|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
8-347 |
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: 576.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHILVGKPAVSRRTSHPDKTAALFKRAMGSNTNWRLGSD 87
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVDEDGSILVGRAAKERLVTHPDRTAASFKRFMGTDKQYRLGNH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 88 TFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELAGLNAVRLINEPTAAAMAYGLHTQQ-NT 166
Cdd:cd10235 81 TFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELAGLKVERLINEPTAAALAYGLHKREdET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 167 RSLVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVDEVLKRADVARTTLNESELGALYACVEAAKCSNQS 246
Cdd:cd10235 161 RFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFLKKHRLDFTSLSPSELAALRKRAEQAKRQLSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 247 PLH--IRWQYQDETRECEFYENELEDLWLPLLNRLRVPIEQALRDARLKPSQIDSLVLVGGASQMPLVQRIAVRLFGKLP 324
Cdd:cd10235 241 QDSaeIRLTYRGEELEIELTREEFEELCAPLLERLRQPIERALRDAGLKPSDIDAVILVGGATRMPLVRQLIARLFGRLP 320
|
330 340
....*....|....*....|...
gi 446290036 325 YQSYDPSTIVALGAAIQAACRLR 347
Cdd:cd10235 321 LSSLDPDEAVALGAAIQAALKAR 343
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
7-472 |
4.08e-161 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 467.38 E-value: 4.08e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 7 AIGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHILVGKPAVSRRTSHPDKTAALFKRAMGSNTNW---R 83
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPKDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFDeatE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 84 LGSDTFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELAGLNAVRLINEPTAAAMAYGL-HT 162
Cdd:COG0443 81 VGGKRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARIAGLEVLRLLNEPTAAALAYGLdKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 163 QQNTRSLVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVDEV---LKRADVARTTLNESELGALYACVEA 239
Cdd:COG0443 161 KEEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVapeFGKEEGIDLRLDPAALQRLREAAEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 240 AKC----SNQSPLHIRwQYQDETRECEFYENELEDLWLPLLNRLRVPIEQALRDARLKPSQIDSLVLVGGASQMPLVQRI 315
Cdd:COG0443 241 AKIelssADEAEINLP-FSGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADAGLSPSDIDAVLLVGGSTRMPAVRER 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 316 AVRLFGKLPYQSYDPSTIVALGAAIQAAcrLRSEDIEEvilTDICPYSLGVEVnrqgVSGIFSPIIERNTTVPVSRVETY 395
Cdd:COG0443 320 VKELFGKEPLKGVDPDEAVALGAAIQAG--VLAGDVKD---LDVTPLSLGIET----LGGVFTKLIPRNTTIPTAKSQVF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 396 STMHPEQDSITVNVYQGENHKVKNNILVESFDV---PLKKTGAYQsIDIRFSYDINGLLEVDVLLEDGSVKSRVINHSPV 472
Cdd:COG0443 391 STAADNQTAVEIHVLQGERELAADNRSLGRFELtgiPPAPRGVPQ-IEVTFDIDANGILSVSAKDLGTGKEQSITIKEEI 469
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
8-345 |
6.18e-142 |
|
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: 413.90 E-value: 6.18e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVW-KDGAAQLIPNKFGEYLTPSIISMDENNHILVGKPAVSRRTSHPDKTAALFKRAMGSNTNWR--L 84
Cdd:cd24029 1 VGIDLGTTNSAVAYWdGNGAEVIIENSEGKRTTPSVVYFDKDGEVLVGEEAKNQALLDPENTIYSVKRLMGRDTKDKeeI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 85 GSDTFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELAGLNAVRLINEPTAAAMAYGLH-TQ 163
Cdd:cd24029 81 GGKEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAELAGLNVLRLINEPTAAALAYGLDkEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 164 QNTRSLVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVDEVLKRADVAR----TTLNESELGALYACVEA 239
Cdd:cd24029 161 KDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEKIGIETgildDKEDERARARLREAAEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 240 AKC----SNQSPLHIRWQYQDETRECEFYENELEDLWLPLLNRLRVPIEQALRDARLKPSQIDSLVLVGGASQMPLVQRI 315
Cdd:cd24029 241 AKIelssSDSTDILILDDGKGGELEIEITREEFEELIAPLIERTIDLLEKALKDAKLSPEDIDRVLLVGGSSRIPLVREM 320
|
330 340 350
....*....|....*....|....*....|
gi 446290036 316 AVRLFGKLPYQSYDPSTIVALGAAIQAACR 345
Cdd:cd24029 321 LEEYFGREPISSVDPDEAVAKGAAIYAASL 350
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
7-542 |
2.11e-127 |
|
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: 385.51 E-value: 2.11e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 7 AIGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHILVGKPAVSRRTSHPDKTAALFKRAMG--------- 77
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNGERLVGQPAKRQAVTNPENTIYSIKRFMGrrfdevtee 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 78 ------------SNTNWRLGSDTFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELAGLNAV 145
Cdd:TIGR02350 82 akrvpykvvgdgGDVRVKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAGLEVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 146 RLINEPTAAAMAYGLHTQ-QNTRSLVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVD------------ 212
Cdd:TIGR02350 162 RIINEPTAAALAYGLDKSkKDEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDwladefkkeegi 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 213 -------------EVLKRADVARTTLNESELGALYACVEAakcsnQSPLHIRwqyQDETREcefyenELEDLWLPLLNRL 279
Cdd:TIGR02350 242 dlskdkmalqrlkEAAEKAKIELSSVLSTEINLPFITADA-----SGPKHLE---MTLTRA------KFEELTADLVERT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 280 RVPIEQALRDARLKPSQIDSLVLVGGASQMPLVQRIAVRLFGKLPYQSYDPSTIVALGAAIQAAcrLRSEDIEEVILTDI 359
Cdd:TIGR02350 308 KEPVRQALKDAGLSASDIDEVILVGGSTRIPAVQELVKDFFGKEPNKSVNPDEVVAIGAAIQGG--VLKGDVKDVLLLDV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 360 CPYSLGVEVnrqgVSGIFSPIIERNTTVPVSRVETYSTMHPEQDSITVNVYQGENHKVKNNILVESF---DVPLKKTGAY 436
Cdd:TIGR02350 386 TPLSLGIET----LGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFeltGIPPAPRGVP 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 437 QsIDIRFSYDINGLLEVDVlLEDGSVKSRVIN-HSPVTLSAQQI-----------EESRTRLSALKIYPR-DMLINRTFK 503
Cdd:TIGR02350 462 Q-IEVTFDIDANGILHVSA-KDKGTGKEQSITiTASSGLSEEEIermvkeaeanaEEDKKRKEEIEARNNaDSLAYQAEK 539
|
570 580 590
....*....|....*....|....*....|....*....
gi 446290036 504 AkLEELWARALGDEREEIGRVITDFDAALQSNDMARVDE 542
Cdd:TIGR02350 540 T-LKEAGDKLPAEEKEKIEKAVAELKEALKGEDVEEIKA 577
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
7-536 |
1.49e-125 |
|
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: 380.84 E-value: 1.49e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 7 AIGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHiLVGKPAVSRRTSHPDKTAALFKRAMGSNTNW---- 82
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPKER-LVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDpvvq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 83 ----------------------RLGSDTFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELA 140
Cdd:pfam00012 80 rdikhlpykvvklpngdagvevRYLGETFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 141 GLNAVRLINEPTAAAMAYGLHTQQNTRS-LVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVDEVLKRA- 218
Cdd:pfam00012 160 GLNVLRIVNEPTAAALAYGLDKTDKERNiAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEEFk 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 219 -----DVARTTLNESELgaLYACvEAAKC---SNQSPLHIRWQYQDE---------TREcefyenELEDLWLPLLNRLRV 281
Cdd:pfam00012 240 kkygiDLSKDKRALQRL--REAA-EKAKIelsSNQTNINLPFITAMAdgkdvsgtlTRA------KFEELVADLFERTLE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 282 PIEQALRDARLKPSQIDSLVLVGGASQMPLVQRIAVRLFGKLPYQSYDPSTIVALGAAIQAACRLRSEDIEEVILTDICP 361
Cdd:pfam00012 311 PVEKALKDAGLSKSEIDEVVLVGGSTRIPAVQELVKEFFGKEPSKGVNPDEAVAIGAAVQAGVLSGTFDVKDFLLLDVTP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 362 YSLGVEVnrqgVSGIFSPIIERNTTVPVSRVETYSTMHPEQDSITVNVYQGENHKVKNNILVESFDV----PLKKTGayQ 437
Cdd:pfam00012 391 LSLGIET----LGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELdgipPAPRGV--P 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 438 SIDIRFSYDINGLLEVDVLLEDGSVKSRVINHSPVTLSAQQIEE---------SRTRLSALKIYPR---DMLINRTfKAK 505
Cdd:pfam00012 465 QIEVTFDIDANGILTVSAKDKGTGKEQEITIEASEGLSDDEIERmvkdaeeyaEEDKKRKERIEAKneaEEYVYSL-EKS 543
|
570 580 590
....*....|....*....|....*....|.
