|
Name |
Accession |
Description |
Interval |
E-value |
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
1-641 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 1245.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 1 MGKIIGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDGEILVGQPAKRQAITNPKNTLFAIKRLIGRRfeDD 80
Cdd:PRK00290 1 MGKIIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRLMGRR--DE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 81 EVQRDLKIMPYAIAKADNGDAWVEVKGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRI 160
Cdd:PRK00290 79 EVQKDIKLVPYKIVKADNGDAWVEIDGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDAGKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 161 AGLDVKRIINEPTAAAFAYGVNKvKGERKVAVYDLGGGTFDISIIEIdeveGETTFEVLATNGNTHLGGEDFDNRVINYL 240
Cdd:PRK00290 159 AGLEVLRIINEPTAAALAYGLDK-KGDEKILVYDLGGGTFDVSILEI----GDGVFEVLSTNGDTHLGGDDFDQRIIDYL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 241 VDEFKREQGIDLRNDQLALQRLKDAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDMVKDSLEPV 320
Cdd:PRK00290 234 ADEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEINLPFITADASGPKHLEIKLTRAKFEELTEDLVERTIEPC 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 321 RVALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGAVLSGDKTDVLLLDVTPLSLG 400
Cdd:PRK00290 314 KQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLAGDVKDVLLLDVTPLSLG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 401 IETMGSVMTALIEKNTTIPTKKSQVFSTAEDNQSAVTIHVLQGERKRASDNKSLGQFNLEGIRPAPRGLPQIEVTFDIDA 480
Cdd:PRK00290 394 IETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDIDA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 481 NGILHVSAKDKETNKEQKITIQASSGLSDDEIERMVREAEANAAEDKKFEELVQARNQADGLVHSVRKQITEAGEALPAD 560
Cdd:PRK00290 474 NGIVHVSAKDKGTGKEQSITITASSGLSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKELGDKVPAD 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 561 EKTKIETALSELETAIKGDDKAAIEAKQQALLEASQKLMEiaqqqaqAQGAAGADAGQSSSSAKADDDVVDAEFEEVKDD 640
Cdd:PRK00290 554 EKEKIEAAIKELKEALKGEDKEAIKAKTEELTQASQKLGE-------AMYQQAQAAQGAAGAAAKDDDVVDAEFEEVKDD 626
|
.
gi 2058542806 641 K 641
Cdd:PRK00290 627 K 627
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
3-600 |
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: 1027.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 3 KIIGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDGEILVGQPAKRQAITNPKNTLFAIKRLIGRRFedDEV 82
Cdd:TIGR02350 1 KIIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNGERLVGQPAKRQAVTNPENTIYSIKRFMGRRF--DEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 83 QRDLKIMPYAIaKADNGDAWVEVKGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAG 162
Cdd:TIGR02350 79 TEEAKRVPYKV-VGDGGDVRVKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 163 LDVKRIINEPTAAAFAYGVNKVKGERKVAVYDLGGGTFDISIIEIdeveGETTFEVLATNGNTHLGGEDFDNRVINYLVD 242
Cdd:TIGR02350 158 LEVLRIINEPTAAALAYGLDKSKKDEKILVFDLGGGTFDVSILEI----GDGVFEVLSTAGDTHLGGDDFDQRIIDWLAD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 243 EFKREQGIDLRNDQLALQRLKDAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDMVKDSLEPVRV 322
Cdd:TIGR02350 234 EFKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINLPFITADASGPKHLEMTLTRAKFEELTADLVERTKEPVRQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 323 ALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGAVLSGDKTDVLLLDVTPLSLGIE 402
Cdd:TIGR02350 314 ALKDAGLSASDIDEVILVGGSTRIPAVQELVKDFFGKEPNKSVNPDEVVAIGAAIQGGVLKGDVKDVLLLDVTPLSLGIE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 403 TMGSVMTALIEKNTTIPTKKSQVFSTAEDNQSAVTIHVLQGERKRASDNKSLGQFNLEGIRPAPRGLPQIEVTFDIDANG 482
Cdd:TIGR02350 394 TLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDANG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 483 ILHVSAKDKETNKEQKITIQASSGLSDDEIERMVREAEANAAEDKKFEELVQARNQADGLVHSVRKQITEAGEALPADEK 562
Cdd:TIGR02350 474 ILHVSAKDKGTGKEQSITITASSGLSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAGDKLPAEEK 553
|
570 580 590
....*....|....*....|....*....|....*...
gi 2058542806 563 TKIETALSELETAIKGDDKAAIEAKQQALLEASQKLME 600
Cdd:TIGR02350 554 EKIEKAVAELKEALKGEDVEEIKAKTEELQQALQKLAE 591
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
4-600 |
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: 925.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 4 IIGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDgEILVGQPAKRQAITNPKNTLFAIKRLIGRRFEDDEVQ 83
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPK-ERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 84 RDLKIMPYAIAKADNGDAWVEV--KGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIA 161
Cdd:pfam00012 80 RDIKHLPYKVVKLPNGDAGVEVryLGETFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 162 GLDVKRIINEPTAAAFAYGVNKVKGERKVAVYDLGGGTFDISIIEIdeveGETTFEVLATNGNTHLGGEDFDNRVINYLV 241
Cdd:pfam00012 160 GLNVLRIVNEPTAAALAYGLDKTDKERNIAVYDLGGGTFDVSILEI----GRGVFEVKATNGDTHLGGEDFDLRLVDHLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 242 DEFKREQGIDLRNDQLALQRLKDAAEKAKIELSSAQqTDVNLPYITADATGpKHMNIKVTRAKLESLVEDMVKDSLEPVR 321
Cdd:pfam00012 236 EEFKKKYGIDLSKDKRALQRLREAAEKAKIELSSNQ-TNINLPFITAMADG-KDVSGTLTRAKFEELVADLFERTLEPVE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 322 VALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGAVLSGDK--TDVLLLDVTPLSL 399
Cdd:pfam00012 314 KALKDAGLSKSEIDEVVLVGGSTRIPAVQELVKEFFGKEPSKGVNPDEAVAIGAAVQAGVLSGTFdvKDFLLLDVTPLSL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 400 GIETMGSVMTALIEKNTTIPTKKSQVFSTAEDNQSAVTIHVLQGERKRASDNKSLGQFNLEGIRPAPRGLPQIEVTFDID 479
Cdd:pfam00012 394 GIETLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDID 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 480 ANGILHVSAKDKETNKEQKITIQASSGLSDDEIERMVREAEANAAEDKKFEELVQARNQADGLVHSVRKQITEAGEALPA 559
Cdd:pfam00012 474 ANGILTVSAKDKGTGKEQEITIEASEGLSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGDKVPE 553
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2058542806 560 DEKTKIETALSELETAIKGDDKAAIEAKQQALLEASQKLME 600
Cdd:pfam00012 554 AEKSKVESAIEWLKDELEGDDKEEIEAKTEELAQVSQKIGE 594
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
2-598 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 851.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 2 GKIIGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDGEILVGQPAKRQAITNPKNTLFAIKRLIGRRFEDDE 81
Cdd:PTZ00400 41 GDIVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDGQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEDA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 82 VQRDLKIMPYAIAKADNGDAWVEVKGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIA 161
Cdd:PTZ00400 121 TKKEQKILPYKIVRASNGDAWIEAQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAGKIA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 162 GLDVKRIINEPTAAAFAYGVNKVKGeRKVAVYDLGGGTFDISIIEIdeVEGetTFEVLATNGNTHLGGEDFDNRVINYLV 241
Cdd:PTZ00400 201 GLDVLRIINEPTAAALAFGMDKNDG-KTIAVYDLGGGTFDISILEI--LGG--VFEVKATNGNTSLGGEDFDQRILNYLI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 242 DEFKREQGIDLRNDQLALQRLKDAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDMVKDSLEPVR 321
Cdd:PTZ00400 276 AEFKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQTEINLPFITADQSGPKHLQIKLSRAKLEELTHDLLKKTIEPCE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 322 VALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGAVLSGDKTDVLLLDVTPLSLGI 401
Cdd:PTZ00400 356 KCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIFGKEPSKGVNPDEAVAMGAAIQAGVLKGEIKDLLLLDVTPLSLGI 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 402 ETMGSVMTALIEKNTTIPTKKSQVFSTAEDNQSAVTIHVLQGERKRASDNKSLGQFNLEGIRPAPRGLPQIEVTFDIDAN 481
Cdd:PTZ00400 436 ETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTFDVDAN 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 482 GILHVSAKDKETNKEQKITIQASSGLSDDEIERMVREAEANAAEDKKFEELVQARNQADGLVHSVRKQITEAGEALPADE 561
Cdd:PTZ00400 516 GIMNISAVDKSTGKKQEITIQSSGGLSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSDLKDKISDAD 595
|
570 580 590
....*....|....*....|....*....|....*..
