|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
34-424 |
0e+00 |
|
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: 591.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 34 AVMSVDLGSESMKVAIVKPGVPMEIVLNKESRRKTPVIVTLKENERFFGDSAASMAIKNPKATLRYFQHLLGkqadnphv 113
Cdd:cd10230 1 AVLGIDLGSEFIKVALVKPGVPFEIVLNEESKRKTPSAVAFRNGERLFGDDALALATRFPENTFSYLKDLLG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 114 alyqarfpeheltfdpqrqtvhfqissqlqFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVLQAAR 193
Cdd:cd10230 73 ------------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 194 MAGLKVLQLINDNTATALSYGVFRRKDiNTTAQNIMFYDMGSGSTVCTIVTYQMVKTKEAGM---QPQLQIRGVGFDRTL 270
Cdd:cd10230 123 IAGLNVLSLINDNTAAALNYGIDRRFE-NNEPQNVLFYDMGASSTSATVVEFSSVKEKDKGKnktVPQVEVLGVGWDRTL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 271 GGLEMELRLRERLAGLFNEQRKGqrAKDVRENPRAMAKLLREANRLKTVLSANADHMAQIEGLMDDVDFKAKVTRVEFEE 350
Cdd:cd10230 202 GGLEFDLRLADHLADEFNEKHKK--DKDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDDIDFRTKITREEFEE 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5453832 351 LCADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKEELGKNINADEAAAMGAVYQAA 424
Cdd:cd10230 280 LCADLFERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELGKHLNADEAAALGAAFYAA 353
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
38-424 |
6.61e-111 |
|
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: 348.01 E-value: 6.61e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 38 VDLGSESMKVAIVKPGVpMEIVLNKESRRKTPVIVTLKENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNPHVALYQ 117
Cdd:cd11732 3 IDFGNQNSVVAAARRGG-IDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 118 ARFPEHELTFDPQRQTVHFQISSQLQ-FSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVLQAARMAG 196
Cdd:cd11732 82 KLLPFKLVELEDGKVGIEVSYNGEEVvFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEIAG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 197 LKVLQLINDNTATALSYGVFRRKD--INTTAQNIMFYDMGSGSTVCTIVTYQmvktkeagmQPQLQIRGVGFDRTLGGLE 274
Cdd:cd11732 162 LNCLRLINETTAAALDYGIYKSDLleSEEKPRIVAFVDMGHSSTQVSIAAFT---------KGKLKVLSTAFDRNLGGRD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 275 MELRLRERLAGLFNEQRKGqrakDVRENPRAMAKLLREANRLKTVLSANADHMAQIEGLMDDVDFKAKVTRVEFEELCAD 354
Cdd:cd11732 233 FDRALVEHFAEEFKKKYKI----DPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEDIDFSGQIKREEFEELIQP 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 355 LFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKeELGKNINADEAAAMGAVYQAA 424
Cdd:cd11732 309 LLARLEAPIKKALAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVFGK-DLSTTLNADEAVARGCALQAA 377
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
34-435 |
6.77e-101 |
|
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: 321.95 E-value: 6.77e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 34 AVMSVDLGSESMKVAIVKPGVpMEIVLNKESRRKTPVIVTLKENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNPHV 113
Cdd:cd24095 2 SVVGIDFGNENCVVAVARKGG-IDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 114 ALYQARFPEHELTFDPQRQTVHFQ-ISSQLQFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVLQAA 192
Cdd:cd24095 81 QRDLKLFPFKVTEGPDGEIGINVNyLGEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 193 RMAGLKVLQLINDNTATALSYGVFRRKDINTTAQNIMFYDMGSGSTVCTIVTYQmvktkeagmQPQLQIRGVGFDRTLGG 272
Cdd:cd24095 161 QIAGLNCLRLMNETTATALAYGIYKTDLPETDPTNVVFVDVGHSSTQVCVVAFK---------KGQLKVLSHAFDRNLGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 273 LEMELRLRERLAGLFNEQRKgqraKDVRENPRAMAKLLREANRLKTVLSANADHMAQIEGLMDDVDFKAKVTRVEFEELC 352
Cdd:cd24095 232 RDFDEVLFDHFAAEFKEKYK----IDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMEDKDVKGMITREEFEELA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 353 ADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKeELGKNINADEAAAMGAVYQAAALSKAFKV 432
Cdd:cd24095 308 APLLERLLEPLEKALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFFGK-EPSRTMNASECVARGCALQCAMLSPTFKV 386
|
...
gi 5453832 433 KPF 435
Cdd:cd24095 387 REF 389
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
35-676 |
1.59e-94 |
|
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: 311.89 E-value: 1.59e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 35 VMSVDLGSESMKVAIVKPGVPmEIVLNKESRRKTPVIVTLKENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNPHVA 114
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGP-EVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 115 LYQARFPEH--ELTFDPQRQTVHFQissQLQFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVLQAA 192
Cdd:pfam00012 80 RDIKHLPYKvvKLPNGDAGVEVRYL---GETFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 193 RMAGLKVLQLINDNTATALSYGVFrRKDINttaQNIMFYDMGSGSTVCTIVTYQmvktkeagmQPQLQIRGVGFDRTLGG 272
Cdd:pfam00012 157 QIAGLNVLRIVNEPTAAALAYGLD-KTDKE---RNIAVYDLGGGTFDVSILEIG---------RGVFEVKATNGDTHLGG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 273 LEMELRLRERLAGLFneqrKGQRAKDVRENPRAMAKLLREANRLKTVLSANA-DHMAQIEGLM-DDVDFKAKVTRVEFEE 350
Cdd:pfam00012 224 EDFDLRLVDHLAEEF----KKKYGIDLSKDKRALQRLREAAEKAKIELSSNQtNINLPFITAMaDGKDVSGTLTRAKFEE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 351 LCADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKeELGKNINADEAAAMGAVYQAAALSKAF 430
Cdd:pfam00012 300 LVADLFERTLEPVEKALKDAGLSKSEIDEVVLVGGSTRIPAVQELVKEFFGK-EPSKGVNPDEAVAIGAAVQAGVLSGTF 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 431 KVKPFVVRDAVVYPILVEFTREVEEEpgihslkhnkrvLFSRMGPYPQRK-----VITFNRYShdFNFHINYGDLGFLgp 505
Cdd:pfam00012 379 DVKDFLLLDVTPLSLGIETLGGVMTK------------LIPRNTTIPTKKsqifsTAADNQTA--VEIQVYQGEREMA-- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 506 EDLRVFGSQNLTTVklkgvgdsfKKYPDYESKgIKAHFNLDESGVLSLdrvesvfetlvedSAEEESTLTKLGNTISSlf 585
Cdd:pfam00012 443 PDNKLLGSFELDGI---------PPAPRGVPQ-IEVTFDIDANGILTV-------------SAKDKGTGKEQEITIEA-- 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 586 GGGTTPDAKENgtdtVQEEEESPAEGSKdEPGEQVELKEEAEAPV--------EDGSQPPPPEPKG--DATPEGEKATEK 655
Cdd:pfam00012 498 SEGLSDDEIER----MVKDAEEYAEEDK-KRKERIEAKNEAEEYVysleksleEEGDKVPEAEKSKveSAIEWLKDELEG 572
|
650 660
....*....|....*....|.