gi 446290036 506 LEELWARALGDEREEIGRVITDFDAALQSND 536
Cdd:pfam00012 544 LEEEGDKVPEAEKSKVESAIEWLKDELEGDD 574
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
7-542 |
2.34e-122 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 373.28 E-value: 2.34e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 7 AIGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHILVGKPAVSRRTSHPDKTAALFKRAMGSNTN----- 81
Cdd:PRK00290 4 IIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRLMGRRDEevqkd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 82 -----------------WRLGSDTFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELAGLNA 144
Cdd:PRK00290 84 iklvpykivkadngdawVEIDGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAGLEV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 145 VRLINEPTAAAMAYGLHTQQNTRSLVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHM----LVDEVLK---- 216
Cdd:PRK00290 164 LRIINEPTAAALAYGLDKKGDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRiidyLADEFKKengi 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 217 --RADV-ARTTLNESelgalyacVEAAKC--SNQS---------------PLHIrwqyqDE--TREcefyenELEDLWLP 274
Cdd:PRK00290 244 dlRKDKmALQRLKEA--------AEKAKIelSSAQqteinlpfitadasgPKHL-----EIklTRA------KFEELTED 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 275 LLNRLRVPIEQALRDARLKPSQIDSLVLVGGASQMPLVQRIAVRLFGKLPYQSYDPSTIVALGAAIQAAcrLRSEDIEEV 354
Cdd:PRK00290 305 LVERTIEPCKQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGG--VLAGDVKDV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 355 ILTDICPYSLGVEVnrQGvsGIFSPIIERNTTVPVSRVETYSTMHPEQDSITVNVYQGENHKVKNNILVESFD------- 427
Cdd:PRK00290 383 LLLDVTPLSLGIET--LG--GVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNltgippa 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 428 ---VPlkktgayQsIDIRFSYDINGLLEV---DvlLEDGSVKSRVINHSpVTLSAQQI------------------EESR 483
Cdd:PRK00290 459 prgVP-------Q-IEVTFDIDANGIVHVsakD--KGTGKEQSITITAS-SGLSDEEIermvkdaeanaeedkkrkELVE 527
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 446290036 484 TRLSAlkiyprDMLINRTFKAkLEELWARALGDEREEIGRVITDFDAALQSNDMARVDE 542
Cdd:PRK00290 528 ARNQA------DSLIYQTEKT-LKELGDKVPADEKEKIEAAIKELKEALKGEDKEAIKA 579
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
7-533 |
3.29e-117 |
|
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: 359.28 E-value: 3.29e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 7 AIGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHILVGKPAVSRRTSHPDKTAALFKRAMG--------- 77
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYLKDGGVEVGKEALAAAAEDPKNTISSVKRLMGrsiediktf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 78 SNTNWRLGSDTFNAP------------ELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELAGLNAV 145
Cdd:TIGR01991 81 SILPYRFVDGPGEMVrlrtvqgtvtpvEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARLAGLNVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 146 RLINEPTAAAMAYGLHTQQNTRSLVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVDEVLKRADVaRTTL 225
Cdd:TIGR01991 161 RLLNEPTAAAVAYGLDKASEGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWILKQLGI-SADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 226 NESELGALYACVEAAK--CSNQSPLHIRWQYQDETRECEFYENELEDLWLPLLNRLRVPIEQALRDARLKPSQIDSLVLV 303
Cdd:TIGR01991 240 NPEDQRLLLQAARAAKeaLTDAESVEVDFTLDGKDFKGKLTRDEFEALIQPLVQKTLSICRRALRDAGLSVEEIKGVVLV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 304 GGASQMPLVQRIAVRLFGKLPYQSYDPSTIVALGAAIQAACRLRSEDIEEVILTDICPYSLGVEVnrqgVSGIFSPIIER 383
Cdd:TIGR01991 320 GGSTRMPLVRRAVAELFGQEPLTDIDPDQVVALGAAIQADLLAGNRIGNDLLLLDVTPLSLGIET----MGGLVEKIIPR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 384 NTTVPVSRVETYSTMHPEQDSITVNVYQGENHKVKNNILVESFD---VPLKKTGAYQsIDIRFSYDINGLLEVDVLLEDG 460
Cdd:TIGR01991 396 NTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFElrgIPPMVAGAAR-IRVTFQVDADGLLTVSAQEQST 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446290036 461 SVKSRVINHSPVTLSAQQIEEsrtrlsalkiyprdMLINRTFKAKlEELWARALGDEREEIGRVITDFDAALQ 533
Cdd:TIGR01991 475 GVEQSIQVKPSYGLSDEEIER--------------MLKDSFKHAE-EDMYARALAEQKVEAERILEALQAALA 532
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
8-453 |
4.19e-110 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 341.71 E-value: 4.19e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHILVGKPAVSRRTSHPDKTAALFKRAMGSNTN------ 81
Cdd:CHL00094 5 VGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKGDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSeiseea 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 82 ----WRLGSDT--------------FNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELAGLN 143
Cdd:CHL00094 85 kqvsYKVKTDSngnikiecpalnkdFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAGKIAGLE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 144 AVRLINEPTAAAMAYGLHTQQNTRSLVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVDEVLKRADVART 223
Cdd:CHL00094 165 VLRIINEPTAASLAYGLDKKNNETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLIKEFKKKEG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 224 TLNESELGALYACVEAA-----KCSNQS---------------PLHIRwqyQDETREcefyenELEDLWLPLLNRLRVPI 283
Cdd:CHL00094 245 IDLSKDRQALQRLTEAAekakiELSNLTqteinlpfitatqtgPKHIE---KTLTRA------KFEELCSDLINRCRIPV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 284 EQALRDARLKPSQIDSLVLVGGASQMPLVQRIAVRLFGKLPYQSYDPSTIVALGAAIQAACrLRSEdIEEVILTDICPYS 363
Cdd:CHL00094 316 ENALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLLGKKPNQSVNPDEVVAIGAAVQAGV-LAGE-VKDILLLDVTPLS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 364 LGVEVnrqgVSGIFSPIIERNTTVPVSRVETYSTMHPEQDSITVNVYQGENHKVKNNILVESF---DVPLKKTGAYQsID 440
Cdd:CHL00094 394 LGVET----LGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFrldGIPPAPRGVPQ-IE 468
|
490
....*....|...
gi 446290036 441 IRFSYDINGLLEV 453
Cdd:CHL00094 469 VTFDIDANGILSV 481
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
8-343 |
3.30e-108 |
|
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: 328.28 E-value: 3.30e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHILVGKPAVSRRTSHPDKTAALFKRAMGSNTN------ 81
Cdd:cd10234 2 IGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKevever 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 82 ----------------WRLGSDTFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELAGLNAV 145
Cdd:cd10234 82 kqvpypvvsagngdawVEIGGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIAGLEVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 146 RLINEPTAAAMAYGLHTQQNTRSLVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVDEVLK--------- 216
Cdd:cd10234 162 RIINEPTAAALAYGLDKKKDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADefkkeegid 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 217 -RADV-ARTTLNESelgalyacVEAAKC----------------SNQS-PLHIRwqyQDETREcefyenELEDLWLPLLN 277
Cdd:cd10234 242 lSKDKmALQRLKEA--------AEKAKIelssvleteinlpfitADASgPKHLE---MKLTRA------KFEELTEDLVE 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446290036 278 RLRVPIEQALRDARLKPSQIDSLVLVGGASQMPLVQRIAVRLFGKLPYQSYDPSTIVALGAAIQAA 343
Cdd:cd10234 305 RTIEPVEQALKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGG 370
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
8-453 |
3.41e-106 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 332.75 E-value: 3.41e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHILVGKPAvsRRTS--HPDKTAALFKRAMGS------- 78
Cdd:PRK13410 5 VGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTKDGELLVGQLA--RRQLvlNPQNTFYNLKRFIGRrydeldp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 79 -------------NTNWRLGSDTFN---APE-LSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELAG 141
Cdd:PRK13410 83 eskrvpytirrneQGNVRIKCPRLErefAPEeLSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDAGRIAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 142 LNAVRLINEPTAAAMAYGLHTQQNTRSLVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVD----EVLKR 217
Cdd:PRK13410 163 LEVERILNEPTAAALAYGLDRSSSQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDwlaeQFLEK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 218 --ADVARttlNESELGALYACVEAAKC-----------------SNQSPLHIrwqyqdETReceFYENELEDLWLPLLNR 278
Cdd:PRK13410 243 egIDLRR---DRQALQRLTEAAEKAKIelsgvsvtdislpfitaTEDGPKHI------ETR---LDRKQFESLCGDLLDR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 279 LRVPIEQALRDARLKPSQIDSLVLVGGASQMPLVQRIAVRLFGKLPYQSYDPSTIVALGAAIQAAcrLRSEDIEEVILTD 358
Cdd:PRK13410 311 LLRPVKRALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLIPREPNQNVNPDEVVAVGAAIQAG--ILAGELKDLLLLD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 359 ICPYSLGVEVnrqgVSGIFSPIIERNTTVPVSRVETYSTMHPEQDSITVNVYQGENHKVKNNILVESFD---VPLKKTGA 435
Cdd:PRK13410 389 VTPLSLGLET----IGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKlsgIPPAPRGV 464
|
490
....*....|....*...
