPLAISGSP--------LREKTIQITREEADEVFAPLIRRLatpcQTALRGA-- 296
Cdd:cd10170 200 RSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLggglpelgLEKGTLLLTEEEIRDLFDPVIDKI----LELIEEQle 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1759976916 297 STKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIV----DPDLTVAQGAAI 346
Cdd:cd10170 276 AKSGTPPDAVVLVGGFSRSPYLRERLRERFGSAGIIIVlrsdDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
4-350 |
2.21e-45 |
|
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: 163.69 E-value: 2.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 4 VVIGIDLGTTNSVAAHYGPEG-IRFIPNETGELLTPSAVAF---DERTGSycvgrRAKNLIALDPRNGARKFKTTMGTDa 79
Cdd:cd10232 1 VVIGISFGNSNSSIAIINKDGrAEVIANEDGDRQIPSILAYhgdEEYHGS-----QAKAQLVRNPKNTVANFRDLLGTT- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 80 qytirkdRFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEMAGLTVERILNEPTAAAIAYGL 159
Cdd:cd10232 75 -------TLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAAAAGLEVLQLIPEPAAAALAYDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 160 QKQADVHR-----FLIFDLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALLNYV----LKKEGQDfDRLLSRSp 230
Cdd:cd10232 148 RAETSGDTikdktVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVGHFakefKKKTKTD-PRKNARS- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 231 eTAGLMMKrAELAKQQLSTNDTVPLAISGspLREK---TIQITREEADEVFAPLIRRLATPCQTALRGASTKISNLDAVV 307
Cdd:cd10232 226 -LAKLRNA-AEITKRALSQGTSAPCSVES--LADGidfHSSINRTRYELLASKVFQQFADLVTDAIEKAGLDPLDIDEVL 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1759976916 308 LVGGATRMPCVRNFIEDYF----ETEALAIVDPDLTVAQGAAIQAAL 350
Cdd:cd10232 302 LAGGASRTPKLASNFEYLFpestIIRAPTQINPDELIARGAALQASL 348
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
6-349 |
3.76e-45 |
|
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; This subgroup 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). They 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: 466826 [Multi-domain] Cd Length: 378 Bit Score: 163.60 E-value: 3.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 6 IGIDLGTTNSVAAHYGPEGIRFIPNETGELLTPSAVAFDERTgsYCVGRRAKNLIALDPRNGARKFKTTMG--------- 76
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKN--RSMGVAAKNQAITNLKNTVSGFKRLLGrkfddpfvq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 77 ---TDAQYTIRKDRFNSI----------------ELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGE 137
Cdd:cd10228 79 kelKHLPYKVVKLPNGSVgikvqylgeehvftpeQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 138 MAGLTVERILNEPTAAAIAYGLQKQ-----ADVHRFLIF-DLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHALL 211
Cdd:cd10228 159 IAGLNCLRLLNDTTAVALAYGIYKQdlpaeEEKPRNVVFvDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 212 NYVLKKEGQDFDRLLSRSPETAGLMMKRAELAKQQLSTNDT-VPLAI---------SGSplrektiqITREEADEVFAPL 281
Cdd:cd10228 239 EHFAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSANATeLPLNIecfmddkdvSGK--------MKRAEFEELCAPL 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1759976916 282 IRRLATPCQTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIVDPDLTVAQGAAIQAA 349
Cdd:cd10228 311 FARVEVPLRSALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVFGKEPSTTLNQDEAVARGCALQCA 378
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
5-350 |
1.74e-40 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; HSPA4, also called HSP70RY, , HS24/P52, hsp70 RY, and HSPH2, or heat shock 70-related protein APG-2, responds to acidic pH stress, is involved in the radioadaptive response, is required for normal spermatogenesis and is overexpressed in hepatocellular carcinoma. It participates in a pathway along with NBS1 (Nijmegen breakage syndrome 1, also known as p85 or nibrin), heat shock transcription factor 4b (HDF4b), and HSPA14 (belonging to a different HSP70 subfamily) that induces tumor migration, invasion, and transformation. HSPA4 expression in sperm was increased in men with oligozoospermia, especially in those with varicocele. HSPA4 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: 466843 [Multi-domain] Cd Length: 381 Bit Score: 151.25 E-value: 1.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 5 VIGIDLGTTNSVAAHYGPEGIRFIPNETGELLTPSAVAFDERTGSycVGRRAKNLIALDPRNGARKFKT----------- 73
Cdd:cd11737 2 VVGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRS--IGAAAKSQVISNAKNTVQGFKRfhgrafsdpfv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 74 -----------------TMGTDAQYTIRKDRFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAG 136
Cdd:cd11737 80 qaekpslayelvqlptgTTGIKVMYMEEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 137 EMAGLTVERILNEPTAAAIAYGLQKQ-----ADVHRFLIF-DLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHAL 210
