|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
1-612 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 1159.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 1 MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDD 80
Cdd:PTZ00009 1 MTKGPAIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 81 PVVHSDMKHWPFNVINDG-GRPKVQVEYKGETKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATK 159
Cdd:PTZ00009 81 SVVQSDMKHWPFKVTTGGdDKPMIEVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 160 DAGTISGLNVLRIINEPTAAAIAYGLDKKVGSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVN 239
Cdd:PTZ00009 161 DAGTIAGLNVLRIINEPTAAAIAYGLDKKGDGEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 240 HFVGEFKRKHK-KDITENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSLTRARFEELNADLFRGTLEPVE 318
Cdd:PTZ00009 241 FCVQDFKRKNRgKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 319 KALRDAKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFNGRELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTP 398
Cdd:PTZ00009 321 KVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGEQSSQVQDLLLLDVTP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 399 LSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVFEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTF 478
Cdd:PTZ00009 401 LSLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 479 DIDANGIMNVSAVDKSTGKENKITITNDKGRLSKDEIERMVQEADRYKTEDEAQRDKISAKNSLESLAFNMKSTVEDEKL 558
Cdd:PTZ00009 481 DIDANGILNVSAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDEKV 560
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 291290899 559 KDKISQEDKQKILDKCNEVISWLDRNQMAEKEEYEHQQKELQNLCNPIITKLYQ 612
Cdd:PTZ00009 561 KGKLSDSDKATIEKAIDEALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMYQ 614
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
6-612 |
0e+00 |
|
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: 941.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDPVVHS 85
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 86 DMKHWPFNVIND-GGRPKVQVEYKGETktFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTI 164
Cdd:pfam00012 81 DIKHLPYKVVKLpNGDAGVEVRYLGET--FTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 165 SGLNVLRIINEPTAAAIAYGLDKKvGSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFVGE 244
Cdd:pfam00012 159 AGLNVLRIVNEPTAAALAYGLDKT-DKERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 245 FKRKHKKDITENKRAVRRLRTACERAKRTLSS-STQASIEIDSLYE-GIDFYTSLTRARFEELNADLFRGTLEPVEKALR 322
Cdd:pfam00012 238 FKKKYGIDLSKDKRALQRLREAAEKAKIELSSnQTNINLPFITAMAdGKDVSGTLTRAKFEELVADLFERTLEPVEKALK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 323 DAKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSGDksENVQDLLLLDVTPLSLG 402
Cdd:pfam00012 318 DAGLSKSEIDEVVLVGGSTRIPAVQELVKEFF-GKEPSKGVNPDEAVAIGAAVQAGVLSGT--FDVKDFLLLDVTPLSLG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 403 IETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVFEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDA 482
Cdd:pfam00012 395 IETLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 483 NGIMNVSAVDKSTGKENKITITNDKGrLSKDEIERMVQEADRYKTEDEAQRDKISAKNSLESLAFNMKSTVEDEklKDKI 562
Cdd:pfam00012 475 NGILTVSAKDKGTGKEQEITIEASEG-LSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEE--GDKV 551
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 291290899 563 SQEDKQKIldkcNEVISWLDRN-QMAEKEEYEHQQKELQNLCNPIITKLYQ 612
Cdd:pfam00012 552 PEAEKSKV----ESAIEWLKDElEGDDKEEIEAKTEELAQVSQKIGERMYQ 598
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
6-380 |
0e+00 |
|
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: 909.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDPVVHS 85
Cdd:cd10233 1 AIGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 86 DMKHWPFNVINDGGRPKVQVEYKGETKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTIS 165
Cdd:cd10233 81 DMKHWPFKVVSGGDKPKIQVEYKGETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 166 GLNVLRIINEPTAAAIAYGLDKKVGSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFVGEF 245
Cdd:cd10233 161 GLNVLRIINEPTAAAIAYGLDKKGKGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 246 KRKHKKDITENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSLTRARFEELNADLFRGTLEPVEKALRDAK 325
Cdd:cd10233 241 KRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELCADLFRSTLEPVEKVLRDAK 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 291290899 326 MDKAQIHDIVLVGGSTRIPKIQKLLQDFFNGRELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd10233 321 LDKSQIHEIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
1-612 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 871.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 1 MSKgpAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTVFDAKRLIGRRfd 79
Cdd:PRK00290 1 MGK--IIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRLMGRR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 80 DPVVHSDMKHWPFNVIN-DGGRPKVQVEykgeTKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQAT 158
Cdd:PRK00290 77 DEEVQKDIKLVPYKIVKaDNGDAWVEID----GKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQAT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 159 KDAGTISGLNVLRIINEPTAAAIAYGLDKKvgSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMV 238
Cdd:PRK00290 153 KDAGKIAGLEVLRIINEPTAAALAYGLDKK--GDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRII 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 239 NHFVGEFKRKHKKDITENKRAVRRLRTACERAKRTLSSSTQASIeidSLyegiDFYT-----------SLTRARFEELNA 307
Cdd:PRK00290 231 DYLADEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEI---NL----PFITadasgpkhleiKLTRAKFEELTE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 308 DLFRGTLEPVEKALRDAKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSGDksen 387
Cdd:PRK00290 304 DLVERTIEPCKQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLAGD---- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 388 VQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVFEGERAMTKDNNLLGKFELTGIPPA 467
Cdd:PRK00290 379 VKDVLLLDVTPLSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPA 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 468 PRGVPQIEVTFDIDANGIMNVSAVDKSTGKENKITITNDKGrLSKDEIERMVQEADRYKTEDEAQRDKISAKNSLESLAF 547
Cdd:PRK00290 459 PRGVPQIEVTFDIDANGIVHVSAKDKGTGKEQSITITASSG-LSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIY 537
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291290899 548 NMKSTVEDekLKDKISQEDKQKILDKCNEVISWLDRNqmaEKEEYEHQQKELQNLCNPIITKLYQ 612
Cdd:PRK00290 538 QTEKTLKE--LGDKVPADEKEKIEAAIKELKEALKGE---DKEAIKAKTEELTQASQKLGEAMYQ 597
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
6-612 |
0e+00 |
|
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE chaperone system. All members of the seed alignment were taken from completely sequenced bacterial or archaeal genomes and (except for Mycoplasma sequence) found clustered with other genes of this systems. This model excludes DnaK homologs that are not DnaK itself, such as the heat shock cognate protein HscA (TIGR01991). However, it is not designed to distinguish among DnaK paralogs in eukaryotes. Note that a number of dnaK genes have shadow ORFs in the same reverse (relative to dnaK) reading frame, a few of which have been assigned glutamate dehydrogenase activity. The significance of this observation is unclear; lengths of such shadow ORFs are highly variable as if the presumptive protein product is not conserved. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274091 [Multi-domain] Cd Length: 595 Bit Score: 801.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDpvVH 84
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNgERLVGQPAKRQAVTNPENTIYSIKRFMGRRFDE--VT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 85 SDMKHWPFNVINDGGRPKVQVEykgeTKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTI 164
Cdd:TIGR02350 80 EEAKRVPYKVVGDGGDVRVKVD----GKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 165 SGLNVLRIINEPTAAAIAYGLDKKVGSERnVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFVGE 244
Cdd:TIGR02350 156 AGLEVLRIINEPTAAALAYGLDKSKKDEK-ILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 245 FKRKHKKDITENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGID----FYTSLTRARFEELNADLFRGTLEPVEKA 320
Cdd:TIGR02350 235 FKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINLPFITADASgpkhLEMTLTRAKFEELTADLVERTKEPVRQA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 321 LRDAKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSGDksenVQDLLLLDVTPLS 400
Cdd:TIGR02350 315 LKDAGLSASDIDEVILVGGSTRIPAVQELVKDFF-GKEPNKSVNPDEVVAIGAAIQGGVLKGD----VKDVLLLDVTPLS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 401 LGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVFEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDI 480
Cdd:TIGR02350 390 LGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 481 DANGIMNVSAVDKSTGKENKITITNDKGrLSKDEIERMVQEADRYKTEDEAQRDKISAKNSLESLAFNMKSTVEDekLKD 560
Cdd:TIGR02350 470 DANGILHVSAKDKGTGKEQSITITASSG-LSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKE--AGD 546
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 291290899 561 KISQEDKQKILDKCNEVISWLDRNQMAEKEEyehQQKELQNLCNPIITKLYQ 612
Cdd:TIGR02350 547 KLPAEEKEKIEKAVAELKEALKGEDVEEIKA---KTEELQQALQKLAEAMYQ 595
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
4-380 |
0e+00 |
|
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: 752.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 4 GPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDPVV 83
Cdd:cd10241 1 GTVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 84 HSDMKHWPFNVINDGGRPKVQVEYKGETKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGT 163
Cdd:cd10241 81 QKDIKLLPFKIVNKNGKPYIQVEVKGEKKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 164 ISGLNVLRIINEPTAAAIAYGLDKKvGSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFVG 243
Cdd:cd10241 161 IAGLNVLRIINEPTAAAIAYGLDKK-GGEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFIK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 244 EFKRKHKKDITENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSLTRARFEELNADLFRGTLEPVEKALRD 323
Cdd:cd10241 240 LFKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGEDFSETLTRAKFEELNMDLFRKTLKPVQKVLED 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 291290899 324 AKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFNGRELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd10241 320 AGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFNGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
6-380 |
0e+00 |
|
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: 746.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDPVVHS 85
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 86 DMKHWPFNVINDG-GRPKVQVEYKGETKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTI 164
Cdd:cd24028 81 DIKHWPFKVVEDEdGKPKIEVTYKGEEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAATI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 165 SGLNVLRIINEPTAAAIAYGLDKKVGSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFVGE 244
Cdd:cd24028 161 AGLNVLRIINEPTAAALAYGLDKKSSGERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLVEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 245 FKRKHKKDITENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSLTRARFEELNADLFRGTLEPVEKALRDA 324
Cdd:cd24028 241 FKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGIDFETTITRAKFEELCEDLFKKCLEPVEKVLKDA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 291290899 325 KMDKAQIHDIVLVGGSTRIPKIQKLLQDFFNGRELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd24028 321 KLSKDDIDEVVLVGGSTRIPKIQELLSEFFGGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
4-612 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 700.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 4 GPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDpv 82
Cdd:CHL00094 2 GKVVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKgDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 83 VHSDMKHWPFNVINDGgRPKVQVEYKGETKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAG 162
