|
Name |
Accession |
Description |
Interval |
E-value |
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
1-638 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 1267.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 1 MGKIIGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRfqDE 80
Cdd:PRK00290 1 MGKIIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRLMGRR--DE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 81 EVQRDVSIMPYKIVAADNGDAWLDVKGTKTAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRI 160
Cdd:PRK00290 79 EVQKDIKLVPYKIVKADNGDAWVEIDGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDAGKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 161 AGLEVKRIINEPTAAALAYGLDKEvGNRTIAVYDLGGGTFDISIIEIdevdGEKTFEVLATNGDTHLGGEDFDTRLINYL 240
Cdd:PRK00290 159 AGLEVLRIINEPTAAALAYGLDKK-GDEKILVYDLGGGTFDVSILEI----GDGVFEVLSTNGDTHLGGDDFDQRIIDYL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 241 VDEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDLVNRSIEPL 320
Cdd:PRK00290 234 ADEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEINLPFITADASGPKHLEIKLTRAKFEELTEDLVERTIEPC 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 321 KVALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLTGEVKDVLLLDVTPLSLG 400
Cdd:PRK00290 314 KQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLAGDVKDVLLLDVTPLSLG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 401 IETMGGVMTALINKNTTIPTKHSQVFSTAEDNQSAVTIHVIQGERKRASDNKSLGQFNLDGINPAPRGMPQIEVTFDIDA 480
Cdd:PRK00290 394 IETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDIDA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 481 DGILHVSAKDKNSGKEQKITIKASSGLNEEEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLPAD 560
Cdd:PRK00290 474 NGIVHVSAKDKGTGKEQSITITASSGLSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKELGDKVPAD 553
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2005139737 561 DKTAIESALTALETSLKGEDKADIEAKMQALAQASQKLMEiaqqQHAQQQAGGADASESNAKDDDVVDAEFEEVKDKK 638
Cdd:PRK00290 554 EKEKIEAAIKELKEALKGEDKEAIKAKTEELTQASQKLGE----AMYQQAQAAQGAAGAAAKDDDVVDAEFEEVKDDK 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: 1028.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 3 KIIGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFqdEEV 82
Cdd:TIGR02350 1 KIIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNGERLVGQPAKRQAVTNPENTIYSIKRFMGRRF--DEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 83 QRDVSIMPYKIVAaDNGDAWLDVKGTKTAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAG 162
Cdd:TIGR02350 79 TEEAKRVPYKVVG-DGGDVRVKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 163 LEVKRIINEPTAAALAYGLDKEVGNRTIAVYDLGGGTFDISIIEIdevdGEKTFEVLATNGDTHLGGEDFDTRLINYLVD 242
Cdd:TIGR02350 158 LEVLRIINEPTAAALAYGLDKSKKDEKILVFDLGGGTFDVSILEI----GDGVFEVLSTAGDTHLGGDDFDQRIIDWLAD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 243 EFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDLVNRSIEPLKV 322
Cdd:TIGR02350 234 EFKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINLPFITADASGPKHLEMTLTRAKFEELTADLVERTKEPVRQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 323 ALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLTGEVKDVLLLDVTPLSLGIE 402
Cdd:TIGR02350 314 ALKDAGLSASDIDEVILVGGSTRIPAVQELVKDFFGKEPNKSVNPDEVVAIGAAIQGGVLKGDVKDVLLLDVTPLSLGIE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 403 TMGGVMTALINKNTTIPTKHSQVFSTAEDNQSAVTIHVIQGERKRASDNKSLGQFNLDGINPAPRGMPQIEVTFDIDADG 482
Cdd:TIGR02350 394 TLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDANG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 483 ILHVSAKDKNSGKEQKITIKASSGLNEEEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLPADDK 562
Cdd:TIGR02350 474 ILHVSAKDKGTGKEQSITITASSGLSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAGDKLPAEEK 553
|
570 580 590
....*....|....*....|....*....|....*...
gi 2005139737 563 TAIESALTALETSLKGEDKADIEAKMQALAQASQKLME 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: 955.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 4 IIGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTQDgETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQ 83
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPK-ERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 84 RDVSIMPYKIVAADNGDAWLDV--KGTKTAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIA 161
Cdd:pfam00012 80 RDIKHLPYKVVKLPNGDAGVEVryLGETFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 162 GLEVKRIINEPTAAALAYGLDKEVGNRTIAVYDLGGGTFDISIIEIDevDGekTFEVLATNGDTHLGGEDFDTRLINYLV 241
Cdd:pfam00012 160 GLNVLRIVNEPTAAALAYGLDKTDKERNIAVYDLGGGTFDVSILEIG--RG--VFEVKATNGDTHLGGEDFDLRLVDHLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 242 DEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQqTDVNLPYITADATGpKHMNIKVTRAKLESLVEDLVNRSIEPLK 321
Cdd:pfam00012 236 EEFKKKYGIDLSKDKRALQRLREAAEKAKIELSSNQ-TNINLPFITAMADG-KDVSGTLTRAKFEELVADLFERTLEPVE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 322 VALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLTG--EVKDVLLLDVTPLSL 399
Cdd:pfam00012 314 KALKDAGLSKSEIDEVVLVGGSTRIPAVQELVKEFFGKEPSKGVNPDEAVAIGAAVQAGVLSGtfDVKDFLLLDVTPLSL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 400 GIETMGGVMTALINKNTTIPTKHSQVFSTAEDNQSAVTIHVIQGERKRASDNKSLGQFNLDGINPAPRGMPQIEVTFDID 479
Cdd:pfam00012 394 GIETLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDID 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 480 ADGILHVSAKDKNSGKEQKITIKASSGLNEEEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLPA 559
Cdd:pfam00012 474 ANGILTVSAKDKGTGKEQEITIEASEGLSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGDKVPE 553
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2005139737 560 DDKTAIESALTALETSLKGEDKADIEAKMQALAQASQKLME 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: 858.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 2 GKIIGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEE 81