gi 5453832 656 ENGDKSEAQKPSEKAEAGPEG 676
Cdd:pfam00012 573 DDKEEIEAKTEELAQVSQKIG 593
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
35-426 |
1.15e-91 |
|
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: 296.73 E-value: 1.15e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 35 VMSVDLGSESMKVAIVKPGVpMEIVLNKESRRKTPVIVTLKENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNPHVA 114
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGK-VEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 115 LYQARFPeHELTFDPQrQTVHFQISS---QLQFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVLQA 191
Cdd:cd24028 80 SDIKHWP-FKVVEDED-GKPKIEVTYkgeEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 192 ARMAGLKVLQLINDNTATALSYGVFRRKDintTAQNIMFYDMGSGSTVCTIVTyqmVKTKEagmqpqLQIRGVGFDRTLG 271
Cdd:cd24028 158 ATIAGLNVLRIINEPTAAALAYGLDKKSS---GERNVLVFDLGGGTFDVSLLS---IDNGV------FEVKATAGDTHLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 272 GLEMELRLRERLAGLFNEQRKgqraKDVRENPRAMAKLLREANRLKTVLSANADHMAQIEGLMDDVDFKAKVTRVEFEEL 351
Cdd:cd24028 226 GEDFDNRLVEYLVEEFKKKHG----KDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGIDFETTITRAKFEEL 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5453832 352 CADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKEELGKNINADEAAAMGAVYQAAAL 426
Cdd:cd24028 302 CEDLFKKCLEPVEKVLKDAKLSKDDIDEVVLVGGSTRIPKIQELLSEFFGGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
39-424 |
4.97e-89 |
|
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: 289.56 E-value: 4.97e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 39 DLGSESMKVAIVKPGVpMEIVLNKESRRKTPVIVTLKENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNPHVALYQA 118
Cdd:cd10228 4 DFGNLSCYIAVARAGG-IETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQKELK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 119 RFPeHELTFDPQRQT---VHFQiSSQLQFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVLQAARMA 195
Cdd:cd10228 83 HLP-YKVVKLPNGSVgikVQYL-GEEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 196 GLKVLQLINDNTATALSYGVFrRKDINTTAQ---NIMFYDMGSGSTVCTIVTYqmVKTKeagmqpqLQIRGVGFDRTLGG 272
Cdd:cd10228 161 GLNCLRLLNDTTAVALAYGIY-KQDLPAEEEkprNVVFVDMGHSSLQVSVCAF--NKGK-------LKVLATAADPNLGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 273 LEMELRLRERLAGLFNEQRKgqraKDVRENPRAMAKLLREANRLKTVLSANADHMA-QIEGLMDDVDFKAKVTRVEFEEL 351
Cdd:cd10228 231 RDFDELLVEHFAEEFKTKYK----IDVKSKPRALLRLLTECEKLKKLMSANATELPlNIECFMDDKDVSGKMKRAEFEEL 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5453832 352 CADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKeELGKNINADEAAAMGAVYQAA 424
Cdd:cd10228 307 CAPLFARVEVPLRSALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVFGK-EPSTTLNQDEAVARGCALQCA 378
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
38-433 |
1.67e-81 |
|
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: 269.63 E-value: 1.67e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 38 VDLGSESMKVAIVKP-GVpmEIVLNKESRRKTPVIVTLKENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNPHVALY 116
Cdd:cd24094 3 LDLGNLNSVIAVARNrGI--DIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 117 QARFpEHELTfDPQRQT---VHFQISSQLqFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVLQAAR 193
Cdd:cd24094 81 EKYF-TAKLV-DANGEVgaeVNYLGEKHV-FSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 194 MAGLKVLQLINDNTATALSYGVFRRK--DINTTAQNIMFYDMGSGSTVCTIVTYQmvktkeagmQPQLQIRGVGFDRTLG 271
Cdd:cd24094 158 IAGLNPLRLMNDTTAAALGYGITKTDlpEPEEKPRIVAFVDIGHSSYTVSIVAFK---------KGQLTVKGTAYDRHFG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 272 GLEMELRLRERLAGLFNEQRKgqraKDVRENPRAMAKLLREANRLKTVLSANADHMAQIEGLMDDVDFKAKVTRVEFEEL 351
Cdd:cd24094 229 GRDFDKALTDHFADEFKEKYK----IDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVSSMLKREEFEEL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 352 CADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKeELGKNINADEAAAMGAVYQAAALSKAFK 431
Cdd:cd24094 305 IAPLLERVTAPLEKALAQAGLTKDEIDFVELVGGTTRVPALKESISAFFGK-PLSTTLNQDEAVARGAAFACAILSPVFR 383
|
..
gi 5453832 432 VK 433
Cdd:cd24094 384 VR 385
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
35-426 |
6.71e-75 |
|
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: 251.36 E-value: 6.71e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 35 VMSVDLGSESMKVAIVKPGvPMEIVLNKESRRKTPVIVTLKENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNPHVA 114
Cdd:cd10241 3 VIGIDLGTTYSCVGVFKNG-RVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKEVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 115 LYQARFPeHELTFDPQRQTVHFQISSQL-QFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVLQAAR 193
Cdd:cd10241 82 KDIKLLP-FKIVNKNGKPYIQVEVKGEKkTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 194 MAGLKVLQLINDNTATALSYGVfrrkDINTTAQNIMFYDMGSGS---TVCTIvtyqmvktkEAGMQPQLQIRGvgfDRTL 270
Cdd:cd10241 161 IAGLNVLRIINEPTAAAIAYGL----DKKGGEKNILVFDLGGGTfdvSLLTI---------DNGVFEVLATNG---DTHL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 271 GGLEMELRLRERLAGLFNEQRKgqraKDVRENPRAMAKLLREANRLKTVLSANADHMAQIEGLMDDVDFKAKVTRVEFEE 350
Cdd:cd10241 225 GGEDFDQRVMDHFIKLFKKKTG----KDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGEDFSETLTRAKFEE 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5453832 351 LCADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKEELGKNINADEAAAMGAVYQAAAL 426
Cdd:cd10241 301 LNMDLFRKTLKPVQKVLEDAGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFNGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
34-427 |
9.82e-73 |
|
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: 245.60 E-value: 9.82e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 34 AVMSVDLGSESMKVAIVKPGvPMEIVLNKESRRKTPVIVTLKENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNPHV 113
Cdd:cd11738 1 SVVGIDVGFQNCYIAVARSG-GIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 114 ALYQARFPeHELTFDPQRQT---VHFqISSQLQFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVLQ 190
Cdd:cd11738 80 QAEKIKLP-YELQKMPNGSTgvkVRY-LDEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 191 AARMAGLKVLQLINDNTATALSYGVFrRKDINT---TAQNIMFYDMGSGSTVCTIVTYQMVKtkeagmqpqLQIRGVGFD 267
Cdd:cd11738 158 AAQIAGLNCLRLMNETTAVALAYGIY-KQDLPAleeKPRNVVFVDMGHSAYQVSICAFNKGK---------LKVLATTFD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 268 RTLGGLEMElrlrERLAGLFNEQRKGQRAKDVRENPRAMAKLLREANRLKTVLSANA-DHMAQIEGLMDDVDFKAKVTRV 346
Cdd:cd11738 228 PYLGGRNFD----EVLVDYFCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSANAsDLPLNIECFMNDIDVSSKMNRA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 347 EFEELCADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKeELGKNINADEAAAMGAVYQAAAL 426
Cdd:cd11738 304 QFEELCASLLARVEPPLKAVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFFGK-DISTTLNADEAVARGCALQCAIL 382
|
.
gi 5453832 427 S 427
Cdd:cd11738 383 S 383
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
34-424 |
1.51e-70 |
|
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: 239.46 E-value: 1.51e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 34 AVMSVDLGSESMKVAIVKPGvPMEIVLNKESRRKTPVIVTLKENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNPHV 113
Cdd:cd11737 1 SVVGFDLGFQSCYVAVARAG-GIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 114 ALYQARFPeHELTFDPQRQT---VHFqISSQLQFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVLQ 190
Cdd:cd11737 80 QAEKPSLA-YELVQLPTGTTgikVMY-MEEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 191 AARMAGLKVLQLINDNTATALSYGVFRRK--DINTTAQNIMFYDMGSGSTVCTIVTYQMVKtkeagmqpqLQIRGVGFDR 268
Cdd:cd11737 158 ATQIAGLNCLRLMNETTAVALAYGIYKQDlpAPEEKPRNVVFVDMGHSAYQVSVCAFNKGK---------LKVLATAFDP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 269 TLGGLEMElrlrERLAGLFNEQRKGQRAKDVRENPRAMAKLLREANRLKTVLSANADHMA-QIEGLMDDVDFKAKVTRVE 347
Cdd:cd11737 229 TLGGRKFD----EVLVNHFCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSANASDLPlNIECFMNDIDVSGTMNRGQ 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5453832 348 FEELCADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKeELGKNINADEAAAMGAVYQAA 424
Cdd:cd11737 305 FEEMCADLLARVEPPLRSVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFFGK-EVSTTLNADEAVARGCALQCA 380
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
47-553 |