Cdd:cd11737 160 QIAGLNCLRLMNETTAVALAYGIYKQdlpapEEKPRNVVFvDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 211 LNYVLKKEGQDFDRLLSRSPETAGLMMKRAELAKQQLSTNDT-VPLAI---------SGSplrektiqITREEADEVFAP 280
Cdd:cd11737 240 VNHFCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSANASdLPLNIecfmndidvSGT--------MNRGQFEEMCAD 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 281 LIRRLATPCQTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIVDPDLTVAQGAAIQAAL 350
Cdd:cd11737 312 LLARVEPPLRSVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFFGKEVSTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
5-350 |
1.07e-36 |
|
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: 140.44 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 5 VIGIDLGTTNSVAAHYGPEGIRFIPNETGELLTPSAVAFDERTGSycVGRRAKNLIALDPRNGARKFKTTMG-------- 76
Cdd:cd11738 2 VVGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRA--IGNAAKSQIVTNAKNTIHGFKKFHGrafddpfv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 77 ----TDAQYTIRK---------------DRFNSIE-LSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAG 136
Cdd:cd11738 80 qaekIKLPYELQKmpngstgvkvryldeERVFAIEqVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 137 EMAGLTVERILNEPTAAAIAYGLQKQ-----ADVHRFLIF-DLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHAL 210
Cdd:cd11738 160 QIAGLNCLRLMNETTAVALAYGIYKQdlpalEEKPRNVVFvDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 211 LNYVLKKEGQDFDRLLSRSPETAGLMMKRAELAKQQLSTNDT-VPLAI---------SGsplrektiQITREEADEVFAP 280
Cdd:cd11738 240 VDYFCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSANASdLPLNIecfmndidvSS--------KMNRAQFEELCAS 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 281 LIRRLATPCQTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIVDPDLTVAQGAAIQAAL 350
Cdd:cd11738 312 LLARVEPPLKAVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
5-349 |
2.42e-34 |
|
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar proteins; HSPH1, also called heat shock protein 105 kDa, antigen NY-CO-25, heat shock 110 kDa protein, acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release. It prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. It inhibits HSPA8/HSC70 ATPase and chaperone activities. HSPH1 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: 466845 [Multi-domain] Cd Length: 380 Bit Score: 133.83 E-value: 2.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 5 VIGIDLGTTNSVAAHYGPEGIRFIPNETGELLTPSAVAFDERtgSYCVGRRAKNLIALDPRNGARKFKT----------- 73
Cdd:cd11739 2 VVGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSK--NRTIGVAAKNQQITNANNTVSNFKRfhgrafndpfv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 74 -----------------TMGTDAQYTIRKDRFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAG 136
Cdd:cd11739 80 qkekenlsydlvplkngGVGVKVMYLDEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 137 EMAGLTVERILNEPTAAAIAYGLQKQ-----ADVHRFLIF-DLGGGTFDVCVMEHDEGILETLSVAGISQLGGEDFSHAL 210
Cdd:cd11739 160 QIVGLNCLRLMNDMTAVALNYGIYKQdlpapDEKPRIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 211 LNYVLKKEGQDFdRLLSRSPETAGL-MMKRAELAKQQLSTNDT-VPLAISgSPLREKTI--QITREEADEVFAPLIRRLA 286
Cdd:cd11739 240 VEHFCAEFKTKY-KLDVKSKIRALLrLYQECEKLKKLMSSNSTdLPLNIE-CFMNDKDVsgKMNRSQFEELCADLLQRIE 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1759976916 287 TPCQTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIVDPDLTVAQGAAIQAA 349
Cdd:cd11739 318 VPLYSLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFFGKDVSTTLNADEAVARGCALQCA 380
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
6-345 |
1.24e-30 |
|
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: 123.92 E-value: 1.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 6 IGIDLGTTNSVAAHYGPEGIRFIPNETGELLTPSAVAFDER----TGSYCVGRRAKNLIALDPRNG--ARKFKTTMGTDA 79
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRReeegAESIYFGNDAIDAYLNDPEEGrlIKSVKSFLGSSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 80 QY--TIRKDRFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQAT-------RKAGEMAGLTVERILNEP 150
Cdd:cd10231 81 FDetTIFGRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDDaqaesrlRDAARRAGFRNVEFQYEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 151 TAAAIAYGLQKQADvHRFLIFDLGGGTFDVCVMEHDEGILET----LSVAGISqLGGEDFS------------------- 207
Cdd:cd10231 161 IAAALDYEQRLDRE-ELVLVVDFGGGTSDFSVLRLGPNRTDRradiLATSGVG-IGGDDFDrelalkkvmphlgrgstyv 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 208 -------------------HALLNYVLKKEGQDFDRLLSRS--PETAGLMM------------KRAELAKQQLSTNDTVP 254
Cdd:cd10231 239 sgdkglpvpawlyadlsnwHAISLLYTKKTLRLLLDLRRDAadPEKIERLLslvedqlghrlfRAVEQAKIALSSADEAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 255 LAISGSPlREKTIQITREEADEVFAPLIRRLATPCQTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIV 334
Cdd:cd10231 319 LSFDFIE-ISIKVTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRVFLTGGSSQSPAVRQALASLFGQARLVEG 397
|
410
....*....|.