gi 2058542806 562 KTKIETALSELETAIKGDDKAAIEAKQQALLEASQKL 598
Cdd:PTZ00400 596 KDELKQKITKLRSTLSSEDVDSIKDKTKQLQEASWKI 632
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
1-636 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 812.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 1 MGKIIGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDGEILVGQPAKRQAITNPKNTLFAIKRLIGRRFedD 80
Cdd:CHL00094 1 MGKVVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKGDLLVGQIAKRQAVINPENTFYSVKRFIGRKF--S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 81 EVQRDLKIMPYAIAKADNGDAWVE--VKGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAG 158
Cdd:CHL00094 79 EISEEAKQVSYKVKTDSNGNIKIEcpALNKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 159 RIAGLDVKRIINEPTAAAFAYGVNKVKGErKVAVYDLGGGTFDISIIEIdeveGETTFEVLATNGNTHLGGEDFDNRVIN 238
Cdd:CHL00094 159 KIAGLEVLRIINEPTAASLAYGLDKKNNE-TILVFDLGGGTFDVSILEV----GDGVFEVLSTSGDTHLGGDDFDKKIVN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 239 YLVDEFKREQGIDLRNDQLALQRLKDAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDMVKDSLE 318
Cdd:CHL00094 234 WLIKEFKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINLPFITATQTGPKHIEKTLTRAKFEELCSDLINRCRI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 319 PVRVALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGAVLSGDKTDVLLLDVTPLS 398
Cdd:CHL00094 314 PVENALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLLGKKPNQSVNPDEVVAIGAAVQAGVLAGEVKDILLLDVTPLS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 399 LGIETMGSVMTALIEKNTTIPTKKSQVFSTAEDNQSAVTIHVLQGERKRASDNKSLGQFNLEGIRPAPRGLPQIEVTFDI 478
Cdd:CHL00094 394 LGVETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDI 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 479 DANGILHVSAKDKETNKEQKITIQASSGLSDDEIERMVREAEANAAEDKKFEELVQARNQADGLVHSVRKQITEAGEALP 558
Cdd:CHL00094 474 DANGILSVTAKDKGTGKEQSITIQGASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKELKDKIS 553
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2058542806 559 ADEKTKIETALSELETAIKGDDKAAIEAKQQALLEAsqkLMEIaqqqaqaqGAAGADAGQSSSSAKADDDVVDAEFEE 636
Cdd:CHL00094 554 EEKKEKIENLIKKLRQALQNDNYESIKSLLEELQKA---LMEI--------GKEVYSSTSTTDPASNDDDVIDTDFSE 620
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
1-593 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 798.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 1 MGKIIGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDGEILVGQPAKRQAITNPKNTLFAIKRLIGRRFEDD 80
Cdd:PRK13411 1 MGKVIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSGDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 81 EVQRDLkiMPYAIAKADNGDAWVEVKGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRI 160
Cdd:PRK13411 81 EEERSR--VPYTCVKGRDDTVNVQIRGRNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAGTI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 161 AGLDVKRIINEPTAAAFAYGVNKVKGERKVAVYDLGGGTFDISIIEIdeveGETTFEVLATNGNTHLGGEDFDNRVINYL 240
Cdd:PRK13411 159 AGLEVLRIINEPTAAALAYGLDKQDQEQLILVFDLGGGTFDVSILQL----GDGVFEVKATAGNNHLGGDDFDNCIVDWL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 241 VDEFKREQGIDLRNDQLALQRLKDAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDMVKDSLEPV 320
Cdd:PRK13411 235 VENFQQQEGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINLPFITADETGPKHLEMELTRAKFEELTKDLVEATIEPM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 321 RVALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFF-GKEPRKDVNPDEAVAMGAAIQGAVLSGDKTDVLLLDVTPLSL 399
Cdd:PRK13411 315 QQALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFgGKQPDRSVNPDEAVALGAAIQAGVLGGEVKDLLLLDVTPLSL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 400 GIETMGSVMTALIEKNTTIPTKKSQVFSTAEDNQSAVTIHVLQGERKRASDNKSLGQFNLEGIRPAPRGLPQIEVTFDID 479
Cdd:PRK13411 395 GIETLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSFEID 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 480 ANGILHVSAKDKETNKEQKITIQASSGLSDDEIERMVREAEANAAEDKKFEELVQARNQADGLVHSVRKQITEAGEALPA 559
Cdd:PRK13411 475 VNGILKVSAQDQGTGREQSIRITNTGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKENGELISE 554
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2058542806 560 DEKTKIETALSELETAIKGDD------KAAIEAKQQALLE 593
Cdd:PRK13411 555 ELKQRAEQKVEQLEAALTDPNisleelKQQLEEFQQALLA 594
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
1-594 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 777.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 1 MGKIIGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDGEILVGQPAKRQAITNPKNTLFAIKRLIGRRFedD 80
Cdd:PRK13410 1 MGRIVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTKDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRY--D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 81 EVQRDLKIMPYAIAKADNGDawVEVK----GKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKD 156
Cdd:PRK13410 79 ELDPESKRVPYTIRRNEQGN--VRIKcprlEREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 157 AGRIAGLDVKRIINEPTAAAFAYGVNKvKGERKVAVYDLGGGTFDISIIEIdeveGETTFEVLATNGNTHLGGEDFDNRV 236
Cdd:PRK13410 157 AGRIAGLEVERILNEPTAAALAYGLDR-SSSQTVLVFDLGGGTFDVSLLEV----GNGVFEVKATSGDTQLGGNDFDKRI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 237 INYLVDEFKREQGIDLRNDQLALQRLKDAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDMVKDS 316
Cdd:PRK13410 232 VDWLAEQFLEKEGIDLRRDRQALQRLTEAAEKAKIELSGVSVTDISLPFITATEDGPKHIETRLDRKQFESLCGDLLDRL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 317 LEPVRVALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGAVLSGDKTDVLLLDVTP 396
Cdd:PRK13410 312 LRPVKRALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLIPREPNQNVNPDEVVAVGAAIQAGILAGELKDLLLLDVTP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 397 LSLGIETMGSVMTALIEKNTTIPTKKSQVFSTAEDNQSAVTIHVLQGERKRASDNKSLGQFNLEGIRPAPRGLPQIEVTF 476
Cdd:PRK13410 392 LSLGLETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 477 DIDANGILHVSAKDKETNKEQKITIQASSGLSDDEIERMVREAEANAAEDKKFEELVQARNQADGLVHSVRKQITEA--- 553
Cdd:PRK13410 472 DIDANGILQVSATDRTTGREQSVTIQGASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERRLRDAale 551
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 2058542806 554 -GEALPADEKTKIETALSELETAIKGDDKAAIEAKQQALLEA 594
Cdd:PRK13410 552 fGPYFAERQRRAVESAMRDVQDSLEQDDDRELDLAVADLQEA 593
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
4-516 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 758.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 4 IIGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDGEILVGQPAKRQAITNPKNTLFAIKRLIGRRFEDdevq 83
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPKDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 84 rdlkimpyaiakadngdAWVEVKGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGL 163
Cdd:COG0443 77 -----------------EATEVGGKRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARIAGL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 164 DVKRIINEPTAAAFAYGVNKVKGERKVAVYDLGGGTFDISIIEIdeveGETTFEVLATNGNTHLGGEDFDNRVINYLVDE 243
Cdd:COG0443 140 EVLRLLNEPTAAALAYGLDKGKEEETILVYDLGGGTFDVSILRL----GDGVFEVLATGGDTHLGGDDFDQALADYVAPE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 244 FKREQGIDLRNDQLALQRLKDAAEKAKIELSSAQQTDVNLPYitadaTGPKHMNIKVTRAKLESLVEDMVKDSLEPVRVA 323
Cdd:COG0443 216 FGKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINLPF-----SGGKHLDVELTRAEFEELIAPLVERTLDPVRQA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 324 LKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGAVLSGDKTDvllLDVTPLSLGIET 403
Cdd:COG0443 291 LADAGLSPSDIDAVLLVGGSTRMPAVRERVKELFGKEPLKGVDPDEAVALGAAIQAGVLAGDVKD---LDVTPLSLGIET 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 404 MGSVMTALIEKNTTIPTKKSQVFSTAEDNQSAVTIHVLQGERKRASDNKSLGQFNLEGIRPAPRGLPQIEVTFDIDANGI 483
Cdd:COG0443 368 LGGVFTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGI 447
|
490 500 510
....*....|....*....|....*....|...
gi 2058542806 484 LHVSAKDKETNKEQKITIqassglsDDEIERMV 516
Cdd:COG0443 448 LSVSAKDLGTGKEQSITI-------KEEIERML 473
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
3-636 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 728.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 3 KIIGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDGEILVGQPAKRQAITNPKNTLFAIKRLIGRRFedDEV 82
Cdd:PLN03184 40 KVVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNGDRLVGQIAKRQAVVNPENTFFSVKRFIGRKM--SEV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 83 QRDLKIMPYAIAKADNGDAWVE--VKGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRI 160
Cdd:PLN03184 118 DEESKQVSYRVVRDENGNVKLDcpAIGKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 161 AGLDVKRIINEPTAAAFAYGVNKvKGERKVAVYDLGGGTFDISIIEIdeveGETTFEVLATNGNTHLGGEDFDNRVINYL 240
Cdd:PLN03184 198 AGLEVLRIINEPTAASLAYGFEK-KSNETILVFDLGGGTFDVSVLEV----GDGVFEVLSTSGDTHLGGDDFDKRIVDWL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 241 VDEFKREQGIDLRNDQLALQRLKDAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDMVKDSLEPV 320
Cdd:PLN03184 273 ASNFKKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISLPFITATADGPKHIDTTLTRAKFEELCSDLLDRCKTPV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 321 RVALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGAVLSGDKTDVLLLDVTPLSLG 400
Cdd:PLN03184 353 ENALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKLTGKDPNVTVNPDEVVALGAAVQAGVLAGEVSDIVLLDVTPLSLG 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 401 IETMGSVMTALIEKNTTIPTKKSQVFSTAEDNQSAVTIHVLQGERKRASDNKSLGQFNLEGIRPAPRGLPQIEVTFDIDA 480
Cdd:PLN03184 433 LETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFDIDA 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 481 NGILHVSAKDKETNKEQKITIQASSGLSDDEIERMVREAEANAAEDKKFEELVQARNQADGLVHSVRKQITEAGEALPAD 560
Cdd:PLN03184 513 NGILSVSATDKGTGKKQDITITGASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKELGDKVPAD 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 561 EKTKIETALSELETAIKGDD----KAAIEAKQQALLEASQKLM-EIAQQQAQAQGAAGADAGQSSSSAKADDDVVDAEFE 635
Cdd:PLN03184 593 VKEKVEAKLKELKDAIASGStqkmKDAMAALNQEVMQIGQSLYnQPGAGGAGPAPGGEAGSSSSSSSGGDGDDVIDADFT 672
|
.
gi 2058542806 636 E 636
Cdd:PLN03184 673 D 673
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
2-593 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 724.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 2 GKIIGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDgEILVGQPAKRQAITNPKNTLFAIKRLIGRRFEDDE 81
Cdd:PTZ00186 27 GDVIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGS-EKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 82 VQRDLKIMPYAIAKADNGDAWVE-VKGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRI 160
Cdd:PTZ00186 106 IQKDIKNVPYKIVRAGNGDAWVQdGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 161 AGLDVKRIINEPTAAAFAYGVNKVKgERKVAVYDLGGGTFDISIIEIdeveGETTFEVLATNGNTHLGGEDFDNRVINYL 240
Cdd:PTZ00186 186 AGLNVIRVVNEPTAAALAYGMDKTK-DSLIAVYDLGGGTFDISVLEI----AGGVFEVKATNGDTHLGGEDFDLALSDYI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 241 VDEFKREQGIDLRNDQLALQRLKDAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDMVKDSLEPV 320
Cdd:PTZ00186 261 LEEFRKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADGAQHIQMHISRSKFEGITQRLIERSIAPC 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 321 RVALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGAVLSGDKTDVLLLDVTPLSLG 400
Cdd:PTZ00186 341 KQCMKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFFQKDPFRGVNPDEAVALGAATLGGVLRGDVKGLVLLDVTPLSLG 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 401 IETMGSVMTALIEKNTTIPTKKSQVFSTAEDNQSAVTIHVLQGERKRASDNKSLGQFNLEGIRPAPRGLPQIEVTFDIDA 480
Cdd:PTZ00186 421 IETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDIDA 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 481 NGILHVSAKDKETNKEQKITIQASSGLSDDEIERMVREAEANAAEDKKFEELVQARNQADGLVHSVRKQITEAGEALPAd 560
Cdd:PTZ00186 501 NGICHVTAKDKATGKTQNITITANGGLSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGEWKYVSDA- 579
|
570 580 590
....*....|....*....|....*....|....*....