1.13e-69 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 240.11 E-value: 1.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 47 VAIVKPGVPmEIVLNKESRRKTPVIVTL-KENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNPHVALYQARFpehel 125
Cdd:COG0443 13 VAVVEGGEP-QVIPNAEGRRTLPSVVAFpKDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFDEATEVGGKRY----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 126 tfdpqrqtvhfqissqlqfSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVLQAARMAGLKVLQLIND 205
Cdd:COG0443 87 -------------------SPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARIAGLEVLRLLNE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 206 NTATALSYGVfrrkDINTTAQNIMFYDMGSGSTVCTIVTYQmvktkeagmQPQLQIRGVGFDRTLGGLEMELRLRERLAG 285
Cdd:COG0443 148 PTAAALAYGL----DKGKEEETILVYDLGGGTFDVSILRLG---------DGVFEVLATGGDTHLGGDDFDQALADYVAP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 286 LFNEQRKGqrakDVRENPRAMAKLLREANRLKTVLSANADHMAQIEGLmDDVDFKAKVTRVEFEELCADLFERVPGPVQQ 365
Cdd:COG0443 215 EFGKEEGI----DLRLDPAALQRLREAAEKAKIELSSADEAEINLPFS-GGKHLDVELTRAEFEELIAPLVERTLDPVRQ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 366 ALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKEELgKNINADEAAAMGAVYQAAALSKAfkvkpfvVRDAVVYPI 445
Cdd:COG0443 290 ALADAGLSPSDIDAVLLVGGSTRMPAVRERVKELFGKEPL-KGVDPDEAVALGAAIQAGVLAGD-------VKDLDVTPL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 446 LVeftreveeepGIHSLKHNKRVLFSRMGPYPQRKVITFnryshdFNFHINYGDLGF--LGPEDLRVFGSQNLTTVKLKG 523
Cdd:COG0443 362 SL----------GIETLGGVFTKLIPRNTTIPTAKSQVF------STAADNQTAVEIhvLQGERELAADNRSLGRFELTG 425
|
490 500 510
....*....|....*....|....*....|
gi 5453832 524 VGDSFKKYPdyeskGIKAHFNLDESGVLSL 553
Cdd:COG0443 426 IPPAPRGVP-----QIEVTFDIDANGILSV 450
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
57-426 |
5.50e-69 |
|
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: 235.22 E-value: 5.50e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 57 EIVLNKESRRKTPVIVTLKENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNPHVALYQARFPEHELTFD--PQRQtV 134
Cdd:cd10233 22 EIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQSDMKHWPFKVVSGGdkPKIQ-V 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 135 HFQISSQlQFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVLQAARMAGLKVLQLINDNTATALSYG 214
Cdd:cd10233 101 EYKGETK-TFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 215 VFRRKDintTAQNIMFYDMGSGSTVCTIVTYqmvktkEAGMqpqLQIRGVGFDRTLGGLEMELRLRERLAGLFNEQRKgq 294
Cdd:cd10233 180 LDKKGK---GERNVLIFDLGGGTFDVSLLTI------EDGI---FEVKATAGDTHLGGEDFDNRLVNHFVQEFKRKHK-- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 295 raKDVRENPRAMAKLLREANRLKTVLSANADHMAQIEGLMDDVDFKAKVTRVEFEELCADLFERVPGPVQQALQSAEMSL 374
Cdd:cd10233 246 --KDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELCADLFRSTLEPVEKVLRDAKLDK 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 5453832 375 DEIEQVILVGGATRVPRVQEVLLKAVGKEELGKNINADEAAAMGAVYQAAAL 426
Cdd:cd10233 324 SQIHEIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
34-426 |
4.38e-65 |
|
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: 224.43 E-value: 4.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 34 AVMSVDLGSESMKVAIVKPGvPMEIVLNKESRRKTPVIVTLKENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNPHV 113
Cdd:cd10238 1 AAFGVHFGNTNACVAVYKDG-RTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 114 ALYQARFP----EH--ELTFDPQRQtvhfqiSSQLQFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRA 187
Cdd:cd10238 80 QELKKESKckiiEKdgKPGYEIELE------EKKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 188 VLQAARMAGLKVLQLINDNTATALSYGVfrRKDINTTAQNIMFYDMGSGSTVCTIVTYQmvktkeAGMQpqlQIRGVGFD 267
Cdd:cd10238 154 LKEAAEKAGFNVLRVISEPSAAALAYGI--GQDDPTENSNVLVYRLGGTSLDVTVLSVN------NGMY---RVLATRTD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 268 RTLGGLEMELRLRERLAGLFNEQRKgqraKDVRENPRAMAKLLREANRLKTVLSANADHMAQIEGLMDDVDFKAKVTRVE 347
Cdd:cd10238 223 DNLGGDDFTEALAEHLASEFKRQWK----QDVRENKRAMAKLMNAAEVCKHVLSTLNTATCSVESLYDGMDFQCNVSRAR 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5453832 348 FEELCADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKEELGKNINADEAAAMGAVYQAAAL 426
Cdd:cd10238 299 FESLCSSLFQQCLEPIQEVLNSAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFPSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
36-426 |
1.28e-63 |
|
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: 220.24 E-value: 1.28e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 36 MSVDLGSESMKVAIVKPGVpmEIVLNKESRRKTPVIVTLKENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNPHVAL 115
Cdd:cd24093 2 IGIDLGTTYSCVATYESSV--EIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 116 YQARFPeHELTFDPQRQTVHFQ-ISSQLQFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVLQAARM 194
Cdd:cd24093 80 DMKTWP-FKVIDVNGNPVIEVQyLGETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 195 AGLKVLQLINDNTATALSYGVFRRKdiNTTAQNIMFYDMGSGSTVCTIVTYQmvktkeAGMqpqLQIRGVGFDRTLGGLE 274
Cdd:cd24093 159 AGLNVLRIINEPTAAAIAYGLGAGK--SEKERHVLIFDLGGGTFDVSLLHIA------GGV---YTVKSTSGNTHLGGQD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 275 MELRLRERlaglFNEQRKGQRAKDVRENPRAMAKLLREANRLKTVLSANADHMAQIEGLMDDVDFKAKVTRVEFEELCAD 354
Cdd:cd24093 228 FDTNLLEH----FKAEFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSITRARFEDLNAA 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5453832 355 LFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKEELGKNINADEAAAMGAVYQAAAL 426
Cdd:cd24093 304 LFKSTLEPVEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
34-424 |
9.95e-63 |
|
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: 217.81 E-value: 9.95e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 34 AVMSVDLGSESMKVAIVKPGvPMEIVLNKESRRKTPVIVTLKENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNPHV 113
Cdd:cd11739 1 SVVGFDVGFQNCYIAVARAG-GIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 114 ALYQARFPEHELTFDPQRQTVHFQISSQLQ-FSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVLQAA 192
Cdd:cd11739 80 QKEKENLSYDLVPLKNGGVGVKVMYLDEEHhFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 193 RMAGLKVLQLINDNTATALSYGVFrRKDINTTAQN---IMFYDMGSGSTVCTIVTYQMVKtkeagmqpqLQIRGVGFDRT 269
Cdd:cd11739 160 QIVGLNCLRLMNDMTAVALNYGIY-KQDLPAPDEKpriVVFVDMGHSAFQVSACAFNKGK---------LKVLGTAFDPY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 270 LGGLEMElrlrERLAGLFNEQRKGQRAKDVRENPRAMAKLLREANRLKTVLSANA-DHMAQIEGLMDDVDFKAKVTRVEF 348
Cdd:cd11739 230 LGGRNFD----EKLVEHFCAEFKTKYKLDVKSKIRALLRLYQECEKLKKLMSSNStDLPLNIECFMNDKDVSGKMNRSQF 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5453832 349 EELCADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKeELGKNINADEAAAMGAVYQAA 424
Cdd:cd11739 306 EELCADLLQRIEVPLYSLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFFGK-DVSTTLNADEAVARGCALQCA 380
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
38-427 |
5.94e-61 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 220.44 E-value: 5.94e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 38 VDLGSESMKVAIVKPGVpMEIVLNKESRRKTPVIVTLKENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNPHValyq 117
Cdd:PTZ00009 9 IDLGTTYSCVGVWKNEN-VEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDSVV---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 118 arfpEHELTFDPQRQT----------VHFQiSSQLQFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRA 187
Cdd:PTZ00009 84 ----QSDMKHWPFKVTtggddkpmieVTYQ-GEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 188 VLQAARMAGLKVLQLINDNTATALSYGVFRRKDintTAQNIMFYDMGSGSTVCTIVTYqmvktkEAGMqpqLQIRGVGFD 267
Cdd:PTZ00009 159 TKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGD---GEKNVLIFDLGGGTFDVSLLTI------EDGI---FEVKATAGD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 268 RTLGGLEMELRLRERLAGLFNEQRKGqraKDVRENPRAMAKLLREANRLKTVLSANADHMAQIEGLMDDVDFKAKVTRVE 347
Cdd:PTZ00009 227 THLGGEDFDNRLVEFCVQDFKRKNRG---KDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRAR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 348 FEELCADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKEELGKNINADEAAAMGAVYQAAALS 427
Cdd:PTZ00009 304 FEELCGDYFRNTLQPVEKVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILT 383
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
35-427 |
7.49e-60 |
|
