|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
1-611 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 1159.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 1 MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGD 80
Cdd:PTZ00009 1 MTKGPAIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 81 PVVQSDMKHWPFQVINDG-DKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATK 159
Cdd:PTZ00009 81 SVVQSDMKHWPFKVTTGGdDKPMIEVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 160 DAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVN 239
Cdd:PTZ00009 161 DAGTIAGLNVLRIINEPTAAAIAYGLDKKGDGEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 240 HFVEEFKRKHK-KDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVE 318
Cdd:PTZ00009 241 FCVQDFKRKNRgKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 319 KALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAP 398
Cdd:PTZ00009 321 KVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGEQSSQVQDLLLLDVTP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 399 LSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTF 478
Cdd:PTZ00009 401 LSLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 479 DIDANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEGL 558
Cdd:PTZ00009 481 DIDANGILNVSAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDEKV 560
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 167466173 559 KGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGLY 611
Cdd:PTZ00009 561 KGKLSDSDKATIEKAIDEALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMY 613
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
6-611 |
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: 945.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 6 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQS 85
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 86 DMKHWPFQVIND-GDKPKVQVSYKGETkaFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVI 164
Cdd:pfam00012 81 DIKHLPYKVVKLpNGDAGVEVRYLGET--FTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 165 AGLNVLRIINEPTAAAIAYGLDRTGKgERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEE 244
Cdd:pfam00012 159 AGLNVLRIVNEPTAAALAYGLDKTDK-ERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 245 FKRKHKKDISQNKRAVRRLRTACERAKRTLSS-STQASLEIDSLFE-GIDFYTSITRARFEELCSDLFRSTLEPVEKALR 322
Cdd:pfam00012 238 FKKKYGIDLSKDKRALQRLREAAEKAKIELSSnQTNINLPFITAMAdGKDVSGTLTRAKFEELVADLFERTLEPVEKALK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 323 DAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDksENVQDLLLLDVAPLSLG 402
Cdd:pfam00012 318 DAGLSKSEIDEVVLVGGSTRIPAVQELVKEFF-GKEPSKGVNPDEAVAIGAAVQAGVLSGT--FDVKDFLLLDVTPLSLG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 403 LETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDA 482
Cdd:pfam00012 395 IETLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 483 NGILNVTATDKSTGKANKITITNDKGrLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEGlkGKI 562
Cdd:pfam00012 475 NGILTVSAKDKGTGKEQEITIEASEG-LSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEG--DKV 551
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 167466173 563 SEADKKKVldkcQEVISWLDANTL-AEKDEFEHKRKELEQVCNPIISGLY 611
Cdd:pfam00012 552 PEAEKSKV----ESAIEWLKDELEgDDKEEIEAKTEELAQVSQKIGERMY 597
|
|
| 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: 910.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 6 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQS 85
Cdd:cd10233 1 AIGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 86 DMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIA 165
Cdd:cd10233 81 DMKHWPFKVVSGGDKPKIQVEYKGETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 166 GLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEF 245
Cdd:cd10233 161 GLNVLRIINEPTAAAIAYGLDKKGKGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 246 KRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAK 325
Cdd:cd10233 241 KRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELCADLFRSTLEPVEKVLRDAK 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 167466173 326 LDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd10233 321 LDKSQIHEIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
1-611 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 870.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 1 MAKAaaIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVALNPQNTVFDAKRLIGRKfg 79
Cdd:PRK00290 1 MGKI--IGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRLMGRR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 80 DPVVQSDMKHWPFQVIN-DGDKPKVQVsykgETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQAT 158
Cdd:PRK00290 77 DEEVQKDIKLVPYKIVKaDNGDAWVEI----DGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQAT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 159 KDAGVIAGLNVLRIINEPTAAAIAYGLDRtgKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLV 238
Cdd:PRK00290 153 KDAGKIAGLEVLRIINEPTAAALAYGLDK--KGDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRII 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 239 NHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQAslEIDSLFEGID------FYTSITRARFEELCSDLFRS 312
Cdd:PRK00290 231 DYLADEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQT--EINLPFITADasgpkhLEIKLTRAKFEELTEDLVER 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 313 TLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDksenVQDLL 392
Cdd:PRK00290 309 TIEPCKQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLAGD----VKDVL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 393 LLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVP 472
Cdd:PRK00290 384 LLDVTPLSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 473 QIEVTFDIDANGILNVTATDKSTGKANKITITNDKGrLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSA 552
Cdd:PRK00290 464 QIEVTFDIDANGIVHVSAKDKGTGKEQSITITASSG-LSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKT 542
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 167466173 553 VEDegLKGKISEADKKKVLDKCQEVISWLDANtlaEKDEFEHKRKELEQVCNPIISGLY 611
Cdd:PRK00290 543 LKE--LGDKVPADEKEKIEAAIKELKEALKGE---DKEAIKAKTEELTQASQKLGEAMY 596
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
6-611 |
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: 802.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 6 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDpvVQ 84
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNgERLVGQPAKRQAVTNPENTIYSIKRFMGRRFDE--VT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 85 SDMKHWPFQVINDGDKPKVQVsykgETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVI 164
Cdd:TIGR02350 80 EEAKRVPYKVVGDGGDVRVKV----DGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 165 AGLNVLRIINEPTAAAIAYGLDRTGKGERnVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEE 244
Cdd:TIGR02350 156 AGLEVLRIINEPTAAALAYGLDKSKKDEK-ILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 245 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQAslEIDSLFEGID------FYTSITRARFEELCSDLFRSTLEPVE 318
Cdd:TIGR02350 235 FKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLST--EINLPFITADasgpkhLEMTLTRAKFEELTADLVERTKEPVR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 319 KALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDksenVQDLLLLDVAP 398
Cdd:TIGR02350 313 QALKDAGLSASDIDEVILVGGSTRIPAVQELVKDFF-GKEPNKSVNPDEVVAIGAAIQGGVLKGD----VKDVLLLDVTP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 399 LSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTF 478
Cdd:TIGR02350 388 LSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTF 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 479 DIDANGILNVTATDKSTGKANKITITNDKGrLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDegL 558
Cdd:TIGR02350 468 DIDANGILHVSAKDKGTGKEQSITITASSG-LSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKE--A 544
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 167466173 559 KGKISEADKKKVLDKCQEVISWLDANTlaeKDEFEHKRKELEQVCNPIISGLY 611
Cdd:TIGR02350 545 GDKLPAEEKEKIEKAVAELKEALKGED---VEEIKAKTEELQQALQKLAEAMY 594
|
|
| 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: 757.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 6 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQS 85
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 86 DMKHWPFQVINDG-DKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVI 164
Cdd:cd24028 81 DIKHWPFKVVEDEdGKPKIEVTYKGEEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAATI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 165 AGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEE 244
Cdd:cd24028 161 AGLNVLRIINEPTAAALAYGLDKKSSGERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLVEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 245 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDA 324
Cdd:cd24028 241 FKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGIDFETTITRAKFEELCEDLFKKCLEPVEKVLKDA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 167466173 325 KLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd24028 321 KLSKDDIDEVVLVGGSTRIPKIQELLSEFFGGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
7-380 |
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: 751.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 7 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSD 86
Cdd:cd10241 4 IGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKEVQKD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 87 MKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAG 166
Cdd:cd10241 84 IKLLPFKIVNKNGKPYIQVEVKGEKKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 167 LNVLRIINEPTAAAIAYGLDRTGkGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFK 246
Cdd:cd10241 164 LNVLRIINEPTAAAIAYGLDKKG-GEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFIKLFK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 247 RKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKL 326
Cdd:cd10241 243 KKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGEDFSETLTRAKFEELNMDLFRKTLKPVQKVLEDAGL 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 167466173 327 DKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd10241 323 KKSDIDEIVLVGGSTRIPKVQQLLKDFFNGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
1-602 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 702.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 1 MAKAaaIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVALNPQNTVFDAKRLIGRKFG 79
Cdd:CHL00094 1 MGKV--VGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKgDLLVGQIAKRQAVINPENTFYSVKRFIGRKFS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 80 DpvVQSDMKHWPFQVINDG-DKPKVQVSYKGetKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQAT 158