gi 446290036 436 YQsIDIRFSYDINGLLEV 453
Cdd:PRK13410 465 PQ-VQVAFDIDANGILQV 481
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
8-483 |
3.53e-106 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 332.49 E-value: 3.53e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHILVGKPAVSRRTSHPDKTAALFKRAMG---------- 77
Cdd:PRK13411 5 IGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSGDRLVGQLAKRQAVTNAENTVYSIKRFIGrrwddteeer 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 78 ------------SNTNWRLGSDTFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELAGLNAV 145
Cdd:PRK13411 85 srvpytcvkgrdDTVNVQIRGRNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAGTIAGLEVL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 146 RLINEPTAAAMAYGLHTQ-QNTRSLVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVD---EVLKRADVA 221
Cdd:PRK13411 165 RIINEPTAAALAYGLDKQdQEQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDwlvENFQQQEGI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 222 RTTLNESELGALYACVEAAKCSNQSPL----HIRWQYQDETR----ECEFYENELEDLWLPLLNRLRVPIEQALRDARLK 293
Cdd:PRK13411 245 DLSQDKMALQRLREAAEKAKIELSSMLttsiNLPFITADETGpkhlEMELTRAKFEELTKDLVEATIEPMQQALKDAGLK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 294 PSQIDSLVLVGGASQMPLVQRIAVRLF-GKLPYQSYDPSTIVALGAAIQAAcrLRSEDIEEVILTDICPYSLGVEVnrqg 372
Cdd:PRK13411 325 PEDIDRVILVGGSTRIPAVQEAIQKFFgGKQPDRSVNPDEAVALGAAIQAG--VLGGEVKDLLLLDVTPLSLGIET---- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 373 VSGIFSPIIERNTTVPVSRVETYSTMHPEQDSITVNVYQGENHKVKNNILVESFD---VPLKKTGAYQsIDIRFSYDING 449
Cdd:PRK13411 399 LGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLltgIPPAPRGVPQ-IEVSFEIDVNG 477
|
490 500 510
....*....|....*....|....*....|....*
gi 446290036 450 LLEVDVLLE-DGSVKSRVINHSPvTLSAQQIEESR 483
Cdd:PRK13411 478 ILKVSAQDQgTGREQSIRITNTG-GLSSNEIERMR 511
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
7-343 |
9.14e-104 |
|
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: 317.15 E-value: 9.14e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 7 AIGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENnHILVGKPAVSRRTSHPDKTAALFKRAMG--------- 77
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDG-ERLVGEAAKNQAASNPENTIFDVKRLIGrkfddpsvq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 78 ---SNTNWRLGSD----------------TFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAE 138
Cdd:cd24028 80 sdiKHWPFKVVEDedgkpkievtykgeekTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 139 LAGLNAVRLINEPTAAAMAYGLHTQQNTRS--LVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVD---E 213
Cdd:cd24028 160 IAGLNVLRIINEPTAAALAYGLDKKSSGERnvLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEylvE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 214 VLKRADVARTTLNESELGALYACVEAAK----CSNQSPLHIRWQYQDETRECEFYENELEDLWLPLLNRLRVPIEQALRD 289
Cdd:cd24028 240 EFKKKHGKDLRENPRAMRRLRSACERAKrtlsTSTSATIEIDSLYDGIDFETTITRAKFEELCEDLFKKCLEPVEKVLKD 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 446290036 290 ARLKPSQIDSLVLVGGASQMPLVQRIAVRLF-GKLPYQSYDPSTIVALGAAIQAA 343
Cdd:cd24028 320 AKLSKDDIDEVVLVGGSTRIPKIQELLSEFFgGKELCKSINPDEAVAYGAAIQAA 374
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
5-342 |
2.30e-102 |
|
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: 313.00 E-value: 2.30e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 5 ELAIGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHILVGKPAVSRRTSHPDKTAALFKRAMGSNTN--- 81
Cdd:cd10236 2 RLAVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITVGEKAKENAITDPENTISSVKRLMGRSLAdvk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 82 -------WRLGSDT------------FNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELAGL 142
Cdd:cd10236 82 eelpllpYRLVGDEnelprfrtgagnLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARLAGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 143 NAVRLINEPTAAAMAYGLHTQQNTRSLVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVDEVLKRADvAR 222
Cdd:cd10236 162 NVLRLLNEPTAAALAYGLDQKKEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWILKQIG-ID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 223 TTLNESELGALYACVEAAK--CSNQSPLHIRWQYQDETRECEFYENELEDLWLPLLNRLRVPIEQALRDARLKPSQIDSL 300
Cdd:cd10236 241 ARLDPAVQQALLQAARRAKeaLSDADSASIEVEVEGKDWEREITREEFEELIQPLVKRTLEPCRRALKDAGLEPADIDEV 320
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446290036 301 VLVGGASQMPLVQRIAVRLFGKLPYQSYDPSTIVALGAAIQA 342
Cdd:cd10236 321 VLVGGSTRIPLVRQRVAEFFGREPLTSINPDEVVALGAAIQA 362
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
6-533 |
3.86e-99 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 312.88 E-value: 3.86e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 6 LAIGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNhILVGKPAVSRRTSHPDKTAALFKRAMGSNTNwRLG 85
Cdd:PRK05183 20 LAVGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDG-IEVGYEARANAAQDPKNTISSVKRFMGRSLA-DIQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 86 SDTFNAP-----------------------ELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELAGL 142
Cdd:PRK05183 98 QRYPHLPyqfvasengmplirtaqglkspvEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARLAGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 143 NAVRLINEPTAAAMAYGLHTQQNTRSLVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVDEVLKRADVAr 222
Cdd:PRK05183 178 NVLRLLNEPTAAAIAYGLDSGQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWILEQAGLS- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 223 TTLNESELGALYACVEAAK--CSNQSplHIRWQYQDE----TREcefyenELEDLWLPLLNRLRVPIEQALRDARLKPSQ 296
Cdd:PRK05183 257 PRLDPEDQRLLLDAARAAKeaLSDAD--SVEVSVALWqgeiTRE------QFNALIAPLVKRTLLACRRALRDAGVEADE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 297 IDSLVLVGGASQMPLVQRIAVRLFGKLPYQSYDPSTIVALGAAIQAacrlrseDI-------EEVILTDICPYSLGVEVn 369
Cdd:PRK05183 329 VKEVVMVGGSTRVPLVREAVGEFFGRTPLTSIDPDKVVAIGAAIQA-------DIlagnkpdSDMLLLDVIPLSLGLET- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 370 rqgVSGIFSPIIERNTTVPVSRVETYSTMHPEQDSITVNVYQGENHKVKNNILVESF---DVPLKKTGAYQsIDIRFSYD 446
Cdd:PRK05183 401 ---MGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFelrGIPPMAAGAAR-IRVTFQVD 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 447 INGLLEVDVlLEDGS-VKSRVINHSPVTLSAQQIEesrtrlsalkiyprDMLINRTFKAKlEELWARALGDEREEIGRVI 525
Cdd:PRK05183 477 ADGLLSVTA-MEKSTgVEASIQVKPSYGLTDDEIA--------------RMLKDSMSHAE-EDMQARALAEQKVEAERVL 540
|
....*...
gi 446290036 526 TDFDAALQ 533
Cdd:PRK05183 541 EALQAALA 548
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
4-540 |
6.12e-99 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 314.09 E-value: 6.12e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 4 AELAIGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHILVGKPAVSRRTSHPDKTAALFKRAMG------ 77
Cdd:PLN03184 38 AEKVVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNGDRLVGQIAKRQAVVNPENTFFSVKRFIGrkmsev 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 78 --------------SNTNWRLGS----DTFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAEL 139
Cdd:PLN03184 118 deeskqvsyrvvrdENGNVKLDCpaigKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 140 AGLNAVRLINEPTAAAMAYGLHTQQNTRSLVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVDEV---LK 216
Cdd:PLN03184 198 AGLEVLRIINEPTAASLAYGFEKKSNETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLasnFK 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 217 RADVARTTLNESELGALYACVEAAKCSNQS-----------------PLHIrwqyqdetrECEFYENELEDLWLPLLNRL 279
Cdd:PLN03184 278 KDEGIDLLKDKQALQRLTEAAEKAKIELSSltqtsislpfitatadgPKHI---------DTTLTRAKFEELCSDLLDRC 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 280 RVPIEQALRDARLKPSQIDSLVLVGGASQMPLVQRIAVRLFGKLPYQSYDPSTIVALGAAIQAAcrLRSEDIEEVILTDI 359
Cdd:PLN03184 349 KTPVENALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKLTGKDPNVTVNPDEVVALGAAVQAG--VLAGEVSDIVLLDV 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 360 CPYSLGVEVnrqgVSGIFSPIIERNTTVPVSRVETYSTMHPEQDSITVNVYQGENHKVKNNILVESF---DVPLKKTGAY 436
Cdd:PLN03184 427 TPLSLGLET----LGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFrldGIPPAPRGVP 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 437 QsIDIRFSYDINGLLEVDVlLEDGSVKSRVINHSPV-TLSAQQIE-----------ESRTRLSALKIYPR-DMLINRTFK 503
Cdd:PLN03184 503 Q-IEVKFDIDANGILSVSA-TDKGTGKKQDITITGAsTLPKDEVErmvqeaekfakEDKEKRDAVDTKNQaDSVVYQTEK 580
|
570 580 590
....*....|....*....|....*....|....*..
gi 446290036 504 aKLEELWARALGDEREEIGRVITDFDAALQSNDMARV 540
Cdd:PLN03184 581 -QLKELGDKVPADVKEKVEAKLKELKDAIASGSTQKM 616
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
2-542 |
3.59e-95 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 303.64 E-value: 3.59e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 2 DNAELAIGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHiLVGKPAVSRRTSHPDKTAALFKRAMGSN-- 79
Cdd:PTZ00009 1 MTKGPAIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTER-LIGDAAKNQVARNPENTVFDAKRLIGRKfd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 80 --------TNWRL----GSD--------------TFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHT 133
Cdd:PTZ00009 80 dsvvqsdmKHWPFkvttGGDdkpmievtyqgekkTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 134 RLAAELAGLNAVRLINEPTAAAMAYGLHTQQNTRS--LVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLV 211