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: 209.25 E-value: 7.49e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 35 VMSVDLGSESMKVAIVKPGVPmEIVLNKESRRKTPVIVTL-KENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNPHV 113
Cdd:cd10234 1 IIGIDLGTTNSCVAVMEGGKP-TVIPNAEGGRTTPSVVAFtKDGERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 114 ALYQARFPEHELTFDPQRQTVHfqissQLQFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVLQAAR 193
Cdd:cd10234 80 ERKQVPYPVVSAGNGDAWVEIG-----GKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 194 MAGLKVLQLINDNTATALSYGVFRRKDinttaQNIMFYDMGSGSTVCTIV-----TYQMVKTkeAGmqpqlqirgvgfDR 268
Cdd:cd10234 155 IAGLEVLRIINEPTAAALAYGLDKKKD-----EKILVYDLGGGTFDVSILeigdgVFEVLST--NG------------DT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 269 TLGGLEMELRLRERLAGLFneqrKGQRAKDVRENPRAMAKLLREANRLKTVLS-------------ANAD---HMAQieg 332
Cdd:cd10234 216 HLGGDDFDQRIIDYLADEF----KKEEGIDLSKDKMALQRLKEAAEKAKIELSsvleteinlpfitADASgpkHLEM--- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 333 lmddvdfkaKVTRVEFEELCADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKEELgKNINAD 412
Cdd:cd10234 289 ---------KLTRAKFEELTEDLVERTIEPVEQALKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFFGKEPN-KGVNPD 358
|
410
....*....|....*
gi 5453832 413 EAAAMGAVYQAAALS 427
Cdd:cd10234 359 EVVAIGAAIQGGVLA 373
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
39-424 |
1.19e-54 |
|
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: 193.95 E-value: 1.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 39 DLGSESMKVAIVKPGVPMEIVLNKESRRKTPVIVTLKENERF-FGDSAASMAIKNPKATLRYFQHLLGKQadnphvalyq 117
Cdd:cd24029 4 DLGTTNSAVAYWDGNGAEVIIENSEGKRTTPSVVYFDKDGEVlVGEEAKNQALLDPENTIYSVKRLMGRD---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 118 arFPEHELTFDPqrqtvhfqissqlQFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVLQAARMAGL 197
Cdd:cd24029 74 --TKDKEEIGGK-------------EYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAELAGL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 198 KVLQLINDNTATALSYGVFRRKDinttAQNIMFYDMGSGSTVCTIVTYQMVKtkeagmqpqLQIRGVGFDRTLGGLEmel 277
Cdd:cd24029 139 NVLRLINEPTAAALAYGLDKEGK----DGTILVYDLGGGTFDVSILEIENGK---------FEVLATGGDNFLGGDD--- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 278 rLRERLAGLFNEQRKGQR-AKDVRENPRAMAKLLREANRLKTVLSANADHMAQIEGLMDDVDFKAKVTRVEFEELCADLF 356
Cdd:cd24029 203 -FDEAIAELILEKIGIETgILDDKEDERARARLREAAEEAKIELSSSDSTDILILDDGKGGELEIEITREEFEELIAPLI 281
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5453832 357 ERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKEELgKNINADEAAAMGAVYQAA 424
Cdd:cd24029 282 ERTIDLLEKALKDAKLSPEDIDRVLLVGGSSRIPLVREMLEEYFGREPI-SSVDPDEAVAKGAAIYAA 348
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
38-427 |
1.83e-54 |
|
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: 193.97 E-value: 1.83e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 38 VDLGSESMKVAIVKPGVPmEIVLNKESRRKTPVIVTLKENERFF-GDSAASMAIKNPKATLRYFQHLLGKQADNphVALY 116
Cdd:cd10236 7 IDLGTTNSLVATVRSGQP-EVLPDEKGEALLPSVVHYGEDGKITvGEKAKENAITDPENTISSVKRLMGRSLAD--VKEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 117 QARFPeHELTFDPQrQTVHFQISsQLQFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVLQAARMAG 196
Cdd:cd10236 84 LPLLP-YRLVGDEN-ELPRFRTG-AGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 197 LKVLQLINDNTATALSYGVFRRKDinttaQNIMFYDMGSGSTVCTIvtyqmvktkeagmqpqLQI-RGV------GFDRT 269
Cdd:cd10236 161 LNVLRLLNEPTAAALAYGLDQKKE-----GTIAVYDLGGGTFDISI----------------LRLsDGVfevlatGGDTA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 270 LGGLEMElrlrERLAGLFNEQRKgqraKDVRENPRAMAKLLREANRLKTVLSaNADHmAQIEGLMDDVDFKAKVTRVEFE 349
Cdd:cd10236 220 LGGDDFD----HLLADWILKQIG----IDARLDPAVQQALLQAARRAKEALS-DADS-ASIEVEVEGKDWEREITREEFE 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5453832 350 ELCADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKEELgKNINADEAAAMGAVYQAAALS 427
Cdd:cd10236 290 ELIQPLVKRTLEPCRRALKDAGLEPADIDEVVLVGGSTRIPLVRQRVAEFFGREPL-TSINPDEVVALGAAIQADILA 366
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
34-426 |
2.31e-52 |
|
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: 188.24 E-value: 2.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 34 AVMSVDLGSESMKVAIVKPGVPmEIVLNKESRRKTPVIVT-LKENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNPH 112
Cdd:cd11733 2 DVIGIDLGTTNSCVAVMEGKTP-KVIENAEGARTTPSVVAfTADGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 113 VAlyqarfpeheltfdPQRQTVHFQI-----------SSQLQFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFN 181
Cdd:cd11733 81 VQ--------------KDIKMVPYKIvkasngdawveAHGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 182 QAERRAVLQAARMAGLKVLQLINDNTATALSYGVFRRKDinttaQNIMFYDMGSGSTVCTIvtyqmvktkeagmqpqLQI 261
Cdd:cd11733 147 DSQRQATKDAGQIAGLNVLRIINEPTAAALAYGLDKKDD-----KIIAVYDLGGGTFDISI----------------LEI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 262 RGVGF-------DRTLGGLEMELRLRERLAGLFneqrKGQRAKDVRENPRAMAKLLREANRLKTVLSANADHMAQIEGLM 334
Cdd:cd11733 206 QKGVFevkatngDTFLGGEDFDNALLNYLVAEF----KKEQGIDLSKDNLALQRLREAAEKAKIELSSSLQTDINLPFIT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 335 DDVD----FKAKVTRVEFEELCADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKEElGKNIN 410
Cdd:cd11733 282 ADASgpkhLNMKLTRAKFESLVGDLIKRTVEPCKKCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIFGKAP-SKGVN 360
|
410
....*....|....*.
gi 5453832 411 ADEAAAMGAVYQAAAL 426
Cdd:cd11733 361 PDEAVAMGAAIQGGVL 376
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
39-427 |
4.64e-52 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 193.78 E-value: 4.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 39 DLGSESMKVAIVKPGVPmEIVLNKESRRKTPVIVTLKEN-ERFFGDSAASMAIKNPKATLRYFQHLLGKqaDNPHVALYQ 117
Cdd:PRK00290 8 DLGTTNSCVAVMEGGEP-KVIENAEGARTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRLMGR--RDEEVQKDI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 118 ARFPEHELTFDPQRQTVHfqISSQlQFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVLQAARMAGL 197
Cdd:PRK00290 85 KLVPYKIVKADNGDAWVE--IDGK-KYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 198 KVLQLINDNTATALSYGVFRRKDinttaQNIMFYDMGSGSTVCTIV-----TYQMVKTkeAGmqpqlqirgvgfDRTLGG 272
Cdd:PRK00290 162 EVLRIINEPTAAALAYGLDKKGD-----EKILVYDLGGGTFDVSILeigdgVFEVLST--NG------------DTHLGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 273 LEMELRLRERLAGLFneqrKGQRAKDVRENPRAMAKLLREANRLKTVLS-------------ANAD---HMAQieglmdd 336
Cdd:PRK00290 223 DDFDQRIIDYLADEF----KKENGIDLRKDKMALQRLKEAAEKAKIELSsaqqteinlpfitADASgpkHLEI------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 337 vdfkaKVTRVEFEELCADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKeELGKNINADEAAA 416
Cdd:PRK00290 292 -----KLTRAKFEELTEDLVERTIEPCKQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFFGK-EPNKGVNPDEVVA 365
|
410
....*....|.
gi 5453832 417 MGAVYQAAALS 427
Cdd:PRK00290 366 IGAAIQGGVLA 376
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
35-431 |
4.87e-51 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 191.76 E-value: 4.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 35 VMSVDLGSESMKVAIVKPGVPMEIVlNKESRRKTPVIVTL-KENERFFGDSAASMAIKNPKATLRYFQHLLGKQADnphv 113
Cdd:PRK13410 4 IVGIDLGTTNSVVAVMEGGKPVVIA-NAEGMRTTPSVVGFtKDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYD---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 114 alyqarfpehELtfDPQRQTVHFQISS-------------QLQFSPEEVLGMVLnysRSLAEDfAE----QPIKDAVITV 176
Cdd:PRK13410 79 ----------EL--DPESKRVPYTIRRneqgnvrikcprlEREFAPEELSAMIL---RKLADD-ASrylgEPVTGAVITV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 177 PVFFNQAERRAVLQAARMAGLKVLQLINDNTATALSYGVFRrkdinTTAQNIMFYDMGSGstvctivTYQmVKTKEAGmQ 256
Cdd:PRK13410 143 PAYFNDSQRQATRDAGRIAGLEVERILNEPTAAALAYGLDR-----SSSQTVLVFDLGGG-------TFD-VSLLEVG-N 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 257 PQLQIRGVGFDRTLGGLEMELRLRERLAGLFNEQRKgqraKDVRENPRAMAKLLREANRLKTVLS-------------AN 323
Cdd:PRK13410 209 GVFEVKATSGDTQLGGNDFDKRIVDWLAEQFLEKEG----IDLRRDRQALQRLTEAAEKAKIELSgvsvtdislpfitAT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 324 ADHMAQIEglmddvdfkAKVTRVEFEELCADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKE 403
Cdd:PRK13410 285 EDGPKHIE---------TRLDRKQFESLCGDLLDRLLRPVKRALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLIPRE 355
|
410 420
....*....|....*....|....*...