Cdd:CHL00094 79 E--ISEEAKQVSYKVKTDSnGNIKIECPALN--KDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQAT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 159 KDAGVIAGLNVLRIINEPTAAAIAYGLDRtgKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLV 238
Cdd:CHL00094 155 KDAGKIAGLEVLRIINEPTAASLAYGLDK--KNNETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 239 NHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLE---IDSLFEG-IDFYTSITRARFEELCSDLFRSTL 314
Cdd:CHL00094 233 NWLIKEFKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINlpfITATQTGpKHIEKTLTRAKFEELCSDLINRCR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 315 EPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDksenVQDLLLL 394
Cdd:CHL00094 313 IPVENALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLL-GKKPNQSVNPDEVVAIGAAVQAGVLAGE----VKDILLL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 395 DVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQI 474
Cdd:CHL00094 388 DVTPLSLGVETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQI 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 475 EVTFDIDANGILNVTATDKSTGKANKITITNdKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVE 554
Cdd:CHL00094 468 EVTFDIDANGILSVTAKDKGTGKEQSITIQG-ASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLK 546
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 167466173 555 DegLKGKISEADKKKVldkcQEVISWLDANTlaEKDEFEHKRKELEQV 602
Cdd:CHL00094 547 E--LKDKISEEKKEKI----ENLIKKLRQAL--QNDNYESIKSLLEEL 586
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
1-611 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 695.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 1 MAKAaaIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVALNPQNTVFDAKRLIGRKFG 79
Cdd:PRK13411 1 MGKV--IGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSgDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 80 DpvVQSDMKHWPFQVINdGDKPKVQVSYKGetKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATK 159
Cdd:PRK13411 79 D--TEEERSRVPYTCVK-GRDDTVNVQIRG--RNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 160 DAGVIAGLNVLRIINEPTAAAIAYGLDRTGKgERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVN 239
Cdd:PRK13411 154 DAGTIAGLEVLRIINEPTAAALAYGLDKQDQ-EQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 240 HFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASleIDSLFEGID------FYTSITRARFEELCSDLFRST 313
Cdd:PRK13411 233 WLVENFQQQEGIDLSQDKMALQRLREAAEKAKIELSSMLTTS--INLPFITADetgpkhLEMELTRAKFEELTKDLVEAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 314 LEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDksenVQDLLL 393
Cdd:PRK13411 311 IEPMQQALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFGGKQPDRSVNPDEAVALGAAIQAGVLGGE----VKDLLL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 394 LDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQ 473
Cdd:PRK13411 387 LDVTPLSLGIETLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQ 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 474 IEVTFDIDANGILNVTATDKSTGKANKITITNdKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAV 553
Cdd:PRK13411 467 IEVSFEIDVNGILKVSAQDQGTGREQSIRITN-TGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTL 545
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 167466173 554 EDEGlkGKISEADKKKVLDKCQEVISWLDaNTLAEKDEFEHKRKELEQVCNPIISGLY 611
Cdd:PRK13411 546 KENG--ELISEELKQRAEQKVEQLEAALT-DPNISLEELKQQLEEFQQALLAIGAEVY 600
|
|
| 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: 683.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 6 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQ 84
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPkDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFDEATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 85 sdmkhwpfqvINDGDKPkvqvsykgetkafyPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVI 164
Cdd:COG0443 81 ----------VGGKRYS--------------PEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 165 AGLNVLRIINEPTAAAIAYGLDRtGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEE 244
Cdd:COG0443 137 AGLEVLRLLNEPTAAALAYGLDK-GKEEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 245 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDsLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDA 324
Cdd:COG0443 216 FGKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINLP-FSGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 325 KLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDKSEnvqdlllLDVAPLSLGLE 404
Cdd:COG0443 295 GLSPSDIDAVLLVGGSTRMPAVRERVKELF-GKEPLKGVDPDEAVALGAAIQAGVLAGDVKD-------LDVTPLSLGIE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 405 TAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANG 484
Cdd:COG0443 367 TLGGVFTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANG 446
|
490 500 510
....*....|....*....|....*....|....*
gi 167466173 485 ILNVTATDKSTGKANKITItndkgrlsKEEIERMV 519
Cdd:COG0443 447 ILSVSAKDLGTGKEQSITI--------KEEIERML 473
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
7-611 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 678.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 7 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQS 85
Cdd:PTZ00400 44 VGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDgQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEDATKK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 86 DMKHWPFQVINDgdkPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIA 165
Cdd:PTZ00400 124 EQKILPYKIVRA---SNGDAWIEAQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAGKIA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 166 GLNVLRIINEPTAAAIAYGLDRT-GKgerNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEE 244
Cdd:PTZ00400 201 GLDVLRIINEPTAAALAFGMDKNdGK---TIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYLIAE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 245 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQAslEIDSLFEGID------FYTSITRARFEELCSDLFRSTLEPVE 318
Cdd:PTZ00400 278 FKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQT--EINLPFITADqsgpkhLQIKLSRAKLEELTHDLLKKTIEPCE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 319 KALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDksenVQDLLLLDVAP 398
Cdd:PTZ00400 356 KCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIF-GKEPSKGVNPDEAVAMGAAIQAGVLKGE----IKDLLLLDVTP 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 399 LSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTF 478
Cdd:PTZ00400 431 LSLGIETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTF 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 479 DIDANGILNVTATDKSTGKANKITITNDKGrLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDegL 558
Cdd:PTZ00400 511 DVDANGIMNISAVDKSTGKKQEITIQSSGG-LSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSD--L 587
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 167466173 559 KGKISEADKKKVLDKCQEVISWLDANTLaekDEFEHKRKELEQVCNPIISGLY 611
Cdd:PTZ00400 588 KDKISDADKDELKQKITKLRSTLSSEDV---DSIKDKTKQLQEASWKISQQAY 637
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
7-590 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 678.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 7 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDpvVQS 85
Cdd:PRK13410 5 VGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTkDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDE--LDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 86 DMKHWPFQVINDgDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIA 165
Cdd:PRK13410 83 ESKRVPYTIRRN-EQGNVRIKCPRLEREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDAGRIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 166 GLNVLRIINEPTAAAIAYGLDRtgKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEF 245
Cdd:PRK13410 162 GLEVERILNEPTAAALAYGLDR--SSSQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWLAEQF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 246 KRKHKKDISQNKRAVRRLRTACERAKRTLS--SSTQASLE-IDSLFEG---IDfyTSITRARFEELCSDLFRSTLEPVEK 319
Cdd:PRK13410 240 LEKEGIDLRRDRQALQRLTEAAEKAKIELSgvSVTDISLPfITATEDGpkhIE--TRLDRKQFESLCGDLLDRLLRPVKR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 320 ALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDksenVQDLLLLDVAPL 399
Cdd:PRK13410 318 ALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLI-PREPNQNVNPDEVVAVGAAIQAGILAGE----LKDLLLLDVTPL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 400 SLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFD 479
Cdd:PRK13410 393 SLGLETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 480 IDANGILNVTATDKSTGKANKITITNdKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFN----MKSAVED 555
Cdd:PRK13410 473 IDANGILQVSATDRTTGREQSVTIQG-ASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQaerrLRDAALE 551
|
570 580 590
....*....|....*....|....*....|....*
gi 167466173 556 EGLKGkiSEADKKKVLDKCQEVISWLDANTLAEKD 590
Cdd:PRK13410 552 FGPYF--AERQRRAVESAMRDVQDSLEQDDDRELD 584
|
|
| 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: 633.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 6 AIGIDLGTTYSCVGVFQhGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQS 85
Cdd:cd24093 1 AIGIDLGTTYSCVATYE-SSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 86 DMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIA 165
Cdd:cd24093 80 DMKTWPFKVIDVNGNPVIEVQYLGETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 166 GLNVLRIINEPTAAAIAYGLD-RTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEE 244
Cdd:cd24093 160 GLNVLRIINEPTAAAIAYGLGaGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 245 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDA 324
Cdd:cd24093 240 FKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSITRARFEDLNAALFKSTLEPVEQVLKDA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 167466173 325 KLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd24093 320 KISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
7-602 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 630.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 7 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDpvVQS 85
Cdd:PLN03184 42 VGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNgDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSE--VDE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 86 DMKHWPFQVINDgDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIA 165