Cdd:PTZ00009 160 KDAGTIAGLNVLRIINEPTAAAIAYGLDKKGDGEKnvLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 212 D---EVLKRADVART-TLNESELGALYACVEAAK----CSNQSPLHIRWQYQDETRECEFYENELEDLWLPLLNRLRVPI 283
Cdd:PTZ00009 240 EfcvQDFKRKNRGKDlSSNQRALRRLRTQCERAKrtlsSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 284 EQALRDARLKPSQIDSLVLVGGASQMPLVQRIAVRLF-GKLPYQSYDPSTIVALGAAIQAACRL--RSEDIEEVILTDIC 360
Cdd:PTZ00009 320 EKVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFnGKEPCKSINPDEAVAYGAAVQAAILTgeQSSQVQDLLLLDVT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 361 PYSLGVEVnrqgVSGIFSPIIERNTTVPVSRVETYSTMHPEQDSITVNVYQGENHKVKNNILVESFD---VPLKKTGAYQ 437
Cdd:PTZ00009 400 PLSLGLET----AGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHldgIPPAPRGVPQ 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 438 sIDIRFSYDINGLLEVDVlLEDGSVKSrviNHSPVT-----LSAQQI--------------EESRTRLSA---LKIYPRD 495
Cdd:PTZ00009 476 -IEVTFDIDANGILNVSA-EDKSTGKS---NKITITndkgrLSKADIdrmvneaekykaedEANRERVEAkngLENYCYS 550
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 446290036 496 M---LINRTFKAKLEElwaralgDEREEIGRVITDFDAALQSNDMARVDE 542
Cdd:PTZ00009 551 MkntLQDEKVKGKLSD-------SDKATIEKAIDEALEWLEKNQLAEKEE 593
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
8-481 |
1.59e-92 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 297.12 E-value: 1.59e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHILVGKPAVSRRTSHPDKTAALFKRAMG---------- 77
Cdd:PTZ00400 44 VGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDGQRLVGIVAKRQAVTNPENTVFATKRLIGrrydedatkk 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 78 -------------SNTNW-RLGSDTFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELAGLN 143
Cdd:PTZ00400 124 eqkilpykivrasNGDAWiEAQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAGKIAGLD 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 144 AVRLINEPTAAAMAYGLHTQQNTRSLVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHM----LVDEVLKRA- 218
Cdd:PTZ00400 204 VLRIINEPTAAALAFGMDKNDGKTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRilnyLIAEFKKQQg 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 219 -DVARTTLnesELGALYACVEAAK----CSNQSPLHIRWQYQDET----RECEFYENELEDLWLPLLNRLRVPIEQALRD 289
Cdd:PTZ00400 284 iDLKKDKL---ALQRLREAAETAKielsSKTQTEINLPFITADQSgpkhLQIKLSRAKLEELTHDLLKKTIEPCEKCIKD 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 290 ARLKPSQIDSLVLVGGASQMPLVQRIAVRLFGKLPYQSYDPSTIVALGAAIQAACrLRSEdIEEVILTDICPYSLGVEVn 369
Cdd:PTZ00400 361 AGVKKDELNDVILVGGMTRMPKVSETVKKIFGKEPSKGVNPDEAVAMGAAIQAGV-LKGE-IKDLLLLDVTPLSLGIET- 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 370 rqgVSGIFSPIIERNTTVPVSRVETYSTMHPEQDSITVNVYQGENHKVKNNILVESFD---VPLKKTGAYQsIDIRFSYD 446
Cdd:PTZ00400 438 ---LGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDlvgIPPAPRGVPQ-IEVTFDVD 513
|
490 500 510
....*....|....*....|....*....|....*
gi 446290036 447 INGLLEVDVLLEDGSVKSRVINHSPVTLSAQQIEE 481
Cdd:PTZ00400 514 ANGIMNISAVDKSTGKKQEITIQSSGGLSDEEIEK 548
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
8-541 |
2.34e-86 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 280.80 E-value: 2.34e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMdENNHILVGKPAVSRRTSHPDKTAALFKRAMGSN-TNWRLGS 86
Cdd:PTZ00186 30 IGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAF-KGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRfEDEHIQK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 87 DTFNAP------------------------ELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELAGL 142
Cdd:PTZ00186 109 DIKNVPykivragngdawvqdgngkqyspsQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTIAGL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 143 NAVRLINEPTAAAMAYGLHTQQNTRSLVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVDEVL---KRAD 219
Cdd:PTZ00186 189 NVIRVVNEPTAAALAYGMDKTKDSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYILeefRKTS 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 220 VARTTLNESELGALYACVEAAKCSNQSPLHIRWQY------QDETRECEFY--ENELEDLWLPLLNRLRVPIEQALRDAR 291
Cdd:PTZ00186 269 GIDLSKERMALQRVREAAEKAKCELSSAMETEVNLpfitanADGAQHIQMHisRSKFEGITQRLIERSIAPCKQCMKDAG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 292 LKPSQIDSLVLVGGASQMPLVQRIAVRLFGKLPYQSYDPSTIVALGAAIQAACrLRSeDIEEVILTDICPYSLGVEVnrq 371
Cdd:PTZ00186 349 VELKEINDVVLVGGMTRMPKVVEEVKKFFQKDPFRGVNPDEAVALGAATLGGV-LRG-DVKGLVLLDVTPLSLGIET--- 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 372 gVSGIFSPIIERNTTVPVSRVETYSTMHPEQDSITVNVYQGENHKVKNNILVESFD---VPLKKTGAYQsIDIRFSYDIN 448
Cdd:PTZ00186 424 -LGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDlvgIPPAPRGVPQ-IEVTFDIDAN 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 449 GLLEVDVLLEDGSVKSRVINHSPVTLSAQQIE----ESRTRLSALKIyPRDMLINR--------TFKAKLEElWARALGD 516
Cdd:PTZ00186 502 GICHVTAKDKATGKTQNITITANGGLSKEQIEqmirDSEQHAEADRV-KRELVEVRnnaetqltTAERQLGE-WKYVSDA 579
|
570 580
....*....|....*....|....*
gi 446290036 517 EREEIGRVITDFDAALQSNDMARVD 541
Cdd:PTZ00186 580 EKENVKTLVAELRKAMENPNVAKDD 604
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
8-343 |
4.89e-82 |
|
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: 261.89 E-value: 4.89e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWK--DGAAQLIPNKFGEYLTPSIISMDENNHILVGKPAVSRRTSHPDKTAALFKRAMGSN------ 79
Cdd:cd10237 25 VGIDLGTTYSCVGVYHavTGEVEVIPDDDGHKSIPSVVAFTPDGGVLVGYDALAQAEHNPSNTIYDAKRFIGKTftkeel 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 80 -----------TNWRLGSDTFN----------APE-LSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAA 137
Cdd:cd10237 105 eeeakrypfkvVNDNIGSAFFEvplngstlvvSPEdIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRKAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 138 ELAGLNAVRLINEPTAAAMAYGLHTQQNTRS-LVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVDEVLK 216
Cdd:cd10237 185 NLAGLEVLRVINEPTAAAMAYGLHKKSDVNNvLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQYLID 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 217 R--ADVARTTLNESELGALYACVEAAKCS----NQSPLHIRWQYQDETRECEFYENEL-----EDLWLPLLNRLRVPIEQ 285
Cdd:cd10237 265 RiaKKFGKTLTDKEDIQRLRQAVEEVKLNltnhNSASLSLPLQISLPSAFKVKFKEEItrdlfETLNEDLFQRVLEPIRQ 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 446290036 286 ALRDARLKPSQIDSLVLVGGASQMPLVQRIAVRLFGKLPYQSYDPSTIVALGAAIQAA 343
Cdd:cd10237 345 VLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFFGKDPNTSVDPELAVVTGVAIQAG 402
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
8-342 |
5.43e-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: 255.65 E-value: 5.43e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHILVGKPAVSRRTSHPDKTAALFKRAMG---------- 77
Cdd:cd11733 4 IGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPENTLYATKRLIGrrfddpevqk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 78 ------------SNTN-W-RLGSDTFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELAGLN 143
Cdd:cd11733 84 dikmvpykivkaSNGDaWvEAHGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDAGQIAGLN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 144 AVRLINEPTAAAMAYGLHTQQNTRSLVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDF----THMLVDEvLKRA- 218
Cdd:cd11733 164 VLRIINEPTAAALAYGLDKKDDKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFdnalLNYLVAE-FKKEq 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 219 --DVARTTLnesELGALYACVEAAKC----SNQS-------------PLHIRWQYqdeTRecefyeNELEDLWLPLLNRL 279
Cdd:cd11733 243 giDLSKDNL---ALQRLREAAEKAKIelssSLQTdinlpfitadasgPKHLNMKL---TR------AKFESLVGDLIKRT 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446290036 280 RVPIEQALRDARLKPSQIDSLVLVGGASQMPLVQRIAVRLFGKLPYQSYDPSTIVALGAAIQA 342
Cdd:cd11733 311 VEPCKKCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIFGKAPSKGVNPDEAVAMGAAIQG 373
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
8-343 |
1.55e-79 |
|
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: 254.44 E-value: 1.55e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHiLVGKPAVSRRTSHPDKTAALFKRAMGSNTN------ 81
Cdd:cd10241 4 IGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGER-LIGDAAKNQATSNPENTVFDVKRLIGRKFDdkevqk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 82 ---------------------WRLGSDTFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELA 140
Cdd:cd10241 83 dikllpfkivnkngkpyiqveVKGEKKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 141 GLNAVRLINEPTAAAMAYGLHTQQNTRS-LVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVDEVLKR-- 217
Cdd:cd10241 163 GLNVLRIINEPTAAAIAYGLDKKGGEKNiLVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFIKLfk 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 218 ----ADVARttlNESELGALYACVEAAKCSNQSplhirwqyQDETR-ECE-FYENE----------LEDLWLPLLNRLRV 281
Cdd:cd10241 243 kktgKDISK---DKRAVQKLRREVEKAKRALSS--------QHQARiEIEsLFDGEdfsetltrakFEELNMDLFRKTLK 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446290036 282 PIEQALRDARLKPSQIDSLVLVGGASQMPLVQRIAVRLF-GKLPYQSYDPSTIVALGAAIQAA 343
Cdd:cd10241 312 PVQKVLEDAGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFnGKEPSRGINPDEAVAYGAAVQAG 374
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
7-343 |
1.54e-76 |
|
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: 246.77 E-value: 1.54e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 7 AIGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSII-----------------SMDENNHILVGKPAVSRRTSHP---- 65