gi 2058542806 561 EKTKIETALSELETAI------KGDDKAAIEAKQQALLE 593
Cdd:PTZ00186 580 EKENVKTLVAELRKAMenpnvaKDDLAAATDKLQKAVME 618
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
4-383 |
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: 699.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 4 IIGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDGEILVGQPAKRQAITNPKNTLFAIKRLIGRRFEDDEVQ 83
Cdd:cd10234 1 IIGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 84 RDLKIMPYAiaKADNGDAWVEVKGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGL 163
Cdd:cd10234 81 RKQVPYPVV--SAGNGDAWVEIGGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIAGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 164 DVKRIINEPTAAAFAYGVNKvKGERKVAVYDLGGGTFDISIIEIdeveGETTFEVLATNGNTHLGGEDFDNRVINYLVDE 243
Cdd:cd10234 159 EVLRIINEPTAAALAYGLDK-KKDEKILVYDLGGGTFDVSILEI----GDGVFEVLSTNGDTHLGGDDFDQRIIDYLADE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 244 FKREQGIDLRNDQLALQRLKDAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDMVKDSLEPVRVA 323
Cdd:cd10234 234 FKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLETEINLPFITADASGPKHLEMKLTRAKFEELTEDLVERTIEPVEQA 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 324 LKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGAVLS 383
Cdd:cd10234 314 LKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
2-382 |
0e+00 |
|
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: 675.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 2 GKIIGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDGEILVGQPAKRQAITNPKNTLFAIKRLIGRRFEDDE 81
Cdd:cd11733 1 GDVIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 82 VQRDLKIMPYAIAKADNGDAWVEVKGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIA 161
Cdd:cd11733 81 VQKDIKMVPYKIVKASNGDAWVEAHGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDAGQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 162 GLDVKRIINEPTAAAFAYGVNKvKGERKVAVYDLGGGTFDISIIEIDevegETTFEVLATNGNTHLGGEDFDNRVINYLV 241
Cdd:cd11733 161 GLNVLRIINEPTAAALAYGLDK-KDDKIIAVYDLGGGTFDISILEIQ----KGVFEVKATNGDTFLGGEDFDNALLNYLV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 242 DEFKREQGIDLRNDQLALQRLKDAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDMVKDSLEPVR 321
Cdd:cd11733 236 AEFKKEQGIDLSKDNLALQRLREAAEKAKIELSSSLQTDINLPFITADASGPKHLNMKLTRAKFESLVGDLIKRTVEPCK 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2058542806 322 VALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGAVL 382
Cdd:cd11733 316 KCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIFGKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
5-600 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 621.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 5 IGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDgEILVGQPAKRQAITNPKNTLFAIKRLIGRRFEDDEVQR 84
Cdd:PTZ00009 7 IGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDSVVQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 85 DLKIMPYAIAKADNGDAWVEV----KGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRI 160
Cdd:PTZ00009 86 DMKHWPFKVTTGGDDKPMIEVtyqgEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAGTI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 161 AGLDVKRIINEPTAAAFAYGVNKV-KGERKVAVYDLGGGTFDISIIEIDEvegeTTFEVLATNGNTHLGGEDFDNRVINY 239
Cdd:PTZ00009 166 AGLNVLRIINEPTAAAIAYGLDKKgDGEKNVLIFDLGGGTFDVSLLTIED----GIFEVKATAGDTHLGGEDFDNRLVEF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 240 LVDEFKRE-QGIDLRNDQLALQRLKDAAEKAKIELSSAQQTDVNLPYITADATGpkhmNIKVTRAKLESLVEDMVKDSLE 318
Cdd:PTZ00009 242 CVQDFKRKnRGKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDY----NVTISRARFEELCGDYFRNTLQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 319 PVRVALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFF-GKEPRKDVNPDEAVAMGAAIQGAVLSGDKT----DVLLLD 393
Cdd:PTZ00009 318 PVEKVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFnGKEPCKSINPDEAVAYGAAVQAAILTGEQSsqvqDLLLLD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 394 VTPLSLGIETMGSVMTALIEKNTTIPTKKSQVFSTAEDNQSAVTIHVLQGERKRASDNKSLGQFNLEGIRPAPRGLPQIE 473
Cdd:PTZ00009 398 VTPLSLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 474 VTFDIDANGILHVSAKDKETNKEQKITIQASSG-LSDDEIERMVREAEANAAEDKKFEELVQARNQADGLVHSVRKQITE 552
Cdd:PTZ00009 478 VTFDIDANGILNVSAEDKSTGKSNKITITNDKGrLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQD 557
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 2058542806 553 A--GEALPADEKTKIETALSEletAIKGDDKAAIEAKQQalLEASQKLME 600
Cdd:PTZ00009 558 EkvKGKLSDSDKATIEKAIDE---ALEWLEKNQLAEKEE--FEHKQKEVE 602
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
5-596 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 613.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 5 IGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDGeILVGQPAKRQAITNPKNTLFAIKRLIGRRFEDdeVQR 84
Cdd:PRK05183 22 VGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDG-IEVGYEARANAAQDPKNTISSVKRFMGRSLAD--IQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 85 DLKIMPYAIAKADNGDAWVEVKGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGLD 164
Cdd:PRK05183 99 RYPHLPYQFVASENGMPLIRTAQGLKSPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARLAGLN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 165 VKRIINEPTAAAFAYGVNKVKgERKVAVYDLGGGTFDISIIEIDE-VegettFEVLATNGNTHLGGEDFDNRVINYLvde 243
Cdd:PRK05183 179 VLRLLNEPTAAAIAYGLDSGQ-EGVIAVYDLGGGTFDISILRLSKgV-----FEVLATGGDSALGGDDFDHLLADWI--- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 244 fkREQ-GIDLRNDQLALQRLKDAAEKAKIELSSAQQTDVNLpyitADATGpkhmniKVTRAKLESLVEDMVKDSLEPVRV 322
Cdd:PRK05183 250 --LEQaGLSPRLDPEDQRLLLDAARAAKEALSDADSVEVSV----ALWQG------EITREQFNALIAPLVKRTLLACRR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 323 ALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGAVLSGDKT--DVLLLDVTPLSLG 400
Cdd:PRK05183 318 ALRDAGVEADEVKEVVMVGGSTRVPLVREAVGEFFGRTPLTSIDPDKVVAIGAAIQADILAGNKPdsDMLLLDVIPLSLG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 401 IETMGSVMTALIEKNTTIPTKKSQVFSTAEDNQSAVTIHVLQGERKRASDNKSLGQFNLEGIRPAPRGLPQIEVTFDIDA 480
Cdd:PRK05183 398 LETMGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 481 NGILHVSAKDKETNKEQKITIQASSGLSDDEIERMVREAEANAAEDKKFEELVQARNQADGLVHSVRKQITEAGEALPAD 560
Cdd:PRK05183 478 DGLLSVTAMEKSTGVEASIQVKPSYGLTDDEIARMLKDSMSHAEEDMQARALAEQKVEAERVLEALQAALAADGDLLSAA 557
|
570 580 590
....*....|....*....|....*....|....*.
gi 2058542806 561 EKTKIETALSELETAIKGDDKAAIEAKQQALLEASQ 596
Cdd:PRK05183 558 ERAAIDAAMAALREVAQGDDADAIEAAIKALDKATQ 593
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
2-384 |
0e+00 |
|
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: 597.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 2 GKIIGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDGEILVGQPAKRQAITNPKNTLFAIKRLIGRRFEDDE 81
Cdd:cd11734 1 GPVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTKDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 82 VQRDLKIMPYAIAKADNGDAWVEVKGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIA 161
Cdd:cd11734 81 VQRDIKEVPYKIVKHSNGDAWVEARGQKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAGQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 162 GLDVKRIINEPTAAAFAYGVNKvKGERKVAVYDLGGGTFDISIIEIDevegETTFEVLATNGNTHLGGEDFDNRVINYLV 241
Cdd:cd11734 161 GLNVLRVINEPTAAALAYGLDK-SGDKVIAVYDLGGGTFDISILEIQ----KGVFEVKSTNGDTHLGGEDFDIALVRHIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 242 DEFKREQGIDLRNDQLALQRLKDAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDMVKDSLEPVR 321
Cdd:cd11734 236 SEFKKESGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINLPFITADASGPKHINMKLTRAQFESLVKPLVDRTVEPCK 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2058542806 322 VALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGAVLSG 384
Cdd:cd11734 316 KALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIFGREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
4-595 |
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: 592.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 4 IIGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDGEILVGQPAKRQAITNPKNTLFAIKRLIGRRFEDDEVQ 83
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYLKDGGVEVGKEALAAAAEDPKNTISSVKRLMGRSIEDIKTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 84 RDLkimPYAIAKADNGDAWVEVKGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGL 163
Cdd:TIGR01991 81 SIL---PYRFVDGPGEMVRLRTVQGTVTPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARLAGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 164 DVKRIINEPTAAAFAYGVNKVKgERKVAVYDLGGGTFDISIIEIDEvegeTTFEVLATNGNTHLGGEDFDNRvinyLVDE 243
Cdd:TIGR01991 158 NVLRLLNEPTAAAVAYGLDKAS-EGIYAVYDLGGGTFDVSILKLTK----GVFEVLATGGDSALGGDDFDHA----LAKW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 244 FKREQGIDLRNDQLALQRLKDAAEKAKIELSSAQQTDVNLpyitadATGPKHMNIKVTRAKLESLVEDMVKDSLEPVRVA 323
Cdd:TIGR01991 229 ILKQLGISADLNPEDQRLLLQAARAAKEALTDAESVEVDF------TLDGKDFKGKLTRDEFEALIQPLVQKTLSICRRA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 324 LKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGAVLSGDKT--DVLLLDVTPLSLGI 401
Cdd:TIGR01991 303 LRDAGLSVEEIKGVVLVGGSTRMPLVRRAVAELFGQEPLTDIDPDQVVALGAAIQADLLAGNRIgnDLLLLDVTPLSLGI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 402 ETMGSVMTALIEKNTTIPTKKSQVFSTAEDNQSAVTIHVLQGERKRASDNKSLGQFNLEGIRPAPRGLPQIEVTFDIDAN 481
Cdd:TIGR01991 383 ETMGGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDAD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 482 GILHVSAKDKETNKEQKITIQASSGLSDDEIERMVREAEANAAEDKKFEELVQARNQADGLVHSVRKQITEAGEALPADE 561
Cdd:TIGR01991 463 GLLTVSAQEQSTGVEQSIQVKPSYGLSDEEIERMLKDSFKHAEEDMYARALAEQKVEAERILEALQAALAADGDLLSEDE 542
|
570 580 590
....*....|....*....|....*....|....