Cdd:PLN03184 120 ESKQVSYRVVRD-ENGNVKLDCPAIGKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRIA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 166 GLNVLRIINEPTAAAIAYGLDRtgKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEF 245
Cdd:PLN03184 199 GLEVLRIINEPTAASLAYGFEK--KSNETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLASNF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 246 KRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLE---IDSLFEG---IDfyTSITRARFEELCSDLFRSTLEPVEK 319
Cdd:PLN03184 277 KKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISlpfITATADGpkhID--TTLTRAKFEELCSDLLDRCKTPVEN 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 320 ALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFfNGRDLNKSINPDEAVAYGAAVQAAILMGDksenVQDLLLLDVAPL 399
Cdd:PLN03184 355 ALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKL-TGKDPNVTVNPDEVVALGAAVQAGVLAGE----VSDIVLLDVTPL 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 400 SLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFD 479
Cdd:PLN03184 430 SLGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFD 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 480 IDANGILNVTATDKSTGKANKITITNdKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDegLK 559
Cdd:PLN03184 510 IDANGILSVSATDKGTGKKQDITITG-ASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKE--LG 586
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 167466173 560 GKISEADKKKVLDKCQEVISWLDA-NTLAEKDEFEHKRKELEQV 602
Cdd:PLN03184 587 DKVPADVKEKVEAKLKELKDAIASgSTQKMKDAMAALNQEVMQI 630
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
7-601 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 605.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 7 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSD 86
Cdd:PTZ00186 30 IGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEHIQKD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 87 MKHWPFQVI--NDGDKpKVQvsyKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVI 164
Cdd:PTZ00186 110 IKNVPYKIVraGNGDA-WVQ---DGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 165 AGLNVLRIINEPTAAAIAYGLDRTGkgERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEE 244
Cdd:PTZ00186 186 AGLNVIRVVNEPTAAALAYGMDKTK--DSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYILEE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 245 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGID----FYTSITRARFEELCSDLFRSTLEPVEKA 320
Cdd:PTZ00186 264 FRKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADgaqhIQMHISRSKFEGITQRLIERSIAPCKQC 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 321 LRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDksenVQDLLLLDVAPLS 400
Cdd:PTZ00186 344 MKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFF-QKDPFRGVNPDEAVALGAATLGGVLRGD----VKGLVLLDVTPLS 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 401 LGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDI 480
Cdd:PTZ00186 419 LGIETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDI 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 481 DANGILNVTATDKSTGKANKITITNDKGrLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAfnmKSAVEDEGLKG 560
Cdd:PTZ00186 499 DANGICHVTAKDKATGKTQNITITANGG-LSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQL---TTAERQLGEWK 574
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 167466173 561 KISEADKKKVLDKCQEVISWLDaNTLAEKDEFEHKRKELEQ 601
Cdd:PTZ00186 575 YVSDAEKENVKTLVAELRKAME-NPNVAKDDLAAATDKLQK 614
|
|
| 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: 555.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 7 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQS 85
Cdd:cd10234 2 IGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 86 DMKHWPFQVINDGDkpkvqVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIA 165
Cdd:cd10234 82 KQVPYPVVSAGNGD-----AWVEIGGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 166 GLNVLRIINEPTAAAIAYGLDRtgKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEF 245
Cdd:cd10234 157 GLEVLRIINEPTAAALAYGLDK--KKDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 246 KRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQAslEIDSLFEGID------FYTSITRARFEELCSDLFRSTLEPVEK 319
Cdd:cd10234 235 KKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLET--EINLPFITADasgpkhLEMKLTRAKFEELTEDLVERTIEPVEQ 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167466173 320 ALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILM 381
Cdd:cd10234 313 ALKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
6-544 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 554.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 6 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDpvVQS 85
Cdd:PRK05183 21 AVGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKNTISSVKRFMGRSLAD--IQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 86 DMKHWPFQvINDGDKPKVQVSYKGETKAfyPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIA 165
Cdd:PRK05183 99 RYPHLPYQ-FVASENGMPLIRTAQGLKS--PVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 166 GLNVLRIINEPTAAAIAYGLDRtgKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEF 245
Cdd:PRK05183 176 GLNVLRLLNEPTAAAIAYGLDS--GQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWILEQA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 246 KRKHKKDISQnkraVRRLRTACERAKRTLSSSTQASLEIdSLFEGIdfytsITRARFEELCSDLFRSTLEPVEKALRDAK 325
Cdd:PRK05183 254 GLSPRLDPED----QRLLLDAARAAKEALSDADSVEVSV-ALWQGE-----ITREQFNALIAPLVKRTLLACRRALRDAG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 326 LDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDKSENvqDLLLLDVAPLSLGLET 405
Cdd:PRK05183 324 VEADEVKEVVMVGGSTRVPLVREAVGEFF-GRTPLTSIDPDKVVAIGAAIQADILAGNKPDS--DMLLLDVIPLSLGLET 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 406 AGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGI 485
Cdd:PRK05183 401 MGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADGL 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167466173 486 LNVTATDKSTGKANKITITNDKGrLSKEEIERMVQEAEKYKAEDEVQR----ERVSAKNALES 544
Cdd:PRK05183 481 LSVTAMEKSTGVEASIQVKPSYG-LTDDEIARMLKDSMSHAEEDMQARalaeQKVEAERVLEA 542
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
6-579 |
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: 533.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 6 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAF-TDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQ 84
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYlKDGGVEVGKEALAAAAEDPKNTISSVKRLMGRSIEDIKTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 85 SDMkhwPFqVINDGDKPKVQVSYKGETKAfyPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVI 164
Cdd:TIGR01991 81 SIL---PY-RFVDGPGEMVRLRTVQGTVT--PVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 165 AGLNVLRIINEPTAAAIAYGLDRTGKGerNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEE 244
Cdd:TIGR01991 155 AGLNVLRLLNEPTAAAVAYGLDKASEG--IYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWILKQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 245 FKRKHKKDISQNKRAVRRLRTACERAkrtlssSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDA 324
Cdd:TIGR01991 233 LGISADLNPEDQRLLLQAARAAKEAL------TDAESVEVDFTLDGKDFKGKLTRDEFEALIQPLVQKTLSICRRALRDA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 325 KLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDKSENvqDLLLLDVAPLSLGLE 404
Cdd:TIGR01991 307 GLSVEEIKGVVLVGGSTRMPLVRRAVAELF-GQEPLTDIDPDQVVALGAAIQADLLAGNRIGN--DLLLLDVTPLSLGIE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 405 TAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANG 484
Cdd:TIGR01991 384 TMGGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDADG 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 485 ILNVTATDKSTGKANKITITNDKGrLSKEEIERMVQEAEKYKAED-----------EVQRERVSAKNALEsyafnmksav 553
Cdd:TIGR01991 464 LLTVSAQEQSTGVEQSIQVKPSYG-LSDEEIERMLKDSFKHAEEDmyaralaeqkvEAERILEALQAALA---------- 532
|
570 580
....*....|....*....|....*....
gi 167466173 554 EDEGLkgkISEADKKKV---LDKCQEVIS 579
Cdd:TIGR01991 533 ADGDL---LSEDERAAIdaaMEALQKALQ 558
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
5-380 |
1.87e-175 |
|
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: 503.34 E-value: 1.87e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 5 AAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVV 83
Cdd:cd11733 2 DVIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDPEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 84 QSDMKHWPFQVI--NDGDkpkVQVSYKGetKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDA 161
Cdd:cd11733 82 QKDIKMVPYKIVkaSNGD---AWVEAHG--KKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 162 GVIAGLNVLRIINEPTAAAIAYGLDRtgKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHF 241
Cdd:cd11733 157 GQIAGLNVLRIINEPTAAALAYGLDK--KDDKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNYL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 242 VEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQAslEIDSLFEGID------FYTSITRARFEELCSDLFRSTLE 315
Cdd:cd11733 235 VAEFKKEQGIDLSKDNLALQRLREAAEKAKIELSSSLQT--DINLPFITADasgpkhLNMKLTRAKFESLVGDLIKRTVE 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167466173 316 PVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd11733 313 PCKKCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIF-GKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
4-382 |
1.52e-158 |
|
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: 460.37 E-value: 1.52e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 4 AAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPV 82
Cdd:cd11734 1 GPVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTkDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 83 VQSDMKHWPFQVI--NDGDkpkVQVSYKGETkaFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKD 160
Cdd:cd11734 81 VQRDIKEVPYKIVkhSNGD---AWVEARGQK--YSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 161 AGVIAGLNVLRIINEPTAAAIAYGLDRTgkGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNH 240
Cdd:cd11734 156 AGQIAGLNVLRVINEPTAAALAYGLDKS--GDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 241 FVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQAslEIDSLFEGID------FYTSITRARFEELCSDLFRSTL 314
Cdd:cd11734 234 IVSEFKKESGIDLSKDRMAIQRIREAAEKAKIELSSTLQT--DINLPFITADasgpkhINMKLTRAQFESLVKPLVDRTV 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167466173 315 EPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMG 382
Cdd:cd11734 312 EPCKKALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIF-GREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
7-382 |
2.74e-149 |
|