Cdd:cd10233 1 AIGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVaftdterligdaaknqvAMNPTNTVFDAKRLIGRKFDDPvvqs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 66 DKTAALFKRAMGSNT-----NWRLGSDTFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELA 140
Cdd:cd10233 81 DMKHWPFKVVSGGDKpkiqvEYKGETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 141 GLNAVRLINEPTAAAMAYGL----HTQQNTrsLVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVD---E 213
Cdd:cd10233 161 GLNVLRIINEPTAAAIAYGLdkkgKGERNV--LIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNhfvQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 214 VLKRADVARTTLNESELGALYACVEAAK----CSNQSPLHIrwqyqDETRE-CEFYEN----ELEDLWLPLLNRLRVPIE 284
Cdd:cd10233 239 EFKRKHKKDISGNPRALRRLRTACERAKrtlsSSTQASIEI-----DSLFEgIDFYTSitraRFEELCADLFRSTLEPVE 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 285 QALRDARLKPSQIDSLVLVGGASQMPLVQRIAVRLF-GKLPYQSYDPSTIVALGAAIQAA 343
Cdd:cd10233 314 KVLRDAKLDKSQIHEIVLVGGSTRIPKVQKLLQDFFnGKELNKSINPDEAVAYGAAVQAA 373
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
7-343 |
4.23e-76 |
|
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: 245.43 E-value: 4.23e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 7 AIGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHILVGKPAVSRRTSHPDKTAALFKRAMG--------- 77
Cdd:cd11734 3 VIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTKDGERLVGVPAKRQAVVNPENTLFATKRLIGrkfddaevq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 78 -----------SNTN---W-RLGSDTFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELAGL 142
Cdd:cd11734 83 rdikevpykivKHSNgdaWvEARGQKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAGQIAGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 143 NAVRLINEPTAAAMAYGLHTQQNTRSLVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVDEVL---KRAD 219
Cdd:cd11734 163 NVLRVINEPTAAALAYGLDKSGDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHIVsefKKES 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 220 VARTTLNESELGALYACVEAAKC----SNQSPLHIRWQYQDETR----ECEFYENELEDLWLPLLNRLRVPIEQALRDAR 291
Cdd:cd11734 243 GIDLSKDRMAIQRIREAAEKAKIelssTLQTDINLPFITADASGpkhiNMKLTRAQFESLVKPLVDRTVEPCKKALKDAG 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 446290036 292 LKPSQIDSLVLVGGASQMPLVQRIAVRLFGKLPYQSYDPSTIVALGAAIQAA 343
Cdd:cd11734 323 VKTSEINEVILVGGMSRMPKVQETVKSIFGREPSKGVNPDEAVAIGAAIQGG 374
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
7-343 |
1.45e-70 |
|
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: 231.03 E-value: 1.45e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 7 AIGIDLGTTNSLIAVWkDGAAQLIPNKFGEYLTPSIISMDENNHiLVGKPAVSRRTSHPDKTAALFKRAMGSN------- 79
Cdd:cd24093 1 AIGIDLGTTYSCVATY-ESSVEIIANEQGNRVTPSFVAFTPEER-LIGDAAKNQAALNPRNTVFDAKRLIGRRfddesvq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 80 ---TNW----------------RLG-SDTFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAEL 139
Cdd:cd24093 79 kdmKTWpfkvidvngnpvievqYLGeTKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 140 AGLNAVRLINEPTAAAMAYGLHTQQNTRS---LVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVDEV-- 214
Cdd:cd24093 159 AGLNVLRIINEPTAAAIAYGLGAGKSEKErhvLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFka 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 215 -LKRADVARTTLNESELGALYACVEAAKCS----NQSPLHIRWQYQDETRECEFYENELEDLWLPLLNRLRVPIEQALRD 289
Cdd:cd24093 239 eFKKKTGLDISDDARALRRLRTAAERAKRTlssvTQTTVEVDSLFDGEDFESSITRARFEDLNAALFKSTLEPVEQVLKD 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 446290036 290 ARLKPSQIDSLVLVGGASQMPLVQRIAVRLF-GKLPYQSYDPSTIVALGAAIQAA 343
Cdd:cd24093 319 AKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGA 373
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
5-453 |
1.59e-69 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 234.75 E-value: 1.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 5 ELAIGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHILVGKPAVS-------RRTSHPDKTAALF---KR 74
Cdd:PRK01433 19 QIAVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIGNNKGLRsikrlfgKTLKEILNTPALFslvKD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 75 AMGSNTN---WRLGSDTFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELAGLNAVRLINEP 151
Cdd:PRK01433 99 YLDVNSSelkLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLAAKIAGFEVLRLIAEP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 152 TAAAMAYGLHTQQNTRSLVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDfthmlVDEVLKRADVARTTLNESELg 231
Cdd:PRK01433 179 TAAAYAYGLNKNQKGCYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGND-----IDVVITQYLCNKFDLPNSID- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 232 ALYACVEAA------KCSNQSPLHIRWQyqdetrecefyenELEDLWLPLLNRLRVPIEQALRDArlKPSQIDSLVLVGG 305
Cdd:PRK01433 253 TLQLAKKAKetltykDSFNNDNISINKQ-------------TLEQLILPLVERTINIAQECLEQA--GNPNIDGVILVGG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 306 ASQMPLVQRIAVRLFGKLPYQSYDPSTIVALGAAIQAAcRLRSEDIEEvILTDICPYSLGVEVnrqgVSGIFSPIIERNT 385
Cdd:PRK01433 318 ATRIPLIKDELYKAFKVDILSDIDPDKAVVWGAALQAE-NLIAPHTNS-LLIDVVPLSLGMEL----YGGIVEKIIMRNT 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446290036 386 TVPVSRVETYSTMHPEQDSITVNVYQGENHKVKNNILVESFD---VPLKKTGaYQSIDIRFSYDINGLLEV 453
Cdd:PRK01433 392 PIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFElkgLPPMKAG-SIRAEVTFAIDADGILSV 461
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
8-343 |
5.10e-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: 203.17 E-value: 5.10e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHiLVGKPAVSRRTSHPDKTAALFKRAMGSNTN------ 81
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEKER-LIGEAAKSQQKSNYKNTIRNFKRLIGLKFDdpevqk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 82 --WRLGSD--------------------TFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAEL 139
Cdd:cd11732 80 eiKLLPFKlveledgkvgievsyngeevVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 140 AGLNAVRLINEPTAAAMAYG------LHTQQNTRSLVF-DLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVD 212
Cdd:cd11732 160 AGLNCLRLINETTAAALDYGiyksdlLESEEKPRIVAFvDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 213 EVLK------RADV-----ARTTLneselgaLYACVEAAK--CSNQS-PLHIRWQYQDE------TREcefyenELEDLW 272
Cdd:cd11732 240 HFAEefkkkyKIDPlenpkARLRL-------LDACEKLKKvlSANGEaPLNVECLMEDIdfsgqiKRE------EFEELI 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446290036 273 LPLLNRLRVPIEQALRDARLKPSQIDSLVLVGGASQMPLVQRIAVRLFGKLPYQSYDPSTIVALGAAIQAA 343
Cdd:cd11732 307 QPLLARLEAPIKKALAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVFGKDLSTTLNADEAVARGCALQAA 377
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
7-343 |
1.11e-55 |
|
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: 191.69 E-value: 1.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 7 AIGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENnHILVGKPAVSRRTSHPDKTAALFKRAMGSNT------ 80
Cdd:cd10238 2 AFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDN-EKIVGLAAKQGLIRNASNTVVRVKQLLGRSFddpavq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 81 ---------------------NWRLGSDTFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAEL 139
Cdd:cd10238 81 elkkeskckiiekdgkpgyeiELEEKKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 140 AGLNAVRLINEPTAAAMAYGLhtQQNTRS-----LVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVdEV 214
Cdd:cd10238 161 AGFNVLRVISEPSAAALAYGI--GQDDPTensnvLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALA-EH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 215 LK-------RADVartTLNESELGALYACVEAAK----------CSNQSpLHIRWQYQdetreCEFYENELEDLWLPLLN 277
Cdd:cd10238 238 LAsefkrqwKQDV---RENKRAMAKLMNAAEVCKhvlstlntatCSVES-LYDGMDFQ-----CNVSRARFESLCSSLFQ 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446290036 278 RLRVPIEQALRDARLKPSQIDSLVLVGGASQMPLVQRIAVRLF-GKLPYQSYDPSTIVALGAAIQAA 343
Cdd:cd10238 309 QCLEPIQEVLNSAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFpSAEVLSSIPPDEVIAIGAAKQAG 375
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
8-343 |
1.75e-54 |
|
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: 188.64 E-value: 1.75e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHILvGKPAVSRRTSHPDKTAALFKRAMGSNTN------ 81
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSM-GVAAKNQAITNLKNTVSGFKRLLGRKFDdpfvqk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 82 ---------------------WRLGSD-TFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAEL 139
Cdd:cd10228 80 elkhlpykvvklpngsvgikvQYLGEEhVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 140 AGLNAVRLINEPTAAAMAYGLHTQ------QNTRSLVF-DLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVD 212
Cdd:cd10228 160 AGLNCLRLLNDTTAVALAYGIYKQdlpaeeEKPRNVVFvDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 213 EVLK------RADVA---RTTLNeselgaLYACVEAAK---CSNQS--PLHIrwqyqdetrECeFYEN----------EL 268
Cdd:cd10228 240 HFAEefktkyKIDVKskpRALLR------LLTECEKLKklmSANATelPLNI---------EC-FMDDkdvsgkmkraEF 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 269 EDLWLPLLNRLRVPIEQALRDARLKPSQIDSLVLVGGASQMPLVQRIAVRLFGKlpyqsyDPSTI------VALGAAIQA 342
Cdd:cd10228 304 EELCAPLFARVEVPLRSALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVFGK------EPSTTlnqdeaVARGCALQC 377
|
.