Cdd:CHL00094 80 ISEEAKQVSYKVKTDS-NGNIKIECPALNKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 163 TISGLNVLRIINEPTAAAIAYGLDKKvgSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFV 242
Cdd:CHL00094 159 KIAGLEVLRIINEPTAASLAYGLDKK--NNETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 243 GEFKRKHKKDITENKRAVRRLRTACERAKRTLSSSTQASIE---IDSLYEG-IDFYTSLTRARFEELNADLFRGTLEPVE 318
Cdd:CHL00094 237 KEFKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINlpfITATQTGpKHIEKTLTRAKFEELCSDLINRCRIPVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 319 KALRDAKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSGDksenVQDLLLLDVTP 398
Cdd:CHL00094 317 NALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLL-GKKPNQSVNPDEVVAIGAAVQAGVLAGE----VKDILLLDVTP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 399 LSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVFEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTF 478
Cdd:CHL00094 392 LSLGVETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 479 DIDANGIMNVSAVDKSTGKENKITITNdKGRLSKDEIERMVQEADRYKTEDEAQRDKISAKNSLESLAFNMKSTVEDekL 558
Cdd:CHL00094 472 DIDANGILSVTAKDKGTGKEQSITIQG-ASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKE--L 548
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 291290899 559 KDKISQEDKQKIldkcNEVISWLDRN-QMAEKEEYEHQQKELQNLCNPIITKLYQ 612
Cdd:CHL00094 549 KDKISEEKKEKI----ENLIKKLRQAlQNDNYESIKSLLEELQKALMEIGKEVYS 599
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
4-612 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 698.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 4 GPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDpv 82
Cdd:PRK13411 2 GKVIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSgDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDD-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 83 VHSDMKHWPFNVINdGGRPKVQVEYKGetKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAG 162
Cdd:PRK13411 80 TEEERSRVPYTCVK-GRDDTVNVQIRG--RNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 163 TISGLNVLRIINEPTAAAIAYGLDKKvGSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFV 242
Cdd:PRK13411 157 TIAGLEVLRIINEPTAAALAYGLDKQ-DQEQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWLV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 243 GEFKRKHKKDITENKRAVRRLRTACERAKRTLSSSTQASIEIDslyegidFYTS-----------LTRARFEELNADLFR 311
Cdd:PRK13411 236 ENFQQQEGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINLP-------FITAdetgpkhlemeLTRAKFEELTKDLVE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 312 GTLEPVEKALRDAKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFNGRELNKSINPDEAVAYGAAVQAAILSGDksenVQDL 391
Cdd:PRK13411 309 ATIEPMQQALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFGGKQPDRSVNPDEAVALGAAIQAGVLGGE----VKDL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 392 LLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVFEGERAMTKDNNLLGKFELTGIPPAPRGV 471
Cdd:PRK13411 385 LLLDVTPLSLGIETLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 472 PQIEVTFDIDANGIMNVSAVDKSTGKENKITITNdKGRLSKDEIERMVQEADRYKTEDEAQRDKISAKNSLESLAFNMKS 551
Cdd:PRK13411 465 PQIEVSFEIDVNGILKVSAQDQGTGREQSIRITN-TGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYES 543
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291290899 552 TVEDEklKDKISQEDKQKILDKCNEVISWLdRNQMAEKEEYEHQQKELQNLCNPIITKLYQ 612
Cdd:PRK13411 544 TLKEN--GELISEELKQRAEQKVEQLEAAL-TDPNISLEELKQQLEEFQQALLAIGAEVYQ 601
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
4-612 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 681.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 4 GPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDPV 82
Cdd:PTZ00400 41 GDIVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDgQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEDA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 83 VHSDMKHWPFNVINDGGRpKVQVEYKGetKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAG 162
Cdd:PTZ00400 121 TKKEQKILPYKIVRASNG-DAWIEAQG--KKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 163 TISGLNVLRIINEPTAAAIAYGLDKKVGseRNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFV 242
Cdd:PTZ00400 198 KIAGLDVLRIINEPTAAALAFGMDKNDG--KTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYLI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 243 GEFKRKHKKDITENKRAVRRLRTACERAKRTLSSSTQASIEIDslyegidFYTS-----------LTRARFEELNADLFR 311
Cdd:PTZ00400 276 AEFKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQTEINLP-------FITAdqsgpkhlqikLSRAKLEELTHDLLK 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 312 GTLEPVEKALRDAKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSGDksenVQDL 391
Cdd:PTZ00400 349 KTIEPCEKCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIF-GKEPSKGVNPDEAVAMGAAIQAGVLKGE----IKDL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 392 LLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVFEGERAMTKDNNLLGKFELTGIPPAPRGV 471
Cdd:PTZ00400 424 LLLDVTPLSLGIETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGV 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 472 PQIEVTFDIDANGIMNVSAVDKSTGKENKITITNDKGrLSKDEIERMVQEADRYKTEDEAQRDKISAKNSLESLAFNMKS 551
Cdd:PTZ00400 504 PQIEVTFDVDANGIMNISAVDKSTGKKQEITIQSSGG-LSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEK 582
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291290899 552 TVEDekLKDKISQEDKQKILDKCNEVISWLdrnQMAEKEEYEHQQKELQNLCNPIITKLYQ 612
Cdd:PTZ00400 583 QLSD--LKDKISDADKDELKQKITKLRSTL---SSEDVDSIKDKTKQLQEASWKISQQAYK 638
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
6-519 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 681.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDPvvh 84
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPkDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFDE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 85 sdmkhwpfnvindggrpkvQVEYKGETKTFyaEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTI 164
Cdd:COG0443 78 -------------------ATEVGGKRYSP--EEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 165 SGLNVLRIINEPTAAAIAYGLDKKvGSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFVGE 244
Cdd:COG0443 137 AGLEVLRLLNEPTAAALAYGLDKG-KEEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 245 FKRKHKKDITENKRAVRRLRTACERAKRTLSSSTQASIEIDsLYEGIDFYTSLTRARFEELNADLFRGTLEPVEKALRDA 324
Cdd:COG0443 216 FGKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINLP-FSGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 325 KMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSGDKSEnvqdlllLDVTPLSLGIE 404
Cdd:COG0443 295 GLSPSDIDAVLLVGGSTRMPAVRERVKELF-GKEPLKGVDPDEAVALGAAIQAGVLAGDVKD-------LDVTPLSLGIE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 405 TAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVFEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANG 484
Cdd:COG0443 367 TLGGVFTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANG 446
|
490 500 510
....*....|....*....|....*....|....*
gi 291290899 485 IMNVSAVDKSTGKENKITItndkgrlsKDEIERMV 519
Cdd:COG0443 447 ILSVSAKDLGTGKEQSITI--------KEEIERML 473
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
4-588 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 654.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 4 GPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDpv 82
Cdd:PRK13410 2 GRIVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTkDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 83 VHSDMKHWPFNV-INDGGrpKVQVEYKGETKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDA 161
Cdd:PRK13410 80 LDPESKRVPYTIrRNEQG--NVRIKCPRLEREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 162 GTISGLNVLRIINEPTAAAIAYGLDKkvGSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHF 241
Cdd:PRK13410 158 GRIAGLEVERILNEPTAAALAYGLDR--SSSQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 242 VGEFKRKHKKDITENKRAVRRLRTACERAKRTLS--SSTQASIE-IDSLYEG---IDfyTSLTRARFEELNADLFRGTLE 315
Cdd:PRK13410 236 AEQFLEKEGIDLRRDRQALQRLTEAAEKAKIELSgvSVTDISLPfITATEDGpkhIE--TRLDRKQFESLCGDLLDRLLR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 316 PVEKALRDAKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSGDksenVQDLLLLD 395
Cdd:PRK13410 314 PVKRALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLI-PREPNQNVNPDEVVAVGAAIQAGILAGE----LKDLLLLD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 396 VTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVFEGERAMTKDNNLLGKFELTGIPPAPRGVPQIE 475
Cdd:PRK13410 389 VTPLSLGLETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQ 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 476 VTFDIDANGIMNVSAVDKSTGKENKITITNdKGRLSKDEIERMVQEADRYKTEDEAQRDKISAKNSLESLAFNmkstvED 555
Cdd:PRK13410 469 VAFDIDANGILQVSATDRTTGREQSVTIQG-ASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQ-----AE 542
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 291290899 556 EKLKDkISQE--------DKQKILDKCNEVISWLDRNQMAE 588
Cdd:PRK13410 543 RRLRD-AALEfgpyfaerQRRAVESAMRDVQDSLEQDDDRE 582
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
6-380 |
0e+00 |
|
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: 642.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 6 AVGIDLGTTYSCVGVFQhGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDPVVHS 85
Cdd:cd24093 1 AIGIDLGTTYSCVATYE-SSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 86 DMKHWPFNVINDGGRPKVQVEYKGETKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTIS 165
Cdd:cd24093 80 DMKTWPFKVIDVNGNPVIEVQYLGETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 166 GLNVLRIINEPTAAAIAYGLD-KKVGSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFVGE 244
Cdd:cd24093 160 GLNVLRIINEPTAAAIAYGLGaGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 245 FKRKHKKDITENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSLTRARFEELNADLFRGTLEPVEKALRDA 324
Cdd:cd24093 240 FKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSITRARFEDLNAALFKSTLEPVEQVLKDA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 291290899 325 KMDKAQIHDIVLVGGSTRIPKIQKLLQDFFNGRELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd24093 320 KISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
7-577 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 633.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDpvVHS 85
Cdd:PLN03184 42 VGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNgDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSE--VDE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 86 DMKHWPFNVINDGGrPKVQVEYKGETKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTIS 165
Cdd:PLN03184 120 ESKQVSYRVVRDEN-GNVKLDCPAIGKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRIA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 166 GLNVLRIINEPTAAAIAYGLDKKvgSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFVGEF 245
Cdd:PLN03184 199 GLEVLRIINEPTAASLAYGFEKK--SNETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLASNF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 246 KRKHKKDITENKRAVRRLRTACERAKRTLSSSTQASIE---IDSLYEG---IDfyTSLTRARFEELNADLFRGTLEPVEK 319
Cdd:PLN03184 277 KKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISlpfITATADGpkhID--TTLTRAKFEELCSDLLDRCKTPVEN 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 320 ALRDAKMDKAQIHDIVLVGGSTRIPKIQKLLQDFfNGRELNKSINPDEAVAYGAAVQAAILSGDksenVQDLLLLDVTPL 399
Cdd:PLN03184 355 ALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKL-TGKDPNVTVNPDEVVALGAAVQAGVLAGE----VSDIVLLDVTPL 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 400 SLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVFEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFD 479
Cdd:PLN03184 430 SLGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFD 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 480 IDANGIMNVSAVDKSTGKENKITITNdKGRLSKDEIERMVQEADRYKTEDEAQRDKISAKNSLESLAFNMKSTVEDekLK 559
Cdd:PLN03184 510 IDANGILSVSATDKGTGKKQDITITG-ASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKE--LG 586
|
570
....*....|....*...