gi 1759976916 335 DPDLTVAQGAA 345
Cdd:cd10231 398 DEFGSVAAGLA 408
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
4-346 |
1.76e-25 |
|
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: 108.13 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 4 VVIGIDLGTTNS---VAAHYGPEGIRFIPNETGE------LLTPSAVAFDERTGSYCVGRRAKNLIALDPRNGARK--FK 72
Cdd:cd10229 1 VVVAIDFGTTYSgyaYSFITDPGDIHTMYNWWGAptgvssPKTPTCLLLNPDGEFHSFGYEAREKYSDLAEDEEHQwlYF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 73 TTMGTDAQYTIRKDR-----------FNSIELSSMVLKSLKADA----ERLFGFEVN----RAVITVPAYFSEAQRQATR 133
Cdd:cd10229 81 FKFKMMLLSEKELTRdtkvkavngksMPALEVFAEALRYLKDHAlkelRDRSGSSLDeddiRWVLTVPAIWSDAAKQFMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 134 KAGEMAGLTVE------RILNEPTAAAIAYG-LQKQADVH------RFLIFDLGGGTFDVCVME-HDEGILETLSVAGIS 199
Cdd:cd10229 161 EAAVKAGLISEenseqlIIALEPEAAALYCQkLLAEGEEKelkpgdKYLVVDCGGGTVDITVHEvLEDGKLEELLKASGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 200 QLGGEDFSHALLNYVLKKEGQDF-DRLLSRSPETAGLMMKRAELAKQQLStndtvplaisgsplrektIQITREEADEVF 278
Cdd:cd10229 241 PWGSTSVDEEFEELLEEIFGDDFmEAFKQKYPSDYLDLLQAFERKKRSFK------------------LRLSPELMKSLF 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 279 APLIRRLATPCQTALRGAstKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIV--DPDLTVAQGAAI 346
Cdd:cd10229 303 DPVVKKIIEHIKELLEKP--ELKGVDYIFLVGGFAESPYLQKAVKEAFSTKVKIIIppEPGLAVVKGAVL 370
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
6-346 |
1.63e-18 |
|
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: 86.76 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 6 IGIDLGTTNSVAAHYGpEGIrfIPNEtgelltPSAVAFDERTGSY-CVGRRAKNLIALDPRNGA--RKFKTtmGTDAQYt 82
Cdd:cd10225 2 IGIDLGTANTLVYVKG-KGI--VLNE------PSVVAVDKNTGKVlAVGEEAKKMLGRTPGNIVaiRPLRD--GVIADF- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 83 irkdrfnsiELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEMAGLTVERILNEPTAAAIAYGLqkq 162
Cdd:cd10225 70 ---------EATEAMLRYFIRKAHRRRGFLRPRVVIGVPSGITEVERRAVKEAAEHAGAREVYLIEEPMAAAIGAGL--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 163 aDVHR---FLIFDLGGGTFDVCVMEHDeGILETLSVagisQLGGEDFSHALLNYVLKKEGqdfdrLLsrspetAGLMMkr 239
Cdd:cd10225 138 -PIEEprgSMVVDIGGGTTEIAVISLG-GIVTSRSV----RVAGDEMDEAIINYVRRKYN-----LL------IGERT-- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 240 AELAKQQLST------NDTVPL----AISGSPlreKTIQITREEADEVFAPLIRRLATPCQTALRGASTKISN--LDA-V 306
Cdd:cd10225 199 AERIKIEIGSaypldeELSMEVrgrdLVTGLP---RTIEITSEEVREALEEPVNAIVEAVRSTLERTPPELAAdiVDRgI 275
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1759976916 307 VLVGGATRMPCVRNFIEDyfETEALAIV--DPDLTVAQGAAI 346
Cdd:cd10225 276 VLTGGGALLRGLDELLRE--ETGLPVHVadDPLTCVAKGAGK 315
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
6-346 |
4.06e-15 |
|
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: 76.44 E-value: 4.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 6 IGIDLGTTNSVAaHYGPEGIrfIPNEtgelltPSAVAFDERTGS-YCVGRRAKNLIALDPRN--GARKFKTtmGTDAQYT 82
Cdd:pfam06723 4 IGIDLGTANTLV-YVKGKGI--VLNE------PSVVAINTKTKKvLAVGNEAKKMLGRTPGNivAVRPLKD--GVIADFE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 83 IRKDrfnsielssmVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEMAGLTVERILNEPTAAAIAYGLqkq 162
Cdd:pfam06723 73 VTEA----------MLKYFIKKVHGRRSFSKPRVVICVPSGITEVERRAVKEAAKNAGAREVFLIEEPMAAAIGAGL--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 163 aDVHR---FLIFDLGGGTFDVCVMEHDeGILETLSVagisQLGGEDFSHALLNYVLKKEgqdfdrllsrspetaGLMM-- 237