Cdd:PTZ00400 41 GDIVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDGQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEDA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 82 VQRDVSIMPYKIVAADNGDAWLDVKGTKTAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIA 161
Cdd:PTZ00400 121 TKKEQKILPYKIVRASNGDAWIEAQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAGKIA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 162 GLEVKRIINEPTAAALAYGLDKEVGnRTIAVYDLGGGTFDISIIEIdeVDGekTFEVLATNGDTHLGGEDFDTRLINYLV 241
Cdd:PTZ00400 201 GLDVLRIINEPTAAALAFGMDKNDG-KTIAVYDLGGGTFDISILEI--LGG--VFEVKATNGNTSLGGEDFDQRILNYLI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 242 DEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDLVNRSIEPLK 321
Cdd:PTZ00400 276 AEFKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQTEINLPFITADQSGPKHLQIKLSRAKLEELTHDLLKKTIEPCE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 322 VALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLTGEVKDVLLLDVTPLSLGI 401
Cdd:PTZ00400 356 KCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIFGKEPSKGVNPDEAVAMGAAIQAGVLKGEIKDLLLLDVTPLSLGI 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 402 ETMGGVMTALINKNTTIPTKHSQVFSTAEDNQSAVTIHVIQGERKRASDNKSLGQFNLDGINPAPRGMPQIEVTFDIDAD 481
Cdd:PTZ00400 436 ETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTFDVDAN 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 482 GILHVSAKDKNSGKEQKITIKASSGLNEEEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLPADD 561
Cdd:PTZ00400 516 GIMNISAVDKSTGKKQEITIQSSGGLSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSDLKDKISDAD 595
|
570 580 590
....*....|....*....|....*....|....*..
gi 2005139737 562 KTAIESALTALETSLKGEDKADIEAKMQALAQASQKL 598
Cdd:PTZ00400 596 KDELKQKITKLRSTLSSEDVDSIKDKTKQLQEASWKI 632
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
1-633 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 837.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 1 MGKIIGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFqdE 80
Cdd:CHL00094 1 MGKVVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKGDLLVGQIAKRQAVINPENTFYSVKRFIGRKF--S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 81 EVQRDVSIMPYKIVAADNGDAWLD--VKGTKTAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAG 158
Cdd:CHL00094 79 EISEEAKQVSYKVKTDSNGNIKIEcpALNKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 159 RIAGLEVKRIINEPTAAALAYGLDKEvGNRTIAVYDLGGGTFDISIIEIdevdGEKTFEVLATNGDTHLGGEDFDTRLIN 238
Cdd:CHL00094 159 KIAGLEVLRIINEPTAASLAYGLDKK-NNETILVFDLGGGTFDVSILEV----GDGVFEVLSTSGDTHLGGDDFDKKIVN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 239 YLVDEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDLVNRSIE 318
Cdd:CHL00094 234 WLIKEFKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINLPFITATQTGPKHIEKTLTRAKFEELCSDLINRCRI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 319 PLKVALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLTGEVKDVLLLDVTPLS 398
Cdd:CHL00094 314 PVENALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLLGKKPNQSVNPDEVVAIGAAVQAGVLAGEVKDILLLDVTPLS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 399 LGIETMGGVMTALINKNTTIPTKHSQVFSTAEDNQSAVTIHVIQGERKRASDNKSLGQFNLDGINPAPRGMPQIEVTFDI 478
Cdd:CHL00094 394 LGVETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDI 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 479 DADGILHVSAKDKNSGKEQKITIKASSGLNEEEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLP 558
Cdd:CHL00094 474 DANGILSVTAKDKGTGKEQSITIQGASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKELKDKIS 553
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2005139737 559 ADDKTAIESALTALETSLKGEDKADIEAKMQALAQAsqkLMEIAQQQHAQQQaggadASESNAKDDDVVDAEFEE 633
Cdd:CHL00094 554 EEKKEKIENLIKKLRQALQNDNYESIKSLLEELQKA---LMEIGKEVYSSTS-----TTDPASNDDDVIDTDFSE 620
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
1-594 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 798.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 1 MGKIIGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQ-- 78
Cdd:PRK13410 1 MGRIVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTKDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 79 DEEVQRdvsiMPYKIVAADNGDAWLDVKGTKT--APPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKD 156
Cdd:PRK13410 81 DPESKR----VPYTIRRNEQGNVRIKCPRLERefAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 157 AGRIAGLEVKRIINEPTAAALAYGLDKEvGNRTIAVYDLGGGTFDISIIEIdevdGEKTFEVLATNGDTHLGGEDFDTRL 236
Cdd:PRK13410 157 AGRIAGLEVERILNEPTAAALAYGLDRS-SSQTVLVFDLGGGTFDVSLLEV----GNGVFEVKATSGDTQLGGNDFDKRI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 237 INYLVDEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDLVNRS 316
Cdd:PRK13410 232 VDWLAEQFLEKEGIDLRRDRQALQRLTEAAEKAKIELSGVSVTDISLPFITATEDGPKHIETRLDRKQFESLCGDLLDRL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 317 IEPLKVALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLTGEVKDVLLLDVTP 396
Cdd:PRK13410 312 LRPVKRALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLIPREPNQNVNPDEVVAVGAAIQAGILAGELKDLLLLDVTP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 397 LSLGIETMGGVMTALINKNTTIPTKHSQVFSTAEDNQSAVTIHVIQGERKRASDNKSLGQFNLDGINPAPRGMPQIEVTF 476
Cdd:PRK13410 392 LSLGLETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 477 DIDADGILHVSAKDKNSGKEQKITIKASSGLNEEEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEA--- 553
Cdd:PRK13410 472 DIDANGILQVSATDRTTGREQSVTIQGASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERRLRDAale 551
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 2005139737 554 -GDKLPADDKTAIESALTALETSLKGEDKADIEAKMQALAQA 594