gi 446290036 343 A 343
Cdd:cd10228 378 A 378
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
7-343 |
3.10e-52 |
|
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: 182.90 E-value: 3.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 7 AIGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHILvGKPAVSRRTSHPDKTAALFKRAMGSN------- 79
Cdd:cd24095 3 VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQRFL-GEAAAASILMNPKNTISQLKRLIGRKfddpevq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 80 TNWRL-------GSD--------------TFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAE 138
Cdd:cd24095 82 RDLKLfpfkvteGPDgeiginvnylgeqkVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 139 LAGLNAVRLINEPTAAAMAYG-----LHTQQNTRSLVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFthmlvDE 213
Cdd:cd24095 162 IAGLNCLRLMNETTATALAYGiyktdLPETDPTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDF-----DE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 214 VL-----------KRADVartTLNESELGALYACVEAAK----CSNQSPLHIRWQYQDETRECEFYENELEDLWLPLLNR 278
Cdd:cd24095 237 VLfdhfaaefkekYKIDV---KSNKKASLRLRAACEKVKkilsANPEAPLNIECLMEDKDVKGMITREEFEELAAPLLER 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446290036 279 LRVPIEQALRDARLKPSQIDSLVLVGGASQMPLVQRIAVRLFGKLPYQSYDPSTIVALGAAIQAA 343
Cdd:cd24095 314 LLEPLEKALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFFGKEPSRTMNASECVARGCALQCA 378
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
8-343 |
7.70e-48 |
|
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: 171.02 E-value: 7.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHILvGKPAVSRRTSHPDKTAALFKRAMG---------- 77
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYL-GEAAKTQETSNFKNTVGSLKRLIGrtfsdpevae 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 78 --SNTNWRL--------------GSDT-FNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELA 140
Cdd:cd24094 80 eeKYFTAKLvdangevgaevnylGEKHvFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 141 GLNAVRLINEPTAAAMAYGL------HTQQNTRSLVF-DLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVDE 213
Cdd:cd24094 160 GLNPLRLMNDTTAAALGYGItktdlpEPEEKPRIVAFvDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 214 VLK------RADVARttlNESELGALYACVEAAK----CSNQSPLHIRWQYQDETRECEFYENELEDLWLPLLNRLRVPI 283
Cdd:cd24094 240 FADefkekyKIDVRS---NPKAYFRLLAAAEKLKkvlsANAQAPLNVESLMNDIDVSSMLKREEFEELIAPLLERVTAPL 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 284 EQALRDARLKPSQIDSLVLVGGASQMPLVQRIAVRLFGKLPYQSYDPSTIVALGAAIQAA 343
Cdd:cd24094 317 EKALAQAGLTKDEIDFVELVGGTTRVPALKESISAFFGKPLSTTLNQDEAVARGAAFACA 376
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
7-343 |
8.03e-48 |
|
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: 169.85 E-value: 8.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 7 AIGIDLGTTNSLIA-VWKDGAAQLIPNKFGEYLTPSIISM--DENNHilvGKPAVSRRTSHPDKTAALFKRAmgsntnwr 83
Cdd:cd10232 2 VIGISFGNSNSSIAiINKDGRAEVIANEDGDRQIPSILAYhgDEEYH---GSQAKAQLVRNPKNTVANFRDL-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 84 LGSDTFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELAGLNAVRLINEPTAAAMAYGL--- 160
Cdd:cd10232 71 LGTTTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAAAAGLEVLQLIPEPAAAALAYDLrae 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 161 ---HTQQNTRSLVFDLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVD----EVLKRADVARTTlNESELGAL 233
Cdd:cd10232 151 tsgDTIKDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVGhfakEFKKKTKTDPRK-NARSLAKL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 234 YACVEAAK----CSNQSPLHIRWQYQ--------DETRecefyeneLEDLWLPLLNRLRVPIEQALRDARLKPSQIDSLV 301
Cdd:cd10232 230 RNAAEITKralsQGTSAPCSVESLADgidfhssiNRTR--------YELLASKVFQQFADLVTDAIEKAGLDPLDIDEVL 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446290036 302 LVGGASQMPLVQRIAVRLFG----KLPYQSYDPSTIVALGAAIQAA 343
Cdd:cd10232 302 LAGGASRTPKLASNFEYLFPestiIRAPTQINPDELIARGAALQAS 347
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
8-343 |
6.32e-46 |
|
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: 164.98 E-value: 6.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWKDGAA-QLIPNKFGEYLTPSIISMDeNNHILVGKPAVSRRTSHPDKTAALFKRAMGsntnwrlgs 86
Cdd:cd10230 3 LGIDLGSEFIKVALVKPGVPfEIVLNEESKRKTPSAVAFR-NGERLFGDDALALATRFPENTFSYLKDLLG--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 87 dtFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELAGLNAVRLINEPTAAAMAYGLHTQQN- 165
Cdd:cd10230 73 --YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIAGLNVLSLINDNTAAALNYGIDRRFEn 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 166 ---TRSLVFDLGGGTFDVTVLEYAT------------PVIEVHASAGDNFLGGEDFTH----MLVDEVLKRADVARTTLN 226
Cdd:cd10230 151 nepQNVLFYDMGASSTSATVVEFSSvkekdkgknktvPQVEVLGVGWDRTLGGLEFDLrladHLADEFNEKHKKDKDVRT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 227 ESE-LGALYACVEAAK----CSNQSPLHIRWQYQDE------TREcefyenELEDLWLPLLNRLRVPIEQALRDARLKPS 295
Cdd:cd10230 231 NPRaMAKLLKEANRVKevlsANTEAPASIESLYDDIdfrtkiTRE------EFEELCADLFERVVAPIEEALEKAGLTLD 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 446290036 296 QIDSLVLVGGASQMPLVQRIAVRLFGKLPYQSY---DPStiVALGAAIQAA 343
Cdd:cd10230 305 DIDSVELIGGGTRVPKVQEALKEALGRKELGKHlnaDEA--AALGAAFYAA 353
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
8-343 |
8.03e-45 |
|
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: 162.78 E-value: 8.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHIlVGKPAVSRRTSHPDKTAALFKRAMGSNTN------ 81
Cdd:cd11738 3 VGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRA-IGNAAKSQIVTNAKNTIHGFKKFHGRAFDdpfvqa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 82 ---------------------WRLGSD-TFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAEL 139
Cdd:cd11738 82 ekiklpyelqkmpngstgvkvRYLDEErVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 140 AGLNAVRLINEPTAAAMAYGLHTQ------QNTRSLVF-DLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVD 212
Cdd:cd11738 162 AGLNCLRLMNETTAVALAYGIYKQdlpaleEKPRNVVFvDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVLVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 213 ---EVLKRADVARTTLNESELGALYACVEAAK---CSNQS--PLHIRWQYQDETRECEFYENELEDLWLPLLNRLRVPIE 284
Cdd:cd11738 242 yfcEEFKTKYKLNVKENIRALLRLYQECEKLKklmSANASdlPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEPPLK 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 446290036 285 QALRDARLKPSQIDSLVLVGGASQMPLVQRIAVRLFGKLPYQSYDPSTIVALGAAIQAA 343
Cdd:cd11738 322 AVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCA 380
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
8-343 |
5.22e-44 |
|
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: 160.49 E-value: 5.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHIlVGKPAVSRRTSHPDKTAALFKRAMG---------- 77
Cdd:cd11737 3 VGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRS-IGAAAKSQVISNAKNTVQGFKRFHGrafsdpfvqa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 78 --SNTNWRL-----GSD-----------TFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAEL 139
Cdd:cd11737 82 ekPSLAYELvqlptGTTgikvmymeeerNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 140 AGLNAVRLINEPTAAAMAYGLHTQ------QNTRSLVF-DLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVD 212
Cdd:cd11737 162 AGLNCLRLMNETTAVALAYGIYKQdlpapeEKPRNVVFvDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVLVN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 213 EVLKRADVARTTLNESELGALY----ACVEAAKC----SNQSPLHIRWQYQDETRECEFYENELEDLWLPLLNRLRVPIE 284
Cdd:cd11737 242 HFCEEFGKKYKLDIKSKIRALLrlfqECEKLKKLmsanASDLPLNIECFMNDIDVSGTMNRGQFEEMCADLLARVEPPLR 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 446290036 285 QALRDARLKPSQIDSLVLVGGASQMPLVQRIAVRLFGKLPYQSYDPSTIVALGAAIQAA 343
Cdd:cd11737 322 SVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFFGKEVSTTLNADEAVARGCALQCA 380
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
8-343 |
6.40e-43 |
|
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: 157.33 E-value: 6.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSIISMDENNHIlVGKPAVSRRTSHPDKTAALFKR------------- 74
Cdd:cd11739 3 VGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRT-IGVAAKNQQITNANNTVSNFKRfhgrafndpfvqk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 75 ---------------AMGSNTNWRLGSDTFNAPELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAEL 139
Cdd:cd11739 82 ekenlsydlvplkngGVGVKVMYLDEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 140 AGLNAVRLINEPTAAAMAYGLHTQ------QNTRSLVF-DLGGGTFDVTVLEYATPVIEVHASAGDNFLGGEDFTHMLVD 212
Cdd:cd11739 162 VGLNCLRLMNDMTAVALNYGIYKQdlpapdEKPRIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKLVE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 213 EVLKRADVARTTLNESELGA---LYACVEAAK---CSNQS--PLHIRWQYQDETRECEFYENELEDLWLPLLNRLRVPIE 284
Cdd:cd11739 242 HFCAEFKTKYKLDVKSKIRAllrLYQECEKLKklmSSNSTdlPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEVPLY 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 446290036 285 QALRDARLKPSQIDSLVLVGGASQMPLVQRIAVRLFGKLPYQSYDPSTIVALGAAIQAA 343
Cdd:cd11739 322 SLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFFGKDVSTTLNADEAVARGCALQCA 380
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
8-340 |
7.16e-43 |
|
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: 156.11 E-value: 7.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWKDGAAQLIPNKF---------GEYLTPSIIsmdennhilvgkpavsrrtshpdktaalfkramgs 78
Cdd:cd10170 1 VGIDFGTTYSGVAYALLGPGEPPLVVLqlpwpggdgGSSKVPSVL----------------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 79 ntnwrlgsdtfnapELSSLVLRSLKEDAEEFLQR-------PIKDVVISVPAYFSDEQRKHTRLAAELAGLNA----VRL 147
Cdd:cd10170 46 --------------EVVADFLRALLEHAKAELGDriwelekAPIEVVITVPAGWSDAAREALREAARAAGFGSdsdnVRL 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 148 INEPTAAAMAYGLHTQQNTRS------LVFDLGGGTFDVTVLE----YATPVIEVhASAGDNFLGGEDFTHMLVDEVLKR 217
Cdd:cd10170 112 VSEPEAAALYALEDKGDLLPLkpgdvvLVCDAGGGTVDLSLYEvtsgSPLLLEEV-APGGGALLGGTDIDEAFEKLLREK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 218 ADVARTTLNESELGALYACVEAA-----KCSNQSPLHIRWQYQDETRECEFYENEL-----EDLWLPLLNRLRVPIEQAL 287
Cdd:cd10170 191 LGDKGKDLGRSDADALAKLLREFeeakkRFSGGEEDERLVPSLLGGGLPELGLEKGtllltEEEIRDLFDPVIDKILELI 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 446290036 288 RDA--RLKPSQIDSLVLVGGASQMPLVQRIAVRLFG----KLPYQSYDPSTIVALGAAI 340
Cdd:cd10170 271 EEQleAKSGTPPDAVVLVGGFSRSPYLRERLRERFGsagiIIVLRSDDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
8-339 |
6.10e-36 |
|
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: 138.95 E-value: 6.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSII-----SMDENNHILVGKPAVSRRTSHPDK-----------TAAL 71
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLyfprrEEEGAESIYFGNDAIDAYLNDPEEgrliksvksflGSSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 72 FKRAMGSNTNWRLGsdtfnapELSSLVLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQR-KHT------RLAAELAGLNA 144
Cdd:cd10231 81 FDETTIFGRRYPFE-------DLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAeDDAqaesrlRDAARRAGFRN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 145 VRLINEPTAAAMAYGLHTQQNTRSLVFDLGGGTFDVTVLE------YATPVIevHASAGDnFLGGEDFTHMLVDEVL--- 215
Cdd:cd10231 154 VEFQYEPIAAALDYEQRLDREELVLVVDFGGGTSDFSVLRlgpnrtDRRADI--LATSGV-GIGGDDFDRELALKKVmph 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 216 -------------------KRADVAR--------------------------------TTLNESELG-ALYACVEAAKcs 243
Cdd:cd10231 231 lgrgstyvsgdkglpvpawLYADLSNwhaisllytkktlrllldlrrdaadpekierlLSLVEDQLGhRLFRAVEQAK-- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 244 nqsplhIRWQYQDETR-ECEFYEN---------ELEDLWLPLLNRLRVPIEQALRDARLKPSQIDSLVLVGGASQMPLVQ 313
Cdd:cd10231 309 ------IALSSADEATlSFDFIEIsikvtitrdEFETAIAFPLARILEALERTLNDAGVKPSDVDRVFLTGGSSQSPAVR 382
|
410 420
....*....|....*....|....*.