Cdd:pfam06723 140 -PVEEptgNMVVDIGGGTTEVAVISLG-GIVTSKSV----RVAGDEFDEAIIKYIRKKY---------------NLLIge 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 238 KRAELAKQQLSTN----DTVPLAISGSPLRE---KTIQITREEADEVFAPLIRRLATPCQTALRG-----ASTKISNldA 305
Cdd:pfam06723 199 RTAERIKIEIGSAypteEEEKMEIRGRDLVTglpKTIEISSEEVREALKEPVSAIVEAVKEVLEKtppelAADIVDR--G 276
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1759976916 306 VVLVGGATRMPCVRNFIEDYFETEALAIVDPDLTVAQGAAI 346
Cdd:pfam06723 277 IVLTGGGALLRGLDKLLSDETGLPVHIAEDPLTCVALGTGK 317
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
6-346 |
2.18e-13 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 71.32 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 6 IGIDLGTTNSVAAHYGpEGIrfIPNEtgelltPSAVAFDERTGS-YCVGRRAKNLIAldprngarkfKTTMGTDAQYTIR 84
Cdd:PRK13930 11 IGIDLGTANTLVYVKG-KGI--VLNE------PSVVAIDTKTGKvLAVGEEAKEMLG----------RTPGNIEAIRPLK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 85 KDRFNSIELSSMVLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEMAGLTVERILNEPTAAAIAYGLqkqaD 164
Cdd:PRK13930 72 DGVIADFEATEAMLRYFIKKARGRRFFRKPRIVICVPSGITEVERRAVREAAEHAGAREVYLIEEPMAAAIGAGL----P 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 165 VHRF---LIFDLGGGTFDVCVmehdegiletLSVAGI--SQ---LGGEDFSHALLNYVLKKEGqdfdrLL--SRSpetag 234
Cdd:PRK13930 148 VTEPvgnMVVDIGGGTTEVAV----------ISLGGIvySEsirVAGDEMDEAIVQYVRRKYN-----LLigERT----- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 235 lmmkrAELAKQQLSTndTVPLA------------ISGSPlreKTIQITREEADEVFAPLIRRLATPCQTALRGA----ST 298
Cdd:PRK13930 208 -----AEEIKIEIGS--AYPLDeeesmevrgrdlVTGLP---KTIEISSEEVREALAEPLQQIVEAVKSVLEKTppelAA 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1759976916 299 KISNlDAVVLVGGATRMPCVRNFIEDyfETEALAIV--DPDLTVAQGAAI 346
Cdd:PRK13930 278 DIID-RGIVLTGGGALLRGLDKLLSE--ETGLPVHIaeDPLTCVARGTGK 324
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
6-346 |
4.08e-13 |
|
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: 70.49 E-value: 4.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 6 IGIDLGTTNSVAAHYGpEGIRFipNEtgelltPSAVAFDERTGS-YCVGRRAKNLIALDPRNgarkfkttmgtdaQYTIR 84
Cdd:COG1077 10 IGIDLGTANTLVYVKG-KGIVL--NE------PSVVAIDKKTGKvLAVGEEAKEMLGRTPGN-------------IVAIR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 85 --KD----RFNSIElssMVLKSL--KADAERLFGfeVNRAVITVPAYFSEAQRQATRKAGEMAGLTVERILNEPTAAAIA 156
Cdd:COG1077 68 plKDgviaDFEVTE---AMLKYFikKVHGRRSFF--RPRVVICVPSGITEVERRAVRDAAEQAGAREVYLIEEPMAAAIG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 157 YGLqkqaDVHRF---LIFDLGGGTFDVCVmehdegiletLSVAGI--SQ---LGGEDFSHALLNYVLKKEGqdfdrlLSR 228
Cdd:COG1077 143 AGL----PIEEPtgnMVVDIGGGTTEVAV----------ISLGGIvvSRsirVAGDELDEAIIQYVRKKYN------LLI 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 229 SPETaglmmkrAELAKQQLST----NDTVPLAISGSPLRE---KTIQITREEADEVFAPLIRRLATPCQTALRGA----S 297
Cdd:COG1077 203 GERT-------AEEIKIEIGSayplEEELTMEVRGRDLVTglpKTITITSEEIREALEEPLNAIVEAIKSVLEKTppelA 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1759976916 298 TKISNlDAVVLVGGATRMPCVRNFIEDyfETEALAIV--DPDLTVAQGAAI 346
Cdd:COG1077 276 ADIVD-RGIVLTGGGALLRGLDKLLSE--ETGLPVHVaeDPLTCVARGTGK 323
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
4-346 |
2.11e-11 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar proteins; HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12A 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). No co-chaperones have yet been identified for HSPA12A.