Cdd:PRK13410 552 fGPYFAERQRRAVESAMRDVQDSLEQDDDRELDLAVADLQEA 593
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
1-601 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 793.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 1 MGKIIGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDE 80
Cdd:PRK13411 1 MGKVIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSGDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 81 EVQRdvSIMPYKIVAADNGDAWLDVKGTKTAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRI 160
Cdd:PRK13411 81 EEER--SRVPYTCVKGRDDTVNVQIRGRNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAGTI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 161 AGLEVKRIINEPTAAALAYGLDKEVGNRTIAVYDLGGGTFDISIIEIdevdGEKTFEVLATNGDTHLGGEDFDTRLINYL 240
Cdd:PRK13411 159 AGLEVLRIINEPTAAALAYGLDKQDQEQLILVFDLGGGTFDVSILQL----GDGVFEVKATAGNNHLGGDDFDNCIVDWL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 241 VDEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDLVNRSIEPL 320
Cdd:PRK13411 235 VENFQQQEGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINLPFITADETGPKHLEMELTRAKFEELTKDLVEATIEPM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 321 KVALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFF-GKEPRKDVNPDEAVAIGAAVQGGVLTGEVKDVLLLDVTPLSL 399
Cdd:PRK13411 315 QQALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFgGKQPDRSVNPDEAVALGAAIQAGVLGGEVKDLLLLDVTPLSL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 400 GIETMGGVMTALINKNTTIPTKHSQVFSTAEDNQSAVTIHVIQGERKRASDNKSLGQFNLDGINPAPRGMPQIEVTFDID 479
Cdd:PRK13411 395 GIETLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSFEID 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 480 ADGILHVSAKDKNSGKEQKITIKASSGLNEEEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLPA 559
Cdd:PRK13411 475 VNGILKVSAQDQGTGREQSIRITNTGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKENGELISE 554
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 2005139737 560 DDKTAIESALTALETSLkGEDKADIEAKMQALAQASQKLMEI 601
Cdd:PRK13411 555 ELKQRAEQKVEQLEAAL-TDPNISLEELKQQLEEFQQALLAI 595
|
|
| 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: 774.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 4 IIGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEevq 83
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPKDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFDE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 84 rdvsimpykivaadngdaWLDVKGTKTAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGL 163
Cdd:COG0443 78 ------------------ATEVGGKRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARIAGL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 164 EVKRIINEPTAAALAYGLDKEVGNRTIAVYDLGGGTFDISIIEIdevdGEKTFEVLATNGDTHLGGEDFDTRLINYLVDE 243
Cdd:COG0443 140 EVLRLLNEPTAAALAYGLDKGKEEETILVYDLGGGTFDVSILRL----GDGVFEVLATGGDTHLGGDDFDQALADYVAPE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 244 FKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYitadaTGPKHMNIKVTRAKLESLVEDLVNRSIEPLKVA 323
Cdd:COG0443 216 FGKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINLPF-----SGGKHLDVELTRAEFEELIAPLVERTLDPVRQA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 324 LQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLTGEVKDvllLDVTPLSLGIET 403
Cdd:COG0443 291 LADAGLSPSDIDAVLLVGGSTRMPAVRERVKELFGKEPLKGVDPDEAVALGAAIQAGVLAGDVKD---LDVTPLSLGIET 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 404 MGGVMTALINKNTTIPTKHSQVFSTAEDNQSAVTIHVIQGERKRASDNKSLGQFNLDGINPAPRGMPQIEVTFDIDADGI 483
Cdd:COG0443 368 LGGVFTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGI 447
|
490 500 510
....*....|....*....|....*....|...
gi 2005139737 484 LHVSAKDKNSGKEQKITIKassglneEEIQKMV 516
Cdd:COG0443 448 LSVSAKDLGTGKEQSITIK-------EEIERML 473
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
3-633 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 744.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 3 KIIGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFqdEEV 82
Cdd:PLN03184 40 KVVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNGDRLVGQIAKRQAVVNPENTFFSVKRFIGRKM--SEV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 83 QRDVSIMPYKIVAADNGDAWLD--VKGTKTAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRI 160
Cdd:PLN03184 118 DEESKQVSYRVVRDENGNVKLDcpAIGKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 161 AGLEVKRIINEPTAAALAYGLDKEvGNRTIAVYDLGGGTFDISIIEIdevdGEKTFEVLATNGDTHLGGEDFDTRLINYL 240
Cdd:PLN03184 198 AGLEVLRIINEPTAASLAYGFEKK-SNETILVFDLGGGTFDVSVLEV----GDGVFEVLSTSGDTHLGGDDFDKRIVDWL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 241 VDEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDLVNRSIEPL 320
Cdd:PLN03184 273 ASNFKKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISLPFITATADGPKHIDTTLTRAKFEELCSDLLDRCKTPV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 321 KVALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLTGEVKDVLLLDVTPLSLG 400
Cdd:PLN03184 353 ENALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKLTGKDPNVTVNPDEVVALGAAVQAGVLAGEVSDIVLLDVTPLSLG 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 401 IETMGGVMTALINKNTTIPTKHSQVFSTAEDNQSAVTIHVIQGERKRASDNKSLGQFNLDGINPAPRGMPQIEVTFDIDA 480
Cdd:PLN03184 433 LETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFDIDA 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 481 DGILHVSAKDKNSGKEQKITIKASSGLNEEEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLPAD 560
Cdd:PLN03184 513 NGILSVSATDKGTGKKQDITITGASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKELGDKVPAD 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 561 DKTAIESALTALETSLKGEDKADIEAKMQALaqaSQKLMEIAQQQHAQQQAGGADA-----------SESNAKDDDVVDA 629
Cdd:PLN03184 593 VKEKVEAKLKELKDAIASGSTQKMKDAMAAL---NQEVMQIGQSLYNQPGAGGAGPapggeagssssSSSGGDGDDVIDA 669
|
....