gi 446290036 314 RIAVRLFGKLPYQSYDPSTIVALGAA 339
Cdd:cd10231 383 QALASLFGQARLVEGDEFGSVAAGLA 408
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
96-318 |
5.18e-16 |
|
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: 79.63 E-value: 5.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 96 SLVLRSLKEDAEEFLQR------PIKDV--VISVPAYFSDEQRKHTRLAAELAGLNA------VRLINEPTAAAMAYGLH 161
Cdd:cd10229 114 AEALRYLKDHALKELRDrsgsslDEDDIrwVLTVPAIWSDAAKQFMREAAVKAGLISeenseqLIIALEPEAAALYCQKL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 162 TQQN--------TRSLVFDLGGGTFDVTVLEY--ATPVIEVHASAGDNFlGG----EDFTHMLVDEVLKRADVARTTLNE 227
Cdd:cd10229 194 LAEGeekelkpgDKYLVVDCGGGTVDITVHEVleDGKLEELLKASGGPW-GStsvdEEFEELLEEIFGDDFMEAFKQKYP 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 228 SELGALYACVEAAKCSnqspLHIRWQyqdetrecefyENELEDLWLPLLNRLRVPIEQALRDARLKPsqIDSLVLVGGAS 307
Cdd:cd10229 273 SDYLDLLQAFERKKRS----FKLRLS-----------PELMKSLFDPVVKKIIEHIKELLEKPELKG--VDYIFLVGGFA 335
|
250
....*....|.
gi 446290036 308 QMPLVQRiAVR 318
Cdd:cd10229 336 ESPYLQK-AVK 345
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
8-340 |
9.06e-13 |
|
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: 69.42 E-value: 9.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWKDGaaqLIPNKfgeyltPSIISMDENNH--ILVGKPAVSR--RTshPDKTAALfkRAMgsntnwR 83
Cdd:cd10225 2 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAVDKNTGkvLAVGEEAKKMlgRT--PGNIVAI--RPL------R 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 84 LG--SDtFNAPE--LSSLVLRSLKEdaeEFLQRPikDVVISVPAYFSDEQRKHTRLAAELAGLNAVRLINEPTAAAMAYG 159
Cdd:cd10225 63 DGviAD-FEATEamLRYFIRKAHRR---RGFLRP--RVVIGVPSGITEVERRAVKEAAEHAGAREVYLIEEPMAAAIGAG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 160 LHTQQNTRSLVFDLGGGTFDVTVLeyatpvievhaSAGD----NFL--GGEDFTHMLVDEVLKRADVA---RTTlnES-- 228
Cdd:cd10225 137 LPIEEPRGSMVVDIGGGTTEIAVI-----------SLGGivtsRSVrvAGDEMDEAIINYVRRKYNLLigeRTA--ERik 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 229 -ELGALYACVEAAKCSnqspLHIRWQYQDETRECEFYENELEDLWLPLLNRlrvpIEQALRDA--RLKP---SQI--DSL 300
Cdd:cd10225 204 iEIGSAYPLDEELSME----VRGRDLVTGLPRTIEITSEEVREALEEPVNA----IVEAVRSTleRTPPelaADIvdRGI 275
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446290036 301 VLVGGASQMP-LVQRIAVRLfgKLP-YQSYDPSTIVALGAAI 340
Cdd:cd10225 276 VLTGGGALLRgLDELLREET--GLPvHVADDPLTCVAKGAGK 315
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
8-183 |
5.30e-11 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 64.00 E-value: 5.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWKDGaaqLIPNKfgeyltPSIISMD-ENNHIL-VGKPAvsrrtshpdktaalfkRAMgsntnwrLG 85
Cdd:PRK13930 11 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAIDtKTGKVLaVGEEA----------------KEM-------LG 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 86 sdtfNAPElSSLVLRSLK-------EDAEEFLQRPIK-----------DVVISVPAYFSDEQRKHTRLAAELAGLNAVRL 147
Cdd:PRK13930 59 ----RTPG-NIEAIRPLKdgviadfEATEAMLRYFIKkargrrffrkpRIVICVPSGITEVERRAVREAAEHAGAREVYL 133
|
170 180 190
....*....|....*....|....*....|....*.
gi 446290036 148 INEPTAAAMAYGLHTQQNTRSLVFDLGGGTFDVTVL 183
Cdd:PRK13930 134 IEEPMAAAIGAGLPVTEPVGNMVVDIGGGTTEVAVI 169
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
8-200 |
1.34e-10 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 63.00 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWKDGaaqLIPNKfgeyltPSIISMDEN-NHIL-VGKPAVSR--RTshPDKTAALfkRAMgsntnwR 83
Cdd:PRK13928 6 IGIDLGTANVLVYVKGKG---IVLNE------PSVVAIDKNtNKVLaVGEEARRMvgRT--PGNIVAI--RPL------R 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 84 LG--SDTfnapELSSLVLRSL--KEDAEEFLQRPIkdVVISVPAYFSDEQRKHTRLAAELAGLNAVRLINEPTAAAMAYG 159
Cdd:PRK13928 67 DGviADY----DVTEKMLKYFinKACGKRFFSKPR--IMICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAG 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446290036 160 LHTQQNTRSLVFDLGGGTFDVTVLEYATPVieVHAS---AGDNF 200
Cdd:PRK13928 141 LDISQPSGNMVVDIGGGTTDIAVLSLGGIV--TSSSikvAGDKF 182
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
8-183 |
2.30e-09 |
|
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 440695 [Multi-domain] Cd Length: 339 Bit Score: 58.94 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVwkdgaaqliPNKFGEYLTPSIISMDENNH--ILVGKPAvsrrtshpdktaalfkRAMgsntnwrLG 85
Cdd:COG1077 10 IGIDLGTANTLVYV---------KGKGIVLNEPSVVAIDKKTGkvLAVGEEA----------------KEM-------LG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 86 sdtfNAPElSSLVLRSLK-------EDAEEFLQRPIK-----------DVVISVPAYFSDEQRKHTRLAAELAGLNAVRL 147
Cdd:COG1077 58 ----RTPG-NIVAIRPLKdgviadfEVTEAMLKYFIKkvhgrrsffrpRVVICVPSGITEVERRAVRDAAEQAGAREVYL 132
|
170 180 190
....*....|....*....|....*....|....*.
gi 446290036 148 INEPTAAAMAYGLHTQQNTRSLVFDLGGGTFDVTVL 183
Cdd:COG1077 133 IEEPMAAAIGAGLPIEEPTGNMVVDIGGGTTEVAVI 168
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
98-339 |
7.91e-09 |
|
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: 56.92 E-value: 7.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 98 VLRSLKEDAEEFLQRPIKDVVISVP-AYFSDEQrkhtrlAAELAGLNAVRLINEPTAAamAYGLHTQQNTRS--LVFDLG 174
Cdd:cd24004 51 SIKELLKELEEKLGSKLKDVVIAIAkVVESLLN------VLEKAGLEPVGLTLEPFAA--ANLLIPYDMRDLniALVDIG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 175 GGTFDVTVLEYATPVievhaSAGDNFLGGEDFThmlvdEVLkrADVARTTLNESelgalyacvEAAKCSnqsplHIRWQY 254
Cdd:cd24004 123 AGTTDIALIRNGGIE-----AYRMVPLGGDDFT-----KAI--AEGFLISFEEA---------EKIKRT-----YGIFLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 255 QDETRECEFYEN--ELEDLWLPLLNRLRVPIEQALRDARLKPSQIDSLVLVGGASQMPL------------VQRIAVRLF 320
Cdd:cd24004 177 IEAKDQLGFTINkkEVYDIIKPVLEELASGIANAIEEYNGKFKLPDAVYLVGGGSKLPGlnealaeklglpVERIAPRNI 256
|
250 260
....*....|....*....|....*
gi 446290036 321 GKLPY------QSYDPSTIVALGAA 339
Cdd:cd24004 257 GAISDitdetsKAKGPEFVTPLGIA 281
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
8-184 |
2.65e-08 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 56.41 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWKDGAAQLIPNKFGEYLTPSII-SMDENnhiLVGKpAVSRRtsHPDKT-----AALFKRAMGSNTN 81
Cdd:PRK11678 3 IGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTLcAPTRE---AVSE-WLYRH--LDVPAydderQALLRRAIRYNRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 82 WRLGSDT-------------FNAPE-----------LSSLVLR----SLKED------------AEEFLQRPIKDVVISV 121
Cdd:PRK11678 77 EDIDVTAqsvffglaalaqyLEDPEevyfvkspksfLGASGLKpqqvALFEDlvcammlhikqqAEAQLQAAITQAVIGR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446290036 122 PAYF----SDEQRKHT----RLAAELAGLNAVRLINEPTAAAMAYGLHTQQNTRSLVFDLGGGTFDVTVLE 184
Cdd:PRK11678 157 PVNFqglgGEEANRQAegilERAAKRAGFKDVEFQFEPVAAGLDFEATLTEEKRVLVVDIGGGTTDCSMLL 227
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
8-183 |
9.03e-08 |
|
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: 54.10 E-value: 9.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWKDGaaqLIPNKfgeyltPSIISMDENNH--ILVGKPA--VSRRTshPDKTAALfkRAMgsntnwR 83
Cdd:pfam06723 4 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAINTKTKkvLAVGNEAkkMLGRT--PGNIVAV--RPL------K 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 84 LG--SDTFNAPELSSLVLRSLKEDaeEFLQRPIkdVVISVPAYFSDEQRKHTRLAAELAGLNAVRLINEPTAAAMAYGLH 161
Cdd:pfam06723 65 DGviADFEVTEAMLKYFIKKVHGR--RSFSKPR--VVICVPSGITEVERRAVKEAAKNAGAREVFLIEEPMAAAIGAGLP 140
|
170 180
....*....|....*....|..