gi 291290899 560 DKISQEDKQKILDKCNEV 577
Cdd:PLN03184 587 DKVPADVKEKVEAKLKEL 604
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
3-600 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 588.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 3 KGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDPV 82
Cdd:PTZ00186 26 QGDVIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 83 VHSDMKHWPFNVINDG-GRPKVQveyKGETKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDA 161
Cdd:PTZ00186 106 IQKDIKNVPYKIVRAGnGDAWVQ---DGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 162 GTISGLNVLRIINEPTAAAIAYGLDKKVGSErnVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHF 241
Cdd:PTZ00186 183 GTIAGLNVIRVVNEPTAAALAYGMDKTKDSL--IAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 242 VGEFKRKHKKDITENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGID----FYTSLTRARFEELNADLFRGTLEPV 317
Cdd:PTZ00186 261 LEEFRKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADgaqhIQMHISRSKFEGITQRLIERSIAPC 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 318 EKALRDAKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSGDksenVQDLLLLDVT 397
Cdd:PTZ00186 341 KQCMKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFF-QKDPFRGVNPDEAVALGAATLGGVLRGD----VKGLVLLDVT 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 398 PLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVFEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVT 477
Cdd:PTZ00186 416 PLSLGIETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVT 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 478 FDIDANGIMNVSAVDKSTGKENKITITNDKGrLSKDEIERMVQEADRYKTEDEAQRDKISAKNSLESLAFNMKSTVEDEK 557
Cdd:PTZ00186 496 FDIDANGICHVTAKDKATGKTQNITITANGG-LSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGEWK 574
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 291290899 558 LKDKISQEDKQKILDKCNEVIswldRNQMAEKEEYEHQQKELQ 600
Cdd:PTZ00186 575 YVSDAEKENVKTLVAELRKAM----ENPNVAKDDLAAATDKLQ 613
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
6-545 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 552.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDpvVHS 85
Cdd:PRK05183 21 AVGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKNTISSVKRFMGRSLAD--IQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 86 DMKHWPFN-VINDGGRPKVQVeyKGETKTfyAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTI 164
Cdd:PRK05183 99 RYPHLPYQfVASENGMPLIRT--AQGLKS--PVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 165 SGLNVLRIINEPTAAAIAYGLDKkvGSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFVGE 244
Cdd:PRK05183 175 AGLNVLRLLNEPTAAAIAYGLDS--GQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWILEQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 245 FKRKHKKDITEnkraVRRLRTACERAKRTLSSSTQASIEIdSLYEGIdfytsLTRARFEELNADLFRGTLEPVEKALRDA 324
Cdd:PRK05183 253 AGLSPRLDPED----QRLLLDAARAAKEALSDADSVEVSV-ALWQGE-----ITREQFNALIAPLVKRTLLACRRALRDA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 325 KMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSGDKSENvqDLLLLDVTPLSLGIE 404
Cdd:PRK05183 323 GVEADEVKEVVMVGGSTRVPLVREAVGEFF-GRTPLTSIDPDKVVAIGAAIQADILAGNKPDS--DMLLLDVIPLSLGLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 405 TAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVFEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANG 484
Cdd:PRK05183 400 TMGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADG 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291290899 485 IMNVSAVDKSTGKENKITITNDKGrLSKDEIERMVQEADRYKTEDEAQR----DKISAKNSLESL 545
Cdd:PRK05183 480 LLSVTAMEKSTGVEASIQVKPSYG-LTDDEIARMLKDSMSHAEEDMQARalaeQKVEAERVLEAL 543
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
7-381 |
0e+00 |
|
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: 542.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDPVVHS 85
Cdd:cd10234 2 IGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 86 DMKHWPFNVINDGGrpkvqVEYKGETKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTIS 165
Cdd:cd10234 82 KQVPYPVVSAGNGD-----AWVEIGGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 166 GLNVLRIINEPTAAAIAYGLDKKvgSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFVGEF 245
Cdd:cd10234 157 GLEVLRIINEPTAAALAYGLDKK--KDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 246 KRKHKKDITENKRAVRRLRTACERAKRTLSSSTQASIE---IDSLYEG-IDFYTSLTRARFEELNADLFRGTLEPVEKAL 321
Cdd:cd10234 235 KKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLETEINlpfITADASGpKHLEMKLTRAKFEELTEDLVERTIEPVEQAL 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 322 RDAKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILS 381
Cdd:cd10234 315 KDAKLSPSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
6-570 |
0e+00 |
|
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act together as chaperones. HscA resembles DnaK but belongs in a separate clade. The apparent function is to aid assembly of iron-sulfur cluster proteins. Homologs from Buchnera and Wolbachia are clearly in the same clade but are highly derived and score lower than some examples of DnaK. [Protein fate, Protein folding and stabilization]
Pssm-ID: 273915 [Multi-domain] Cd Length: 599 Bit Score: 538.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAF-TDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDPVVH 84
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYlKDGGVEVGKEALAAAAEDPKNTISSVKRLMGRSIEDIKTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 85 SDMkhwPFNVINDGGRpKVQVEYKGETKTfyAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTI 164
Cdd:TIGR01991 81 SIL---PYRFVDGPGE-MVRLRTVQGTVT--PVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 165 SGLNVLRIINEPTAAAIAYGLDKkvGSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFVge 244
Cdd:TIGR01991 155 AGLNVLRLLNEPTAAAVAYGLDK--ASEGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWIL-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 245 fkRKHKKDITENKRAVRRLRTACERAKRTLSssTQASIEIDSLYEGIDFYTSLTRARFEELNADLFRGTLEPVEKALRDA 324
Cdd:TIGR01991 231 --KQLGISADLNPEDQRLLLQAARAAKEALT--DAESVEVDFTLDGKDFKGKLTRDEFEALIQPLVQKTLSICRRALRDA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 325 KMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSGDKSENvqDLLLLDVTPLSLGIE 404
Cdd:TIGR01991 307 GLSVEEIKGVVLVGGSTRMPLVRRAVAELF-GQEPLTDIDPDQVVALGAAIQADLLAGNRIGN--DLLLLDVTPLSLGIE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 405 TAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVFEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANG 484
Cdd:TIGR01991 384 TMGGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDADG 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 485 IMNVSAVDKSTGKENKITITNDKGrLSKDEIERMVQEADRYKTEDEAQR----DKISAKNSLESLAfnmKSTVEDEKLkd 560
Cdd:TIGR01991 464 LLTVSAQEQSTGVEQSIQVKPSYG-LSDEEIERMLKDSFKHAEEDMYARalaeQKVEAERILEALQ---AALAADGDL-- 537
|
570
....*....|
gi 291290899 561 kISQEDKQKI 570
Cdd:TIGR01991 538 -LSEDERAAI 546
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
4-380 |
1.12e-170 |
|
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: 491.78 E-value: 1.12e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 4 GPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDPV 82
Cdd:cd11733 1 GDVIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 83 VHSDMKHWPFNVI--NDGgrpKVQVEYKGetKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKD 160
Cdd:cd11733 81 VQKDIKMVPYKIVkaSNG---DAWVEAHG--KKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 161 AGTISGLNVLRIINEPTAAAIAYGLDKKvgSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNH 240
Cdd:cd11733 156 AGQIAGLNVLRIINEPTAAALAYGLDKK--DDKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 241 FVGEFKRKHKKDITENKRAVRRLRTACERAKRTLSSSTQAsiEIDSLYEGID------FYTSLTRARFEELNADLFRGTL 314
Cdd:cd11733 234 LVAEFKKEQGIDLSKDNLALQRLREAAEKAKIELSSSLQT--DINLPFITADasgpkhLNMKLTRAKFESLVGDLIKRTV 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291290899 315 EPVEKALRDAKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd11733 312 EPCKKCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIF-GKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
4-382 |
4.31e-156 |
|
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: 454.60 E-value: 4.31e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 4 GPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDPV 82
Cdd:cd11734 1 GPVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTkDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 83 VHSDMKHWPFNVI--NDGgrpKVQVEYKGetKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKD 160
Cdd:cd11734 81 VQRDIKEVPYKIVkhSNG---DAWVEARG--QKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 161 AGTISGLNVLRIINEPTAAAIAYGLDKKvgSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNH 240
Cdd:cd11734 156 AGQIAGLNVLRVINEPTAAALAYGLDKS--GDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 241 FVGEFKRKHKKDITENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGID----FYTSLTRARFEELNADLFRGTLEP 316
Cdd:cd11734 234 IVSEFKKESGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINLPFITADASgpkhINMKLTRAQFESLVKPLVDRTVEP 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291290899 317 VEKALRDAKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSG 382
Cdd:cd11734 314 CKKALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIF-GREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
7-382 |
2.56e-148 |
|
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: 436.00 E-value: 2.56e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 7 VGIDLGTTYSCVGVFQH--GKVEIIANDQGNRTTPSYVAFTDTER-LIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDPVV 83
Cdd:cd10237 25 VGIDLGTTYSCVGVYHAvtGEVEVIPDDDGHKSIPSVVAFTPDGGvLVGYDALAQAEHNPSNTIYDAKRFIGKTFTKEEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 84 HSDMKHWPFNVINDG-GRPKVQVEYKGETKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAG 162
Cdd:cd10237 105 EEEAKRYPFKVVNDNiGSAFFEVPLNGSTLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRKAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 163 TISGLNVLRIINEPTAAAIAYGLDKKVGSErNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFV 242
Cdd:cd10237 185 NLAGLEVLRVINEPTAAAMAYGLHKKSDVN-NVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQYLI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 243 GEFKRKHKKDITeNKRAVRRLRTACERAKRTLSS--STQASIEIDSLYEGID---FYTSLTRARFEELNADLFRGTLEPV 317