gi 2005139737 630 EFEE 633
Cdd:PLN03184 670 DFTD 673
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
2-594 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 737.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 2 GKIIGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYtQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEE 81
Cdd:PTZ00186 27 GDVIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAF-KGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 82 VQRDVSIMPYKIVAADNGDAWL-DVKGTKTAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRI 160
Cdd:PTZ00186 106 IQKDIKNVPYKIVRAGNGDAWVqDGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 161 AGLEVKRIINEPTAAALAYGLDKeVGNRTIAVYDLGGGTFDISIIEIdevdGEKTFEVLATNGDTHLGGEDFDTRLINYL 240
Cdd:PTZ00186 186 AGLNVIRVVNEPTAAALAYGMDK-TKDSLIAVYDLGGGTFDISVLEI----AGGVFEVKATNGDTHLGGEDFDLALSDYI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 241 VDEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDLVNRSIEPL 320
Cdd:PTZ00186 261 LEEFRKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADGAQHIQMHISRSKFEGITQRLIERSIAPC 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 321 KVALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLTGEVKDVLLLDVTPLSLG 400
Cdd:PTZ00186 341 KQCMKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFFQKDPFRGVNPDEAVALGAATLGGVLRGDVKGLVLLDVTPLSLG 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 401 IETMGGVMTALINKNTTIPTKHSQVFSTAEDNQSAVTIHVIQGERKRASDNKSLGQFNLDGINPAPRGMPQIEVTFDIDA 480
Cdd:PTZ00186 421 IETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDIDA 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 481 DGILHVSAKDKNSGKEQKITIKASSGLNEEEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEAgdKLPAD 560
Cdd:PTZ00186 501 NGICHVTAKDKATGKTQNITITANGGLSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGEW--KYVSD 578
|
570 580 590
....*....|....*....|....*....|....*..
gi 2005139737 561 -DKTAIESALTALETSLKGED--KADIEAKMQALAQA 594
Cdd:PTZ00186 579 aEKENVKTLVAELRKAMENPNvaKDDLAAATDKLQKA 615
|
|
| 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: 714.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 4 IIGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQ 83
Cdd:cd10234 1 IIGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 84 RDvsIMPYKIVAADNGDAWLDVKGTKTAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGL 163
Cdd:cd10234 81 RK--QVPYPVVSAGNGDAWVEIGGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIAGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 164 EVKRIINEPTAAALAYGLDKEvGNRTIAVYDLGGGTFDISIIEIdevdGEKTFEVLATNGDTHLGGEDFDTRLINYLVDE 243
Cdd:cd10234 159 EVLRIINEPTAAALAYGLDKK-KDEKILVYDLGGGTFDVSILEI----GDGVFEVLSTNGDTHLGGDDFDQRIIDYLADE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 244 FKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDLVNRSIEPLKVA 323
Cdd:cd10234 234 FKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLETEINLPFITADASGPKHLEMKLTRAKFEELTEDLVERTIEPVEQA 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 324 LQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLT 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: 699.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 2 GKIIGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEE 81
Cdd:cd11733 1 GDVIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 82 VQRDVSIMPYKIVAADNGDAWLDVKGTKTAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIA 161
Cdd:cd11733 81 VQKDIKMVPYKIVKASNGDAWVEAHGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDAGQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 162 GLEVKRIINEPTAAALAYGLDKEvGNRTIAVYDLGGGTFDISIIEIDevdgEKTFEVLATNGDTHLGGEDFDTRLINYLV 241
Cdd:cd11733 161 GLNVLRIINEPTAAALAYGLDKK-DDKIIAVYDLGGGTFDISILEIQ----KGVFEVKATNGDTFLGGEDFDNALLNYLV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 242 DEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDLVNRSIEPLK 321
Cdd:cd11733 236 AEFKKEQGIDLSKDNLALQRLREAAEKAKIELSSSLQTDINLPFITADASGPKHLNMKLTRAKFESLVGDLIKRTVEPCK 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2005139737 322 VALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVL 382
Cdd:cd11733 316 KCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIFGKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
5-596 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 628.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 5 IGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTQDGeTLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDeeVQR 84
Cdd:PRK05183 22 VGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDG-IEVGYEARANAAQDPKNTISSVKRFMGRSLAD--IQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 85 DVSIMPYKIVAADNGDAWLD-VKGTKTaPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGL 163
Cdd:PRK05183 99 RYPHLPYQFVASENGMPLIRtAQGLKS-PVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARLAGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 164 EVKRIINEPTAAALAYGLDKEVgNRTIAVYDLGGGTFDISIIEIDE-VdgektFEVLATNGDTHLGGEDFDTRLINYLVD 242
Cdd:PRK05183 178 NVLRLLNEPTAAAIAYGLDSGQ-EGVIAVYDLGGGTFDISILRLSKgV-----FEVLATGGDSALGGDDFDHLLADWILE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 243 EfkkdQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLpyitADATGpkhmniKVTRAKLESLVEDLVNRSIEPLKV 322
Cdd:PRK05183 252 Q----AGLSPRLDPEDQRLLLDAARAAKEALSDADSVEVSV----ALWQG------EITREQFNALIAPLVKRTLLACRR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 323 ALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLTG--EVKDVLLLDVTPLSLG 400
Cdd:PRK05183 318 ALRDAGVEADEVKEVVMVGGSTRVPLVREAVGEFFGRTPLTSIDPDKVVAIGAAIQADILAGnkPDSDMLLLDVIPLSLG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 401 IETMGGVMTALINKNTTIPTKHSQVFSTAEDNQSAVTIHVIQGERKRASDNKSLGQFNLDGINPAPRGMPQIEVTFDIDA 480
Cdd:PRK05183 398 LETMGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 481 DGILHVSAKDKNSGKEQKITIKASSGLNEEEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLPAD 560
Cdd:PRK05183 478 DGLLSVTAMEKSTGVEASIQVKPSYGLTDDEIARMLKDSMSHAEEDMQARALAEQKVEAERVLEALQAALAADGDLLSAA 557
|
570 580 590
....*....|....*....|....*....|....*.