gi 2058542806 562 KTKIETALSELETAIKGDDKAAIEAKQQALLEAS 595
Cdd:TIGR01991 543 RAAIDAAMEALQKALQGDDADAIKAAIEALEEAT 576
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
4-382 |
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: 522.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 4 IIGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYaDDGEILVGQPAKRQAITNPKNTLFAIKRLIGRRFEDDEVQ 83
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAF-TDGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 84 RDLKIMPYAIAKADNGDAWVEV----KGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGR 159
Cdd:cd24028 80 SDIKHWPFKVVEDEDGKPKIEVtykgEEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 160 IAGLDVKRIINEPTAAAFAYGVN-KVKGERKVAVYDLGGGTFDISIIEIDevEGEttFEVLATNGNTHLGGEDFDNRVIN 238
Cdd:cd24028 160 IAGLNVLRIINEPTAAALAYGLDkKSSGERNVLVFDLGGGTFDVSLLSID--NGV--FEVKATAGDTHLGGEDFDNRLVE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 239 YLVDEFKREQGIDLRNDQLALQRLKDAAEKAKIELSSAQQT--DVNLPYITADatgpkhMNIKVTRAKLESLVEDMVKDS 316
Cdd:cd24028 236 YLVEEFKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSAtiEIDSLYDGID------FETTITRAKFEELCEDLFKKC 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2058542806 317 LEPVRVALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFF-GKEPRKDVNPDEAVAMGAAIQGAVL 382
Cdd:cd24028 310 LEPVEKVLKDAKLSKDDIDEVVLVGGSTRIPKIQELLSEFFgGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
2-382 |
2.62e-177 |
|
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: 508.29 E-value: 2.62e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 2 GKIIGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADdGEILVGQPAKRQAITNPKNTLFAIKRLIGRRFEDDE 81
Cdd:cd10241 1 GTVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTD-GERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 82 VQRDLKIMPYAIAKADNGDAW-VEVKGKK--MAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAG 158
Cdd:cd10241 80 VQKDIKLLPFKIVNKNGKPYIqVEVKGEKktFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 159 RIAGLDVKRIINEPTAAAFAYGVNKVKGERKVAVYDLGGGTFDISIIEIDevegETTFEVLATNGNTHLGGEDFDNRVIN 238
Cdd:cd10241 160 TIAGLNVLRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSLLTID----NGVFEVLATNGDTHLGGEDFDQRVMD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 239 YLVDEFKREQGIDLRNDQLALQRLKDAAEKAKIELSSAQQTDVNlpyITADATGpKHMNIKVTRAKLESLVEDMVKDSLE 318
Cdd:cd10241 236 HFIKLFKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIE---IESLFDG-EDFSETLTRAKFEELNMDLFRKTLK 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2058542806 319 PVRVALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFF-GKEPRKDVNPDEAVAMGAAIQGAVL 382
Cdd:cd10241 312 PVQKVLEDAGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFnGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
5-382 |
1.62e-163 |
|
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: 472.88 E-value: 1.62e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 5 IGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDgEILVGQPAKRQAITNPKNTLFAIKRLIGRRFEDDEVQR 84
Cdd:cd10233 2 IGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 85 DLKIMPY-AIAKADNGDAWVEVKG--KKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIA 161
Cdd:cd10233 81 DMKHWPFkVVSGGDKPKIQVEYKGetKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 162 GLDVKRIINEPTAAAFAYGVNK-VKGERKVAVYDLGGGTFDISIIEIDevegETTFEVLATNGNTHLGGEDFDNRVINYL 240
Cdd:cd10233 161 GLNVLRIINEPTAAAIAYGLDKkGKGERNVLIFDLGGGTFDVSLLTIE----DGIFEVKATAGDTHLGGEDFDNRLVNHF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 241 VDEFKREQGIDLRNDQLALQRLKDAAEKAKIELSSAQQTDVNLP--YITADatgpkhMNIKVTRAKLESLVEDMVKDSLE 318
Cdd:cd10233 237 VQEFKRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDslFEGID------FYTSITRARFEELCADLFRSTLE 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2058542806 319 PVRVALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFF-GKEPRKDVNPDEAVAMGAAIQGAVL 382
Cdd:cd10233 311 PVEKVLRDAKLDKSQIHEIVLVGGSTRIPKVQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
1-384 |
2.60e-156 |
|
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: 454.37 E-value: 2.60e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 1 MGKIIGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDGEILVGQPAKRQAITNPKNTLFAIKRLIGRRFEDd 80
Cdd:cd10236 1 HRLAVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITVGEKAKENAITDPENTISSVKRLMGRSLAD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 81 eVQRDLKIMPYAIAKADNGDAWVEVKGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRI 160
Cdd:cd10236 80 -VKEELPLLPYRLVGDENELPRFRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 161 AGLDVKRIINEPTAAAFAYGVNKvKGERKVAVYDLGGGTFDISIIEI-DEVegettFEVLATNGNTHLGGEDFDNRVINY 239
Cdd:cd10236 159 AGLNVLRLLNEPTAAALAYGLDQ-KKEGTIAVYDLGGGTFDISILRLsDGV-----FEVLATGGDTALGGDDFDHLLADW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 240 LVDefkrEQGIDLRNDQLALQRLKDAAEKAKIELSSAQQTDVNLPYITADATGPkhmnikVTRAKLESLVEDMVKDSLEP 319
Cdd:cd10236 233 ILK----QIGIDARLDPAVQQALLQAARRAKEALSDADSASIEVEVEGKDWERE------ITREEFEELIQPLVKRTLEP 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2058542806 320 VRVALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGAVLSG 384
Cdd:cd10236 303 CRRALKDAGLEPADIDEVVLVGGSTRIPLVRQRVAEFFGREPLTSINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
5-383 |
4.53e-147 |
|
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: 430.07 E-value: 4.53e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 5 IGIDLGTTNSCVAILDGDHARVI-ENAEGDRTTPSIIAYADDGEILVGQPAKRQAITNPKNTLFAIKRLIGRRFEDDEvq 83
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAEVIiENSEGKRTTPSVVYFDKDGEVLVGEEAKNQALLDPENTIYSVKRLMGRDTKDKE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 84 rdlkimpyaiakadngdawvEVKGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGL 163
Cdd:cd24029 79 --------------------EIGGKEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAELAGL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 164 DVKRIINEPTAAAFAYGVNKVKGERKVAVYDLGGGTFDISIIEIDEVegetTFEVLATNGNTHLGGEDFDNRVINYLVDE 243
Cdd:cd24029 139 NVLRLINEPTAAALAYGLDKEGKDGTILVYDLGGGTFDVSILEIENG----KFEVLATGGDNFLGGDDFDEAIAELILEK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 244 FKREQGI-DLRNDQLALQRLKDAAEKAKIELSSAQQTDVNLPyitaDATGPKHMNIKVTRAKLESLVEDMVKDSLEPVRV 322
Cdd:cd24029 215 IGIETGIlDDKEDERARARLREAAEEAKIELSSSDSTDILIL----DDGKGGELEIEITREEFEELIAPLIERTIDLLEK 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2058542806 323 ALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGAVLS 383
Cdd:cd24029 291 ALKDAKLSPEDIDRVLLVGGSSRIPLVREMLEEYFGREPISSVDPDEAVAKGAAIYAASLA 351
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
5-382 |
1.01e-132 |
|
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: 394.35 E-value: 1.01e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 5 IGIDLGTTNSCVAILDGDhARVIENAEGDRTTPSIIAYADDgEILVGQPAKRQAITNPKNTLFAIKRLIGRRFEDDEVQR 84
Cdd:cd24093 2 IGIDLGTTYSCVATYESS-VEIIANEQGNRVTPSFVAFTPE-ERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 85 DLKIMPYAIAKaDNGDAWVEV----KGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRI 160
Cdd:cd24093 80 DMKTWPFKVID-VNGNPVIEVqylgETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 161 AGLDVKRIINEPTAAAFAYGVN--KVKGERKVAVYDLGGGTFDISIIEIdeveGETTFEVLATNGNTHLGGEDFDNRVIN 238
Cdd:cd24093 159 AGLNVLRIINEPTAAAIAYGLGagKSEKERHVLIFDLGGGTFDVSLLHI----AGGVYTVKSTSGNTHLGGQDFDTNLLE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 239 YLVDEFKREQGIDLRNDQLALQRLKDAAEKAKIELSSAQQTDVNLPYITADatgpKHMNIKVTRAKLESLVEDMVKDSLE 318
Cdd:cd24093 235 HFKAEFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDG----EDFESSITRARFEDLNAALFKSTLE 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2058542806 319 PVRVALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFF-GKEPRKDVNPDEAVAMGAAIQGAVL 382
Cdd:cd24093 311 PVEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
5-380 |
1.27e-123 |
|
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: 369.65 E-value: 1.27e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 5 IGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDGEILVGQPAKRQAITNPKNTLFAIKRLIGRrfeddevqr 84
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVDEDGSILVGRAAKERLVTHPDRTAASFKRFMGT--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 85 dlkimpyaiakadngDAWVEVKGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGLD 164
Cdd:cd10235 72 ---------------DKQYRLGNHTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELAGLK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 165 VKRIINEPTAAAFAYGVNKVKGERKVAVYDLGGGTFDISIIEIDevegETTFEVLATNGNTHLGGEDFDNRVINYLVDEF 244
Cdd:cd10235 137 VERLINEPTAAALAYGLHKREDETRFLVFDLGGGTFDVSVLELF----EGVIEVHASAGDNFLGGEDFTHALADYFLKKH 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 245 KREQGIDLRNDqlaLQRLKDAAEKAKIELSSAQQTDVNLPYitadatGPKHMNIKVTRAKLESLVEDMVKDSLEPVRVAL 324
Cdd:cd10235 213 RLDFTSLSPSE---LAALRKRAEQAKRQLSSQDSAEIRLTY------RGEELEIELTREEFEELCAPLLERLRQPIERAL 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2058542806 325 KDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGA 380
Cdd:cd10235 284 RDAGLKPSDIDAVILVGGATRMPLVRQLIARLFGRLPLSSLDPDEAVALGAAIQAA 339
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
3-384 |
2.72e-121 |
|
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: 366.28 E-value: 2.72e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 3 KIIGIDLGTTNSCVAI---LDGdHARVIENAEGDRTTPSIIAYADDGEILVGQPAKRQAITNPKNTLFAIKRLIGRRFED 79
Cdd:cd10237 23 KIVGIDLGTTYSCVGVyhaVTG-EVEVIPDDDGHKSIPSVVAFTPDGGVLVGYDALAQAEHNPSNTIYDAKRFIGKTFTK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 80 DEVQRDLKIMPYAIAKADNGDAWVEVKG----KKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATK 155
Cdd:cd10237 102 EELEEEAKRYPFKVVNDNIGSAFFEVPLngstLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 156 DAGRIAGLDVKRIINEPTAAAFAYGVNKVKGERKVAVYDLGGGTFDISIIeidEVEGeTTFEVLATNGNTHLGGEDFDNR 235
Cdd:cd10237 182 KAANLAGLEVLRVINEPTAAAMAYGLHKKSDVNNVLVVDLGGGTLDVSLL---NVQG-GMFLTRAMAGNNHLGGQDFNQR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 236 VINYLVDEFKREQGIDLrNDQLALQRLKDAAEKAKIELSSAQQTDVNLPYITADATGPK-HMNIKVTRAKLESLVEDMVK 314
Cdd:cd10237 258 LFQYLIDRIAKKFGKTL-TDKEDIQRLRQAVEEVKLNLTNHNSASLSLPLQISLPSAFKvKFKEEITRDLFETLNEDLFQ 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 315 DSLEPVRVALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGAVLSG 384
Cdd:cd10237 337 RVLEPIRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFFGKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
5-585 |
4.04e-116 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 359.17 E-value: 4.04e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 5 IGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDGeILVGQpakrqaitnpKNTLFAIKRLIGRRFEDDEVQR 84
Cdd:PRK01433 22 VGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNN-FTIGN----------NKGLRSIKRLFGKTLKEILNTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 85 DLKIMPYAIAKADNGDAWVEVKGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGLD 164
Cdd:PRK01433 91 ALFSLVKDYLDVNSSELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLAAKIAGFE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 165 VKRIINEPTAAAFAYGVNKVKGERKVaVYDLGGGTFDISIIEIDEvegeTTFEVLATNGNTHLGGEDFDNRVINYLVDEF 244
Cdd:PRK01433 171 VLRLIAEPTAAAYAYGLNKNQKGCYL-VYDLGGGTFDVSILNIQE----GIFQVIATNGDNMLGGNDIDVVITQYLCNKF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 245 kreqgiDLRNDQLALQrlkdAAEKAKIELSSAQQTDVNlpyitadatgpkhmNIKVTRAKLESLVEDMVKDSLEPVRVAL 324
Cdd:PRK01433 246 ------DLPNSIDTLQ----LAKKAKETLTYKDSFNND--------------NISINKQTLEQLILPLVERTINIAQECL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 325 KDSGLAvgEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGAVLSGDKTDVLLLDVTPLSLGIETM 404
Cdd:PRK01433 302 EQAGNP--NIDGVILVGGATRIPLIKDELYKAFKVDILSDIDPDKAVVWGAALQAENLIAPHTNSLLIDVVPLSLGMELY 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 405 GSVMTALIEKNTTIPTKKSQVFSTAEDNQSAVTIHVLQGERKRASDNKSLGQFNLEGIRPAPRGLPQIEVTFDIDANGIL 484
Cdd:PRK01433 380 GGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDADGIL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 485 HVSAKDKETNKEQKITIQASSGLSDDEIERMVREAEANAAEDKKFEELVQARNQADGLVHSVRKQITEAGEALPADEKTK 564
Cdd:PRK01433 460 SVSAYEKISNTSHAIEVKPNHGIDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAIAELTTLLSESEISI 539
|
570 580
....*....|....*....|.