Pssm-ID: 466841 [Multi-domain] Cd Length: 413 Bit Score: 66.18 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 4 VVIGIDLGTTNSVAAHY---GPEGIRFIPNETG------ELLTPSAVAFDERTGSYCVGRRAKNLIA-LDPRNGAR---- 69
Cdd:cd11735 1 VVVAIDFGTTSSGYAYSftkEPECIHVMRRWEGgdpgvsNQKTPTTILLTPERKFHSFGYAARDFYHdLDPNESKQwlyf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 70 -KFKTTMGTDAQYTIRKD-------RFNSIELSSMVLKSLKADAERLFG------FEVN--RAVITVPAYFSEAQRQATR 133
Cdd:cd11735 81 eKFKMKLHTTGNLTMETDltaangkKVKALEIFAYALQFFKEQALKELSdqagseFDNSdvRWVITVPAIWKQPAKQFMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 134 KAGEMAGLTVER------ILNEPTAAAIAYGLQKQADVHRFLIFDLGGGTFDVCVME--HDEGILETLSVAGISQLGGED 205
Cdd:cd11735 161 QAAYKAGLASPEnpeqliIALEPEAASIYCRKLRLHQMDRYVVVDCGGGTVDLTVHQirLPEGHLKELYKASGGPYGSLG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 206 FSHALLNYVLKKEGQDF-DRLLSRSPETAGLMMKRAELAKQQLSTNDTVPLAIS-----------------GSPLREKTI 267
Cdd:cd11735 241 VDYEFEKLLCKIFGEDFiDQFKIKRPAAWVDLMIAFESRKRAAAPDRTNPLNITlpfsfidyykkfrghsvEHALRKSNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 268 QITR-----------EEADEVFAPLIRRLATPCQTALRgaSTKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIVDP 336
Cdd:cd11735 321 DFVKwssqgmlrmspDAMNALFKPTIDHIIQHLTDLFQ--KPEVSGVKFLFLVGGFAESPLLQQAVQNAFGDQCRVIIPH 398
|
410
....*....|..
gi 1759976916 337 D--LTVAQGAAI 346
Cdd:cd11735 399 DvgLTILKGAVL 410
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
4-346 |
2.37e-11 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar proteins; 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. HSPA12B 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). No co-chaperones have yet been identified for HSPA12B.
Pssm-ID: 466842 [Multi-domain] Cd Length: 361 Bit Score: 65.37 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 4 VVIGIDLGTTNSVAAHY---GPEGIRFIPNETG------ELLTPSAVAFDERTGSYCVGRRAKNLIA-LDPRNgAR---- 69
Cdd:cd11736 1 VVVAIDFGTTSSGYAFSfssDPEAIHMMRKWEGgdpgvaNQKTPTSLLLTPDGAFHSFGYTARDYYHdLDPEE-ARdwly 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 70 --KFKTTMGTDAQYTIRKD-------RFNSIELSSMVL--------KSLKADAERLFGFEVNRAVITVPAYFSEAQRQAT 132
Cdd:cd11736 80 feKFKMKIHSTSDLTMETEleavngkKVQALEVFAHALrffkehalQELKDQSPSLPEKDAVRWVLTVPAIWKQPAKQFM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 133 RKAGEMAGL----TVERILN--EPTAAAIaygLQKQADvhRFLIFDLGGGTFDVCV--MEHDEGILETLSVAGISQLGGE 204
Cdd:cd11736 160 REAAYLAGLvspeNPEQLLIalEPEAASI---YCRKLD--RYIVADCGGGTVDLTVhqIEQPQGTLKELYKASGGPYGAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 205 DFSHALLNYVLKKEGQDFDRLLSRSPETAGLMMKRAELAKQqlstndtvplaisgsplREKTIQITREEADEVFAPLIRR 284
Cdd:cd11736 235 GVDLAFEKLLCQIFGEDFIATFKAKRPAAWVDLTIAFEARK-----------------RTAALRMSSEAMNELFQPTISQ 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1759976916 285 LATPCQTALrgASTKISNLDAVVLVGGATRMPCVRNFIEDYFETEALAIVDPD--LTVAQGAAI 346