gi 2005139737 561 DKTAIESALTALETSLKGEDKADIEAKMQALAQASQ 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: 624.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 2 GKIIGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEE 81
Cdd:cd11734 1 GPVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTKDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 82 VQRDVSIMPYKIVAADNGDAWLDVKGTKTAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIA 161
Cdd:cd11734 81 VQRDIKEVPYKIVKHSNGDAWVEARGQKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAGQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 162 GLEVKRIINEPTAAALAYGLDKEvGNRTIAVYDLGGGTFDISIIEIDevdgEKTFEVLATNGDTHLGGEDFDTRLINYLV 241
Cdd:cd11734 161 GLNVLRVINEPTAAALAYGLDKS-GDKVIAVYDLGGGTFDISILEIQ----KGVFEVKSTNGDTHLGGEDFDIALVRHIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 242 DEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDLVNRSIEPLK 321
Cdd:cd11734 236 SEFKKESGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINLPFITADASGPKHINMKLTRAQFESLVKPLVDRTVEPCK 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2005139737 322 VALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLTG 384
Cdd:cd11734 316 KALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIFGREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
5-599 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 609.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 5 IGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTqDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQR 84
Cdd:PTZ00009 7 IGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDSVVQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 85 DVSIMPYKIVAADNGDAWLDV--KGTKTA--PPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRI 160
Cdd:PTZ00009 86 DMKHWPFKVTTGGDDKPMIEVtyQGEKKTfhPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAGTI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 161 AGLEVKRIINEPTAAALAYGLDK-EVGNRTIAVYDLGGGTFDISIIEIDevDGekTFEVLATNGDTHLGGEDFDTRLINY 239
Cdd:PTZ00009 166 AGLNVLRIINEPTAAAIAYGLDKkGDGEKNVLIFDLGGGTFDVSLLTIE--DG--IFEVKATAGDTHLGGEDFDNRLVEF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 240 LVDEFK-KDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGpkhmNIKVTRAKLESLVEDLVNRSIE 318
Cdd:PTZ00009 242 CVQDFKrKNRGKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDY----NVTISRARFEELCGDYFRNTLQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 319 PLKVALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFF-GKEPRKDVNPDEAVAIGAAVQGGVLTGE----VKDVLLLD 393
Cdd:PTZ00009 318 PVEKVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFnGKEPCKSINPDEAVAYGAAVQAAILTGEqssqVQDLLLLD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 394 VTPLSLGIETMGGVMTALINKNTTIPTKHSQVFSTAEDNQSAVTIHVIQGERKRASDNKSLGQFNLDGINPAPRGMPQIE 473
Cdd:PTZ00009 398 VTPLSLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 474 VTFDIDADGILHVSAKDKNSGKEQKITIKASSG-LNEEEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEE 552
Cdd:PTZ00009 478 VTFDIDANGILNVSAEDKSTGKSNKITITNDKGrLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQD 557
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2005139737 553 A--GDKLPADDKTAIESALTA----LETSLKGEdKADIEAKMQALAQASQKLM 599
Cdd:PTZ00009 558 EkvKGKLSDSDKATIEKAIDEalewLEKNQLAE-KEEFEHKQKEVESVCNPIM 609
|
|
| 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: 602.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 4 IIGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQ 83
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYLKDGGVEVGKEALAAAAEDPKNTISSVKRLMGRSIEDIKTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 84 rdvSIMPYKIVAADNGDAWLDVKGTKTAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGL 163
Cdd:TIGR01991 81 ---SILPYRFVDGPGEMVRLRTVQGTVTPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARLAGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 164 EVKRIINEPTAAALAYGLDKEvGNRTIAVYDLGGGTFDISIIEIdeVDGekTFEVLATNGDTHLGGEDFDTRLINYLVde 243
Cdd:TIGR01991 158 NVLRLLNEPTAAAVAYGLDKA-SEGIYAVYDLGGGTFDVSILKL--TKG--VFEVLATGGDSALGGDDFDHALAKWIL-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 244 fkKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLpyitadATGPKHMNIKVTRAKLESLVEDLVNRSIEPLKVA 323
Cdd:TIGR01991 231 --KQLGISADLNPEDQRLLLQAARAAKEALTDAESVEVDF------TLDGKDFKGKLTRDEFEALIQPLVQKTLSICRRA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 324 LQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLTGEV--KDVLLLDVTPLSLGI 401
Cdd:TIGR01991 303 LRDAGLSVEEIKGVVLVGGSTRMPLVRRAVAELFGQEPLTDIDPDQVVALGAAIQADLLAGNRigNDLLLLDVTPLSLGI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 402 ETMGGVMTALINKNTTIPTKHSQVFSTAEDNQSAVTIHVIQGERKRASDNKSLGQFNLDGINPAPRGMPQIEVTFDIDAD 481
Cdd:TIGR01991 383 ETMGGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDAD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 482 GILHVSAKDKNSGKEQKITIKASSGLNEEEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLPADD 561
Cdd:TIGR01991 463 GLLTVSAQEQSTGVEQSIQVKPSYGLSDEEIERMLKDSFKHAEEDMYARALAEQKVEAERILEALQAALAADGDLLSEDE 542
|
570 580 590
....*....|....*....|....*....|....