gi 5453832 404 ElGKNINADEAAAMGAVYQAAALSKAFK 431
Cdd:PRK13410 356 P-NQNVNPDEVVAVGAAIQAGILAGELK 382
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
34-427 |
1.16e-50 |
|
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: 183.42 E-value: 1.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 34 AVMSVDLGSESMKVAIVKPGVPmEIVLNKESRRKTPVIVTL-KENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNPH 112
Cdd:cd11734 2 PVIGIDLGTTNSCVAVMEGKTP-RVIENAEGARTTPSVVAFtKDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 113 ValyqarfpEHELTFDPQRQTVHFQISSQLQ-----FSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRA 187
Cdd:cd11734 81 V--------QRDIKEVPYKIVKHSNGDAWVEargqkYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 188 VLQAARMAGLKVLQLINDNTATALSYGVFRRKDinttaQNIMFYDMGSGSTVCTIVTYQmvktkeagmQPQLQIRGVGFD 267
Cdd:cd11734 153 TKDAGQIAGLNVLRVINEPTAAALAYGLDKSGD-----KVIAVYDLGGGTFDISILEIQ---------KGVFEVKSTNGD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 268 RTLGGLEMELRLRERLAGLFneqrKGQRAKDVRENPRAMAKLLREANRLKTVLSANADHMAQIEGLMDDVD----FKAKV 343
Cdd:cd11734 219 THLGGEDFDIALVRHIVSEF----KKESGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINLPFITADASgpkhINMKL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 344 TRVEFEELCADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKEElGKNINADEAAAMGAVYQA 423
Cdd:cd11734 295 TRAQFESLVKPLVDRTVEPCKKALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIFGREP-SKGVNPDEAVAIGAAIQG 373
|
....
gi 5453832 424 AALS 427
Cdd:cd11734 374 GVLS 377
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
35-426 |
2.60e-50 |
|
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: 183.31 E-value: 2.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 35 VMSVDLGSESMKVAIVKPGVPMEIVLNKESRRK-TPVIVTLKENERFF-GDSAASMAIKNPKATLRYFQHLLGKQADNPH 112
Cdd:cd10237 24 IVGIDLGTTYSCVGVYHAVTGEVEVIPDDDGHKsIPSVVAFTPDGGVLvGYDALAQAEHNPSNTIYDAKRFIGKTFTKEE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 113 VALYQARFPEHeLTFDpQRQTVHFQISSQLQF---SPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVL 189
Cdd:cd10237 104 LEEEAKRYPFK-VVND-NIGSAFFEVPLNGSTlvvSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 190 QAARMAGLKVLQLINDNTATALSYGVFRRKDINttaqNIMFYDMGSGSTVCTIVTyqmvktKEAGMqpqLQIRGVGFDRT 269
Cdd:cd10237 182 KAANLAGLEVLRVINEPTAAAMAYGLHKKSDVN----NVLVVDLGGGTLDVSLLN------VQGGM---FLTRAMAGNNH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 270 LGGLEMELRLRERLAGLFNEQ--RKGQRAKDVRenpramakLLREA-NRLKTVLSANADHMAQIEGLMDD-----VDFKA 341
Cdd:cd10237 249 LGGQDFNQRLFQYLIDRIAKKfgKTLTDKEDIQ--------RLRQAvEEVKLNLTNHNSASLSLPLQISLpsafkVKFKE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 342 KVTRVEFEELCADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKeELGKNINADEAAAMGAVY 421
Cdd:cd10237 321 EITRDLFETLNEDLFQRVLEPIRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFFGK-DPNTSVDPELAVVTGVAI 399
|
....*
gi 5453832 422 QAAAL 426
Cdd:cd10237 400 QAGII 404
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
35-431 |
5.34e-50 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 188.42 E-value: 5.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 35 VMSVDLGSESMKVAIVKPGVPMeIVLNKESRRKTPVIVTL-KENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNphV 113
Cdd:PRK13411 4 VIGIDLGTTNSCVAVLEGGKPI-VIPNSEGGRTTPSIVGFgKSGDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDD--T 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 114 ALYQARFPEHELtfdPQR-QTVHFQISSQlQFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVLQAA 192
Cdd:PRK13411 81 EEERSRVPYTCV---KGRdDTVNVQIRGR-NYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 193 RMAGLKVLQLINDNTATALSYGVfrrkDINTTAQNIMFYDMGSGSTVCTIVtyqmvktkeagmqpQL-----QIRGVGFD 267
Cdd:PRK13411 157 TIAGLEVLRIINEPTAAALAYGL----DKQDQEQLILVFDLGGGTFDVSIL--------------QLgdgvfEVKATAGN 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 268 RTLGGLEMELRLRERLAGLFNEQRKgqraKDVRENPRAMAKLLREANRLKTVLSANADHMAQIEGLM-DDVDFK---AKV 343
Cdd:PRK13411 219 NHLGGDDFDNCIVDWLVENFQQQEG----IDLSQDKMALQRLREAAEKAKIELSSMLTTSINLPFITaDETGPKhleMEL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 344 TRVEFEELCADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKEELGKNINADEAAAMGAVYQA 423
Cdd:PRK13411 295 TRAKFEELTKDLVEATIEPMQQALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFGGKQPDRSVNPDEAVALGAAIQA 374
|
....*...
gi 5453832 424 AALSKAFK 431
Cdd:PRK13411 375 GVLGGEVK 382
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
38-424 |
1.05e-49 |
|
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: 179.36 E-value: 1.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 38 VDLGSESMKVAIVKPGVPmEIVLNKESRRKTPVIVTLKENERFF-GDSAASMAIKNPKATLRYFQHLLGKqadnphvaly 116
Cdd:cd10235 3 IDLGTTNSLVAVWRDGGA-ELIPNALGEYLTPSVVSVDEDGSILvGRAAKERLVTHPDRTAASFKRFMGT---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 117 qarfpEHELTFDPQRqtvhfqissqlqFSPEEVLGMVLnysRSLAEDfAE----QPIKDAVITVPVFFNQAERRAVLQAA 192
Cdd:cd10235 72 -----DKQYRLGNHT------------FRAEELSALVL---KSLKED-AEaylgEPVTEAVISVPAYFNDEQRKATKDAG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 193 RMAGLKVLQLINDNTATALSYGVFRRKDiNTTaqnIMFYDMGSGSTVCTIVTYqmvktkeagMQPQLQIRGVGFDRTLGG 272
Cdd:cd10235 131 ELAGLKVERLINEPTAAALAYGLHKRED-ETR---FLVFDLGGGTFDVSVLEL---------FEGVIEVHASAGDNFLGG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 273 LEMELRLRERLAGlfnEQRKGQRAkdvrENPRAMAKLLREANRLKTVLSANADHMAQIegLMDDVDFKAKVTRVEFEELC 352
Cdd:cd10235 198 EDFTHALADYFLK---KHRLDFTS----LSPSELAALRKRAEQAKRQLSSQDSAEIRL--TYRGEELEIELTREEFEELC 268
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5453832 353 ADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKEELgKNINADEAAAMGAVYQAA 424
Cdd:cd10235 269 APLLERLRQPIERALRDAGLKPSDIDAVILVGGATRMPLVRQLIARLFGRLPL-SSLDPDEAVALGAAIQAA 339
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
34-424 |
2.47e-49 |
|
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: 178.71 E-value: 2.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 34 AVMSVDLGSESMKVAIVKPGVPMEIVLNKESRRKTPVIVTLKENERFFGDSAASMAIKNPKATLRYFQHLLGKqadnphv 113
Cdd:cd10232 1 VVIGISFGNSNSSIAIINKDGRAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPKNTVANFRDLLGT------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 114 alyqarfpeheltfdpqrqtvhfqissqLQFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVLQAAR 193
Cdd:cd10232 74 ----------------------------TTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 194 MAGLKVLQLINDNTATALSYGVFRRKDINTTA-QNIMFYDMGSGSTVCTIVTYQmvktkeAGMQPQLqirGVGFDRTLGG 272
Cdd:cd10232 126 AAGLEVLQLIPEPAAAALAYDLRAETSGDTIKdKTVVVADLGGTRSDVTVVAVR------GGLYTIL---ATVHDYELGG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 273 LEMELRLRERLAGLFNEQRKGqrakDVRENPRAMAKLLREANRLKTVLSANADHMAQIEGLMDDVDFKAKVTRVEFEELC 352
Cdd:cd10232 197 VALDDVLVGHFAKEFKKKTKT----DPRKNARSLAKLRNAAEITKRALSQGTSAPCSVESLADGIDFHSSINRTRYELLA 272
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5453832 353 ADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEV---LLKAVGKEELGKNINADEAAAMGAVYQAA 424
Cdd:cd10232 273 SKVFQQFADLVTDAIEKAGLDPLDIDEVLLAGGASRTPKLASNfeyLFPESTIIRAPTQINPDELIARGAALQAS 347
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
35-427 |
1.76e-46 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 178.12 E-value: 1.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 35 VMSVDLGSESMKVAIVKPGVPMeIVLNKESRRKTPVIVTLKEN-ERFFGDSAASMAIKNPKATLRYFQHLLGKQADnpHV 113