gi 446290036 162 TQQNTRSLVFDLGGGTFDVTVL 183
Cdd:pfam06723 141 VEEPTGNMVVDIGGGTTEVAVI 162
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
8-220 |
1.20e-07 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 53.76 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVWKDGaaqLIPNKfgeyltPSIISMD-ENNHIL-VGKPAVSRRTSHPDKTAALFKRAMGSNTNWRLG 85
Cdd:PRK13929 7 IGIDLGTANILVYSKNKG---IILNE------PSVVAVDtETKAVLaIGTEAKNMIGKTPGKIVAVRPMKDGVIADYDMT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 86 SDTFNApelsslVLRSLKEDAEEFLQRPikDVVISVPAYFSDEQRKHTRLAAELAGLNAVRLINEPTAAAMAYGLHTQQN 165
Cdd:PRK13929 78 TDLLKQ------IMKKAGKNIGMTFRKP--NVVVCTPSGSTAVERRAISDAVKNCGAKNVHLIEEPVAAAIGADLPVDEP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446290036 166 TRSLVFDLGGGTFDVTVLEYATpVIEVHASAgdnfLGGEDFTHMLVDEVLKRADV 220
Cdd:PRK13929 150 VANVVVDIGGGTTEVAIISFGG-VVSCHSIR----IGGDQLDEDIVSFVRKKYNL 199
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
98-340 |
3.84e-07 |
|
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: 51.50 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 98 VLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELAGLNAVRLINEPTAAAMAYGLhtqqnTRSLVFDLGGGT 177
Cdd:cd24047 48 IVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGI-----RDGAVVDIGGGT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 178 FDVTVLEYAtpviEVHASAgDNFLGGedfTHMlvDEVLKradvarttlneselGALYACVEAAKCSNQSPLHIRwqyqde 257
Cdd:cd24047 123 TGIAVLKDG----KVVYTA-DEPTGG---THL--SLVLA--------------GNYGISFEEAEIIKRDPARHK------ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 258 trecefyenELEDLWLPLLNRLRVPIEQALRDARlkpsqIDSLVLVGGASQMPLVQRIAVRLFGKLPYQSYDPSTIVALG 337
Cdd:cd24047 173 ---------ELLPVVRPVIEKMASIVKRHIKGYK-----VKDLYLVGGTCCLPGIEEVFEKETGLPVYKPSNPLLVTPLG 238
|
...
gi 446290036 338 AAI 340
Cdd:cd24047 239 IAL 241
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
98-184 |
9.56e-07 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 50.60 E-value: 9.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 98 VLRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELAGLNAVRLINEPTAAAMAYGLhtqqnTRSLVFDLGGGT 177
Cdd:PRK15080 72 IVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGI-----DNGAVVDIGGGT 146
|
....*..
gi 446290036 178 FDVTVLE 184
Cdd:PRK15080 147 TGISILK 153
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
8-183 |
2.33e-06 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 49.70 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGTTNSLIAVwKDGAAQLipnkfgeyLTPSIISMD-ENNHIL-VGKPAvsrrtshpdktaalfKRAMGsntnwrlg 85
Cdd:PRK13927 8 LGIDLGTANTLVYV-KGKGIVL--------NEPSVVAIRtDTKKVLaVGEEA---------------KQMLG-------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 86 sdtfNAPElSSLVLRSLK-------EDAEEFLQRPIKDV----------VISVPAYFSDEQRKHTRLAAELAGLNAVRLI 148
Cdd:PRK13927 56 ----RTPG-NIVAIRPMKdgviadfDVTEKMLKYFIKKVhknfrpsprvVICVPSGITEVERRAVRESALGAGAREVYLI 130
|
170 180 190
....*....|....*....|....*....|....*
gi 446290036 149 NEPTAAAMAYGLHTQQNTRSLVFDLGGGTFDVTVL 183
Cdd:PRK13927 131 EEPMAAAIGAGLPVTEPTGSMVVDIGGGTTEVAVI 165
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
8-217 |
3.65e-06 |
|
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466825 [Multi-domain] Cd Length: 263 Bit Score: 48.67 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 8 IGIDLGttNSLI-AVWKDGAAQLIPNKFGEYLTPSIISMDENNHI---------LVGKPAVSRrtshpdktaalfkramg 77
Cdd:cd10227 1 IGIDIG--NGNTkVVTGGGKEFKFPSAVAEARESSLDDGLLEDDIiveyngkryLVGELALRE----------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 78 SNTNWRLGSDTFNAPELSSLVLRSLKEDAEEFLQrpIKDVVISVPA--YFSDEQRKHTRLAAELAG-----------LNA 144
Cdd:cd10227 62 GGGGRSTGDDKKKSEDALLLLLAALALLGDDEEV--DVNLVVGLPIseYKEEKKELKKKLLKGLHEftfngkerritIND 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446290036 145 VRLINEPTAAAMAYGL--HTQQNTRSLVFDLGGGTFDVTVLEYATPVIEvhasAGDNFLGGEDFTHMLVDEVLKR 217
Cdd:cd10227 140 VKVLPEGAGAYLDYLLddDELEDGNVLVIDIGGGTTDILTFENGKPIEE----SSDTLPGGEEALEKYADDILNE 210
|
|
| ASKHA_NBD_ScArp9-like |
cd10208 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ... |
117-307 |
3.67e-06 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and similar proteins; Saccharomyces cerevisiae Arp9, also called actin-like protein 9, chromatin structure-remodeling complex protein ARP9, or SWI/SNF complex component ARP9, is a component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. It is also part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, which is required for the positive and negative regulation of gene expression of many genes. Arp9 forms a stable heterodimer with Arp7 protein in both the RSC and SWI/SNF chromatin-remodeling complexes. It has been suggested that this dimer functions as a module with DNA bending proteins, to achieve correct architecture and facilitate complex-complex interactions. Fission yeast SWI/SNF and RSC complexes do not contain Arp7 and Arp8, but instead contain Arp9 and Arp42.
Pssm-ID: 466814 Cd Length: 356 Bit Score: 49.23 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 117 VVISVPAYFS-DEQRKHTRLAAELAGLNAVRLINEPTAAAMAYGLhtqqnTRSLVFDLGGGTFDVT-VLEYATPVIEVHA 194
Cdd:cd10208 73 VLLSVPPSWSkSDLELLTQLFFERLNVPAFAILEAPLAALYAAGA-----TSGIVVDIGHEKTDITpIVDSQVVPHALVS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 195 SAgdnfLGGEDFTHMLVDeVLKRADVARTTLNESELGALYACVEAAKCSNQS----------------PLHIRWQYqdet 258
Cdd:cd10208 148 IP----IGGQDCTAHLAQ-LLKSDEPELKSQAESGEEATLDLAEALKKSPICevlsdgadlasgteitVGKERFRA---- 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446290036 259 reCE-FYENELEDLWLPLLNRLRVPIEQALRDARLKPSQIDSLVLVGGAS 307
Cdd:cd10208 219 --CEpLFKPSSLRVDLLIAAIAGALVLNASDEPDKRPALWENIIIVGGGS 266
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
99-322 |
4.90e-06 |
|
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: 48.81 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 99 LRSLKEDAEEFLQRPIKDVVISVPAYFSDEQRKHTRLAAELAGL----NAVRLIN--EPTAAAmaygLHTQQNTRSLVFD 172
Cdd:cd11736 125 LQELKDQSPSLPEKDAVRWVLTVPAIWKQPAKQFMREAAYLAGLvspeNPEQLLIalEPEAAS----IYCRKLDRYIVAD 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 173 LGGGTFDVTVLEYATP---VIEVHASAGDNF--LGgedfthmlvdevlkrADVARTTLNESELGALY-ACVEAAKCSNQS 246
Cdd:cd11736 201 CGGGTVDLTVHQIEQPqgtLKELYKASGGPYgaVG---------------VDLAFEKLLCQIFGEDFiATFKAKRPAAWV 265
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446290036 247 PLHIRWQYQDETRECEFYENELEDLWLPLLNRLRVPIEQALRDARLKpsQIDSLVLVGGASQMPLVQRIAVRLFGK 322
Cdd:cd11736 266 DLTIAFEARKRTAALRMSSEAMNELFQPTISQIIQHIDDLMKKPEVK--GIKFLFLVGGFAESPMLQRAVQAAFGN 339
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
118-321 |
5.98e-06 |
|
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: 48.85 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 118 VISVPAYFSDEQRKHTRLAAELAGL----NAVRLIN--EPTAAAM-AYGLHTQQNTRSLVFDLGGGTFDVTVLEYATP-- 188
Cdd:cd11735 144 VITVPAIWKQPAKQFMRQAAYKAGLaspeNPEQLIIalEPEAASIyCRKLRLHQMDRYVVVDCGGGTVDLTVHQIRLPeg 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 189 -VIEVHASAGDNF--LG-------------GEDFTH-------------MLVDEVLKRAdVARTTLNESELGALYACVE- 238
Cdd:cd11735 224 hLKELYKASGGPYgsLGvdyefekllckifGEDFIDqfkikrpaawvdlMIAFESRKRA-AAPDRTNPLNITLPFSFIDy 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290036 239 AAKCSNQSPLH---------IRWQYQDETReceFYENELEDLWLPLLNRlrvpIEQALRDARLKP--SQIDSLVLVGGAS 307
Cdd:cd11735 303 YKKFRGHSVEHalrksnvdfVKWSSQGMLR---MSPDAMNALFKPTIDH----IIQHLTDLFQKPevSGVKFLFLVGGFA 375
|
250
....*....|....
gi 446290036 308 QMPLVQRIAVRLFG 321
Cdd:cd11735 376 ESPLLQQAVQNAFG 389
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
285-347 |
7.93e-06 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 48.32 E-value: 7.93e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446290036 285 QALRDARLKPSQIdslVLVGGASQMPLVQRIAVRLFGkLPYQSYDPSTIVALGAAIQAACRLR 347
Cdd:cd07809 385 DILRELGVEIDEI---RLIGGGSKSPVWRQILADVFG-VPVVVPETGEGGALGAALQAAWGAG 443
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
286-355 |
1.24e-04 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 44.82 E-value: 1.24e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446290036 286 ALRDARLKPSQIdslVLVGGASQMPLVQRIAVRLFGkLPYQSYDPSTIVALGAAIQAACRL-RSEDIEEVI 355
Cdd:COG1070 388 ALEEAGVKIDRI---RATGGGARSPLWRQILADVLG-RPVEVPEAEEGGALGAALLAAVGLgLYDDLEEAA 454
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
116-177 |
5.88e-03 |
|
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.
Pssm-ID: 466786 [Multi-domain] Cd Length: 135 Bit Score: 37.45 E-value: 5.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446290036 116 DVVISVPAYFSDEQR-----------KHTRLAAELAGLNAVRLINEPTAAAMAYGLHTqQNTRSLVFDLGGGT 177
Cdd:cd00012 15 PIVITVAAGDRDANRvatiteailllQTNAATFALFTGPPVRIVNEAVAAAIGALLTL-GPEGLLVVDLGGGT 86
|
|
| |