gi 2058542806 565 IETALSELETAIKGDDKAAIE 585
Cdd:PRK01433 540 INSLLDNIKEAVHARDIILIN 560
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
4-383 |
1.33e-98 |
|
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: 306.93 E-value: 1.33e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 4 IIGIDLGTTNSCVAIldgdhAR-----VIENAEGDRTTPSIIAYaDDGEILVGQPAKRQAITNPKNTLFAIKRLIGRRFE 78
Cdd:cd24095 3 VVGIDFGNENCVVAV-----ARkggidVVLNEESNRETPSMVSF-GEKQRFLGEAAAASILMNPKNTISQLKRLIGRKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 79 DDEVQRDLKIMPYAIAKADNGDAWVEV----KGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQAT 154
Cdd:cd24095 77 DPEVQRDLKLFPFKVTEGPDGEIGINVnylgEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 155 KDAGRIAGLDVKRIINEPTAAAFAYGVNKVKGE----RKVAVYDLGGGTFDISIIEIdeVEGETTfeVLATNGNTHLGGE 230
Cdd:cd24095 157 LDAAQIAGLNCLRLMNETTATALAYGIYKTDLPetdpTNVVFVDVGHSSTQVCVVAF--KKGQLK--VLSHAFDRNLGGR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 231 DFDNRVINYLVDEFKREQGIDLRNDQLALQRLKDAAEKAKIELSSAQQTDVNLPYITADatgpKHMNIKVTRAKLESLVE 310
Cdd:cd24095 233 DFDEVLFDHFAAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMED----KDVKGMITREEFEELAA 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2058542806 311 DMVKDSLEPVRVALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGAVLS 383
Cdd:cd24095 309 PLLERLLEPLEKALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFFGKEPSRTMNASECVARGCALQCAMLS 381
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
5-380 |
1.31e-96 |
|
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: 301.40 E-value: 1.31e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 5 IGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYaDDGEILVGQPAKRQAITNPKNTLFAIKRLIGRRFEDDEVQR 84
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGF-TEKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 85 DLKIMPYAIAKADNGDAWVEV--KGKKM--APPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRI 160
Cdd:cd11732 80 EIKLLPFKLVELEDGKVGIEVsyNGEEVvfSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 161 AGLDVKRIINEPTAAAFAYGVNKVK---GE---RKVAVYDLGGGTFDISIIEIdeVEGEttFEVLATNGNTHLGGEDFDN 234
Cdd:cd11732 160 AGLNCLRLINETTAAALDYGIYKSDlleSEekpRIVAFVDMGHSSTQVSIAAF--TKGK--LKVLSTAFDRNLGGRDFDR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 235 RVINYLVDEFKREQGIDLRNDQLALQRLKDAAEKAKIELSSAQQTDVNLPYITADatgpKHMNIKVTRAKLESLVEDMVK 314
Cdd:cd11732 236 ALVEHFAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMED----IDFSGQIKREEFEELIQPLLA 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2058542806 315 DSLEPVRVALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGA 380
Cdd:cd11732 312 RLEAPIKKALAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVFGKDLSTTLNADEAVARGCALQAA 377
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
5-382 |
4.27e-95 |
|
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: 297.23 E-value: 4.27e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 5 IGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDgEILVGQPAKRQAITNPKNTLFAIKRLIGRRFEDDEVQR 84
Cdd:cd10238 3 FGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDN-EKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAVQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 85 DLKIMPYAIAKaDNGDAWVEV----KGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRI 160
Cdd:cd10238 82 LKKESKCKIIE-KDGKPGYEIeleeKKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 161 AGLDVKRIINEPTAAAFAYGV--NKVKGERKVAVYDLGGGTFDISIIEIDevegETTFEVLATNGNTHLGGEDFDNRVIN 238
Cdd:cd10238 161 AGFNVLRVISEPSAAALAYGIgqDDPTENSNVLVYRLGGTSLDVTVLSVN----NGMYRVLATRTDDNLGGDDFTEALAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 239 YLVDEFKREQGIDLRNDQLALQRLKDAAEKAKIELSSAQ--QTDVNLPYITADatgpkhMNIKVTRAKLESLVEDMVKDS 316
Cdd:cd10238 237 HLASEFKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNtaTCSVESLYDGMD------FQCNVSRARFESLCSSLFQQC 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2058542806 317 LEPVRVALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFF-GKEPRKDVNPDEAVAMGAAIQGAVL 382
Cdd:cd10238 311 LEPIQEVLNSAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFpSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
5-380 |
2.90e-89 |
|
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; This subgroup includes the human proteins, HSPA4 (also known as 70-kDa heat shock protein 4; APG-2; HS24/P52; hsp70 RY; HSPH2), HSPA4L (also known as 70-kDa heat shock protein 4-like; APG-1; HSPH3; OSP94), and HSPH1 (also known as heat shock 105kDa/110kDa protein 1; HSP105; HSP105A; HSP105B; NY-CO-25). They belong to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family, and includes proteins believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466826 [Multi-domain] Cd Length: 378 Bit Score: 282.24 E-value: 2.90e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 5 IGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDGEILvGQPAKRQAITNPKNTLFAIKRLIGRRFEDDEVQR 84
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSM-GVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 85 DLKIMPYAIAKADNGDAWVEV--KGKKM--APPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRI 160
Cdd:cd10228 80 ELKHLPYKVVKLPNGSVGIKVqyLGEEHvfTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 161 AGLDVKRIINEPTAAAFAYGVNK----VKGE--RKVAVYDLGGGTFDISIIEIdeVEGEttFEVLATNGNTHLGGEDFDN 234
Cdd:cd10228 160 AGLNCLRLLNDTTAVALAYGIYKqdlpAEEEkpRNVVFVDMGHSSLQVSVCAF--NKGK--LKVLATAADPNLGGRDFDE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 235 RVINYLVDEFKREQGIDLRNDQLALQRLKDAAEKAKiELSSAQQTDV--NLPYITADatgpKHMNIKVTRAKLESLVEDM 312
Cdd:cd10228 236 LLVEHFAEEFKTKYKIDVKSKPRALLRLLTECEKLK-KLMSANATELplNIECFMDD----KDVSGKMKRAEFEELCAPL 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2058542806 313 VKDSLEPVRVALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGA 380
Cdd:cd10228 311 FARVEVPLRSALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVFGKEPSTTLNQDEAVARGCALQCA 378
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
5-383 |
1.56e-81 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and similar proteins; The subgroup includes two Saccharomyces cerevisiae heat shock protein homologs, Sse1 and Sse2. They may have calcium-dependent calmodulin-binding activities. Both Sse1 and Sse2 belong to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family, and includes proteins believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466944 [Multi-domain] Cd Length: 385 Bit Score: 262.31 E-value: 1.56e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 5 IGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDGEILvGQPAKRQAITNPKNTLFAIKRLIGRRFEDDEVQR 84
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYL-GEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 85 DLKIMPYAIAKAdNGDAWVEV----KGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRI 160
Cdd:cd24094 80 EEKYFTAKLVDA-NGEVGAEVnylgEKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 161 AGLDVKRIINEPTAAAFAYGVNKV------KGERKVAVYDLGGGTFDISIIEIdeVEGEttFEVLATNGNTHLGGEDFDN 234
Cdd:cd24094 159 AGLNPLRLMNDTTAAALGYGITKTdlpepeEKPRIVAFVDIGHSSYTVSIVAF--KKGQ--LTVKGTAYDRHFGGRDFDK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 235 RVINYLVDEFKREQGIDLRNDQLALQRLKDAAEKAKIELSSAQQTDVNLPYITADatgpKHMNIKVTRAKLESLVEDMVK 314
Cdd:cd24094 235 ALTDHFADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMND----IDVSSMLKREEFEELIAPLLE 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2058542806 315 DSLEPVRVALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGAVLS 383
Cdd:cd24094 311 RVTAPLEKALAQAGLTKDEIDFVELVGGTTRVPALKESISAFFGKPLSTTLNQDEAVARGAAFACAILS 379
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
4-380 |
5.71e-79 |
|
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: 254.73 E-value: 5.71e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 4 IIGIDLGTTNSCVAIL-DGDHARVIENAEGDRTTPSIIAYaDDGEILVGQPAKRQAITNPKNTLFAIKRLIGrrfeddev 82
Cdd:cd10230 2 VLGIDLGSEFIKVALVkPGVPFEIVLNEESKRKTPSAVAF-RNGERLFGDDALALATRFPENTFSYLKDLLG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 83 qrdlkimpyaiakadngdawvevkgkkMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAG 162
Cdd:cd10230 73 ---------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIAG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 163 LDVKRIINEPTAAAFAYGVNKVKGE---RKVAVYDLGGGTFDISIIEIDEVEGE--------TTFEVLATNGNTHLGGED 231
Cdd:cd10230 126 LNVLSLINDNTAAALNYGIDRRFENnepQNVLFYDMGASSTSATVVEFSSVKEKdkgknktvPQVEVLGVGWDRTLGGLE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 232 FDNRVINYLVDEFKREQGI--DLRNDQLALQRLKDAAEKAKIELSSAQQTDVNLPYITADatgpKHMNIKVTRAKLESLV 309
Cdd:cd10230 206 FDLRLADHLADEFNEKHKKdkDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDD----IDFRTKITREEFEELC 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2058542806 310 EDMVKDSLEPVRVALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEP-RKDVNPDEAVAMGAAIQGA 380
Cdd:cd10230 282 ADLFERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKElGKHLNADEAAALGAAFYAA 353
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
4-381 |
1.33e-71 |
|
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: 236.37 E-value: 1.33e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 4 IIGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDGEIlVGQPAKRQAITNPKNTLFAIKRLIGRRFEDDEVQ 83
Cdd:cd11737 2 VVGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRS-IGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 84 RDLKIMPYAIAKADNGDAWVEV----KGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGR 159
Cdd:cd11737 81 AEKPSLAYELVQLPTGTTGIKVmymeEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 160 IAGLDVKRIINEPTAAAFAYGVNKV------KGERKVAVYDLGGGTFDISIIEIDevegETTFEVLATNGNTHLGGEDFD 233
Cdd:cd11737 161 IAGLNCLRLMNETTAVALAYGIYKQdlpapeEKPRNVVFVDMGHSAYQVSVCAFN----KGKLKVLATAFDPTLGGRKFD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 234 NRVINYLVDEFKREQGIDLRNDQLALQRLKDAAEKAKiELSSAQQTD--VNLPYITADATGPKHMNikvtRAKLESLVED 311
Cdd:cd11737 237 EVLVNHFCEEFGKKYKLDIKSKIRALLRLFQECEKLK-KLMSANASDlpLNIECFMNDIDVSGTMN----RGQFEEMCAD 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 312 MVKDSLEPVRVALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGAV 381
Cdd:cd11737 312 LLARVEPPLRSVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFFGKEVSTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
4-383 |
1.15e-70 |
|