Cdd:PLN03184 41 VVGIDLGTTNSAVAAMEGGKPT-IVTNAEGQRTTPSVVAYTKNgDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMS--EV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 114 ALYQARFPEHELTFDPQRQTVHFQISSQlQFSPEEVLGMVLnysRSLAED---FAEQPIKDAVITVPVFFNQAERRAVLQ 190
Cdd:PLN03184 118 DEESKQVSYRVVRDENGNVKLDCPAIGK-QFAAEEISAQVL---RKLVDDaskFLNDKVTKAVITVPAYFNDSQRTATKD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 191 AARMAGLKVLQLINDNTATALSYGvFRRKDINTtaqnIMFYDMGSGstvctivTYQmVKTKEAGmQPQLQIRGVGFDRTL 270
Cdd:PLN03184 194 AGRIAGLEVLRIINEPTAASLAYG-FEKKSNET----ILVFDLGGG-------TFD-VSVLEVG-DGVFEVLSTSGDTHL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 271 GGLEMELRLRERLAGLFneqrKGQRAKDVRENPRAMAKLLREANRLKTVLS-------------ANADHMAQIEglmddv 337
Cdd:PLN03184 260 GGDDFDKRIVDWLASNF----KKDEGIDLLKDKQALQRLTEAAEKAKIELSsltqtsislpfitATADGPKHID------ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 338 dfkAKVTRVEFEELCADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKEElGKNINADEAAAM 417
Cdd:PLN03184 330 ---TTLTRAKFEELCSDLLDRCKTPVENALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKLTGKDP-NVTVNPDEVVAL 405
|
410
....*....|
gi 5453832 418 GAVYQAAALS 427
Cdd:PLN03184 406 GAAVQAGVLA 415
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
35-627 |
1.97e-46 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 177.57 E-value: 1.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 35 VMSVDLGSESMKVAIVKPGVPmEIVLNKESRRKTPVIVTLKENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNPHVa 114
Cdd:PTZ00186 29 VIGVDLGTTYSCVATMDGDKA-RVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEHI- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 115 lyqarfpEHELTFDPQR------QTVHFQISSQLQFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAV 188
Cdd:PTZ00186 107 -------QKDIKNVPYKivragnGDAWVQDGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQAT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 189 LQAARMAGLKVLQLINDNTATALSYGVFRRKDinttaQNIMFYDMGSGstvctivTYQMVKTKEAGmqPQLQIRGVGFDR 268
Cdd:PTZ00186 180 KDAGTIAGLNVIRVVNEPTAAALAYGMDKTKD-----SLIAVYDLGGG-------TFDISVLEIAG--GVFEVKATNGDT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 269 TLGGLEMELRLRERLAGLF---------NEQRKGQRAKDVRENPRAMAKLLREANRLKTVLSANADHMAQIEglmddvdf 339
Cdd:PTZ00186 246 HLGGEDFDLALSDYILEEFrktsgidlsKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADGAQHIQ-------- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 340 kAKVTRVEFEELCADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKEELgKNINADEAAAMGA 419
Cdd:PTZ00186 318 -MHISRSKFEGITQRLIERSIAPCKQCMKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFFQKDPF-RGVNPDEAVALGA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 420 VYQAAALSKafKVKPFVVRDavVYPILVeftreveeepGIHSLKHnkrvLFSRMGP----YPQRKVITFNRYSHdfnfhi 495
Cdd:PTZ00186 396 ATLGGVLRG--DVKGLVLLD--VTPLSL----------GIETLGG----VFTRMIPknttIPTKKSQTFSTAAD------ 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 496 NYGDLGFLGPEDLRVFGSQN--LTTVKLKGVGDSFKKYPDyeskgIKAHFNLDESGVLSLdrvesvfetlvedSAEEEST 573
Cdd:PTZ00186 452 NQTQVGIKVFQGEREMAADNqmMGQFDLVGIPPAPRGVPQ-----IEVTFDIDANGICHV-------------TAKDKAT 513
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 5453832 574 LTKLGNTISSlfGGGTTPDAKENgtdtVQEEEESPAEGSKDEPgEQVELKEEAE 627
Cdd:PTZ00186 514 GKTQNITITA--NGGLSKEQIEQ----MIRDSEQHAEADRVKR-ELVEVRNNAE 560
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
35-628 |
2.08e-46 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 176.84 E-value: 2.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 35 VMSVDLGSESMKVAIVKPGVPmEIVLNKESRRKTPVIVTL-KENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNPHV 113
Cdd:CHL00094 4 VVGIDLGTTNSVVAVMEGGKP-TVIPNAEGFRTTPSIVAYtKKGDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSEISE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 114 ALYQARFPeheLTFDPQrQTVHFQISS-QLQFSPEEVLGMVLnysRSLAED---FAEQPIKDAVITVPVFFNQAERRAVL 189
Cdd:CHL00094 83 EAKQVSYK---VKTDSN-GNIKIECPAlNKDFSPEEISAQVL---RKLVEDaskYLGETVTQAVITVPAYFNDSQRQATK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 190 QAARMAGLKVLQLINDNTATALSYGVFRRKdiNTTaqnIMFYDMGSGSTVCTIV-----TYQMVKTkeAGmqpqlqirgv 264
Cdd:CHL00094 156 DAGKIAGLEVLRIINEPTAASLAYGLDKKN--NET---ILVFDLGGGTFDVSILevgdgVFEVLST--SG---------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 265 gfDRTLGGLEMELRLRERLAGLFneqrKGQRAKDVRENPRAMAKLLREANRLKTVLS-------------ANADHMAQIE 331
Cdd:CHL00094 219 --DTHLGGDDFDKKIVNWLIKEF----KKKEGIDLSKDRQALQRLTEAAEKAKIELSnltqteinlpfitATQTGPKHIE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 332 glmddvdfkAKVTRVEFEELCADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKeELGKNINA 411
Cdd:CHL00094 293 ---------KTLTRAKFEELCSDLINRCRIPVENALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLLGK-KPNQSVNP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 412 DEAAAMGAVYQAAALskAFKVKPFVVRDavVYPIlvefTREVEEEPGIHSlkhnkrVLFSRMGPYPQRKVITFNRYSH-- 489
Cdd:CHL00094 363 DEVVAIGAAVQAGVL--AGEVKDILLLD--VTPL----SLGVETLGGVMT------KIIPRNTTIPTKKSEVFSTAVDnq 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 490 -DFNFHINYGDLGFlgpedlrVFGSQNLTTVKLKGVGDSFKKYPDyeskgIKAHFNLDESGVLSLdrvesvfetlvedSA 568
Cdd:CHL00094 429 tNVEIHVLQGEREL-------AKDNKSLGTFRLDGIPPAPRGVPQ-----IEVTFDIDANGILSV-------------TA 483
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 569 EEESTLTKLGNTISslfGGGTTPdaKENGTDTVQEEEESPAEGSKDEpgEQVELKEEAEA 628
Cdd:CHL00094 484 KDKGTGKEQSITIQ---GASTLP--KDEVERMVKEAEKNAAEDKEKR--EKIDLKNQAES 536
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
35-431 |
1.52e-44 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 171.93 E-value: 1.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 35 VMSVDLGSESMKVAIVKPGVPmEIVLNKESRRKTPVIVTL-KENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNPHV 113
Cdd:PTZ00400 43 IVGIDLGTTNSCVAIMEGSQP-KVIENSEGMRTTPSVVAFtEDGQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEDAT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 114 ALYQARFPeHELTFDPQRQTvhfQISSQ-LQFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVLQAA 192
Cdd:PTZ00400 122 KKEQKILP-YKIVRASNGDA---WIEAQgKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 193 RMAGLKVLQLINDNTATALSYGVFRrkdinTTAQNIMFYDMGSGSTVCTIvtyqmvktkeagmqpqLQIRGVGF------ 266
Cdd:PTZ00400 198 KIAGLDVLRIINEPTAAALAFGMDK-----NDGKTIAVYDLGGGTFDISI----------------LEILGGVFevkatn 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 267 -DRTLGGLEMELRLRERLAGLFneqrKGQRAKDVRENPRAMAKLLREANRLKTVLSANADHMAQIEGLMDDVD----FKA 341
Cdd:PTZ00400 257 gNTSLGGEDFDQRILNYLIAEF----KKQQGIDLKKDKLALQRLREAAETAKIELSSKTQTEINLPFITADQSgpkhLQI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 342 KVTRVEFEELCADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKEElGKNINADEAAAMGAVY 421
Cdd:PTZ00400 333 KLSRAKLEELTHDLLKKTIEPCEKCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIFGKEP-SKGVNPDEAVAMGAAI 411
|
410
....*....|
gi 5453832 422 QAAALSKAFK 431
Cdd:PTZ00400 412 QAGVLKGEIK 421
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
33-426 |
2.91e-39 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 155.33 E-value: 2.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 33 LAVmSVDLGSESMKVAIVKPGVPmEIVLNKESRRKTPVIVTLKENERFFGDSAASMAIKNPKATLRYFQHLLGKQADNPh 112