Cdd:cd10237 264 DRIAKKFGKTLT-DKEDIQRLRQAVEEVKLNLTNhnSASLSLPLQISLPSAFkvkFKEEITRDLFETLNEDLFQRVLEPI 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291290899 318 EKALRDAKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSG 382
Cdd:cd10237 343 RQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFF-GKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
6-382 |
1.68e-145 |
|
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: 427.02 E-value: 1.68e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLI-GDAAKNQVAMNPTNTVFDAKRLIGRRFDDpvVH 84
Cdd:cd10236 4 AVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITvGEKAKENAITDPENTISSVKRLMGRSLAD--VK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 85 SDMKHWPFNVINDGGRPKVqveYKGETKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTI 164
Cdd:cd10236 82 EELPLLPYRLVGDENELPR---FRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 165 SGLNVLRIINEPTAAAIAYGLDKKvgSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFVge 244
Cdd:cd10236 159 AGLNVLRLLNEPTAAALAYGLDQK--KEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWIL-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 245 fkRKHKKDITENKRAVRRLRTACERAKRTLSSSTQASIEIDSlyEGIDFYTSLTRARFEELNADLFRGTLEPVEKALRDA 324
Cdd:cd10236 235 --KQIGIDARLDPAVQQALLQAARRAKEALSDADSASIEVEV--EGKDWEREITREEFEELIQPLVKRTLEPCRRALKDA 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 291290899 325 KMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILSG 382
Cdd:cd10236 311 GLEPADIDEVVLVGGSTRIPLVRQRVAEFF-GREPLTSINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
5-380 |
2.23e-145 |
|
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: 427.04 E-value: 2.23e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 5 PAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDPVVH 84
Cdd:cd10238 1 AAFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 85 SDMKHWPFNVINDGGRPKVQVEYKGETKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTI 164
Cdd:cd10238 81 ELKKESKCKIIEKDGKPGYEIELEEKKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 165 SGLNVLRIINEPTAAAIAYGLDKKVGSE-RNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFVG 243
Cdd:cd10238 161 AGFNVLRVISEPSAAALAYGIGQDDPTEnSNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHLAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 244 EFKRKHKKDITENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSLTRARFEELNADLFRGTLEPVEKALRD 323
Cdd:cd10238 241 EFKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATCSVESLYDGMDFQCNVSRARFESLCSSLFQQCLEPIQEVLNS 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 291290899 324 AKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFNGRELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd10238 321 AGLTKEDIDKVILCGGSSRIPKLQQLIKDLFPSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
7-378 |
1.91e-142 |
|
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: 419.66 E-value: 1.91e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDPVVHSD 86
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 87 MKHWPFNVIN-DGGRPKVQVEYKGETKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTIS 165
Cdd:cd11732 81 IKLLPFKLVElEDGKVGIEVSYNGEEVVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 166 GLNVLRIINEPTAAAIAYGLDKKVGSE-----RNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNH 240
Cdd:cd11732 161 GLNCLRLINETTAAALDYGIYKSDLLEseekpRIVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 241 FVGEFKRKHKKDITENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSLTRARFEELNADLFRGTLEPVEKA 320
Cdd:cd11732 241 FAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEDIDFSGQIKREEFEELIQPLLARLEAPIKKA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 291290899 321 LRDAKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAA 378
Cdd:cd11732 321 LAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVF-GKDLSTTLNADEAVARGCALQAA 377
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
7-381 |
3.80e-141 |
|
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: 415.05 E-value: 3.80e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 7 VGIDLGTTYSCVGVF-QHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFddpvvh 84
Cdd:cd24029 1 VGIDLGTTNSAVAYWdGNGAEVIIENSEGKRTTPSVVYFDkDGEVLVGEEAKNQALLDPENTIYSVKRLMGRDT------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 85 sdmkhWPFNVINDggrpkvqveykgetKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTI 164
Cdd:cd24029 75 -----KDKEEIGG--------------KEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 165 SGLNVLRIINEPTAAAIAYGLDkKVGSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFVGE 244
Cdd:cd24029 136 AGLNVLRLINEPTAAALAYGLD-KEGKDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 245 FKRKH-KKDITENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSLTRARFEELNADLFRGTLEPVEKALRD 323
Cdd:cd24029 215 IGIETgILDDKEDERARARLREAAEEAKIELSSSDSTDILILDDGKGGELEIEITREEFEELIAPLIERTIDLLEKALKD 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 291290899 324 AKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILS 381
Cdd:cd24029 295 AKLSPEDIDRVLLVGGSSRIPLVREMLEEYF-GREPISSVDPDEAVAKGAAIYAASLA 351
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
6-381 |
2.06e-138 |
|
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: 409.78 E-value: 2.06e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDPVVHS 85
Cdd:cd24095 3 VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEVQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 86 DMKHWPFNVINDG-GRPKVQVEYKGETKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTI 164
Cdd:cd24095 83 DLKLFPFKVTEGPdGEIGINVNYLGEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAAQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 165 SGLNVLRIINEPTAAAIAYGL---DKKVGSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHF 241
Cdd:cd24095 163 AGLNCLRLMNETTATALAYGIyktDLPETDPTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFDHF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 242 VGEFKRKHKKDITENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSLTRARFEELNADLFRGTLEPVEKAL 321
Cdd:cd24095 243 AAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMEDKDVKGMITREEFEELAAPLLERLLEPLEKAL 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 322 RDAKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILS 381
Cdd:cd24095 323 ADSGLTVDQIHSVEVVGSGSRIPAILKILTKFF-GKEPSRTMNASECVARGCALQCAMLS 381
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
7-378 |
9.40e-129 |
|
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: 384.70 E-value: 9.40e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDPVVHSD 86
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 87 MKHWPFNVIN-DGGRPKVQVEYKGETKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTIS 165
Cdd:cd10228 81 LKHLPYKVVKlPNGSVGIKVQYLGEEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 166 GLNVLRIINEPTAAAIAYGLDKK---VGSE--RNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNH 240
Cdd:cd10228 161 GLNCLRLLNDTTAVALAYGIYKQdlpAEEEkpRNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 241 FVGEFKRKHKKDITENKRAVRRLRTACERAKRTLSS-STQASIEIDSLYEGIDFYTSLTRARFEELNADLFRGTLEPVEK 319
Cdd:cd10228 241 FAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSAnATELPLNIECFMDDKDVSGKMKRAEFEELCAPLFARVEVPLRS 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 291290899 320 ALRDAKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAA 378
Cdd:cd10228 321 ALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVF-GKEPSTTLNQDEAVARGCALQCA 378
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
7-379 |
4.44e-127 |
|
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: 378.90 E-value: 4.44e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAF-TDTERLIGDAAKNQVAMNPTNTVFDAKRLIGrrfddpvvhS 85
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVdEDGSILVGRAAKERLVTHPDRTAASFKRFMG---------T 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 86 DmKHWPFNvindggrpkvqveykgeTKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTIS 165
Cdd:cd10235 72 D-KQYRLG-----------------NHTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 166 GLNVLRIINEPTAAAIAYGLDKKvGSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFVgef 245
Cdd:cd10235 134 GLKVERLINEPTAAALAYGLHKR-EDETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFL--- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 246 kRKHKKDITENKRAVR-RLRTACERAKRTLSSstQASIEIDSLYEGIDFYTSLTRARFEELNADLFRGTLEPVEKALRDA 324
Cdd:cd10235 210 -KKHRLDFTSLSPSELaALRKRAEQAKRQLSS--QDSAEIRLTYRGEELEIELTREEFEELCAPLLERLRQPIERALRDA 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 291290899 325 KMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAI 379
Cdd:cd10235 287 GLKPSDIDAVILVGGATRMPLVRQLIARLF-GRLPLSSLDPDEAVALGAAIQAAL 340
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
7-381 |
1.21e-122 |
|
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: 369.01 E-value: 1.21e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDPVVHSD 86
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 87 MKHWPFNVINDGGRPKVQVEYKGETKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTISG 166
Cdd:cd24094 81 EKYFTAKLVDANGEVGAEVNYLGEKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 167 LNVLRIINEPTAAAIAYGLDK-----KVGSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHF 241
Cdd:cd24094 161 LNPLRLMNDTTAAALGYGITKtdlpePEEKPRIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDHF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 242 VGEFKRKHKKDITENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSLTRARFEELNADLFRGTLEPVEKAL 321
Cdd:cd24094 241 ADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVSSMLKREEFEELIAPLLERVTAPLEKAL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 322 RDAKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILS 381
Cdd:cd24094 321 AQAGLTKDEIDFVELVGGTTRVPALKESISAFF-GKPLSTTLNQDEAVARGAAFACAILS 379
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
7-378 |
3.62e-115 |
|
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: 348.72 E-value: 3.62e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 7 VGIDLGTTYSCVGVFQHGK-VEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGrrfddpvvhs 85
Cdd:cd10230 3 LGIDLGSEFIKVALVKPGVpFEIVLNEESKRKTPSAVAFRNGERLFGDDALALATRFPENTFSYLKDLLG---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 86 dmkhwpfnvindggrpkvqveykgetktFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTIS 165
Cdd:cd10230 73 ----------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 166 GLNVLRIINEPTAAAIAYGLDKKVGSE--RNVLIFDLGGGTFDVSILTI------EDGI------FEVKSTAGDTHLGGE 231