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: 437.93 E-value: 2.74e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 7 IGIDLGTTYSCVGVFQH--GKVEIIANDQGNRTTPSYVAFTDTER-LIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVV 83
Cdd:cd10237 25 VGIDLGTTYSCVGVYHAvtGEVEVIPDDDGHKSIPSVVAFTPDGGvLVGYDALAQAEHNPSNTIYDAKRFIGKTFTKEEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 84 QSDMKHWPFQVINDGD-KPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAG 162
Cdd:cd10237 105 EEEAKRYPFKVVNDNIgSAFFEVPLNGSTLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRKAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 163 VIAGLNVLRIINEPTAAAIAYGLdRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFV 242
Cdd:cd10237 185 NLAGLEVLRVINEPTAAAMAYGL-HKKSDVNNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQYLI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 243 EEFKRKHKKDISqNKRAVRRLRTACERAKRTLSS--STQASLEIDSLFEGID---FYTSITRARFEELCSDLFRSTLEPV 317
Cdd:cd10237 264 DRIAKKFGKTLT-DKEDIQRLRQAVEEVKLNLTNhnSASLSLPLQISLPSAFkvkFKEEITRDLFETLNEDLFQRVLEPI 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167466173 318 EKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMG 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 |
5.17e-148 |
|
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: 433.18 E-value: 5.17e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 6 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLI-GDAAKNQVALNPQNTVFDAKRLIGRKFGDpvVQ 84
Cdd:cd10236 4 AVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITvGEKAKENAITDPENTISSVKRLMGRSLAD--VK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 85 SDMKHWPFQVINDgdkPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVI 164
Cdd:cd10236 82 EELPLLPYRLVGD---ENELPRFRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 165 AGLNVLRIINEPTAAAIAYGLDRtgKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEE 244
Cdd:cd10236 159 AGLNVLRLLNEPTAAALAYGLDQ--KKEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWILKQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 245 FkrkhKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDslFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDA 324
Cdd:cd10236 237 I----GIDARLDPAVQQALLQAARRAKEALSDADSASIEVE--VEGKDWEREITREEFEELIQPLVKRTLEPCRRALKDA 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 167466173 325 KLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMG 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 |
3.50e-147 |
|
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: 431.28 E-value: 3.50e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 5 AAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQ 84
Cdd:cd10238 1 AAFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 85 SDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVI 164
Cdd:cd10238 81 ELKKESKCKIIEKDGKPGYEIELEEKKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 165 AGLNVLRIINEPTAAAIAYGL---DRTGKGerNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHF 241
Cdd:cd10238 161 AGFNVLRVISEPSAAALAYGIgqdDPTENS--NVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 242 VEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKAL 321
Cdd:cd10238 239 ASEFKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATCSVESLYDGMDFQCNVSRARFESLCSSLFQQCLEPIQEVL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 167466173 322 RDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd10238 319 NSAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFPSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
7-380 |
1.66e-145 |
|
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: 425.84 E-value: 1.66e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 7 IGIDLGTTYSCVGVF-QHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFgdpvvq 84
Cdd:cd24029 1 VGIDLGTTNSAVAYWdGNGAEVIIENSEGKRTTPSVVYFDkDGEVLVGEEAKNQALLDPENTIYSVKRLMGRDT------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 85 sdmkhWPFQVINDGDkpkvqvsykgetkaFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVI 164
Cdd:cd24029 75 -----KDKEEIGGKE--------------YTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 165 AGLNVLRIINEPTAAAIAYGLDRTGKGErNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEE 244
Cdd:cd24029 136 AGLNVLRLINEPTAAALAYGLDKEGKDG-TILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 245 FKRKH-KKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRD 323
Cdd:cd24029 215 IGIETgILDDKEDERARARLREAAEEAKIELSSSDSTDILILDDGKGGELEIEITREEFEELIAPLIERTIDLLEKALKD 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 167466173 324 AKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd24029 295 AKLSPEDIDRVLLVGGSSRIPLVREMLEEYF-GREPISSVDPDEAVAKGAAIYAASL 350
|
|
| 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 |
2.44e-145 |
|
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: 426.59 E-value: 2.44e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 7 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSD 86
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 87 MKHWPFQVIN-DGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIA 165
Cdd:cd11732 81 IKLLPFKLVElEDGKVGIEVSYNGEEVVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 166 GLNVLRIINEPTAAAIAYGLDRTGKGE-----RNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNH 240
Cdd:cd11732 161 GLNCLRLINETTAAALDYGIYKSDLLEseekpRIVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 241 FVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKA 320
Cdd:cd11732 241 FAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEDIDFSGQIKREEFEELIQPLLARLEAPIKKA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 167466173 321 LRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAA 378
Cdd:cd11732 321 LAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVF-GKDLSTTLNADEAVARGCALQAA 377
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
5-380 |
4.48e-140 |
|
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: 413.63 E-value: 4.48e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 5 AAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQ 84
Cdd:cd24095 2 SVVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 85 SDMKHWPFQVINDGD-KPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGV 163
Cdd:cd24095 82 RDLKLFPFKVTEGPDgEIGINVNYLGEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 164 IAGLNVLRIINEPTAAAIAYGLDRTGKGE---RNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNH 240
Cdd:cd24095 162 IAGLNCLRLMNETTATALAYGIYKTDLPEtdpTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFDH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 241 FVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKA 320
Cdd:cd24095 242 FAAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMEDKDVKGMITREEFEELAAPLLERLLEPLEKA 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 321 LRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd24095 322 LADSGLTVDQIHSVEVVGSGSRIPAILKILTKFF-GKEPSRTMNASECVARGCALQCAML 380
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
7-378 |
1.92e-133 |
|
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: 396.26 E-value: 1.92e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 7 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSD 86
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 87 MKHWPFQVINDGD-KPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIA 165
Cdd:cd10228 81 LKHLPYKVVKLPNgSVGIKVQYLGEEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 166 GLNVLRIINEPTAAAIAYG-----LDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNH 240
Cdd:cd10228 161 GLNCLRLLNDTTAVALAYGiykqdLPAEEEKPRNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 241 FVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSS-STQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEK 319
Cdd:cd10228 241 FAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSAnATELPLNIECFMDDKDVSGKMKRAEFEELCAPLFARVEVPLRS 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 167466173 320 ALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAA 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 |
1.39e-128 |
|
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: 382.36 E-value: 1.39e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 7 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAF-TDTERLIGDAAKNQVALNPQNTVFDAKRLIG----RKFGDp 81
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVdEDGSILVGRAAKERLVTHPDRTAASFKRFMGtdkqYRLGN- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 82 vvqsdmkhwpfqvindgdkpkvqvsykgetKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDA 161
Cdd:cd10235 80 ------------------------------HTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 162 GVIAGLNVLRIINEPTAAAIAYGLDRTGKgERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHF 241
Cdd:cd10235 130 GELAGLKVERLINEPTAAALAYGLHKRED-ETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 242 VEefkrKHKKDISQNKRAVR-RLRTACERAKRTLSSSTQAslEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKA 320
Cdd:cd10235 209 LK----KHRLDFTSLSPSELaALRKRAEQAKRQLSSQDSA--EIRLTYRGEELEIELTREEFEELCAPLLERLRQPIERA 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 167466173 321 LRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAI 379
Cdd:cd10235 283 LRDAGLKPSDIDAVILVGGATRMPLVRQLIARLF-GRLPLSSLDPDEAVALGAAIQAAL 340
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
7-380 |
1.61e-123 |
|
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: 370.94 E-value: 1.61e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 7 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSD 86
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 87 MKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAG 166
Cdd:cd24094 81 EKYFTAKLVDANGEVGAEVNYLGEKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 167 LNVLRIINEPTAAAIAYGLDRT---GKGE--RNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHF 241
Cdd:cd24094 161 LNPLRLMNDTTAAALGYGITKTdlpEPEEkpRIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDHF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 242 VEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKAL 321
Cdd:cd24094 241 ADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVSSMLKREEFEELIAPLLERVTAPLEKAL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 167466173 322 RDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd24094 321 AQAGLTKDEIDFVELVGGTTRVPALKESISAFF-GKPLSTTLNQDEAVARGAAFACAIL 378
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
5-378 |
1.27e-119 |
|
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: 359.89 E-value: 1.27e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 5 AAIGIDLGTTYSCVGVFQHGK-VEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGrkfgdpvv 83