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: 233.66 E-value: 1.15e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 4 IIGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDGEIlVGQPAKRQAITNPKNTLFAIKRLIGRRFEDDEVQ 83
Cdd:cd11738 2 VVGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRA-IGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 84 RDLKIMPYAIAKADNGDAWVEVK----GKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGR 159
Cdd:cd11738 81 AEKIKLPYELQKMPNGSTGVKVRyldeERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 160 IAGLDVKRIINEPTAAAFAYGVNKV------KGERKVAVYDLGGGTFDISIIEIDevegETTFEVLATNGNTHLGGEDFD 233
Cdd:cd11738 161 IAGLNCLRLMNETTAVALAYGIYKQdlpaleEKPRNVVFVDMGHSAYQVSICAFN----KGKLKVLATTFDPYLGGRNFD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 234 NRVINYLVDEFKREQGIDLRNDQLALQRLKDAAEKAKiELSSAQQTD--VNLPYITADATGPKHMNikvtRAKLESLVED 311
Cdd:cd11738 237 EVLVDYFCEEFKTKYKLNVKENIRALLRLYQECEKLK-KLMSANASDlpLNIECFMNDIDVSSKMN----RAQFEELCAS 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2058542806 312 MVKDSLEPVRVALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGAVLS 383
Cdd:cd11738 312 LLARVEPPLKAVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILS 383
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
4-380 |
5.34e-67 |
|
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: 223.97 E-value: 5.34e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 4 IIGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDGEIlVGQPAKRQAITNPKNTLFAIKRLIGRRFEDDEVQ 83
Cdd:cd11739 2 VVGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRT-IGVAAKNQQITNANNTVSNFKRFHGRAFNDPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 84 RDLKIMPYAIAKADNGDAWVEV----KGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGR 159
Cdd:cd11739 81 KEKENLSYDLVPLKNGGVGVKVmyldEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 160 IAGLDVKRIINEPTAAAFAYGVNKV------KGERKVAVYDLGGGTFDISIIEIDevegETTFEVLATNGNTHLGGEDFD 233
Cdd:cd11739 161 IVGLNCLRLMNDMTAVALNYGIYKQdlpapdEKPRIVVFVDMGHSAFQVSACAFN----KGKLKVLGTAFDPYLGGRNFD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 234 NRVINYLVDEFKREQGIDLRNDQLALQRLKDAAEKAKiELSSAQQTDV--NLPYITADATGPKHMNikvtRAKLESLVED 311
Cdd:cd11739 237 EKLVEHFCAEFKTKYKLDVKSKIRALLRLYQECEKLK-KLMSSNSTDLplNIECFMNDKDVSGKMN----RSQFEELCAD 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2058542806 312 MVKDSLEPVRVALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAIQGA 380
Cdd:cd11739 312 LLQRIEVPLYSLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFFGKDVSTTLNADEAVARGCALQCA 380
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
4-382 |
5.78e-65 |
|
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: 217.61 E-value: 5.78e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 4 IIGIDLGTTNSCVAILDGD-HARVIENAEGDRTTPSIIAYADDGEIlVGQPAKRQAITNPKNTLFAIKRLIGRrfeddev 82
Cdd:cd10232 2 VIGISFGNSNSSIAIINKDgRAEVIANEDGDRQIPSILAYHGDEEY-HGSQAKAQLVRNPKNTVANFRDLLGT------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 83 qrdlkimpyaiakadngdawvevkgKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAG 162
Cdd:cd10232 74 -------------------------TTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAAAAG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 163 LDVKRIINEPTAAAFAYGVNKVKG-----ERKVAVYDLGGGTFDISIIeidEVEGeTTFEVLATNGNTHLGGEDFDNRVI 237
Cdd:cd10232 129 LEVLQLIPEPAAAALAYDLRAETSgdtikDKTVVVADLGGTRSDVTVV---AVRG-GLYTILATVHDYELGGVALDDVLV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 238 NYLVDEFKREQGIDLRNDQLALQRLKDAAEKAKIELSSAQ--QTDVNLPYITADATGpkhmniKVTRAKLESLVEDMVKD 315
Cdd:cd10232 205 GHFAKEFKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTsaPCSVESLADGIDFHS------SINRTRYELLASKVFQQ 278
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2058542806 316 SLEPVRVALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRK----DVNPDEAVAMGAAIQGAVL 382
Cdd:cd10232 279 FADLVTDAIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLFPESTIIraptQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
5-377 |
5.09e-53 |
|
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: 185.00 E-value: 5.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 5 IGIDLGTTNSCVAILDGDHARVIE---------NAEGDRTTPSIIayaddgeilvgqpakrqaitnpkntlfaikrligr 75
Cdd:cd10170 1 VGIDFGTTYSGVAYALLGPGEPPLvvlqlpwpgGDGGSSKVPSVL----------------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 76 rfeddevqrdlkimpyaiakadngdawvevkgkkmappQISAEVLKKMKKTAEDYLGE-------PVTEAVITVPAYFND 148
Cdd:cd10170 46 --------------------------------------EVVADFLRALLEHAKAELGDriwelekAPIEVVITVPAGWSD 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 149 AQRQATKDAGRIAGL----DVKRIINEPTAAAFAYG-----VNKVKGERKVAVYDLGGGTFDISIIEIDEVEGETTFEVL 219
Cdd:cd10170 88 AAREALREAARAAGFgsdsDNVRLVSEPEAAALYALedkgdLLPLKPGDVVLVCDAGGGTVDLSLYEVTSGSPLLLEEVA 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 220 ATNGNtHLGGEDFDNRVINYLVDEFKREQGIDLRNDQLALQRLKDAAEKAKIELSSAQQTDVNLPYITADATgPKHMNIK 299
Cdd:cd10170 168 PGGGA-LLGGTDIDEAFEKLLREKLGDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGL-PELGLEK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 300 VTRAKLESLVEDMVKDSLEPVRVALKDSGLA--VGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDV----NPDEAVAM 373
Cdd:cd10170 246 GTLLLTEEEIRDLFDPVIDKILELIEEQLEAksGTPPDAVVLVGGFSRSPYLRERLRERFGSAGIIIVlrsdDPDTAVAR 325
|
....
gi 2058542806 374 GAAI 377
Cdd:cd10170 326 GAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
5-376 |
7.70e-46 |
|
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: 167.84 E-value: 7.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 5 IGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIAYADDGE-----ILVGQPAKRQAITNPKNTLF--AIKRLIGRRF 77
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREEegaesIYFGNDAIDAYLNDPEEGRLikSVKSFLGSSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 78 EDDEVqrdlkimpyaiakadngdawveVKGKKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQAT--- 154
Cdd:cd10231 81 FDETT----------------------IFGRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDDaqa 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 155 ----KDAGRIAGLDVKRIINEPTAAAFAYGVnKVKGERKVAVYDLGGGTFDISIIEIDEVEGETTFEVLATNGnTHLGGE 230
Cdd:cd10231 139 esrlRDAARRAGFRNVEFQYEPIAAALDYEQ-RLDREELVLVVDFGGGTSDFSVLRLGPNRTDRRADILATSG-VGIGGD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 231 DFDNRVINYLV-----------------------------------------------------DEFKREQGIDLRNDQL 257
Cdd:cd10231 217 DFDRELALKKVmphlgrgstyvsgdkglpvpawlyadlsnwhaisllytkktlrllldlrrdaaDPEKIERLLSLVEDQL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 258 AlQRLKDAAEKAKIELSSAQQTDVNLPYItadatgPKHMNIKVTRAKLESLVEDMVKDSLEPVRVALKDSGLAVGEIDDV 337
Cdd:cd10231 297 G-HRLFRAVEQAKIALSSADEATLSFDFI------EISIKVTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRV 369
|
410 420 430
....*....|....*....|....*....|....*....
gi 2058542806 338 ILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAA 376
Cdd:cd10231 370 FLTGGSSQSPAVRQALASLFGQARLVEGDEFGSVAAGLA 408
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
4-379 |
7.20e-24 |
|
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: 103.90 E-value: 7.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 4 IIGIDLGTTNSCVAI-LDGDHARV--IENAEGD------RTTPSIIAYADDGE-ILVGQPAKRQaitnpkntlfaikrlI 73
Cdd:cd10229 2 VVAIDFGTTYSGYAYsFITDPGDIhtMYNWWGAptgvssPKTPTCLLLNPDGEfHSFGYEAREK---------------Y 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 74 GRRFEDDEVQR----DLKIMPYAIAKADNGDAWVEVKGKKMAPPQISAEVLKKMKKTAEDYL----GEPVTEA----VIT 141
Cdd:cd10229 67 SDLAEDEEHQWlyffKFKMMLLSEKELTRDTKVKAVNGKSMPALEVFAEALRYLKDHALKELrdrsGSSLDEDdirwVLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 142 VPAYFNDAQRQATKDAGRIAGLDVK------RIINEPTAAAFAYGVNKVKGERKVA-------VYDLGGGTFDISIIEID 208
Cdd:cd10229 147 VPAIWSDAAKQFMREAAVKAGLISEenseqlIIALEPEAAALYCQKLLAEGEEKELkpgdkylVVDCGGGTVDITVHEVL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 209 EVEGETtfEVLATNGNtHLGGEDFDNRVINYLVDEFkreqGIDL-----RNDQLALQRLKDAAEKAKielssaqqtdvnl 283
Cdd:cd10229 227 EDGKLE--ELLKASGG-PWGSTSVDEEFEELLEEIF----GDDFmeafkQKYPSDYLDLLQAFERKK------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 284 pyitadatgpKHMNIKVTRAKLESLVEDMVKDSLEPVRVALkdSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGKepRK 363
Cdd:cd10229 287 ----------RSFKLRLSPELMKSLFDPVVKKIIEHIKELL--EKPELKGVDYIFLVGGFAESPYLQKAVKEAFST--KV 352
|
410 420
....*....|....*....|
gi 2058542806 364 DV----NPDEAVAMGAAIQG 379
Cdd:cd10229 353 KIiippEPGLAVVKGAVLFG 372
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
5-358 |
3.51e-14 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 75.28 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 5 IGIDLGTTNSCVAILDGDHARVIENAEGDRTTPSIIaYADDGEILVGQPAKRQAITNP-KNTLFAIKRLI-GRRFEDDEV 82
Cdd:PRK11678 3 IGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTL-CAPTREAVSEWLYRHLDVPAYdDERQALLRRAIrYNREEDIDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 83 QRD-LKIMPYAIAK--ADNGDAWVeVKGKK-------MAPPQIS------AEVLKKMKKTAEDYLGEPVTEAVITVPAYF 146
Cdd:PRK11678 82 TAQsVFFGLAALAQylEDPEEVYF-VKSPKsflgasgLKPQQVAlfedlvCAMMLHIKQQAEAQLQAAITQAVIGRPVNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 147 N-----DAQRQA----TKDAGRiAGL-DVkRIINEPTAAAFAYGVNkVKGERKVAVYDLGGGTFDISIIE-----IDEVE 211
Cdd:PRK11678 161 QglggeEANRQAegilERAAKR-AGFkDV-EFQFEPVAAGLDFEAT-LTEEKRVLVVDIGGGTTDCSMLLmgpswRGRAD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 212 GETTFevLATNGnTHLGGEDFD-----------------------------------NRV--------------INYLVD 242
Cdd:PRK11678 238 RSASL--LGHSG-QRIGGNDLDialafkqlmpllgmgsetekgialpslpfwnavaiNDVpaqsdfyslangrlLNDLIR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 243 EFKREQGID----LRNDQLALQrLKDAAEKAKIELSSAQQTDVNLPYITADATgpkhmnIKVTRAKLESLVEDMVKDSLE 318
Cdd:PRK11678 315 DAREPEKVArllkVWRQRLSYR-LVRSAEEAKIALSDQAETRASLDFISDGLA------TEISQQGLEEAISQPLARILE 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2058542806 319 PVRVALKDSglavGEIDDVI-LVGGQTRMPLVQKTVA-----------DFFG 358
Cdd:PRK11678 388 LVQLALDQA----QVKPDVIyLTGGSARSPLIRAALAqqlpgipivggDDFG 435
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
117-227 |
3.79e-10 |
|
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: 60.74 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 117 AEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGLDVKRIINEPTAAafaygvNKVKGERKVAVYDLG 196
Cdd:cd24047 46 IRIVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAA------NAVLGIRDGAVVDIG 119
|
90 100 110
....*....|....*....|....*....|.