Cdd:cd10230 125 GLNVLSLINDNTAAALNYGIDRRFENNepQNVLFYDMGASSTSATVVEFssvkekDKGKnktvpqVEVLGVGWDRTLGGL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 232 DFDNRMVNHFVGEFKRKHKK--DITENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSLTRARFEELNADL 309
Cdd:cd10230 205 EFDLRLADHLADEFNEKHKKdkDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDDIDFRTKITREEFEELCADL 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291290899 310 FRGTLEPVEKALRDAKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFNGRELNKSINPDEAVAYGAAVQAA 378
Cdd:cd10230 285 FERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELGKHLNADEAAALGAAFYAA 353
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
6-612 |
1.21e-107 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 337.60 E-value: 1.21e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 6 AVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDaaknqvamnpTNTVFDAKRLIGRRFDD----P 81
Cdd:PRK01433 21 AVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIGN----------NKGLRSIKRLFGKTLKEilntP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 82 VVHSDMKHwpFNVINDGgrpkvQVEYKGETKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDA 161
Cdd:PRK01433 91 ALFSLVKD--YLDVNSS-----ELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 162 GTISGLNVLRIINEPTAAAIAYGLDKkvGSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHF 241
Cdd:PRK01433 164 AKIAGFEVLRLIAEPTAAAYAYGLNK--NQKGCYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQYL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 242 VGEFKRKHKKDITEnkravrrlrtACERAKRTLSSstQASIEIDSLyegidfytSLTRARFEELNADLFRGTLEPVEKAL 321
Cdd:PRK01433 242 CNKFDLPNSIDTLQ----------LAKKAKETLTY--KDSFNNDNI--------SINKQTLEQLILPLVERTINIAQECL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 322 RDAKmdKAQIHDIVLVGGSTRIPKIQKLLQDFFNGRELNkSINPDEAVAYGAAVQAAILSGDKsenvQDLLLLDVTPLSL 401
Cdd:PRK01433 302 EQAG--NPNIDGVILVGGATRIPLIKDELYKAFKVDILS-DIDPDKAVVWGAALQAENLIAPH----TNSLLIDVVPLSL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 402 GIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVFEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDID 481
Cdd:PRK01433 375 GMELYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAID 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 482 ANGIMNVSAVDKSTGKENKITITNDKGrLSKDEIERMVQEADRYKTEDEAQRDKISAKNSLESLAFNMKSTVedEKLKDK 561
Cdd:PRK01433 455 ADGILSVSAYEKISNTSHAIEVKPNHG-IDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAI--AELTTL 531
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 291290899 562 ISQEDKQKI---LDKCNEVISWLDRNQMAE--KEEYEHQQKELQNLCNPIITKLYQ 612
Cdd:PRK01433 532 LSESEISIInslLDNIKEAVHARDIILINNsiKEFKSKIKKSMDTKLNIIINDLLK 587
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
5-380 |
1.34e-102 |
|
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: 316.23 E-value: 1.34e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 5 PAVGIDLGTTYSCVG-VFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGrrfddpvv 83
Cdd:cd10232 1 VVIGISFGNSNSSIAiINKDGRAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPKNTVANFRDLLG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 84 hsdmkhwpfnvindggrpkvqveykgeTKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGT 163
Cdd:cd10232 73 ---------------------------TTTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 164 ISGLNVLRIINEPTAAAIAYGLDKK----VGSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVN 239
Cdd:cd10232 126 AAGLEVLQLIPEPAAAALAYDLRAEtsgdTIKDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 240 HFVGEFKRKHKKDITENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSLTRARFEELNADLFRGTLEPVEK 319
Cdd:cd10232 206 HFAKEFKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTSAPCSVESLADGIDFHSSINRTRYELLASKVFQQFADLVTD 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291290899 320 ALRDAKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFNGR---ELNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd10232 286 AIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLFPEStiiRAPTQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
7-379 |
4.86e-96 |
|
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: 300.32 E-value: 4.86e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDPVVHSD 86
Cdd:cd11737 3 VGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 87 MKHWPFNVIN-DGGRPKVQVEYKGETKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTIS 165
Cdd:cd11737 83 KPSLAYELVQlPTGTTGIKVMYMEEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 166 GLNVLRIINEPTAAAIAYGLDKK-----VGSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNH 240
Cdd:cd11737 163 GLNCLRLMNETTAVALAYGIYKQdlpapEEKPRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVLVNH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 241 FVGEFKRKHKKDITENKRAVRRLRTACERAKRTLSS-STQASIEIDSLYEGIDFYTSLTRARFEELNADLFRGTLEPVEK 319
Cdd:cd11737 243 FCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSAnASDLPLNIECFMNDIDVSGTMNRGQFEEMCADLLARVEPPLRS 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 320 ALRDAKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAI 379
Cdd:cd11737 323 VLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFF-GKEVSTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
7-381 |
5.47e-93 |
|
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: 292.59 E-value: 5.47e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDPVVHSD 86
Cdd:cd11738 3 VGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 87 MKHWPFNVIN-DGGRPKVQVEYKGETKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTIS 165
Cdd:cd11738 83 KIKLPYELQKmPNGSTGVKVRYLDEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 166 GLNVLRIINEPTAAAIAYGLDKK-----VGSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNH 240
Cdd:cd11738 163 GLNCLRLMNETTAVALAYGIYKQdlpalEEKPRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVLVDY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 241 FVGEFKRKHKKDITENKRAVRRLRTACERAKRTLSS-STQASIEIDSLYEGIDFYTSLTRARFEELNADLFRGTLEPVEK 319
Cdd:cd11738 243 FCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSAnASDLPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEPPLKA 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291290899 320 ALRDAKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAAILS 381
Cdd:cd11738 323 VMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCAILS 383
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
7-378 |
1.62e-90 |
|
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: 285.99 E-value: 1.62e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDPVVHSD 86
Cdd:cd11739 3 VGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFVQKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 87 MKHWPFNVI--NDGGrPKVQVEYKGETKTFYAEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTI 164
Cdd:cd11739 83 KENLSYDLVplKNGG-VGVKVMYLDEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 165 SGLNVLRIINEPTAAAIAYGLDKK--VGSERN---VLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVN 239
Cdd:cd11739 162 VGLNCLRLMNDMTAVALNYGIYKQdlPAPDEKpriVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKLVE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 240 HFVGEFKRKHKKDITENKRAVRRLRTACERAKRTLSS-STQASIEIDSLYEGIDFYTSLTRARFEELNADLFRGTLEPVE 318
Cdd:cd11739 242 HFCAEFKTKYKLDVKSKIRALLRLYQECEKLKKLMSSnSTDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEVPLY 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 319 KALRDAKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAAVQAA 378
Cdd:cd11739 322 SLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFF-GKDVSTTLNADEAVARGCALQCA 380
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
7-375 |
7.66e-61 |
|
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: 206.19 E-value: 7.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 7 VGIDLGTTYSCVgvfqhgkveiiandqgnrttpsyvAFTDTERligdaaknqvamnptntvfdakrligrrfDDPVVHSD 86
Cdd:cd10170 1 VGIDFGTTYSGV------------------------AYALLGP-----------------------------GEPPLVVL 27
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 87 MKHWPFNvinDGGRPKVQVEYkgetktfyaeEVSSMVLIKMKEIAEAYLGKTITNA-------VITVPAYFNDSQRQATK 159
Cdd:cd10170 28 QLPWPGG---DGGSSKVPSVL----------EVVADFLRALLEHAKAELGDRIWELekapievVITVPAGWSDAAREALR 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 160 DAGTISGL----NVLRIINEPTAAAIAYGLDKKVGSE----RNVLIFDLGGGTFDVSILTIEDGIFEVK---STAGDTHL 228
Cdd:cd10170 95 EAARAAGFgsdsDNVRLVSEPEAAALYALEDKGDLLPlkpgDVVLVCDAGGGTVDLSLYEVTSGSPLLLeevAPGGGALL 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 229 GGEDFDNRMVNHFVGEFKRKHKKDITENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGID---FYTSLTRARFEEL 305
Cdd:cd10170 175 GGTDIDEAFEKLLREKLGDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGLpelGLEKGTLLLTEEE 254
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291290899 306 NADLFRGTLEPVEKALRDA--KMDKAQIHDIVLVGGSTRIPKIQKLLQDFFNGRELN---KSINPDEAVAYGAAV 375
Cdd:cd10170 255 IRDLFDPVIDKILELIEEQleAKSGTPPDAVVLVGGFSRSPYLRERLRERFGSAGIIivlRSDDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
7-357 |
2.32e-32 |
|
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: 129.70 E-value: 2.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTE------RLIGDAAKNQVAMNPTNTVF--DAKRLIG-RR 77
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREeegaesIYFGNDAIDAYLNDPEEGRLikSVKSFLGsSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 78 FDDPVVHSdmKHWPFnvindggrpkvqveykgetktfyaEEVSSMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQA 157
Cdd:cd10231 81 FDETTIFG--RRYPF------------------------EDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAED 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 158 T-------KDAGTISGLNVLRIINEPTAAAIAYglDKKVGSERNVLIFDLGGGTFDVSIL----TIEDGIFEVKSTAGDt 226
Cdd:cd10231 135 DaqaesrlRDAARRAGFRNVEFQYEPIAAALDY--EQRLDREELVLVVDFGGGTSDFSVLrlgpNRTDRRADILATSGV- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 227 HLGGEDFDNRMVNHFV-----------------------------------------GEFKRKHKKDITENKRAVR---- 261
Cdd:cd10231 212 GIGGDDFDRELALKKVmphlgrgstyvsgdkglpvpawlyadlsnwhaisllytkktLRLLLDLRRDAADPEKIERllsl 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 262 -------RLRTACERAKRTLSSSTQASIEIDSLYEGIDfyTSLTRARFEELNADLFRGTLEPVEKALRDAKMDKAQIHDI 334
Cdd:cd10231 292 vedqlghRLFRAVEQAKIALSSADEATLSFDFIEISIK--VTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRV 369
|
410 420
....*....|....*....|....