Cdd:PRK05183 20 LAV-GIDLGTTNSLVATVRSGQA-EVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKNTISSVKRFMGRSLADI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 113 valyQARFPEHELTFD------PQRQTVhfqissQLQFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERR 186
Cdd:PRK05183 97 ----QQRYPHLPYQFVasengmPLIRTA------QGLKSPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 187 AVLQAARMAGLKVLQLINDNTATALSYGVfrrkDiNTTAQNIMFYDMGSGSTVCTIvtyqmvktkeagmqpqLQI-RGV- 264
Cdd:PRK05183 167 ATKDAARLAGLNVLRLLNEPTAAAIAYGL----D-SGQEGVIAVYDLGGGTFDISI----------------LRLsKGVf 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 265 -----GFDRTLGGLEMELRLRERL---AGLfneqrkgqrakDVRENPRAMAKLLREANRLKTVLSANADHMAQIeglmdd 336
Cdd:PRK05183 226 evlatGGDSALGGDDFDHLLADWIleqAGL-----------SPRLDPEDQRLLLDAARAAKEALSDADSVEVSV------ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 337 VDFKAKVTRVEFEELCADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKEELgKNINADEAAA 416
Cdd:PRK05183 289 ALWQGEITREQFNALIAPLVKRTLLACRRALRDAGVEADEVKEVVMVGGSTRVPLVREAVGEFFGRTPL-TSIDPDKVVA 367
|
410
....*....|
gi 5453832 417 MGAVYQAAAL 426
Cdd:PRK05183 368 IGAAIQADIL 377
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
128-421 |
1.01e-32 |
|
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family chaperones assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some HSP70 family members are not chaperones but instead, function as NEFs to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle, some may function as both chaperones and NEFs. The HSP70 family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466811 [Multi-domain] Cd Length: 329 Bit Score: 129.92 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 128 DPQRQTVHFQISSQLQFSpEEVLGMVLNYSR---SLAEDFAEQPIKDAVITVPVFFNQAERRAVLQAARMAGLK----VL 200
Cdd:cd10170 31 WPGGDGGSSKVPSVLEVV-ADFLRALLEHAKaelGDRIWELEKAPIEVVITVPAGWSDAAREALREAARAAGFGsdsdNV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 201 QLINDNTATALSYgvFRRKDINTTAQ---NIMFYDMGsGSTVCtIVTYQMVKTKeagmQPQLQIRGVGFDRTLGGLEMEL 277
Cdd:cd10170 110 RLVSEPEAAALYA--LEDKGDLLPLKpgdVVLVCDAG-GGTVD-LSLYEVTSGS----PLLLEEVAPGGGALLGGTDIDE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 278 RLRERLAGLFneqrKGQRAKDVRENPRAMAKLLREANRLKTVLSANADHMAQIEGLMDDVDFKA---KVTRVEFEELCAD 354
Cdd:cd10170 182 AFEKLLREKL----GDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGLPELgleKGTLLLTEEEIRD 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5453832 355 LFERVPGPVQQALQSA--EMSLDEIEQVILVGGATRVPRVQEVLLKAVGKEELG---KNINADEAAAMGAVY 421
Cdd:cd10170 258 LFDPVIDKILELIEEQleAKSGTPPDAVVLVGGFSRSPYLRERLRERFGSAGIIivlRSDDPDTAVARGAAL 329
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
35-426 |
1.26e-25 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 113.03 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 35 VMSVDLGSESMKVAIvKPGVPMEIVLNKESRRKTPVIVTLKENerffgdsaaSMAIKNPKAtLRYFQHLLGKQADnpHVA 114
Cdd:PRK01433 21 AVGIDFGTTNSLIAI-ATNRKVKVIKSIDDKELIPTTIDFTSN---------NFTIGNNKG-LRSIKRLFGKTLK--EIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 115 LYQARFPEHELTFDPQRQTVHFQISSQlQFSPEEVLGMVLNYSRSLAEDFAEQPIKDAVITVPVFFNQAERRAVLQAARM 194
Cdd:PRK01433 88 NTPALFSLVKDYLDVNSSELKLNFANK-QLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLAAKI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 195 AGLKVLQLINDNTATALSYGVfrrkDINTTAQNIMfYDMGSGSTVCTIVTYQmvktkeagmQPQLQIRGVGFDRTLGGLE 274
Cdd:PRK01433 167 AGFEVLRLIAEPTAAAYAYGL----NKNQKGCYLV-YDLGGGTFDVSILNIQ---------EGIFQVIATNGDNMLGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 275 MELRLRERLAGLF---NEQRKGQRAKDVRENpramakLLREANRLKTVLSanadhmaqieglmddvdfkakVTRVEFEEL 351
Cdd:PRK01433 233 IDVVITQYLCNKFdlpNSIDTLQLAKKAKET------LTYKDSFNNDNIS---------------------INKQTLEQL 285
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5453832 352 CADLFERVPGPVQQALQSAEMslDEIEQVILVGGATRVPRVQEVLLKAVgKEELGKNINADEAAAMGAVYQAAAL 426
Cdd:PRK01433 286 ILPLVERTINIAQECLEQAGN--PNIDGVILVGGATRIPLIKDELYKAF-KVDILSDIDPDKAVVWGAALQAENL 357
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
78-405 |
8.75e-13 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar proteins; The family includes a group of uncharacterized proteins similar to Escherichia coli chaperone protein YegD that belongs to the heat shock protein 70 family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. YegD lacks the SBD. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some family members are not chaperones but instead, function as NEFs for their Hsp70 partners, other family members function as both chaperones and NEFs.
Pssm-ID: 466829 [Multi-domain] Cd Length: 409 Bit Score: 71.54 E-value: 8.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 78 ERFFGDSAASMAIKNPkATLRYFQhllgkqadNPHVALYQARFPEheltfdpqrQTVHFQissqlQFSPEEVLGMVLNYS 157
Cdd:cd10231 48 SIYFGNDAIDAYLNDP-EEGRLIK--------SVKSFLGSSLFDE---------TTIFGR-----RYPFEDLVAAILRHL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 158 RSLAEDFAEQPIKDAVITVPVFF--------NQAERRaVLQAARMAGLKVLQLINDNTATALSYgvfrrKDINTTAQNIM 229
Cdd:cd10231 105 KRRAERQLGEEIDSVVVGRPVHFsgvgaeddAQAESR-LRDAARRAGFRNVEFQYEPIAAALDY-----EQRLDREELVL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 230 FYDMGSGSTVCTIVtyQMVKTKEAGMQPQLQIRGVG-----FDRTL------------GGLEMELRLRERLAGLFNE--- 289
Cdd:cd10231 179 VVDFGGGTSDFSVL--RLGPNRTDRRADILATSGVGiggddFDRELalkkvmphlgrgSTYVSGDKGLPVPAWLYADlsn 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 290 --------QRKGQRAK-----DVRENPRAMA-----------KLLREANRLKTVLS-ANADHMAqieglMDDVD--FKAK 342
Cdd:cd10231 257 whaisllyTKKTLRLLldlrrDAADPEKIERllslvedqlghRLFRAVEQAKIALSsADEATLS-----FDFIEisIKVT 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5453832 343 VTRVEFEELCADLFERVPGPVQQALQSAEMSLDEIEQVILVGGATRVPRVQEVLLKAVGKEEL 405
Cdd:cd10231 332 ITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRVFLTGGSSQSPAVRQALASLFGQARL 394
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
34-421 |
6.28e-06 |
|
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: 49.58 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 34 AVMSVDLGSESMKVAIVKPGVPMEIVLNK--------ESRRKTPVIVTLKENERF--FGDSAASmaiknpkatlRYFQHl 103
Cdd:cd10229 1 VVVAIDFGTTYSGYAYSFITDPGDIHTMYnwwgaptgVSSPKTPTCLLLNPDGEFhsFGYEARE----------KYSDL- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 104 lgkQADNPHVALYQARFPEHELTFDPQRQTVHFQISSQLQFSPEEVLGMVLNYSRSLA----EDFAEQPIKDA----VIT 175
Cdd:cd10229 70 ---AEDEEHQWLYFFKFKMMLLSEKELTRDTKVKAVNGKSMPALEVFAEALRYLKDHAlkelRDRSGSSLDEDdirwVLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 176 VPVFFNQAERRAVLQAARMAGL------KVLQLINDNTATALSYgvfrRKDINTTAQNIMF----Y---DMGsGSTVcTI 242
Cdd:cd10229 147 VPAIWSDAAKQFMREAAVKAGLiseensEQLIIALEPEAAALYC----QKLLAEGEEKELKpgdkYlvvDCG-GGTV-DI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 243 VTYQMV---KTKEAgmqpqLQIRGVGFdrtlGGLEMELRLRERLAGLF-NEQRKGQRakdvRENPRAMAKLLREANRLKt 318
Cdd:cd10229 221 TVHEVLedgKLEEL-----LKASGGPW----GSTSVDEEFEELLEEIFgDDFMEAFK----QKYPSDYLDLLQAFERKK- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 319 vlsanadhmaqieglmddVDFKAKVTRVEFEELCADLFERVPGPVQQALQSAEMslDEIEQVILVGGATRVPRVQEVLLK 398
Cdd:cd10229 287 ------------------RSFKLRLSPELMKSLFDPVVKKIIEHIKELLEKPEL--KGVDYIFLVGGFAESPYLQKAVKE 346
|
410 420
....*....|....*....|....*..