Cdd:cd10230 1 AVLGIDLGSEFIKVALVKPGVpFEIVLNEESKRKTPSAVAFRNGERLFGDDALALATRFPENTFSYLKDLLG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 84 qsdmkhwpfqvindgdkpkvqvsykgetkaFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGV 163
Cdd:cd10230 73 ------------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 164 IAGLNVLRIINEPTAAAIAYGLDRTGKGE--RNVLIFDLGGGTFDVSILTI------DDGI------FEVKATAGDTHLG 229
Cdd:cd10230 123 IAGLNVLSLINDNTAAALNYGIDRRFENNepQNVLFYDMGASSTSATVVEFssvkekDKGKnktvpqVEVLGVGWDRTLG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 230 GEDFDNRLVNHFVEEFKRKHKK--DISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCS 307
Cdd:cd10230 203 GLEFDLRLADHLADEFNEKHKKdkDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDDIDFRTKITREEFEELCA 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167466173 308 DLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAA 378
Cdd:cd10230 283 DLFERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELGKHLNADEAAALGAAFYAA 353
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
6-610 |
7.71e-112 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 348.38 E-value: 7.71e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 6 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDaaknqvalnpQNTVFDAKRLIGRKFGDPVVQS 85
Cdd:PRK01433 21 AVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIGN----------NKGLRSIKRLFGKTLKEILNTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 86 DMkhwpFQVINDG-DKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVI 164
Cdd:PRK01433 91 AL----FSLVKDYlDVNSSELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLAAKI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 165 AGLNVLRIINEPTAAAIAYGLDRTGKGerNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEE 244
Cdd:PRK01433 167 AGFEVLRLIAEPTAAAYAYGLNKNQKG--CYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQYLCNK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 245 FKRKHKKDISQnkravrrlrtACERAKRTLSSstQASLEIDSLfegidfytSITRARFEELCSDLFRSTLEPVEKALRDA 324
Cdd:PRK01433 245 FDLPNSIDTLQ----------LAKKAKETLTY--KDSFNNDNI--------SINKQTLEQLILPLVERTINIAQECLEQA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 325 KldKAQIHDLVLVGGSTRIPKVQKLLQDFFNgRDLNKSINPDEAVAYGAAVQAAILMGDKsenvQDLLLLDVAPLSLGLE 404
Cdd:PRK01433 305 G--NPNIDGVILVGGATRIPLIKDELYKAFK-VDILSDIDPDKAVVWGAALQAENLIAPH----TNSLLIDVVPLSLGME 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 405 TAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANG 484
Cdd:PRK01433 378 LYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDADG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 485 ILNVTATDKSTGKANKITITNDKGrLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDegLKGKISE 564
Cdd:PRK01433 458 ILSVSAYEKISNTSHAIEVKPNHG-IDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAIAE--LTTLLSE 534
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 167466173 565 ADK---KKVLDKCQEVISWLDANTLAEK-DEFEHK-RKELEQVCNPIISGL 610
Cdd:PRK01433 535 SEIsiiNSLLDNIKEAVHARDIILINNSiKEFKSKiKKSMDTKLNIIINDL 585
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
5-379 |
1.36e-101 |
|
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: 314.57 E-value: 1.36e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 5 AAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQ 84
Cdd:cd11737 1 SVVGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 85 SDMKHWPFQVIN-DGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGV 163
Cdd:cd11737 81 AEKPSLAYELVQlPTGTTGIKVMYMEEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 164 IAGLNVLRIINEPTAAAIAYGL---DRTGKGE--RNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLV 238
Cdd:cd11737 161 IAGLNCLRLMNETTAVALAYGIykqDLPAPEEkpRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 239 NHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSS-STQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPV 317
Cdd:cd11737 241 NHFCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSAnASDLPLNIECFMNDIDVSGTMNRGQFEEMCADLLARVEPPL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167466173 318 EKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAI 379
Cdd:cd11737 321 RSVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFF-GKEVSTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
5-380 |
3.57e-99 |
|
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: 306.98 E-value: 3.57e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 5 AAIGIDLGTTYSCVG-VFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGrkfgdpvv 83
Cdd:cd10232 1 VVIGISFGNSNSSIAiINKDGRAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPKNTVANFRDLLG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 84 qsdmkhwpfqvindgdkpkvqvsykgeTKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGV 163
Cdd:cd10232 73 ---------------------------TTTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 164 IAGLNVLRIINEPTAAAIAYGLDRTGKG----ERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVN 239
Cdd:cd10232 126 AAGLEVLQLIPEPAAAALAYDLRAETSGdtikDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 240 HFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEK 319
Cdd:cd10232 206 HFAKEFKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTSAPCSVESLADGIDFHSSINRTRYELLASKVFQQFADLVTD 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167466173 320 ALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNK----SINPDEAVAYGAAVQAAIL 380
Cdd:cd10232 286 AIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLF-PESTIIraptQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
5-380 |
3.57e-97 |
|
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: 302.99 E-value: 3.57e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 5 AAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQ 84
Cdd:cd11738 1 SVVGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 85 SDMKHWPFQV--INDGDKpKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAG 162
Cdd:cd11738 81 AEKIKLPYELqkMPNGST-GVKVRYLDEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 163 VIAGLNVLRIINEPTAAAIAYG-----LDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRL 237
Cdd:cd11738 160 QIAGLNCLRLMNETTAVALAYGiykqdLPALEEKPRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 238 VNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSS-STQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEP 316
Cdd:cd11738 240 VDYFCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSAnASDLPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEPP 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167466173 317 VEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd11738 320 LKAVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCAIL 382
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
5-378 |
1.87e-96 |
|
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: 301.01 E-value: 1.87e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 5 AAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQ 84
Cdd:cd11739 1 SVVGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 85 SDMKHWPFQVI--NDGdKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAG 162
Cdd:cd11739 81 KEKENLSYDLVplKNG-GVGVKVMYLDEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 163 VIAGLNVLRIINEPTAAAIAYGL---DRTGKGE--RNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRL 237
Cdd:cd11739 160 QIVGLNCLRLMNDMTAVALNYGIykqDLPAPDEkpRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 238 VNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSS-STQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEP 316
Cdd:cd11739 240 VEHFCAEFKTKYKLDVKSKIRALLRLYQECEKLKKLMSSnSTDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEVP 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167466173 317 VEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAA 378
Cdd:cd11739 320 LYSLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFF-GKDVSTTLNADEAVARGCALQCA 380
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
7-375 |
1.49e-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: 207.73 E-value: 1.49e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 7 IGIDLGTTYSCVgvfqhgkveiiandqgnrttpsyvAFTDTERligdaaknqvalnpqntvfdakrligrkfGDPVVQSD 86
Cdd:cd10170 1 VGIDFGTTYSGV------------------------AYALLGP-----------------------------GEPPLVVL 27
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 87 MKHWPFqviNDGDKPKV--QVsykgetkafypeEISSMVLTKMKEIAEAYLGY-------PVTNAVITVPAYFNDSQRQA 157
Cdd:cd10170 28 QLPWPG---GDGGSSKVpsVL------------EVVADFLRALLEHAKAELGDriwelekAPIEVVITVPAGWSDAAREA 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 158 TKDAGVIAGL----NVLRIINEPTAAAIAYGLDRTG----KGERNVLIFDLGGGTFDVSILTIDDGIFEVK---ATAGDT 226
Cdd:cd10170 93 LREAARAAGFgsdsDNVRLVSEPEAAALYALEDKGDllplKPGDVVLVCDAGGGTVDLSLYEVTSGSPLLLeevAPGGGA 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 227 HLGGEDFDNRLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGID---FYTSITRARFE 303
Cdd:cd10170 173 LLGGTDIDEAFEKLLREKLGDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGLpelGLEKGTLLLTE 252
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167466173 304 ELCSDLFRSTLEPVEKALRDAKLDKA--QIHDLVLVGGSTRIPKVQKLLQDFFNGRDLN---KSINPDEAVAYGAAV 375
Cdd:cd10170 253 EEIRDLFDPVIDKILELIEEQLEAKSgtPPDAVVLVGGFSRSPYLRERLRERFGSAGIIivlRSDDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
7-354 |
1.02e-33 |
|
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: 133.55 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 7 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTE------RLIGDAAKNQVALNPQNtvfdakrliGRkfgd 80
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREeegaesIYFGNDAIDAYLNDPEE---------GR---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 81 pVVQSDMKHWPFQVINDGDKPKVQVSYkgetkafypEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQAT-- 158
Cdd:cd10231 68 -LIKSVKSFLGSSLFDETTIFGRRYPF---------EDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDDaq 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 159 -----KDAGVIAGLNVLRIINEPTAAAIAYglDRTGKGERNVLIFDLGGGTFDVSILTID----DGIFEVKATAGDtHLG 229
Cdd:cd10231 138 aesrlRDAARRAGFRNVEFQYEPIAAALDY--EQRLDREELVLVVDFGGGTSDFSVLRLGpnrtDRRADILATSGV-GIG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 230 GEDFDNRLVNHFV-----------------------------------------EEFKRKHKKDiSQNKRAVRRLRT--- 265
Cdd:cd10231 215 GDDFDRELALKKVmphlgrgstyvsgdkglpvpawlyadlsnwhaisllytkktLRLLLDLRRD-AADPEKIERLLSlve 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 266 ---------ACERAKRTLSSSTQASLEIDSLFEGIDfyTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVL 336
Cdd:cd10231 294 dqlghrlfrAVEQAKIALSSADEATLSFDFIEISIK--VTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRVFL 371
|
410
....*....|....*...