gi 291290899 335 VLVGGSTRIPKIQKLLQD-FFNGR 357
Cdd:cd10231 370 FLTGGSSQSPAVRQALASlFGQAR 393
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
7-374 |
1.84e-22 |
|
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: 99.66 E-value: 1.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 7 VGIDLGTTYSCVG-VFQH--GKVEIIANDQG------NRTTPSYVAFTDTERLIG---DAAKNQVAMNPTNTVFDakrli 74
Cdd:cd10229 3 VAIDFGTTYSGYAySFITdpGDIHTMYNWWGaptgvsSPKTPTCLLLNPDGEFHSfgyEAREKYSDLAEDEEHQW----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 75 gRRFDDPVVHSDMKHWPfnvindgGRPKVQVEYKGetKTFYAEEVSSMVL--IK---MKEIAEAYlGKTITNA----VIT 145
Cdd:cd10229 78 -LYFFKFKMMLLSEKEL-------TRDTKVKAVNG--KSMPALEVFAEALryLKdhaLKELRDRS-GSSLDEDdirwVLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 146 VPAYFNDSQ----RQATKDAGTISGLN--VLRIINEPTAAAIAYGLDKKVGSE------RNVLIFDLGGGTFDVSILTI- 212
Cdd:cd10229 147 VPAIWSDAAkqfmREAAVKAGLISEENseQLIIALEPEAAALYCQKLLAEGEEkelkpgDKYLVVDCGGGTVDITVHEVl 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 213 EDGIFEVKSTAGDTHLGGEDFDNRMVN--------HFVGEFKRKHKKDITENKRAVrrlrtacERAKRTlssstqASIEI 284
Cdd:cd10229 227 EDGKLEELLKASGGPWGSTSVDEEFEElleeifgdDFMEAFKQKYPSDYLDLLQAF-------ERKKRS------FKLRL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 285 dslyegidfytslTRARFEELNADLFRGTLEPVEKALRDAKMDKaqIHDIVLVGGSTRIPKIQKLLQDFFNGRelNKSI- 363
Cdd:cd10229 294 -------------SPELMKSLFDPVVKKIIEHIKELLEKPELKG--VDYIFLVGGFAESPYLQKAVKEAFSTK--VKIIi 356
|
410
....*....|...
gi 291290899 364 --NPDEAVAYGAA 374
Cdd:cd10229 357 ppEPGLAVVKGAV 369
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
7-375 |
2.70e-18 |
|
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins; MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466824 [Multi-domain] Cd Length: 317 Bit Score: 86.37 E-value: 2.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 7 VGIDLGTTYSCVgvFQHGKvEIIANDqgnrttPSYVAF-TDTERLI--GDaaknqvamnptntvfDAKRLIGRRFDDPVV 83
Cdd:cd10225 2 IGIDLGTANTLV--YVKGK-GIVLNE------PSVVAVdKNTGKVLavGE---------------EAKKMLGRTPGNIVA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 84 HSDMKHwpfNVINDggrpkvqveykgetktFYAEEvsSMV--LIKMkeiaeAYLGKTITN--AVITVPAYFNDSQRQATK 159
Cdd:cd10225 58 IRPLRD---GVIAD----------------FEATE--AMLryFIRK-----AHRRRGFLRprVVIGVPSGITEVERRAVK 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 160 DAGTISGLNVLRIINEPTAAAIAYGLDkkVGSERNVLIFDLGGGTFDVSILTIeDGIFEVKStagdTHLGGEDFDNRMVN 239
Cdd:cd10225 112 EAAEHAGAREVYLIEEPMAAAIGAGLP--IEEPRGSMVVDIGGGTTEIAVISL-GGIVTSRS----VRVAGDEMDEAIIN 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 240 HfvgeFKRKHKKDITEnkravrrlRTAcERAKRTLSSstqASIEIDSL---YEGIDFYTSLTRARfeELNADLFRGTLEP 316
Cdd:cd10225 185 Y----VRRKYNLLIGE--------RTA-ERIKIEIGS---AYPLDEELsmeVRGRDLVTGLPRTI--EITSEEVREALEE 246
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291290899 317 --------VEKALRDAKMDKAQ-IHD--IVLVGGSTRIPKIQKLLQDffngrELNKSI----NPDEAVAYGAAV 375
Cdd:cd10225 247 pvnaiveaVRSTLERTPPELAAdIVDrgIVLTGGGALLRGLDELLRE-----ETGLPVhvadDPLTCVAKGAGK 315
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
7-374 |
6.12e-14 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 73.24 E-value: 6.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 7 VGIDLGTTYscVGVFQHGKvEIIANDqgnrttPSYVAF-TDTERL--IGDAAKNQVAMNPTNTVfdAKRligrrfddPvv 83
Cdd:PRK13930 11 IGIDLGTAN--TLVYVKGK-GIVLNE------PSVVAIdTKTGKVlaVGEEAKEMLGRTPGNIE--AIR--------P-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 84 hsdMKHwpfNVINDggrpkvqveykgetktFYAEEVssMV--LIKMkeiAEAYLGKTITNAVITVPAYFNDSQRQATKDA 161
Cdd:PRK13930 70 ---LKD---GVIAD----------------FEATEA--MLryFIKK---ARGRRFFRKPRIVICVPSGITEVERRAVREA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 162 GTISGLNVLRIINEPTAAAIAYGLD--KKVGSernvLIFDLGGGTFDVSILTIeDGIFEVKSTAgdthLGGEDFDNRMVN 239
Cdd:PRK13930 123 AEHAGAREVYLIEEPMAAAIGAGLPvtEPVGN----MVVDIGGGTTEVAVISL-GGIVYSESIR----VAGDEMDEAIVQ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 240 HfvgeFKRKHKKDITEnkravrrlRTAcERAKRTLSSSTQA----SIEIdslyEGIDFYTSLTRARfeELNADLFRGTLE 315
Cdd:PRK13930 194 Y----VRRKYNLLIGE--------RTA-EEIKIEIGSAYPLdeeeSMEV----RGRDLVTGLPKTI--EISSEEVREALA 254
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 316 P--------VEKALRDAKMDKAQ-IHD--IVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGAA 374
Cdd:PRK13930 255 EplqqiveaVKSVLEKTPPELAAdIIDrgIVLTGGGALLRGLDKLLSEET-GLPVHIAEDPLTCVARGTG 323
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
7-374 |
5.40e-13 |
|
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 440695 [Multi-domain] Cd Length: 339 Bit Score: 70.49 E-value: 5.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 7 VGIDLGTtySCVGVFQHGKvEIIANDqgnrttPSYVAF-TDTERLI--GDaaknqvamnptntvfDAKRLIGRRFDDPVV 83
Cdd:COG1077 10 IGIDLGT--ANTLVYVKGK-GIVLNE------PSVVAIdKKTGKVLavGE---------------EAKEMLGRTPGNIVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 84 HSDMKHwpfNVINDggrpkvqveykgetktFyaeevssmvlikmkEIAEAYLGKTITNA-----------VITVPAYFND 152
Cdd:COG1077 66 IRPLKD---GVIAD----------------F--------------EVTEAMLKYFIKKVhgrrsffrprvVICVPSGITE 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 153 SQRQATKDAGTISGLNVLRIINEPTAAAIAYGLDkkVGSERNVLIFDLGGGTFDVSILTIeDGIfeVKSTAgdTHLGGED 232
Cdd:COG1077 113 VERRAVRDAAEQAGAREVYLIEEPMAAAIGAGLP--IEEPTGNMVVDIGGGTTEVAVISL-GGI--VVSRS--IRVAGDE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 233 FDNRMVNHFvgefKRKHKKDITEnkravrrlRTAcERAKRTLSS----STQASIEIdslyEGIDFYTSLTRARfeELNAD 308
Cdd:COG1077 186 LDEAIIQYV----RKKYNLLIGE--------RTA-EEIKIEIGSayplEEELTMEV----RGRDLVTGLPKTI--TITSE 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 309 LFRGTLEP----VEKALRDAkMDK------AQIHD--IVLVGGSTRIPKIQKLLQDFFNgreLNKSI--NPDEAVAYGAA 374
Cdd:COG1077 247 EIREALEEplnaIVEAIKSV-LEKtppelaADIVDrgIVLTGGGALLRGLDKLLSEETG---LPVHVaeDPLTCVARGTG 322
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
7-373 |
4.91e-10 |
|
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.