gi 2058542806 197 GGTFDISIIEidevEGETTFEVLATNGNTHL 227
Cdd:cd24047 120 GGTTGIAVLK----DGKVVYTADEPTGGTHL 146
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
5-276 |
9.75e-10 |
|
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: 60.18 E-value: 9.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 5 IGIDLGTTNSCVAIldgDHARVIENaEgdrttPSIIAY-ADDGEIL-VGQPAKRqaitnpkntlfaikrLIGRRFEDDEV 82
Cdd:cd10225 2 IGIDLGTANTLVYV---KGKGIVLN-E-----PSVVAVdKNTGKVLaVGEEAKK---------------MLGRTPGNIVA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 83 QRDLKimpyaiakadNGdawveVkgkkMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAG 162
Cdd:cd10225 58 IRPLR----------DG-----V----IADFEATEAMLRYFIRKAHRRRGFLRPRVVIGVPSGITEVERRAVKEAAEHAG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 163 LDVKRIINEPTAAAFAYGVNkVKGERKVAVYDLGGGTFDISIIEI-DEVEGETtfevlatngnTHLGGEDFDNRVINYLv 241
Cdd:cd10225 119 AREVYLIEEPMAAAIGAGLP-IEEPRGSMVVDIGGGTTEIAVISLgGIVTSRS----------VRVAGDEMDEAIINYV- 186
|
250 260 270
....*....|....*....|....*....|....*..
gi 2058542806 242 defKREQG--IDLRndqlalqrlkdAAEKAKIELSSA 276
Cdd:cd10225 187 ---RRKYNllIGER-----------TAERIKIEIGSA 209
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
103-363 |
2.96e-09 |
|
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466854 [Multi-domain] Cd Length: 282 Bit Score: 58.46 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 103 VEVKGKKMAPPQIS-----AEVLKKMKKTAEDYLGEPVTEAVITVP----AYFNDAQRqatkdagriAGLDVKRIINEPT 173
Cdd:cd24004 30 EEHPERAMGDGQIHdiskvAESIKELLKELEEKLGSKLKDVVIAIAkvveSLLNVLEK---------AGLEPVGLTLEPF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 174 AAAFAYGVNKVKgERKVAVYDLGGGTFDISIIEIDEVEGETTFevlatngntHLGGEDFDNRVIN-YLVDeFKreqgidl 252
Cdd:cd24004 101 AAANLLIPYDMR-DLNIALVDIGAGTTDIALIRNGGIEAYRMV---------PLGGDDFTKAIAEgFLIS-FE------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 253 rndqlalqrlkdAAEKAKIELSSAqqtDVNLPYITADATGPKHMNIKVTRAKLESLVEDmvkdslepVRVALKDSGLAVG 332
Cdd:cd24004 163 ------------EAEKIKRTYGIF---LLIEAKDQLGFTINKKEVYDIIKPVLEELASG--------IANAIEEYNGKFK 219
|
250 260 270
....*....|....*....|....*....|.
gi 2058542806 333 EIDDVILVGGQTRMPLVQKTVADFFGKEPRK 363
Cdd:cd24004 220 LPDAVYLVGGGSKLPGLNEALAEKLGLPVER 250
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
1-382 |
2.10e-08 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 56.29 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 1 MGKIIGIDLGTTNSCVAILDgdhARVIENaEgdrttPSIIAY-ADDGEIL-VGQPAKRqaitnpkntlfaikrLIGRRFE 78
Cdd:PRK13930 7 FSKDIGIDLGTANTLVYVKG---KGIVLN-E-----PSVVAIdTKTGKVLaVGEEAKE---------------MLGRTPG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 79 DDEVQRDLK---IMPYAIAKadngdawvevkgkkmappqisaEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATK 155
Cdd:PRK13930 63 NIEAIRPLKdgvIADFEATE----------------------AMLRYFIKKARGRRFFRKPRIVICVPSGITEVERRAVR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 156 DAGRIAGL-DVkRIINEPTAAAFAYGVNkvkgerkVA------VYDLGGGTFDISIIEIDEVegettfevlATNGNTHLG 228
Cdd:PRK13930 121 EAAEHAGArEV-YLIEEPMAAAIGAGLP-------VTepvgnmVVDIGGGTTEVAVISLGGI---------VYSESIRVA 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 229 GEDFDNRVINYLVDEFKREQGIdlrndqlalqrlkDAAEKAKIELSSAQQTDVNLpyiTADATG-------PKHMNIKvt 301
Cdd:PRK13930 184 GDEMDEAIVQYVRRKYNLLIGE-------------RTAEEIKIEIGSAYPLDEEE---SMEVRGrdlvtglPKTIEIS-- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 302 raklESLVEDMVKDSL----EPVRVALKDS--GLAVGEIDD-VILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMG 374
Cdd:PRK13930 246 ----SEEVREALAEPLqqivEAVKSVLEKTppELAADIIDRgIVLTGGGALLRGLDKLLSEETGLPVHIAEDPLTCVARG 321
|
....*...
gi 2058542806 375 AaiqGAVL 382
Cdd:PRK13930 322 T---GKAL 326
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
116-227 |
6.96e-08 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 54.07 E-value: 6.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 116 SAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGLDVKRIINEPTAAafaygvNKVKGERKVAVYDL 195
Cdd:PRK15080 69 AVTIVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAA------AAVLGIDNGAVVDI 142
|
90 100 110
....*....|....*....|....*....|..
gi 2058542806 196 GGGTFDISIIEidevEGETTFEVLATNGNTHL 227
Cdd:PRK15080 143 GGGTTGISILK----DGKVVYSADEPTGGTHM 170
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
1-377 |
1.15e-07 |
|
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: 53.93 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 1 MGKIIGIDLGTTNSCVAILDGDharVIENaEgdrttPSIIAY-ADDGEIL-VGQPAKRqaitnpkntlfaikrLIGRRFE 78
Cdd:COG1077 6 FSKDIGIDLGTANTLVYVKGKG---IVLN-E-----PSVVAIdKKTGKVLaVGEEAKE---------------MLGRTPG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 79 DDEVQRDLK------------IMPYAIAKAdngdawveVKGKKMAPPQIsaevlkkmkktaedylgepvteaVITVPAYF 146
Cdd:COG1077 62 NIVAIRPLKdgviadfevteaMLKYFIKKV--------HGRRSFFRPRV-----------------------VICVPSGI 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 147 NDAQRQATKDAGRIAGldVKRI--INEPTAAAFAYGVNkVKGERKVAVYDLGGGTFDISIIEIDEVegettfevlATNGN 224
Cdd:COG1077 111 TEVERRAVRDAAEQAG--AREVylIEEPMAAAIGAGLP-IEEPTGNMVVDIGGGTTEVAVISLGGI---------VVSRS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 225 THLGGEDFDNRVINYLvdefKREQG--IDLRndqlalqrlkdAAEKAKIELSSAQQTDVNLpyiTADATG-------PKH 295
Cdd:COG1077 179 IRVAGDELDEAIIQYV----RKKYNllIGER-----------TAEEIKIEIGSAYPLEEEL---TMEVRGrdlvtglPKT 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 296 MNIK---VTRAKLESL--VEDMVKDSLE---PVRVA-LKDSGlavgeiddVILVGG-------------QTRMPlVqkTV 353
Cdd:COG1077 241 ITITseeIREALEEPLnaIVEAIKSVLEktpPELAAdIVDRG--------IVLTGGgallrgldkllseETGLP-V--HV 309
|
410 420
....*....|....*....|....
gi 2058542806 354 ADffgkeprkdvNPDEAVAMGAAI 377
Cdd:COG1077 310 AE----------DPLTCVARGTGK 323
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
290-389 |
1.48e-07 |
|
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: 54.45 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 290 ATGPKHMnikvTRAKLESLVEDMvKDSLEpvrvALKDSGlavGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKdVNPDE 369
Cdd:COG1070 364 SHTRAHL----ARAVLEGVAFAL-RDGLE----ALEEAG---VKIDRIRATGGGARSPLWRQILADVLGRPVEV-PEAEE 430
|
90 100
....*....|....*....|
gi 2058542806 370 AVAMGAAIQGAVLSGDKTDV 389
Cdd:COG1070 431 GGALGAALLAAVGLGLYDDL 450
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
5-377 |
8.92e-07 |
|
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: 51.40 E-value: 8.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 5 IGIDLGTTNSCVAILDgdhARVIENaegdrtTPSIIAY-ADDGEIL-VGQPAKRQAITNPKNtLFAIKRLIGRRFEDDEV 82
Cdd:pfam06723 4 IGIDLGTANTLVYVKG---KGIVLN------EPSVVAInTKTKKVLaVGNEAKKMLGRTPGN-IVAVRPLKDGVIADFEV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 83 -QRDLKimpYAIAKAdngdawveVKGKKMAPPQIsaevlkkmkktaedylgepvteaVITVPAYFNDAQRQATKDAGRIA 161
Cdd:pfam06723 74 tEAMLK---YFIKKV--------HGRRSFSKPRV-----------------------VICVPSGITEVERRAVKEAAKNA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 162 GLDVKRIINEPTAAAFAYGVNkVKGERKVAVYDLGGGTFDISIIEI-DEVEGETtfevlatngnTHLGGEDFDNRVINYL 240
Cdd:pfam06723 120 GAREVFLIEEPMAAAIGAGLP-VEEPTGNMVVDIGGGTTEVAVISLgGIVTSKS----------VRVAGDEFDEAIIKYI 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 241 VDEFKREQGIdlrndqlalqrlkDAAEKAKIELSSAQQTDVNLpyiTADATG-------PKhmNIKVTRAKLESLVEDMV 313
Cdd:pfam06723 189 RKKYNLLIGE-------------RTAERIKIEIGSAYPTEEEE---KMEIRGrdlvtglPK--TIEISSEEVREALKEPV 250
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2058542806 314 KDSLEPVRVALKDSG--LAVGEIDD-VILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMGAAI 377
Cdd:pfam06723 251 SAIVEAVKEVLEKTPpeLAADIVDRgIVLTGGGALLRGLDKLLSDETGLPVHIAEDPLTCVALGTGK 317
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
105-384 |
3.45e-06 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar proteins; HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. HSPA12B belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12B.