gi 2005139737 562 KTAIESALTALETSLKGEDKADIEAKMQALAQAS 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: 527.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 4 IIGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTqDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQ 83
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFT-DGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 84 RDVSIMPYKIVAADNGDAW--LDVKGTKT--APPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGR 159
Cdd:cd24028 80 SDIKHWPFKVVEDEDGKPKieVTYKGEEKtfSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 160 IAGLEVKRIINEPTAAALAYGLDKEV-GNRTIAVYDLGGGTFDISIIEIDevdgEKTFEVLATNGDTHLGGEDFDTRLIN 238
Cdd:cd24028 160 IAGLNVLRIINEPTAAALAYGLDKKSsGERNVLVFDLGGGTFDVSLLSID----NGVFEVKATAGDTHLGGEDFDNRLVE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 239 YLVDEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQT--DVNLPYITADatgpkhMNIKVTRAKLESLVEDLVNRS 316
Cdd:cd24028 236 YLVEEFKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSAtiEIDSLYDGID------FETTITRAKFEELCEDLFKKC 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2005139737 317 IEPLKVALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFF-GKEPRKDVNPDEAVAIGAAVQGGVL 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 |
2.61e-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: 507.90 E-value: 2.61e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 2 GKIIGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTqDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEE 81
Cdd:cd10241 1 GTVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFT-DGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 82 VQRDVSIMPYKIVAADNGDAW-LDVKGTKT--APPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAG 158
Cdd:cd10241 80 VQKDIKLLPFKIVNKNGKPYIqVEVKGEKKtfAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 159 RIAGLEVKRIINEPTAAALAYGLDKEVGNRTIAVYDLGGGTFDISIIEIDevDGekTFEVLATNGDTHLGGEDFDTRLIN 238
Cdd:cd10241 160 TIAGLNVLRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSLLTID--NG--VFEVLATNGDTHLGGEDFDQRVMD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 239 YLVDEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNlpyITADATGpKHMNIKVTRAKLESLVEDLVNRSIE 318
Cdd:cd10241 236 HFIKLFKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIE---IESLFDG-EDFSETLTRAKFEELNMDLFRKTLK 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2005139737 319 PLKVALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFF-GKEPRKDVNPDEAVAIGAAVQGGVL 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 |
2.45e-161 |
|
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: 467.11 E-value: 2.45e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 5 IGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTqDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQR 84
Cdd:cd10233 2 IGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 85 DVSIMPYKIVAaDNGDAWLDV--KG-TKT-APPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRI 160
Cdd:cd10233 81 DMKHWPFKVVS-GGDKPKIQVeyKGeTKTfTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 161 AGLEVKRIINEPTAAALAYGLDKEV-GNRTIAVYDLGGGTFDISIIEIDevdgEKTFEVLATNGDTHLGGEDFDTRLINY 239
Cdd:cd10233 160 AGLNVLRIINEPTAAAIAYGLDKKGkGERNVLIFDLGGGTFDVSLLTIE----DGIFEVKATAGDTHLGGEDFDNRLVNH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 240 LVDEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLP--YITADatgpkhMNIKVTRAKLESLVEDLVNRSI 317
Cdd:cd10233 236 FVQEFKRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDslFEGID------FYTSITRARFEELCADLFRSTL 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2005139737 318 EPLKVALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFF-GKEPRKDVNPDEAVAIGAAVQGGVL 382
Cdd:cd10233 310 EPVEKVLRDAKLDKSQIHEIVLVGGSTRIPKVQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
1-384 |
1.04e-160 |
|
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: 465.15 E-value: 1.04e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 1 MGKIIGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDe 80
Cdd:cd10236 1 HRLAVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITVGEKAKENAITDPENTISSVKRLMGRSLAD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 81 eVQRDVSIMPYKIVAADNGDAWLDVKGTKTAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRI 160
Cdd:cd10236 80 -VKEELPLLPYRLVGDENELPRFRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 161 AGLEVKRIINEPTAAALAYGLDKEvGNRTIAVYDLGGGTFDISIIEIDevDGekTFEVLATNGDTHLGGEDFDTRLINYl 240
Cdd:cd10236 159 AGLNVLRLLNEPTAAALAYGLDQK-KEGTIAVYDLGGGTFDISILRLS--DG--VFEVLATGGDTALGGDDFDHLLADW- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 241 vdeFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPkhmnikVTRAKLESLVEDLVNRSIEPL 320
Cdd:cd10236 233 ---ILKQIGIDARLDPAVQQALLQAARRAKEALSDADSASIEVEVEGKDWERE------ITREEFEELIQPLVKRTLEPC 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2005139737 321 KVALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLTG 384
Cdd:cd10236 304 RRALKDAGLEPADIDEVVLVGGSTRIPLVRQRVAEFFGREPLTSINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
5-382 |
4.23e-155 |
|
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: 450.49 E-value: 4.23e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 5 IGIDLGTTNSCVAIMDGTTARVL-ENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQ 83
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAEVIiENSEGKRTTPSVVYFDKDGEVLVGEEAKNQALLDPENTIYSVKRLMGRDTKDKEEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 84 RDVSIMPykivaadngdawldvkgtktapPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGL 163