Pssm-ID: 399596 [Multi-domain] Cd Length: 327 Bit Score: 61.42 E-value: 4.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 7 VGIDLGTTYSCVGVFQHGkveIIANDqgnrttPSYVAF-TDTERLI--GDaaknqvamnptntvfDAKRLIGRRFDDPVV 83
Cdd:pfam06723 4 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAInTKTKKVLavGN---------------EAKKMLGRTPGNIVA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 84 HSDMKHwpfNVINDggrpkvqveykgetktfyaeevssmvlikmKEIAEA---YLGKTITNA--------VITVPAYFND 152
Cdd:pfam06723 60 VRPLKD---GVIAD------------------------------FEVTEAmlkYFIKKVHGRrsfskprvVICVPSGITE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 153 SQRQATKDAGTISGLNVLRIINEPTAAAIAYGLDkkVGSERNVLIFDLGGGTFDVSILTIeDGIFEVKStagdTHLGGED 232
Cdd:pfam06723 107 VERRAVKEAAKNAGAREVFLIEEPMAAAIGAGLP--VEEPTGNMVVDIGGGTTEVAVISL-GGIVTSKS----VRVAGDE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 233 FDNRMVNHfvgeFKRKHKKDITEnkravrrlRTAcERAKRTLSSSTQA----SIEIdslyEGIDFYTSLTR------ARF 302
Cdd:pfam06723 180 FDEAIIKY----IRKKYNLLIGE--------RTA-ERIKIEIGSAYPTeeeeKMEI----RGRDLVTGLPKtieissEEV 242
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291290899 303 EELNADLFRGTLEPVEKALRDAKMD-KAQIHD--IVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAVAYGA 373
Cdd:pfam06723 243 REALKEPVSAIVEAVKEVLEKTPPElAADIVDrgIVLTGGGALLRGLDKLLSDET-GLPVHIAEDPLTCVALGT 315
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
143-268 |
3.90e-07 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 52.60 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 143 VITVPAYFNDSQRQATKDAGTISGLNVLRIINEPTAAAIAYGLD--KKVGSernvLIFDLGGGTFDVSILTIEdGIFEVK 220
Cdd:PRK13928 99 MICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLDisQPSGN----MVVDIGGGTTDIAVLSLG-GIVTSS 173
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 291290899 221 StagdTHLGGEDFDNRMVNHfvgeFKRKHKKDITEnkravrrlRTACE 268
Cdd:PRK13928 174 S----IKVAGDKFDEAIIRY----IRKKYKLLIGE--------RTAEE 205
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
7-351 |
7.26e-07 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 52.17 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 7 VGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTE-------RLIGDAA---KNQ------VAMN-------P 63
Cdd:PRK11678 3 IGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTLCAPTREavsewlyRHLDVPAyddERQallrraIRYNreedidvT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 64 TNTVFDAKRLIGRRFDDP----VVHSdmkhwPFNVINDGGRPKVQVeykgetkTFYAEEVSSMVLiKMKEIAEAYLGKTI 139
Cdd:PRK11678 83 AQSVFFGLAALAQYLEDPeevyFVKS-----PKSFLGASGLKPQQV-------ALFEDLVCAMML-HIKQQAEAQLQAAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 140 TNAVITVPAYFN-----DSQRQAT---KDAGTISGLNVLRIINEPTAAAIAY--GLDKkvgsERNVLIFDLGGGTFDVSI 209
Cdd:PRK11678 150 TQAVIGRPVNFQglggeEANRQAEgilERAAKRAGFKDVEFQFEPVAAGLDFeaTLTE----EKRVLVVDIGGGTTDCSM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 210 LTIedGIFEVKSTAGDTHL--------GGEDFD-----NRMVNHF-VGEFKRKHKK-------------DI--------T 254
Cdd:PRK11678 226 LLM--GPSWRGRADRSASLlghsgqriGGNDLDialafKQLMPLLgMGSETEKGIAlpslpfwnavainDVpaqsdfysL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 255 ENKRAVRRL--------------------------RTAcERAKRTLSSSTQASIEIDSLYEGIDfyTSLTRARFEELNAD 308
Cdd:PRK11678 304 ANGRLLNDLirdarepekvarllkvwrqrlsyrlvRSA-EEAKIALSDQAETRASLDFISDGLA--TEISQQGLEEAISQ 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 291290899 309 LfrgtLEPVEKALRDAkMDKAQIH-DIV-LVGGSTRIPKIQKLLQ 351
Cdd:PRK11678 381 P----LARILELVQLA-LDQAQVKpDVIyLTGGSARSPLIRAALA 420
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
126-228 |
1.15e-06 |
|
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity.
Pssm-ID: 466897 [Multi-domain] Cd Length: 241 Bit Score: 50.34 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 126 KMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTISGLNVLRIINEPTAAAIAYGLdkkvgseRNVLIFDLGGGTF 205
Cdd:cd24047 51 KLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGI-------RDGAVVDIGGGTT 123
|
90 100
....*....|....*....|....*..
gi 291290899 206 DVSIltIEDGifEVKSTA----GDTHL 228
Cdd:cd24047 124 GIAV--LKDG--KVVYTAdeptGGTHL 146
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
126-228 |
8.67e-06 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 47.90 E-value: 8.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 126 KMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTISGLNVLRIINEPTAAAIAYGLDKKVgsernvlIFDLGGGTF 205
Cdd:PRK15080 75 RLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGIDNGA-------VVDIGGGTT 147
|
90 100
....*....|....*....|....*..
gi 291290899 206 DVSILtiEDGifEVKSTA----GDTHL 228
Cdd:PRK15080 148 GISIL--KDG--KVVYSAdeptGGTHM 170
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
121-355 |
1.35e-05 |
|
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466854 [Multi-domain] Cd Length: 282 Bit Score: 47.29 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 121 SMVLIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKdagtiSGLNVLRIINEPTAAAiaYGLDKKVGSERNVLIFDL 200
Cdd:cd24004 49 AESIKELLKELEEKLGSKLKDVVIAIAKVVESLLNVLEK-----AGLEPVGLTLEPFAAA--NLLIPYDMRDLNIALVDI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 201 GGGTFDVSIltIEDGifEVKSTaGDTHLGGEDFDNRMVNHFvgefkrkhkkDITENKravrrlrtaCERAKRTLSSST-- 278
Cdd:cd24004 122 GAGTTDIAL--IRNG--GIEAY-RMVPLGGDDFTKAIAEGF----------LISFEE---------AEKIKRTYGIFLli 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291290899 279 QASIEIDSLYEGIDFYTSLTRArFEELnadlfrgtLEPVEKALRDAKMDKAQIHDIVLVGGSTRIPKIQKLLQDFFN 355
Cdd:cd24004 178 EAKDQLGFTINKKEVYDIIKPV-LEEL--------ASGIANAIEEYNGKFKLPDAVYLVGGGSKLPGLNEALAEKLG 245
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
143-357 |
3.78e-05 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar proteins; HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12A belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A.