gi 167466173 337 VGGSTRIPKVQKLLQDFF 354
Cdd:cd10231 372 TGGSSQSPAVRQALASLF 389
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
5-374 |
2.82e-21 |
|
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: 96.19 E-value: 2.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 5 AAIGIDLGTTYSCVG-VFQH--GKVEIIANDQG------NRTTPSYVAFTDTERLIG---DAAKNQVALNPQNTV---FD 69
Cdd:cd10229 1 VVVAIDFGTTYSGYAySFITdpGDIHTMYNWWGaptgvsSPKTPTCLLLNPDGEFHSfgyEAREKYSDLAEDEEHqwlYF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 70 AKRLIGRKFGDpvvqsdmkhwpfqvinDGDKPKVQVSYKGETK------AFYPEEISSMVLtkmKEIAEAYLGyPVTNA- 142
Cdd:cd10229 81 FKFKMMLLSEK----------------ELTRDTKVKAVNGKSMpalevfAEALRYLKDHAL---KELRDRSGS-SLDEDd 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 143 ---VITVPAYFNDSQRQATKDAGVIAGL------NVLRIINEPTAAAIAYG-------LDRTGKGERnVLIFDLGGGTFD 206
Cdd:cd10229 141 irwVLTVPAIWSDAAKQFMREAAVKAGLiseensEQLIIALEPEAAALYCQkllaegeEKELKPGDK-YLVVDCGGGTVD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 207 VSILTI-DDGIFE--VKATAGdtHLGGEDFDNRLVN--------HFVEEFKRKHKKDISQNKRAVrrlrtacERAKRTls 275
Cdd:cd10229 220 ITVHEVlEDGKLEelLKASGG--PWGSTSVDEEFEElleeifgdDFMEAFKQKYPSDYLDLLQAF-------ERKKRS-- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 276 sstqASLEidslfegidfytsITRARFEELCSDLFRSTLEPVEKALRDAKLDKaqIHDLVLVGGSTRIPKVQKLLQDFFN 355
Cdd:cd10229 289 ----FKLR-------------LSPELMKSLFDPVVKKIIEHIKELLEKPELKG--VDYIFLVGGFAESPYLQKAVKEAFS 349
|
410 420
....*....|....*....|..
gi 167466173 356 GRdlNKSI---NPDEAVAYGAA 374
Cdd:cd10229 350 TK--VKIIippEPGLAVVKGAV 369
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
7-375 |
4.58e-17 |
|
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: 82.52 E-value: 4.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 7 IGIDLGTTYSCVGVFQHGkveIIANDqgnrttPSYVAF-TDTERLI--GDaaknqvalnpqntvfDAKRLIGRKFGDPVV 83
Cdd:cd10225 2 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAVdKNTGKVLavGE---------------EAKKMLGRTPGNIVA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 84 qsdmkHWPFQ--VINDGdkpkvqvsykgetkafypeeissmvltkmkEIAEAYLGY-----------PVTNAVITVPAYF 150
Cdd:cd10225 58 -----IRPLRdgVIADF------------------------------EATEAMLRYfirkahrrrgfLRPRVVIGVPSGI 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 151 NDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRT-GKGernVLIFDLGGGTFDVSILTIdDGIFEVKAtagdTHLG 229
Cdd:cd10225 103 TEVERRAVKEAAEHAGAREVYLIEEPMAAAIGAGLPIEePRG---SMVVDIGGGTTEIAVISL-GGIVTSRS----VRVA 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 230 GEDFDNRLVNHfveeFKRKHKKDISqnkravrrLRTAcERAKRTLSSstqASLEIDSL---FEGIDFYTSITRARfeELC 306
Cdd:cd10225 175 GDEMDEAIINY----VRRKYNLLIG--------ERTA-ERIKIEIGS---AYPLDEELsmeVRGRDLVTGLPRTI--EIT 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 307 SDLFRSTLEP----VEKALRDAkLDK------AQIHD--LVLVGGSTRIPKVQKLLQDFFngrDLNKSI--NPDEAVAYG 372
Cdd:cd10225 237 SEEVREALEEpvnaIVEAVRST-LERtppelaADIVDrgIVLTGGGALLRGLDELLREET---GLPVHVadDPLTCVAKG 312
|
...
gi 167466173 373 AAV 375
Cdd:cd10225 313 AGK 315
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
7-374 |
2.86e-13 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 71.32 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 7 IGIDLGTTYscVGVFQHGKvEIIANDqgnrttPSYVAF-TDTERL--IGDaaknqvalnpqntvfDAKRLIGRKFGDPVV 83
Cdd:PRK13930 11 IGIDLGTAN--TLVYVKGK-GIVLNE------PSVVAIdTKTGKVlaVGE---------------EAKEMLGRTPGNIEA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 84 QSDMKHwpfQVINDGDKPKVQVSYkgetkaFYpeeisSMVLTKMkeiaeaYLGYPvtNAVITVPAYFNDSQRQATKDAGV 163
Cdd:PRK13930 67 IRPLKD---GVIADFEATEAMLRY------FI-----KKARGRR------FFRKP--RIVICVPSGITEVERRAVREAAE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 164 IAGLNVLRIINEPTAAAIAYGLDRTgKGERNvLIFDLGGGTFDVSILTIdDGIfevkATAGDTHLGGEDFDNRLVNHfve 243
Cdd:PRK13930 125 HAGAREVYLIEEPMAAAIGAGLPVT-EPVGN-MVVDIGGGTTEVAVISL-GGI----VYSESIRVAGDEMDEAIVQY--- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 244 eFKRKHKKDISQnkravrrlRTAcERAKRTLSSSTQA----SLEIdslfEGIDFYTSITRARfeELCSDLFRSTL-EPVE 318
Cdd:PRK13930 195 -VRRKYNLLIGE--------RTA-EEIKIEIGSAYPLdeeeSMEV----RGRDLVTGLPKTI--EISSEEVREALaEPLQ 258
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167466173 319 K---ALRDAkLDK------AQIHD--LVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAA 374
Cdd:PRK13930 259 QiveAVKSV-LEKtppelaADIIDrgIVLTGGGALLRGLDKLLSEET-GLPVHIAEDPLTCVARGTG 323
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
7-374 |
6.09e-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: 6.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 7 IGIDLGTtySCVGVFQHGKvEIIANDqgnrttPSYVAF-TDTERLI--GDAAKNQVALNPQNTVfdAKRligrkfgdpvv 83
Cdd:COG1077 10 IGIDLGT--ANTLVYVKGK-GIVLNE------PSVVAIdKKTGKVLavGEEAKEMLGRTPGNIV--AIR----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 84 qsdmkhwPFQ--VINDgdkpkvqvsykgetkaFypeeissmvltkmkEIAEAYLGY-----------PVTNAVITVPAYF 150
Cdd:COG1077 68 -------PLKdgVIAD----------------F--------------EVTEAMLKYfikkvhgrrsfFRPRVVICVPSGI 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 151 NDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLD---RTGkgernVLIFDLGGGTFDVSILTIdDGIfeVKATAgdTH 227
Cdd:COG1077 111 TEVERRAVRDAAEQAGAREVYLIEEPMAAAIGAGLPieePTG-----NMVVDIGGGTTEVAVISL-GGI--VVSRS--IR 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 228 LGGEDFDNRLVNHfveeFKRKHKKDISQnkravrrlRTAcERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARfeELCS 307
Cdd:COG1077 181 VAGDELDEAIIQY----VRKKYNLLIGE--------RTA-EEIKIEIGSAYPLEEELTMEVRGRDLVTGLPKTI--TITS 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 308 DLFRSTLEP----VEKALRDAkLDK------AQIHD--LVLVGGSTRIPKVQKLLQDFFNgrdLNKSI--NPDEAVAYGA 373
Cdd:COG1077 246 EEIREALEEplnaIVEAIKSV-LEKtppelaADIVDrgIVLTGGGALLRGLDKLLSEETG---LPVHVaeDPLTCVARGT 321
|
.
gi 167466173 374 A 374
Cdd:COG1077 322 G 322
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
123-228 |
1.13e-08 |
|
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity.
Pssm-ID: 466897 [Multi-domain] Cd Length: 241 Bit Score: 56.12 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 123 VLTKMKEIAEAYLGYPVTNAVITVPAyfNDSQRQATKDAGVI--AGLNVLRIINEPTAAAIAYGLdrtgkgeRNVLIFDL 200
Cdd:cd24047 48 IVRKLKETLEKKLGVELTSAATAFPP--GTGERDARAIRNVLegAGLEVSNVVDEPTAANAVLGI-------RDGAVVDI 118
|
90 100 110
....*....|....*....|....*....|..
gi 167466173 201 GGGTFDVSIltIDDGifEVKATA----GDTHL 228
Cdd:cd24047 119 GGGTTGIAV--LKDG--KVVYTAdeptGGTHL 146
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
7-373 |
2.12e-08 |
|
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.