Cdd:cd24029 81 GGKEYTP----------------------EEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAELAGL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 164 EVKRIINEPTAAALAYGLDKEVGNRTIAVYDLGGGTFDISIIEIDevdgEKTFEVLATNGDTHLGGEDFDTRLINYLVDE 243
Cdd:cd24029 139 NVLRLINEPTAAALAYGLDKEGKDGTILVYDLGGGTFDVSILEIE----NGKFEVLATGGDNFLGGDDFDEAIAELILEK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 244 FKKDQGI-DLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPyitaDATGPKHMNIKVTRAKLESLVEDLVNRSIEPLKV 322
Cdd:cd24029 215 IGIETGIlDDKEDERARARLREAAEEAKIELSSSDSTDILIL----DDGKGGELEIEITREEFEELIAPLIERTIDLLEK 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 323 ALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVL 382
Cdd:cd24029 291 ALKDAKLSPEDIDRVLLVGGSSRIPLVREMLEEYFGREPISSVDPDEAVAKGAAIYAASL 350
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
5-382 |
1.66e-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: 393.58 E-value: 1.66e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 5 IGIDLGTTNSCVAIMDGTTaRVLENAEGDRTTPSIIAYTQDgETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQR 84
Cdd:cd24093 2 IGIDLGTTYSCVATYESSV-EIIANEQGNRVTPSFVAFTPE-ERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 85 DVSIMPYKIVAaDNGDAWLDVK---GTKTAPPQ-ISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRI 160
Cdd:cd24093 80 DMKTWPFKVID-VNGNPVIEVQylgETKTFSPQeISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 161 AGLEVKRIINEPTAAALAYGLD--KEVGNRTIAVYDLGGGTFDISIIEIdevdGEKTFEVLATNGDTHLGGEDFDTRLIN 238
Cdd:cd24093 159 AGLNVLRIINEPTAAAIAYGLGagKSEKERHVLIFDLGGGTFDVSLLHI----AGGVYTVKSTSGNTHLGGQDFDTNLLE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 239 YLVDEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADatgpKHMNIKVTRAKLESLVEDLVNRSIE 318
Cdd:cd24093 235 HFKAEFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDG----EDFESSITRARFEDLNAALFKSTLE 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2005139737 319 PLKVALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFF-GKEPRKDVNPDEAVAIGAAVQGGVL 382
Cdd:cd24093 311 PVEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
5-384 |
1.48e-126 |
|
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: 376.97 E-value: 1.48e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 5 IGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGrrfqdeeVQR 84
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVDEDGSILVGRAAKERLVTHPDRTAASFKRFMG-------TDK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 85 DVSImpykivaadngdawldvkGTKT-APPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGL 163
Cdd:cd10235 74 QYRL------------------GNHTfRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELAGL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 164 EVKRIINEPTAAALAYGLDKEVGNRTIAVYDLGGGTFDISIIEIDevdgEKTFEVLATNGDTHLGGEDFDTRLINYLVDE 243
Cdd:cd10235 136 KVERLINEPTAAALAYGLHKREDETRFLVFDLGGGTFDVSVLELF----EGVIEVHASAGDNFLGGEDFTHALADYFLKK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 244 FKKDQGIDlrnDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYitadatGPKHMNIKVTRAKLESLVEDLVNRSIEPLKVA 323
Cdd:cd10235 212 HRLDFTSL---SPSELAALRKRAEQAKRQLSSQDSAEIRLTY------RGEELEIELTREEFEELCAPLLERLRQPIERA 282
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2005139737 324 LQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLTG 384
Cdd:cd10235 283 LRDAGLKPSDIDAVILVGGATRMPLVRQLIARLFGRLPLSSLDPDEAVALGAAIQAALKAR 343
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
3-384 |
2.21e-125 |
|
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: 376.68 E-value: 2.21e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 3 KIIGIDLGTTNSCVAIMDGTTA--RVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDE 80
Cdd:cd10237 23 KIVGIDLGTTYSCVGVYHAVTGevEVIPDDDGHKSIPSVVAFTPDGGVLVGYDALAQAEHNPSNTIYDAKRFIGKTFTKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 81 EVQRDVSIMPYKIVAADNGDAWLDVKGTKT----APPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKD 156
Cdd:cd10237 103 ELEEEAKRYPFKVVNDNIGSAFFEVPLNGStlvvSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 157 AGRIAGLEVKRIINEPTAAALAYGLDKEVGNRTIAVYDLGGGTFDISIIEIDevDGekTFEVLATNGDTHLGGEDFDTRL 236
Cdd:cd10237 183 AANLAGLEVLRVINEPTAAAMAYGLHKKSDVNNVLVVDLGGGTLDVSLLNVQ--GG--MFLTRAMAGNNHLGGQDFNQRL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 237 INYLVDEFKKDQGIDLrNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPK-HMNIKVTRAKLESLVEDLVNR 315
Cdd:cd10237 259 FQYLIDRIAKKFGKTL-TDKEDIQRLRQAVEEVKLNLTNHNSASLSLPLQISLPSAFKvKFKEEITRDLFETLNEDLFQR 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2005139737 316 SIEPLKVALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLTG 384
Cdd:cd10237 338 VLEPIRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFFGKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
5-600 |
3.84e-117 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 361.86 E-value: 3.84e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 5 IGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTQDGETLVGQPAKRqavtnpqntlfAIKRLIGRRFQDEEVQR 84
Cdd:PRK01433 22 VGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIGNNKGLR-----------SIKRLFGKTLKEILNTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 85 DVSIMPYKIVAADNGDAWLDVKGTKTAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGLE 164
Cdd:PRK01433 91 ALFSLVKDYLDVNSSELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLAAKIAGFE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 165 VKRIINEPTAAALAYGLDKEVGNRTIaVYDLGGGTFDISIIEIDEvdgeKTFEVLATNGDTHLGGEDFDTRLINYLVDEF 244