Cdd:cd11736 298 IIQHIDDLM--KKPEVKGIKFLFLVGGFAESPMLQRAVQAAFGNICRVIIPQDvgLTILKGAVL 359
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
6-217 |
3.94e-10 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 61.46 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 6 IGIDLGTTNsVAAHYGPEGIrfIPNEtgelltPSAVAFDERTGS-YCVGRRAKNLIALDPRN--GARKFKTtmGTDAQYt 82
Cdd:PRK13928 6 IGIDLGTAN-VLVYVKGKGI--VLNE------PSVVAIDKNTNKvLAVGEEARRMVGRTPGNivAIRPLRD--GVIADY- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 83 irkdrfnsiELSSMVLKSL--KADAERLFGfeVNRAVITVPAYFSEAQRQATRKAGEMAGLTVERILNEPTAAAIAYGLQ 160
Cdd:PRK13928 74 ---------DVTEKMLKYFinKACGKRFFS--KPRIMICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLD 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1759976916 161 -KQADVHrfLIFDLGGGTFDVCVmehdegiletLSVAGIS-----QLGGEDFSHALLNYVLKK 217
Cdd:PRK13928 143 iSQPSGN--MVVDIGGGTTDIAV----------LSLGGIVtsssiKVAGDKFDEAIIRYIRKK 193
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
6-217 |
7.97e-10 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 60.69 E-value: 7.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 6 IGIDLGTTNsVAAHYGPEGIrfIPNEtgelltPSAVAFDERTGS-YCVGRRAKNLIALDPRN--GARKFKTtmGTDAQYT 82
Cdd:PRK13929 7 IGIDLGTAN-ILVYSKNKGI--ILNE------PSVVAVDTETKAvLAIGTEAKNMIGKTPGKivAVRPMKD--GVIADYD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 83 IRKDrfnsielssmVLKSLKADAERLFGFEVNR--AVITVPAYFSEAQRQATRKAGEMAGLTVERILNEPTAAAIAYGLQ 160
Cdd:PRK13929 76 MTTD----------LLKQIMKKAGKNIGMTFRKpnVVVCTPSGSTAVERRAISDAVKNCGAKNVHLIEEPVAAAIGADLP 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1759976916 161 KQADVHRfLIFDLGGGTFDVCVMEHDeGILETLSVagisQLGGEDFSHALLNYVLKK 217
Cdd:PRK13929 146 VDEPVAN-VVVDIGGGTTEVAIISFG-GVVSCHSI----RIGGDQLDEDIVSFVRKK 196
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
6-217 |
4.40e-08 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 55.10 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 6 IGIDLGTTNSVAAHYGpEGIrfIPNEtgelltPSAVAFDERTGS-YCVGRRAK--------NLIALDP-RNG--ArKFKT 73
Cdd:PRK13927 8 LGIDLGTANTLVYVKG-KGI--VLNE------PSVVAIRTDTKKvLAVGEEAKqmlgrtpgNIVAIRPmKDGviA-DFDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 74 T--MgtdAQYTIRKdrfnsielssmVLKSLKADAerlfgfevnRAVITVPAYFSEAQRQATRKAGEMAG----LTVEril 147
Cdd:PRK13927 78 TekM---LKYFIKK-----------VHKNFRPSP---------RVVICVPSGITEVERRAVRESALGAGarevYLIE--- 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1759976916 148 nEPTAAAIAYGLqkqaDVHR---FLIFDLGGGTFDVCVmehdegiletLSVAGI--SQL---GGEDFSHALLNYVLKK 217
Cdd:PRK13927 132 -EPMAAAIGAGL----PVTEptgSMVVDIGGGTTEVAV----------ISLGGIvySKSvrvGGDKFDEAIINYVRRN 194
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
97-197 |
4.81e-08 |
|
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; 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.