gi 5453832 399 AVGKEelgKNI----NADEAAAMGAVY 421
Cdd:cd10229 347 AFSTK---VKIiippEPGLAVVKGAVL 370
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
593-694 |
1.27e-05 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 48.82 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 593 AKENGTDTVQEEEESPAEGSKDEPGEQVELKEEAEAPVEDGSQPPPPEPKgDATPEGEKATEKENGDKSE----AQKPSE 668
Cdd:PRK13108 353 ADRDGESTPAVEETSEADIEREQPGDLAGQAPAAHQVDAEAASAAPEEPA-ALASEAHDETEPEVPEKAApipdPAKPDE 431
|
90 100
....*....|....*....|....*...
gi 5453832 669 KAEAGPEGVAPAPEGEKKQK--PARKRR 694
Cdd:PRK13108 432 LAVAGPGDDPAEPDGIRRQDdfSSRRRR 459
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
586-694 |
4.09e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 47.27 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 586 GGGTTPDAKENGTDTVQEEEESPAEGSKDEPGEQVELKEEAEAPVEDGSQPPPPEPKGDATPEGEKATEKENGDKSEAQK 665
Cdd:PHA03169 135 SPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEP 214
|
90 100
....*....|....*....|....*....
gi 5453832 666 PSEKAEAGPEGvAPAPEGEKKQKPARKRR 694
Cdd:PHA03169 215 QSPTPQQAPSP-NTQQAVEHEDEPTEPER 242
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
586-690 |
6.09e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 46.50 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 586 GGGTTPDAKENGTDTvQEEEESPAEGSKDEPGEQvelkeeAEAPVEDGSQPPPPEPKGDATPEGEKATEKENGDKSEAQK 665
Cdd:PHA03169 115 ASGLSPENTSGSSPE-SPASHSPPPSPPSHPGPH------EPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEP 187
|
90 100
....*....|....*....|....*
gi 5453832 666 PSEKAEAGPEGVAPAPEGEKKQKPA 690
Cdd:PHA03169 188 DSPGPPQSETPTSSPPPQSPPDEPG 212
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
587-683 |
6.41e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 46.50 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 587 GGTTPDAKENGTDTVQEEEESPAEGSKDEPGEQVELKEEAEAPVEDGS-QPPPPEPKGDATPEGEKATEKENGDKSEaqk 665
Cdd:PHA03169 156 NPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPpQSPPDEPGEPQSPTPQQAPSPNTQQAVE--- 232
|
90
....*....|....*...
gi 5453832 666 pSEKAEAGPEGVAPAPEG 683
Cdd:PHA03169 233 -HEDEPTEPEREGPPFPG 249
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
565-683 |
5.12e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 43.81 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 565 EDSAEEESTLTKLGNTISSLFGGGTTPDA-KENGTDTVQEEEESPAEGSKDE-----PGEQVElkEEAEAPVEDGSQPPP 638
Cdd:PHA03169 102 SPTPSPSGSAEELASGLSPENTSGSSPESpASHSPPPSPPSHPGPHEPAPPEshnpsPNQQPS--SFLQPSHEDSPEEPE 179
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 5453832 639 -----PEPKGDATPEGEKATEKENGdKSEAQKPSEKAEAGPEGvAPAPEG 683
Cdd:PHA03169 180 pptsePEPDSPGPPQSETPTSSPPP-QSPPDEPGEPQSPTPQQ-APSPNT 227
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
596-689 |
6.03e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 43.42 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 596 NGTDTVQEEEESPAEGSKDEPGEQVELKEEAEAPVEDGSQPPPPEPKGDATPeGEKATEKENGDKSEAQKPSEKAEAGPE 675
Cdd:PHA03169 95 SGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGP-HEPAPPESHNPSPNQQPSSFLQPSHED 173
|
90
....*....|....
gi 5453832 676 GVAPAPEGEKKQKP 689
Cdd:PHA03169 174 SPEEPEPPTSEPEP 187
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
172-243 |
1.78e-03 |
|
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: 41.69 E-value: 1.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5453832 172 AVITVPVFFNQAERRAVLQAARMAGLKVLQLINDNTATALSYGVfrrkDInTTAQNIMFYDMGSGSTVCTIV 243
Cdd:cd10225 94 VVIGVPSGITEVERRAVKEAAEHAGAREVYLIEEPMAAAIGAGL----PI-EEPRGSMVVDIGGGTTEIAVI 160
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
36-243 |
2.42e-03 |
|
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.
Pssm-ID: 466899 [Multi-domain] Cd Length: 339 Bit Score: 41.11 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 36 MSVDLGSESMKVAIVKPG-------------VPMEIVLNKESRRKTPVIVTLKE--NERFFGDSAASMAIKNPKATLRYF 100
Cdd:cd24049 1 LGIDIGSSSIKAVELKRSggglvlvafaiipLPEGAIVDGEIADPEALAEALKKllKENKIKGKKVVVALPGSDVIVRTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 101 QhllgkqadNPHValyqarfPEHELtfdpqRQTVHFQISSQLQFSPEEVlgmVLNYSRsLAEDFAEQPIKDAVITVpvff 180
Cdd:cd24049 81 K--------LPKM-------PEKEL-----EEAIRFEAEQYLPFPLEEV---VLDYQI-LGEVEEGGEKLEVLVVA---- 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5453832 181 nqAERRAV---LQAARMAGLKVLQLinDNTATALSYgVFRRKDINTTAQNIMFYDMGSGSTVCTIV 243
Cdd:cd24049 133 --APKEIVesyLELLKEAGLKPVAI--DVESFALAR-ALEYLLPDEEEETVALLDIGASSTTLVIV 193
|
|
| motB |
PRK05996 |
MotB family protein; |
610-700 |
3.18e-03 |
|
MotB family protein;
Pssm-ID: 235665 [Multi-domain] Cd Length: 423 Bit Score: 41.22 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 610 EGSKDEPGEQVELKEEAEAPVEDGSQPPPPEPKGDATPEGEKATEKengDKSEAQKPSEKAEAGPEGvaPAPEGEKKQKP 689
Cdd:PRK05996 201 PGQAREQAQGAKSATAAPATVPQAAPLPQAQPKKAATEEELIADAK---KAATGEPAANAAKAAKPE--PMPDDQQKEAE 275
|
90
....*....|.
gi 5453832 690 ARKRRMVEEIG 700
Cdd:PRK05996 276 QLQAAIAQAIG 286
|
|
| PHA00666 |
PHA00666 |
putative protease |
601-739 |
3.29e-03 |
|
putative protease
Pssm-ID: 222808 [Multi-domain] Cd Length: 233 Bit Score: 40.41 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 601 VQEEEESPAEGSKDEPgeqvelkeeaeAPVEDGSQPPPPEPK---GDATPEGEKateKENGDKSEAQKPSEKAEAGPEGV 677
Cdd:PHA00666 22 SQPAASEPAAGAGDNP-----------APQGDPTQEEGDKPQpaaGADKPEGDK---KADGDKPEEKKPGEKPEGAPEKY 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5453832 678 A-PAPEGEKKQKPARKRrmVEEIGVELvvldlpDLPEDKlaqsVQKLQDLTLRDLEKQEREKA 739
Cdd:PHA00666 88 EfQAAEGVELDTGALGA--FEPVAREL------NLTNEQ----AQKVVDLYTKILPVVQQRQA 138
|
|
| COG5373 |
COG5373 |
Uncharacterized membrane protein [Function unknown]; |
621-700 |
4.26e-03 |
|
Uncharacterized membrane protein [Function unknown];
Pssm-ID: 444140 [Multi-domain] Cd Length: 854 Bit Score: 41.14 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 621 ELKEEAEAPVEDGSQPPPPEPKGDATPEGEK-ATEKENGDKSEAQKPSEKAEAGPEGVAPAPEGEKKQKPARKRRMVEEI 699
Cdd:COG5373 32 ELEAELAEAAEAASAPAEPEPEAAAAATAAApEAAPAPVPEAPAAPPAAAEAPAPAAAAPPAEAEPAAAPAAASSFEEWL 111
|
.
gi 5453832 700 G 700
Cdd:COG5373 112 G 112
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
605-694 |
6.17e-03 |
|
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.
Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 40.14 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453832 605 EESPAEGSKDEPGEQVELKEEAEAPVEDGSQPPPPEPKGDATPEGEKATEKEN------------GDKSEAQKPSEKAEA 672
Cdd:NF040712 224 EGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDageppapgaaetPEAAEPPAPAPAAPA 303
|
90 100
....*....|....*....|....*
gi 5453832 673 G---PEGVAPAPEGEKKQKPARKRR 694
Cdd:NF040712 304 ApaaPEAEEPARPEPPPAPKPKRRR 328
|
|
| |