Pssm-ID: 466842 [Multi-domain] Cd Length: 361 Bit Score: 49.58 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 105 VKGKKMAPPQISAEVLKKMKKTAEDYLGE-----PVTEA---VITVPAYFNDAQRQATKDAGRIAGLdVKR-------II 169
Cdd:cd11736 102 VNGKKVQALEVFAHALRFFKEHALQELKDqspslPEKDAvrwVLTVPAIWKQPAKQFMREAAYLAGL-VSPenpeqllIA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 170 NEPTAAAfaygVNKVKGERKVaVYDLGGGTFDISIIEIDEVEGeTTFEVLATNGN---------------THLGGEDFdn 234
Cdd:cd11736 181 LEPEAAS----IYCRKLDRYI-VADCGGGTVDLTVHQIEQPQG-TLKELYKASGGpygavgvdlafekllCQIFGEDF-- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 235 rvinylVDEFKREQGIDLRNDQLALQRLKDAaekAKIELSSAQQTDVNLPYITADAtgpKHmnikvtrakleslVEDMVK 314
Cdd:cd11736 253 ------IATFKAKRPAAWVDLTIAFEARKRT---AALRMSSEAMNELFQPTISQII---QH-------------IDDLMK 307
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 315 DSlepvrvalkdsglAVGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMgaaIQGAVLSG 384
Cdd:cd11736 308 KP-------------EVKGIKFLFLVGGFAESPMLQRAVQAAFGNICRVIIPQDVGLTI---LKGAVLFG 361
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
107-384 |
4.70e-06 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar proteins; HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12A belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A.
Pssm-ID: 466841 [Multi-domain] Cd Length: 413 Bit Score: 49.23 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 107 GKKMAPPQISAEVLKKMKKTA----EDYLGEPVTEA----VITVPAYFNDAQRQATKDAGRIAGLDVKR------IINEP 172
Cdd:cd11735 104 GKKVKALEIFAYALQFFKEQAlkelSDQAGSEFDNSdvrwVITVPAIWKQPAKQFMRQAAYKAGLASPEnpeqliIALEP 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 173 TAAAFAYGVNKVKGERKVAVYDLGGGTFDISIIEIDEVEGETTFEVLATNGNTHLGGEDFDNRVINY------LVDEFKR 246
Cdd:cd11735 184 EAASIYCRKLRLHQMDRYVVVDCGGGTVDLTVHQIRLPEGHLKELYKASGGPYGSLGVDYEFEKLLCkifgedFIDQFKI 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 247 EQGIDLRNDQLALQRLKDAAEKAKIelssaQQTDVNLPYITADATgPKHMNIKVTRAKLESLVeDMVK-----------D 315
Cdd:cd11735 264 KRPAAWVDLMIAFESRKRAAAPDRT-----NPLNITLPFSFIDYY-KKFRGHSVEHALRKSNV-DFVKwssqgmlrmspD 336
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2058542806 316 SLEPVRVALKDSGLA----------VGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPDEAVAMgaaIQGAVLSG 384
Cdd:cd11735 337 AMNALFKPTIDHIIQhltdlfqkpeVSGVKFLFLVGGFAESPLLQQAVQNAFGDQCRVIIPHDVGLTI---LKGAVLFG 412
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
161-359 |
1.52e-05 |
|
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: 47.53 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 161 AGLDVKRIINEPTAAAfaYGVnKVKGERK--VAVYDLGGGTFDISIIEidevEGETTF-EVLAtngnthLGGEDFDNrvi 237
Cdd:cd24048 172 AGLEVDDIVLSPLASA--EAV-LTEDEKElgVALIDIGGGTTDIAVFK----NGSLRYtAVIP------VGGNHITN--- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 238 nylvdefkreqgiDLRndqLALQRLKDAAEKAKIELSSAQQTDV---NLPYITADATGPkhmNIKVTRAKLESLVEDMVK 314
Cdd:cd24048 236 -------------DIA---IGLNTPFEEAERLKIKYGSALSEEAdedEIIEIPGVGGRE---PREVSRRELAEIIEARVE 296
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2058542806 315 DSLEPVRVALKDSGLAVGEIDDVILVGGQTRMPLVQKTVADFFGK 359
Cdd:cd24048 297 EILELVKKELKESGYEDLLPGGIVLTGGGSQLPGLVELAEEVFGM 341
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
302-384 |
3.01e-05 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 46.77 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 302 RAKLESLVEDMvKDSLEpvrvALKDSGLAVGEIddvILVGGQTRMPLVQKTVADFFGKEPRKdVNPDEAVAMGAAIQGAV 381
Cdd:cd07809 370 RAALEGATFGL-RYGLD----ILRELGVEIDEI---RLIGGGSKSPVWRQILADVFGVPVVV-PETGEGGALGAALQAAW 440
|
...
gi 2058542806 382 LSG 384
Cdd:cd07809 441 GAG 443
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
115-374 |
5.95e-05 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 45.67 E-value: 5.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 115 ISAEVLKKMKKTAEDYLGEPVTE--AVITVPAYFNDAQRQATKDAGRIAGLDVKRIINEPTAAAFAYGVnKVKGERKVAV 192
Cdd:PRK13929 76 MTTDLLKQIMKKAGKNIGMTFRKpnVVVCTPSGSTAVERRAISDAVKNCGAKNVHLIEEPVAAAIGADL-PVDEPVANVV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 193 YDLGGGTFDISIIeidevegetTFEVLATNGNTHLGGEDFDNRVINYLVDEFKREQGidlrndqlalqrlKDAAEKAKIE 272
Cdd:PRK13929 155 VDIGGGTTEVAII---------SFGGVVSCHSIRIGGDQLDEDIVSFVRKKYNLLIG-------------ERTAEQVKME 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 273 LSSA--QQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDMVKDSLEPVRVALKDSGLAV-GEIDD--VILVGGQTRMP 347
Cdd:PRK13929 213 IGYAliEHEPETMEVRGRDLVTGLPKTITLESKEIQGAMRESLLHILEAIRATLEDCPPELsGDIVDrgVILTGGGALLN 292
|
250 260
....*....|....*....|....*..
gi 2058542806 348 LVQKTVADFFGKEPRKDVNPDEAVAMG 374
Cdd:PRK13929 293 GIKEWLSEEIVVPVHVAANPLESVAIG 319
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
3-75 |
1.50e-04 |
|
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466796 [Multi-domain] Cd Length: 436 Bit Score: 44.52 E-value: 1.50e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2058542806 3 KIIGIDLGTTNSCVAILDGDHARVIENAEgdRTTPSIIAYADDGEilvgqpakrqAITNPKNTLFAIKRLIGR 75
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLESGRILESVS--RPTPAPISSDDPGR----------SEQDPEKILEAVRNLIDE 61
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
333-381 |
2.00e-04 |
|
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.
Pssm-ID: 426979 [Multi-domain] Cd Length: 197 Bit Score: 42.70 E-value: 2.00e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2058542806 333 EIDDVILVGGQTRMPLVQKTVADFFGKePRKDVNPDEAVAMGAAIQGAV 381
Cdd:pfam02782 148 PIDTIHVSGGGSRNPLLLQLLADALGL-PVVVPGPDEATALGAALLAAV 195
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
1-245 |
2.66e-04 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 43.74 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 1 MGKIIGIDLGTTN---------------SCVAIldgdharvienaegDRTTPSIIAyaddgeilVGQPAKRQAITNPKNT 65
Cdd:PRK13928 2 FGRDIGIDLGTANvlvyvkgkgivlnepSVVAI--------------DKNTNKVLA--------VGEEARRMVGRTPGNI 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 66 LfAIKRLIGRRFEDDEVQRdlKIMPYAIAKAdngdawvevKGKKM-APPQIsaevlkkmkktaedylgepvteaVITVPA 144
Cdd:PRK13928 60 V-AIRPLRDGVIADYDVTE--KMLKYFINKA---------CGKRFfSKPRI-----------------------MICIPT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 145 YFNDAQRQATKDAGRIAGLDVKRIINEPTAAAFAYGVNKVKGERKVAVyDLGGGTFDISIIEIDEVegettfevlATNGN 224
Cdd:PRK13928 105 GITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLDISQPSGNMVV-DIGGGTTDIAVLSLGGI---------VTSSS 174
|
250 260
....*....|....*....|.
gi 2058542806 225 THLGGEDFDNRVINYLVDEFK 245
Cdd:PRK13928 175 IKVAGDKFDEAIIRYIRKKYK 195
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
138-199 |
4.45e-04 |
|
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: 40.91 E-value: 4.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2058542806 138 AVITVPAYFNDAQRQAT-----------KDAGRIAGLDVKRIINEPTAAafAYGVNKVKGERKVAVYDLGGGT 199
Cdd:cd00012 16 IVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAA--AIGALLTLGPEGLLVVDLGGGT 86
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
290-389 |
8.56e-04 |
|
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466808 [Multi-domain] Cd Length: 482 Bit Score: 42.14 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 290 ATGPKHMnikvTRAKLE----SLvedmvKDSLEpvrvALKDSGLAVGEIddvILVGGQTRMPLVQKTVADFFGKEPRKDV 365
Cdd:cd07808 361 SHTRAHL----ARAVLEgvafSL-----RDSLE----VLKELGIKVKEI---RLIGGGAKSPLWRQILADVLGVPVVVPA 424
|
90 100
....*....|....*....|....
gi 2058542806 366 NPDEAvAMGAAIQGAVLSGDKTDV 389
Cdd:cd07808 425 EEEGS-AYGAALLAAVGAGVFDDL 447
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
289-384 |
1.16e-03 |
|
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466793 [Multi-domain] Cd Length: 443 Bit Score: 41.80 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 289 DATGPKHMnikvTRAKLESLVEDMvKDSLEpvrvALKDSGlavGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPd 368
Cdd:cd07773 361 LGTTRADL----LRAILEGLAFEL-RLNLE----ALEKAG---IPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVP- 427
|
90
....*....|....*.
gi 2058542806 369 EAVAMGAAIQGAVLSG 384
Cdd:cd07773 428 EATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
289-389 |
1.67e-03 |
|
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466798 [Multi-domain] Cd Length: 433 Bit Score: 41.35 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 289 DATGPKHMnikvTRAKLESLVEDMvKDSLEpvrvALKDSGlavGEIDDVILVGGQTRMPLVQKTVADFFGKEPRKDVNPd 368
Cdd:cd07779 322 LSHTRAHL----ARAILEGIAFEL-RDNLE----AMEKAG---VPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETS- 388
|
90 100
....*....|....*....|.
gi 2058542806 369 EAVAMGAAIQGAVLSGDKTDV 389
Cdd:cd07779 389 EATALGAAILAAVGAGIYPDF 409
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
5-276 |
8.49e-03 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 38.92 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 5 IGIDLGTTNSCVAILDGDharVIENAegdrttPSIIAYADD-GEIL-VGQPAKRqaitnpkntlfaikrLIGRRFEDDEV 82
Cdd:PRK13927 8 LGIDLGTANTLVYVKGKG---IVLNE------PSVVAIRTDtKKVLaVGEEAKQ---------------MLGRTPGNIVA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 83 QRDLK------------IMPYAIAKadngdawveVKGKKMAPPQIsaevlkkmkktaedylgepvteaVITVPAYFNDAQ 150
Cdd:PRK13927 64 IRPMKdgviadfdvtekMLKYFIKK---------VHKNFRPSPRV-----------------------VICVPSGITEVE 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058542806 151 RQATKDAGRIAGL-DVkRIINEPTAAAFAYG--VNKVKGerkVAVYDLGGGTFDISIIEIDeveGettfevLATNGNTHL 227
Cdd:PRK13927 112 RRAVRESALGAGArEV-YLIEEPMAAAIGAGlpVTEPTG---SMVVDIGGGTTEVAVISLG---G------IVYSKSVRV 178
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2058542806 228 GGEDFDNRVINYLvdefKREQGIdlrndqLALQRlkdAAEKAKIELSSA 276
Cdd:PRK13927 179 GGDKFDEAIINYV----RRNYNL------LIGER---TAERIKIEIGSA 214
|
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