Pssm-ID: 466841 [Multi-domain] Cd Length: 413 Bit Score: 46.54 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 143 VITVPAYFNDSQRQATKDAGTISGLNV------LRIINEPTAAAIaYGLDKKVGSERNVLIFDLGGGTFDVSILTI---E 213
Cdd:cd11735 144 VITVPAIWKQPAKQFMRQAAYKAGLASpenpeqLIIALEPEAASI-YCRKLRLHQMDRYVVVDCGGGTVDLTVHQIrlpE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 214 DGIFEV-KSTAGDTHLGGEDFDNRMV------NHFVGEFKRKHKKditenkrAVRRLRTACERAKRTLSSSTQASIEIDS 286
Cdd:cd11735 223 GHLKELyKASGGPYGSLGVDYEFEKLlckifgEDFIDQFKIKRPA-------AWVDLMIAFESRKRAAAPDRTNPLNITL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 287 LYEGIDFYTS------------------------LTRARFEELNAdLFRGTLEPVEKALRD--AKMDKAQIHDIVLVGGS 340
Cdd:cd11735 296 PFSFIDYYKKfrghsvehalrksnvdfvkwssqgMLRMSPDAMNA-LFKPTIDHIIQHLTDlfQKPEVSGVKFLFLVGGF 374
|
250
....*....|....*..
gi 291290899 341 TRIPKIQKLLQDFFNGR 357
Cdd:cd11735 375 AESPLLQQAVQNAFGDQ 391
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
167-253 |
4.63e-05 |
|
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466825 [Multi-domain] Cd Length: 263 Bit Score: 45.59 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 167 LNVLRIINEPTAAAIAYGLDKKVGSERNVLIFDLGGGTfdVSILTIEDGIFEVKStaGDTHLGGEDFDNRMVNHFVGEFK 246
Cdd:cd10227 137 INDVKVLPEGAGAYLDYLLDDDELEDGNVLVIDIGGGT--TDILTFENGKPIEES--SDTLPGGEEALEKYADDILNELL 212
|
....*..
gi 291290899 247 RKHKKDI 253
Cdd:cd10227 213 KKLGDEL 219
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
307-382 |
5.57e-05 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 45.98 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 307 ADLFRGTLEPVEKALRDAkMD-----KAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSiNPDEAVAYGAAVQAAILS 381
Cdd:COG1070 368 AHLARAVLEGVAFALRDG-LEaleeaGVKIDRIRATGGGARSPLWRQILADVL-GRPVEVP-EAEEGGALGAALLAAVGL 444
|
.
gi 291290899 382 G 382
Cdd:COG1070 445 G 445
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
1-240 |
8.34e-05 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 45.28 E-value: 8.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 1 MSKGPAVGIDLGTTYSCVGVFQHGkveIIANDqgnrttPSYVAFTDTER---LIGDAAKNQVAMNPTNTVfdAKRligrr 77
Cdd:PRK13929 1 MFQSTEIGIDLGTANILVYSKNKG---IILNE------PSVVAVDTETKavlAIGTEAKNMIGKTPGKIV--AVR----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 78 fddpvvhsdmkhwpfnVINDGgrpkVQVEYkgetktfyaeEVSSMVLIKMKEIAEAYLGKTI--TNAVITVPAYFNDSQR 155
Cdd:PRK13929 65 ----------------PMKDG----VIADY----------DMTTDLLKQIMKKAGKNIGMTFrkPNVVVCTPSGSTAVER 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 156 QATKDAGTISGLNVLRIINEPTAAAIayGLDKKVGSERNVLIFDLGGGTFDVSILTIeDGIFEVKStagdTHLGGEDFDN 235
Cdd:PRK13929 115 RAISDAVKNCGAKNVHLIEEPVAAAI--GADLPVDEPVANVVVDIGGGTTEVAIISF-GGVVSCHS----IRIGGDQLDE 187
|
....*
gi 291290899 236 RMVNH 240
Cdd:PRK13929 188 DIVSF 192
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
143-290 |
1.48e-04 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 44.31 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 143 VITVPAYFNDSQRQATKDAGTISGLNVLRIINEPTAAAIAYGLD--KKVGSernvLIFDLGGGTFDVSILTIeDGIFEVK 220
Cdd:PRK13927 100 VICVPSGITEVERRAVRESALGAGAREVYLIEEPMAAAIGAGLPvtEPTGS----MVVDIGGGTTEVAVISL-GGIVYSK 174
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 221 StagdTHLGGEDFDNRMVNHfvgeFKRKHKKDITEnkravrrlRTAcERAKrtlssstqasIEIDSLYEG 290
Cdd:PRK13927 175 S----VRVGGDKFDEAIINY----VRRNYNLLIGE--------RTA-ERIK----------IEIGSAYPG 217
|
|
| ASKHA_NBD_MamK |
cd24009 |
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ... |
7-373 |
1.57e-04 |
|
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called magnetosome cytoskeleton protein MamK, is a protein with ATPase activity which forms dynamic cytoplasmic filaments (probably with paralog MamK-like) that may organize magnetosomes into long chains running parallel to the long axis of the cell. Turnover of MamK filaments is probably promoted by MamK-like (e.g.. MamJ and/or LimJ), which provides a monomer pool. MamK forms twisted filaments in the presence of ATP or GTP. It serves to close gaps between magnetosomes in the chain. Interaction with MCP10 is involved in controlling the response to magnetic fields, possibly by controlling flagellar rotation. The MamK family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466859 [Multi-domain] Cd Length: 328 Bit Score: 44.12 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 7 VGIDLGTTYSCvgvfqhgkveiIANDQGNR-TTPSYVAFTD---------TERLIGDAA-KNQVAMNptntvfdakrlig 75
Cdd:cd24009 4 IGIDLGTSRSA-----------VVTSRGKRfSFRSVVGYPKdiiarkllgKEVLFGDEAlENRLALD------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 76 rrfddpvvhsdmKHWPFN--VINDGGRPKvqveykgetktfyaEEVSSMVLIKMKEIAEAYLGKTITnAVITVPAYFNDS 153
Cdd:cd24009 60 ------------LRRPLEdgVIKEGDDRD--------------LEAARELLQHLIELALPGPDDEIY-AVIGVPARASAE 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 154 QRQATKDAGTISGLNVLrIINEPTAaaIAYGLDKKVGSernvLIFDLGGGTFDV-----SILTIEDGIfeVKSTAGDthl 228
Cdd:cd24009 113 NKQALLEIARELVDGVM-VVSEPFA--VAYGLDRLDNS----LIVDIGAGTTDLcrmkgTIPTEEDQI--TLPKAGD--- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 229 ggeDFDNRmvnhFVGEFKRKHKK-DITENKraVRRLRtacERAKRTLSSSTQASIE--IDSLYEGIDFyTSLTRARFEEL 305
Cdd:cd24009 181 ---YIDEE----LVDLIKERYPEvQLTLNM--ARRWK---EKYGFVGDASEPVKVElpVDGKPVTYDI-TEELRIACESL 247
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291290899 306 NADLFRGTLEPVEKAlrDAKMDKAQIHDIVLVGGSTRI----PKIQKLLQDFFNGReLNKSINPDEAVAYGA 373
Cdd:cd24009 248 VPDIVEGIKKLIASF--DPEFQEELRNNIVLAGGGSRIrgldTYIEKALKEYGGGK-VTCVDDPVFAGAEGA 316
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
124-357 |
2.56e-04 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar proteins; HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. HSPA12B belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12B.
Pssm-ID: 466842 [Multi-domain] Cd Length: 361 Bit Score: 43.80 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 124 LIKMKEIAEAYLGKTITNAVITVPAYFNDSQRQATKDAGTISGL------NVLRIINEPTAAAI-AYGLDKKVgsernvl 196
Cdd:cd11736 125 LQELKDQSPSLPEKDAVRWVLTVPAIWKQPAKQFMREAAYLAGLvspenpEQLLIALEPEAASIyCRKLDRYI------- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 197 IFDLGGGTFDVSILTIED--GIFE--VKSTAGDTHLGGEDFD-NRMVNHFVGE-----FKRKHKKditenkrAVRRLRTA 266
Cdd:cd11736 198 VADCGGGTVDLTVHQIEQpqGTLKelYKASGGPYGAVGVDLAfEKLLCQIFGEdfiatFKAKRPA-------AWVDLTIA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 267 CERAKRT--LSSSTQASIEidslyegidfytsltrarfeelnadLFRGTLEPVEKALrDAKMDKAQIHDI---VLVGGST 341
Cdd:cd11736 271 FEARKRTaaLRMSSEAMNE-------------------------LFQPTISQIIQHI-DDLMKKPEVKGIkflFLVGGFA 324
|
250
....*....|....*.
gi 291290899 342 RIPKIQKLLQDFFNGR 357
Cdd:cd11736 325 ESPMLQRAVQAAFGNI 340
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
307-382 |
4.05e-04 |
|
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466808 [Multi-domain] Cd Length: 482 Bit Score: 43.30 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 307 ADLFRGTLEPVEKALRDA----KMDKAQIHDIVLVGGSTRIPKIQKLLQDFFnGRELNKSINPDEAvAYGAAVQAAILSG 382
Cdd:cd07808 365 AHLARAVLEGVAFSLRDSlevlKELGIKVKEIRLIGGGAKSPLWRQILADVL-GVPVVVPAEEEGS-AYGAALLAAVGAG 442
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
296-382 |
1.18e-03 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 41.77 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291290899 296 SLTRARFEELN-ADLFRGTLEPVEKALRDAkMDK-----AQIHDIVLVGGSTRIPKIQKLLQDFFNgrelnKSI---NPD 366
Cdd:cd07809 354 SLVGLTLSNFTrANLARAALEGATFGLRYG-LDIlrelgVEIDEIRLIGGGSKSPVWRQILADVFG-----VPVvvpETG 427
|
90
....*....|....*.
gi 291290899 367 EAVAYGAAVQAAILSG 382
Cdd:cd07809 428 EGGALGAALQAAWGAG 443
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
331-374 |
4.63e-03 |
|
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.
Pssm-ID: 466786 [Multi-domain] Cd Length: 135 Bit Score: 37.83 E-value: 4.63e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 291290899 331 IHDIVLVGGSTRIPKIQKLLQDFFNGRELN---KSINPDEAVAYGAA 374
Cdd:cd00012 89 SANVVLVGGGARNNGLAKRLKELLLFRGGLkvvKAVDPDEAVALGAA 135
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
142-204 |
7.82e-03 |
|
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.
Pssm-ID: 466786 [Multi-domain] Cd Length: 135 Bit Score: 37.06 E-value: 7.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291290899 142 AVITVPAYFNDSQRQAT-----------KDAGTISGLNVLRIINEPTAAAIAYGLDKKvgsERNVLIFDLGGGT 204
Cdd:cd00012 16 IVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGALLTLG---PEGLLVVDLGGGT 86
|
|
| |