Pssm-ID: 399596 [Multi-domain] Cd Length: 327 Bit Score: 56.41 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 7 IGIDLGTTYSCVGVFQHGkveIIANDqgnrttPSYVAF-TDTERLI--GDaaknqvalnpqntvfDAKRLIGRKFGDPVV 83
Cdd:pfam06723 4 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAInTKTKKVLavGN---------------EAKKMLGRTPGNIVA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 84 QSDMKhwpfqvinDGdkpkvqvsykgetkafypeeissmVLTKMkEIAEAYLGY-----------PVTNAVITVPAYFND 152
Cdd:pfam06723 60 VRPLK--------DG------------------------VIADF-EVTEAMLKYfikkvhgrrsfSKPRVVICVPSGITE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 153 SQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDrTGKGERNvLIFDLGGGTFDVSILTIdDGIfevkATAGDTHLGGED 232
Cdd:pfam06723 107 VERRAVKEAAKNAGAREVFLIEEPMAAAIGAGLP-VEEPTGN-MVVDIGGGTTEVAVISL-GGI----VTSKSVRVAGDE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 233 FDNRLVNHfveeFKRKHKKDISQnkravrrlRTAcERAKRTLSSSTQA----SLEIdslfEGIDFYT------SITRARF 302
Cdd:pfam06723 180 FDEAIIKY----IRKKYNLLIGE--------RTA-ERIKIEIGSAYPTeeeeKMEI----RGRDLVTglpktiEISSEEV 242
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167466173 303 EELCSDLFRSTLEPVEKALRDAKLD-KAQIHD--LVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGA 373
Cdd:pfam06723 243 REALKEPVSAIVEAVKEVLEKTPPElAADIVDrgIVLTGGGALLRGLDKLLSDET-GLPVHIAEDPLTCVALGT 315
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
7-250 |
2.04e-07 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 53.37 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 7 IGIDLGTtySCVGVFQHGKvEIIANDqgnrttPSYVAF-TDTERLI--GDaaknqvalnpqntvfDAKRLIGRKFGDPVV 83
Cdd:PRK13928 6 IGIDLGT--ANVLVYVKGK-GIVLNE------PSVVAIdKNTNKVLavGE---------------EARRMVGRTPGNIVA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 84 QSDMKHwpfQVINDGDkpkvqvsykgetkafypeeissmvltkmkeIAEAYLGYPVTNA-----------VITVPAYFND 152
Cdd:PRK13928 62 IRPLRD---GVIADYD------------------------------VTEKMLKYFINKAcgkrffskpriMICIPTGITS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 153 SQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTgKGERNVLIfDLGGGTFDVSILTIDDGIfevkaTAGDTHLGGED 232
Cdd:PRK13928 109 VEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLDIS-QPSGNMVV-DIGGGTTDIAVLSLGGIV-----TSSSIKVAGDK 181
|
250
....*....|....*...
gi 167466173 233 FDNRLVNHfveeFKRKHK 250
Cdd:PRK13928 182 FDEAIIRY----IRKKYK 195
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
143-357 |
2.09e-07 |
|
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: 53.86 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 143 VITVPAYFNDSQRQATKDAGVIAGLNV------LRIINEPTAAAIAYGLDRTGKGERNVLIfDLGGGTFDVSI--LTIDD 214
Cdd:cd11735 144 VITVPAIWKQPAKQFMRQAAYKAGLASpenpeqLIIALEPEAASIYCRKLRLHQMDRYVVV-DCGGGTVDLTVhqIRLPE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 215 GIFE--VKATAGDTHLGGEDFD-NRLV-----NHFVEEFKRKHKKdisqnkrAVRRLRTACERAKRTLSSSTQASLEIDS 286
Cdd:cd11735 223 GHLKelYKASGGPYGSLGVDYEfEKLLckifgEDFIDQFKIKRPA-------AWVDLMIAFESRKRAAAPDRTNPLNITL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 287 LFEGIDFYTSITRARFE-----------------------ELCSDLFRSTLEPVEKALRD--AKLDKAQIHDLVLVGGST 341
Cdd:cd11735 296 PFSFIDYYKKFRGHSVEhalrksnvdfvkwssqgmlrmspDAMNALFKPTIDHIIQHLTDlfQKPEVSGVKFLFLVGGFA 375
|
250
....*....|....*.
gi 167466173 342 RIPKVQKLLQDFFNGR 357
Cdd:cd11735 376 ESPLLQQAVQNAFGDQ 391
|
|
| ASKHA_NBD_MamK |
cd24009 |
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ... |
7-373 |
3.94e-07 |
|
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: 52.21 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 7 IGIDLGTTYSCvgvfqhgkveiIANDQGNR-TTPSYVAFTD---------TERLIGDAA-KNQVALNpqntvfdakrlig 75
Cdd:cd24009 4 IGIDLGTSRSA-----------VVTSRGKRfSFRSVVGYPKdiiarkllgKEVLFGDEAlENRLALD------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 76 rkfgdpvvqsdmKHWPFQ--VINDGDKPKvqvsykgetkafypEEISSMVLTKMKEIAEAyLGYPVTNAVITVPAYFNDS 153
Cdd:cd24009 60 ------------LRRPLEdgVIKEGDDRD--------------LEAARELLQHLIELALP-GPDDEIYAVIGVPARASAE 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 154 QRQATKDA--GVIAGLnvlRIINEPTAaaIAYGLDRTgkgeRNVLIFDLGGGTFDV-----SILTIDDGIFEVKAtagdt 226
Cdd:cd24009 113 NKQALLEIarELVDGV---MVVSEPFA--VAYGLDRL----DNSLIVDIGAGTTDLcrmkgTIPTEEDQITLPKA----- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 227 hlgGEDFDNRLvnhfVEEFKRKHkKDISQNKRAVRRLrtaceraKRTLSSSTQASLEIDSLF--EGIDFYTSITrarfEE 304
Cdd:cd24009 179 ---GDYIDEEL----VDLIKERY-PEVQLTLNMARRW-------KEKYGFVGDASEPVKVELpvDGKPVTYDIT----EE 239
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167466173 305 L---CSDLFRSTLEPVEKALRDAKLDKAQ--IHDLVLVGGSTRI----PKVQKLLQDFFNGRdLNKSINPDEAVAYGA 373
Cdd:cd24009 240 LriaCESLVPDIVEGIKKLIASFDPEFQEelRNNIVLAGGGSRIrgldTYIEKALKEYGGGK-VTCVDDPVFAGAEGA 316
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
127-357 |
4.15e-07 |
|
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: 52.66 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 127 MKEIAEAYLGYPVTNA---VITVPAYFNDSQRQATKDAGVIAGL------NVLRIINEPTAAAI-AYGLDRtgkgernVL 196
Cdd:cd11736 125 LQELKDQSPSLPEKDAvrwVLTVPAIWKQPAKQFMREAAYLAGLvspenpEQLLIALEPEAASIyCRKLDR-------YI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 197 IFDLGGGTFDVSILTIDD--GIFE--VKATAGDTHLGGED--FDNRLVNHFVEEFKRKHKkdiSQNKRAVRRLRTACERA 270
Cdd:cd11736 198 VADCGGGTVDLTVHQIEQpqGTLKelYKASGGPYGAVGVDlaFEKLLCQIFGEDFIATFK---AKRPAAWVDLTIAFEAR 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 271 KRTlssstqASLEIDSlfegidfytsitrarfeELCSDLFRSTLEPVEKALRD--AKLDKAQIHDLVLVGGSTRIPKVQK 348
Cdd:cd11736 275 KRT------AALRMSS-----------------EAMNELFQPTISQIIQHIDDlmKKPEVKGIKFLFLVGGFAESPMLQR 331
|
....*....
gi 167466173 349 LLQDFFNGR 357
Cdd:cd11736 332 AVQAAFGNI 340
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
121-355 |
6.14e-07 |
|
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: 51.52 E-value: 6.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 121 SMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKdagviAGLNVLRIINEPTAAAiaYGLDRTGKGERNVLIFDL 200
Cdd:cd24004 49 AESIKELLKELEEKLGSKLKDVVIAIAKVVESLLNVLEK-----AGLEPVGLTLEPFAAA--NLLIPYDMRDLNIALVDI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 201 GGGTFDVSIltIDDGifEVKATaGDTHLGGEDFDNRLVNHFveefkrkhkkDISQNKravrrlrtaCERAKRTLSSST-- 278
Cdd:cd24004 122 GAGTTDIAL--IRNG--GIEAY-RMVPLGGDDFTKAIAEGF----------LISFEE---------AEKIKRTYGIFLli 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167466173 279 QASLEIDSLFEGIDFYTSITRArFEELCSDLFRSTLEpvekalrdakLDK--AQIHDLVLVGGSTRIPKVQKLLQDFFN 355
Cdd:cd24004 178 EAKDQLGFTINKKEVYDIIKPV-LEELASGIANAIEE----------YNGkfKLPDAVYLVGGGSKLPGLNEALAEKLG 245
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
1-240 |
1.33e-05 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 47.59 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 1 MAKAAAIGIDLGTTYSCVGVFQHGkveIIANDqgnrttPSYVAFtDTErligdaAKNQVALNPqntvfDAKRLIGRKFGD 80
Cdd:PRK13929 1 MFQSTEIGIDLGTANILVYSKNKG---IILNE------PSVVAV-DTE------TKAVLAIGT-----EAKNMIGKTPGK 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 81 PVVQSDMKHwpfQVINDGDkpkvqvsykgetkafypeeISSMVLTKMKEIAEAYLGYPV--TNAVITVPAYFNDSQRQAT 158
Cdd:PRK13929 60 IVAVRPMKD---GVIADYD-------------------MTTDLLKQIMKKAGKNIGMTFrkPNVVVCTPSGSTAVERRAI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 159 KDAGVIAGLNVLRIINEPTAAAIAYGLDrTGKGERNVLIfDLGGGTFDVSILTiddgiFEVKATAGDTHLGGEDFDNRLV 238
Cdd:PRK13929 118 SDAVKNCGAKNVHLIEEPVAAAIGADLP-VDEPVANVVV-DIGGGTTEVAIIS-----FGGVVSCHSIRIGGDQLDEDIV 190
|
..