Pssm-ID: 466897 [Multi-domain] Cd Length: 241 Bit Score: 54.19 E-value: 4.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 97 VLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEMAGLTVERILNEPTAAAIAYGLQKQAdvhrflIFDLGGG 176
Cdd:cd24047 48 IVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGIRDGA------VVDIGGG 121
|
90 100 110
....*....|....*....|....*....|.
gi 1759976916 177 TFDVCVME-------HDE---GILETLSVAG 197
Cdd:cd24047 122 TTGIAVLKdgkvvytADEptgGTHLSLVLAG 152
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
97-177 |
2.11e-06 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 49.44 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 97 VLKSLKADAERLFGFEVNRAVITVPAYFSEAQRQATRKAGEMAGLTVERILNEPTAAAIAYGLQKQADVhrflifDLGGG 176
Cdd:PRK15080 72 IVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGIDNGAVV------DIGGG 145
|
.
gi 1759976916 177 T 177
Cdd:PRK15080 146 T 146
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
95-329 |
4.79e-06 |
|
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: 48.44 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 95 SMVLKSLKADAERLFGFEVNRAVITVPAyFSEAQRQATRKAG-EMAGLTVERIlneptaaAIAYGLQKQADVHR-FLIFD 172
Cdd:cd24004 49 AESIKELLKELEEKLGSKLKDVVIAIAK-VVESLLNVLEKAGlEPVGLTLEPF-------AAANLLIPYDMRDLnIALVD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 173 LGGGTFDVCVMEhDEGILETLSVAgisqLGGEDFSHALLNyvlkkegqdfDRLLSrspetaglmMKRAELAKQQLSTNDT 252
Cdd:cd24004 121 IGAGTTDIALIR-NGGIEAYRMVP----LGGDDFTKAIAE----------GFLIS---------FEEAEKIKRTYGIFLL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1759976916 253 VPLAisgsplREKTIQITREEADEVFAPLIRRLATPCQTALRGASTKISNLDAVVLVGGATRMPCVRNFIEDYFETE 329
Cdd:cd24004 177 IEAK------DQLGFTINKKEVYDIIKPVLEELASGIANAIEEYNGKFKLPDAVYLVGGGSKLPGLNEALAEKLGLP 247
|
|
| ASKHA_NBD_MamK |
cd24009 |
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ... |
6-183 |
3.83e-05 |
|
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: 46.05 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 6 IGIDLGTTNSVAAhyGPEGIRFipnetgelLTPSAVAF--DERT-----GSYCVGRRA-KNLIALD---P-RNGArkfkt 73
Cdd:cd24009 4 IGIDLGTSRSAVV--TSRGKRF--------SFRSVVGYpkDIIArkllgKEVLFGDEAlENRLALDlrrPlEDGV----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 74 tmgtdaqytIRKDRFNSIELSSMVLKSLKADAERLFGFEVnRAVITVPAYFSEAQRQATRKAGEMAGLTVeRILNEPTAa 153
Cdd:cd24009 69 ---------IKEGDDRDLEAARELLQHLIELALPGPDDEI-YAVIGVPARASAENKQALLEIARELVDGV-MVVSEPFA- 136
|
170 180 190
....*....|....*....|....*....|
gi 1759976916 154 aIAYGLQKQADVhrfLIFDLGGGTFDVCVM 183
Cdd:cd24009 137 -VAYGLDRLDNS---LIVDIGAGTTDLCRM 162
|
|
| ASKHA_NBD_ParM_pCBH-like |
cd24025 |
nucleotide-binding domain (NBD) of Clostridium botulinum plasmid segregation protein ParM and ... |
5-343 |
4.86e-05 |
|
nucleotide-binding domain (NBD) of Clostridium botulinum plasmid segregation protein ParM and similar proteins from the ParM domain family; The family corresponds to a group of uncharacterized proteins similar to Clostridium botulinum pCBH plasmid segregation protein ParM, an actin-like polymerizing motor. pCBH ParM filament structure is far more complex in comparison to the known filament structures of actin, MreB, and other ParMs. It is bipolar and stiff and like microtubules. The 15 polymerizing strands are likely to exert greater combined force relative to typical two-stranded actin-like filaments.
Pssm-ID: 466875 [Multi-domain] Cd Length: 326 Bit Score: 45.73 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 5 VIGIDLG------TTN--------SVAAHYGPEGIRFIPNETGELLTPSAVAFDERTgsYCVGRRAKNLialdprngark 70
Cdd:cd24025 1 IIAIDVGygytkaVSEngkrvifpSVVGPARERSFAGLLGGEDDLTIRLAVTIDGEE--YFVGELALRQ----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 71 fkttmGTDAQYTIRKDRFNSIElsSMVLksLKADAERLF-GFEVNRAVIT-VPAYFSEAQRQATRKA------------- 135
Cdd:cd24025 68 -----SRALELTLDRDKANSEE--TRVL--LLTALALLAaEDDEPVSLVTgLPLSYYKTQKEALEEMlkglhavvvgvdg 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 136 GEMAGLTVER--ILNEPTAAAIAYGLQKQADVH-------RFLIFDLGGGTFDVCVMEHDEGILETLSvaGISQLGGEDF 206
Cdd:cd24025 139 GTEKRITIDRvrVFPQGAGALYDALLDDDGQIIdkalakgRVGVIDIGYRTTDYVVFEDGEFLVPELS--GSLETGMSTA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 207 SHALLNYvLKKEGqdfdrllsrspetaGLMMKRAELakQQLSTNDTVPLaisgsplREKTIQITrEEADEVFAPLIRRLA 286
Cdd:cd24025 217 YRAIANA-LEEEY--------------GIDLDLHEL--DRALREGKIRV-------RGKEIDLS-DLIDEALKELARQIA 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1759976916 287 TPCQTALRGastKISNLDAVVLVGGATRMpcVRNFIEDYFETEALaIVDPDLTVAQG 343
Cdd:cd24025 272 NEIRSLWGD---GLGDLDAIILAGGGAEL--LAPYLKEMFPNAEV-VPDPQFANARG 322
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
102-323 |
2.59e-03 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 40.62 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 102 KADAERLFGFEVNRAVITVPAYFS-----EAQRQAT---RKAGEMAGLTVERILNEPTAAAIAY--GLQKQADVhrfLIF 171
Cdd:PRK11678 138 KQQAEAQLQAAITQAVIGRPVNFQglggeEANRQAEgilERAAKRAGFKDVEFQFEPVAAGLDFeaTLTEEKRV---LVV 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 172 DLGGGTFDvCVM-----------EHDEGILE-------------TLSVAGISQL---GGE-------------------- 204
Cdd:PRK11678 215 DIGGGTTD-CSMllmgpswrgraDRSASLLGhsgqriggndldiALAFKQLMPLlgmGSEtekgialpslpfwnavaind 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 205 -----DF----SHALLNYVLK--KEGQDFDRLLSRSPETAGL-MMKRAELAKQQLSTNDTVPLAIsgsPLREKTIQ--IT 270
Cdd:PRK11678 294 vpaqsDFyslaNGRLLNDLIRdaREPEKVARLLKVWRQRLSYrLVRSAEEAKIALSDQAETRASL---DFISDGLAteIS 370
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1759976916 271 REEADEVFAPLIRRLATPCQTALRGASTKIsnlDAVVLVGGATRMPCVRNFIE 323
Cdd:PRK11678 371 QQGLEEAISQPLARILELVQLALDQAQVKP---DVIYLTGGSARSPLIRAALA 420
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
483-560 |
3.96e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 39.71 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 483 RTLSAQDIKEATERMSLLKLDLREDRRIR-----ALLVRAELLIKDLPpeqrnaleaeldrfESALDLHDREQIEALYNE 557
Cdd:PRK09473 141 RMLDAVKMPEARKRMKMYPHEFSGGMRQRvmiamALLCRPKLLIADEP--------------TTALDVTVQAQIMTLLNE 206
|
...
gi 1759976916 558 LKR 560
Cdd:PRK09473 207 LKR 209
|
|
| ASKHA_NBD_ParM_R1-like |
cd24022 |
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and ... |
166-345 |
4.63e-03 |
|
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and similar proteins from ParM domain family; Type II plasmid partition systems utilize ParM NTPases in coordination with a centromere-binding protein called ParR to mediate accurate DNA segregation, a process critical for plasmid retention. The family corresponds to a group of uncharacterized proteins similar to Escherichia coli ParM, also called ParA locus 36 kDa protein, or protein StbA. It is a plasmid-encoded protein involved in the control of plasmid partition and required for accurate segregation of low-copy-number plasmid R1.
Pssm-ID: 466872 [Multi-domain] Cd Length: 324 Bit Score: 39.56 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 166 HRFLIFDLGGGTFDVCVMEHDEGILEtlSVAGISQLGGEDFSHALLNYVLKKEGQdfdRLLSRSpetaglMMKRAelakq 245
Cdd:cd24022 174 GPVAVIDIGGTTTDIAVVSGGLSIDH--ARSGTIELGVLDVRDALKDALKKRFGL---SSISDA------ELDRA----- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759976916 246 qlstndtvplaisgspLREKTIQITREEADEVF---APLIRRLATPCQTALRGASTKISNLDAVVLVGGATRMpcVRNFI 322
Cdd:cd24022 238 ----------------LRTGKFRLNGGKEVDVSdlvNEAIAEVAERILNEIKRRLGDASDLDRVIFVGGGAEL--LEDEL 299
|
170 180
....*....|....*....|...
gi 1759976916 323 EDYFETEALAIVDPDLTVAQGAA 345
Cdd:cd24022 300 KEALGPNAIIVDEPEFANARGML 322
|
|
| |