gi 167466173 239 NH 240
Cdd:PRK13929 191 SF 192
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
123-228 |
1.37e-05 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 47.13 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 123 VLTKMKEIAEAYLGYPVTNAVITVPAyfndsqrqAT--KDAGVI------AGLNVLRIINEPTAAAIAYGLDrtgkgerN 194
Cdd:PRK15080 72 IVRRLKATLEEKLGRELTHAATAIPP--------GTseGDPRAIinvvesAGLEVTHVLDEPTAAAAVLGID-------N 136
|
90 100 110
....*....|....*....|....*....|....*...
gi 167466173 195 VLIFDLGGGTFDVSILtiDDGifEVKATA----GDTHL 228
Cdd:PRK15080 137 GAVVDIGGGTTGISIL--KDG--KVVYSAdeptGGTHM 170
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
7-351 |
1.81e-05 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 47.55 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 7 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTE-------RLIGDAA---KNQVAL--------------N 62
Cdd:PRK11678 3 IGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTLCAPTREavsewlyRHLDVPAyddERQALLrrairynreedidvT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 63 PQnTVFDAKRLIGRKFGDP----VVQSdmkhwpfqvindgdkPKvqvSYKGETK------AFYpEEISSMVLTKMKEIAE 132
Cdd:PRK11678 83 AQ-SVFFGLAALAQYLEDPeevyFVKS---------------PK---SFLGASGlkpqqvALF-EDLVCAMMLHIKQQAE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 133 AYLGYPVTNAVITVPAYFN-----DSQRQAT---KDAGVIAGLNVLRIINEPTAAaiayGLD--RTGKGERNVLIFDLGG 202
Cdd:PRK11678 143 AQLQAAITQAVIGRPVNFQglggeEANRQAEgilERAAKRAGFKDVEFQFEPVAA----GLDfeATLTEEKRVLVVDIGG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 203 GTFDVSILTIddgifevkataGDTH-----------------LGGEDFDNRL-VNHFV---------------------- 242
Cdd:PRK11678 219 GTTDCSMLLM-----------GPSWrgradrsasllghsgqrIGGNDLDIALaFKQLMpllgmgsetekgialpslpfwn 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 243 -----------EEFKRKHKKDISQNKR------AVRRL-------------RTAcERAKRTLSSSTQASLEIDSLFEGID 292
Cdd:PRK11678 288 avaindvpaqsDFYSLANGRLLNDLIRdarepeKVARLlkvwrqrlsyrlvRSA-EEAKIALSDQAETRASLDFISDGLA 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167466173 293 fyTSITRARFEELCSdlfrSTLEPVEKALRDAkLDKAQIH-DLV-LVGGSTRIPKVQKLLQ 351
Cdd:PRK11678 367 --TEISQQGLEEAIS----QPLARILELVQLA-LDQAQVKpDVIyLTGGSARSPLIRAALA 420
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
288-382 |
1.93e-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: 47.52 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 288 FEGIDFYTsiTRArfeelcsDLFRSTLEPVEKALRDAkLD-----KAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKS 362
Cdd:COG1070 358 FFGLTLSH--TRA-------HLARAVLEGVAFALRDG-LEaleeaGVKIDRIRATGGGARSPLWRQILADVL-GRPVEVP 426
|
90 100
....*....|....*....|
gi 167466173 363 iNPDEAVAYGAAVQAAILMG 382
Cdd:COG1070 427 -EAEEGGALGAALLAAVGLG 445
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
165-355 |
2.60e-05 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 47.05 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 165 AGLNVLRIINEPTAAAIAYgLDRTGKgERNVLIFDLGGGTFDVSILTidDGIfeVKATAGDThLGGedfdnrlvNHFVee 244
Cdd:COG0849 174 AGLEVEDLVLSPLASAEAV-LTEDEK-ELGVALVDIGGGTTDIAVFK--DGA--LRHTAVIP-VGG--------DHIT-- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 245 fkrkhkKDISqnkravRRLRT---ACERAKRTLSSSTQASLEIDSLFE----GIDFYTSITR--------ARFEELcsdl 309
Cdd:COG0849 237 ------NDIA------IGLRTpleEAERLKIKYGSALASLADEDETIEvpgiGGRPPREISRkelaeiieARVEEI---- 300
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 167466173 310 frstLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFN 355
Cdd:COG0849 301 ----FELVRKELKRSGYEEKLPAGVVLTGGGSQLPGLVELAEEILG 342
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
143-276 |
1.59e-04 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 44.31 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 143 VITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLD---RTGkgernVLIFDLGGGTFDVSILTIdDGIfev 219
Cdd:PRK13927 100 VICVPSGITEVERRAVRESALGAGAREVYLIEEPMAAAIGAGLPvtePTG-----SMVVDIGGGTTEVAVISL-GGI--- 170
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 167466173 220 kATAGDTHLGGEDFDNRLVNHfveeFKRKHKKDISQnkravrrlRTAcERAKRTLSS 276
Cdd:PRK13927 171 -VYSKSVRVGGDKFDEAIINY----VRRNYNLLIGE--------RTA-ERIKIEIGS 213
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
167-255 |
1.78e-04 |
|
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: 43.67 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 167 LNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTfdVSILTIDDGIFEVKatAGDTHLGGEDFDNRLVNHFVEEFK 246
Cdd:cd10227 137 INDVKVLPEGAGAYLDYLLDDDELEDGNVLVIDIGGGT--TDILTFENGKPIEE--SSDTLPGGEEALEKYADDILNELL 212
|
....*....
gi 167466173 247 RKHKKDISQ 255
Cdd:cd10227 213 KKLGDELDS 221
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
165-372 |
2.24e-04 |
|
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; 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. FtsA binds ATP. FtsA interacts with FtsZ. This interaction plays an essential role in cell division.
Pssm-ID: 466898 [Multi-domain] Cd Length: 372 Bit Score: 44.06 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 165 AGLNVLRIINEPTAAAIAYgLDRTGKgERNVLIFDLGGGTFDVSILTidDGIFEvkatagDTH---LGGEDFDNrlvnhf 241
Cdd:cd24048 172 AGLEVDDIVLSPLASAEAV-LTEDEK-ELGVALIDIGGGTTDIAVFK--NGSLR------YTAvipVGGNHITN------ 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 242 veefkrkhkkDISQnkrAVRRLRTACERAKRTLSSSTQASLEIDSLFE--GIDFYTS----------ITRARFEELcsdl 309
Cdd:cd24048 236 ----------DIAI---GLNTPFEEAERLKIKYGSALSEEADEDEIIEipGVGGREPrevsrrelaeIIEARVEEI---- 298
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167466173 310 frstLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFN-----------GRDLNKSINPDEAVAYG 372
Cdd:cd24048 299 ----LELVKKELKESGYEDLLPGGIVLTGGGSQLPGLVELAEEVFGmpvrigrpkniGGLPEEVNDPAYATAVG 368
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
142-204 |
1.26e-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: 39.37 E-value: 1.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167466173 142 AVITVPAYFNDSQRQAT-----------KDAGVIAGLNVLRIINEPTAAAIAYGLDRtgkGERNVLIFDLGGGT 204
Cdd:cd00012 16 IVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGALLTL---GPEGLLVVDLGGGT 86
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
497-602 |
6.66e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 497 KANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAK-NALESYAFNMKSAVED-EGLKGK-------ISEADK 567
Cdd:PRK03918 371 KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARiGELKKEIKELKKAIEElKKAKGKcpvcgreLTEEHR 450
|
90 100 110
....*....|....*....|....*....|....*.
gi 167466173 568 KKVLDKCQEVISWLdANTLAEKDEFEHK-RKELEQV 602
Cdd:PRK03918 451 KELLEEYTAELKRI-EKELKEIEEKERKlRKELREL 485
|
|
| |