Cdd:PRK01433 171 VLRLIAEPTAAAYAYGLNKNQKGCYL-VYDLGGGTFDVSILNIQE----GIFQVIATNGDNMLGGNDIDVVITQYLCNKF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 245 kkdqgiDLRNDPLAMQRLKEAAEKAKIELSSAQQtdvnlpyitadatgpkhmNIKVTRAKLESLVEDLVNRSIEPLKVAL 324
Cdd:PRK01433 246 ------DLPNSIDTLQLAKKAKETLTYKDSFNND------------------NISINKQTLEQLILPLVERTINIAQECL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 325 QDAGlsVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLTGEVKDVLLLDVTPLSLGIETM 404
Cdd:PRK01433 302 EQAG--NPNIDGVILVGGATRIPLIKDELYKAFKVDILSDIDPDKAVVWGAALQAENLIAPHTNSLLIDVVPLSLGMELY 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 405 GGVMTALINKNTTIPTKHSQVFSTAEDNQSAVTIHVIQGERKRASDNKSLGQFNLDGINPAPRGMPQIEVTFDIDADGIL 484
Cdd:PRK01433 380 GGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDADGIL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 485 HVSAKDKNSGKEQKITIKASSGLNEEEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLPADDKTA 564
Cdd:PRK01433 460 SVSAYEKISNTSHAIEVKPNHGIDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAIAELTTLLSESEISI 539
|
570 580 590
....*....|....*....|....*....|....*.
gi 2005139737 565 IESALTALETSLKGEDKADIEAKMQALAQASQKLME 600
Cdd:PRK01433 540 INSLLDNIKEAVHARDIILINNSIKEFKSKIKKSMD 575
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
5-382 |
3.79e-102 |
|
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: 315.72 E-value: 3.79e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 5 IGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTqDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQR 84
Cdd:cd10238 3 FGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFT-DNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAVQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 85 DVSIMPYKIVAADNGDAW-LDVKGTKT--APPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIA 161
Cdd:cd10238 82 LKKESKCKIIEKDGKPGYeIELEEKKKlvSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 162 GLEVKRIINEPTAAALAYGLDKEV--GNRTIAVYDLGGGTFDISIIEIdeVDGekTFEVLATNGDTHLGGEDFDTRLINY 239
Cdd:cd10238 162 GFNVLRVISEPSAAALAYGIGQDDptENSNVLVYRLGGTSLDVTVLSV--NNG--MYRVLATRTDDNLGGDDFTEALAEH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 240 LVDEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQ--QTDVNLPYITADatgpkhMNIKVTRAKLESLVEDLVNRSI 317
Cdd:cd10238 238 LASEFKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNtaTCSVESLYDGMD------FQCNVSRARFESLCSSLFQQCL 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2005139737 318 EPLKVALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFF-GKEPRKDVNPDEAVAIGAAVQGGVL 382
Cdd:cd10238 312 EPIQEVLNSAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFpSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
5-378 |
6.86e-102 |
|
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: 314.88 E-value: 6.86e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 5 IGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTqDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQR 84
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFT-EKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 85 DVSIMPYKIVAADNGDAWLDV--KGTKT--APPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRI 160
Cdd:cd11732 80 EIKLLPFKLVELEDGKVGIEVsyNGEEVvfSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 161 AGLEVKRIINEPTAAALAYGLDKEVGN------RTIAVYDLGGGTFDISIIEIdeVDGEktFEVLATNGDTHLGGEDFDT 234
Cdd:cd11732 160 AGLNCLRLINETTAAALDYGIYKSDLLeseekpRIVAFVDMGHSSTQVSIAAF--TKGK--LKVLSTAFDRNLGGRDFDR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 235 RLINYLVDEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADatgpKHMNIKVTRAKLESLVEDLVN 314
Cdd:cd11732 236 ALVEHFAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMED----IDFSGQIKREEFEELIQPLLA 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2005139737 315 RSIEPLKVALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQ 378
Cdd:cd11732 312 RLEAPIKKALAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVFGKDLSTTLNADEAVARGCALQ 375
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
4-382 |
4.51e-99 |
|
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: 308.09 E-value: 4.51e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 4 IIGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTqDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQ 83
Cdd:cd24095 3 VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFG-EKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 84 RDVSIMPYKIVAADNGDAWLDV--KGTKTA--PPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGR 159
Cdd:cd24095 82 RDLKLFPFKVTEGPDGEIGINVnyLGEQKVftPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 160 IAGLEVKRIINEPTAAALAYGLDK----EVGNRTIAVYDLGGGTFDISIIEIdeVDGEKTfeVLATNGDTHLGGEDFDTR 235
Cdd:cd24095 162 IAGLNCLRLMNETTATALAYGIYKtdlpETDPTNVVFVDVGHSSTQVCVVAF--KKGQLK--VLSHAFDRNLGGRDFDEV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 236 LINYLVDEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADatgpKHMNIKVTRAKLESLVEDLVNR 315
Cdd:cd24095 238 LFDHFAAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMED----KDVKGMITREEFEELAAPLLER 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2005139737 316 SIEPLKVALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVL 382
Cdd:cd24095 314 LLEPLEKALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFFGKEPSRTMNASECVARGCALQCAML 380
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
5-378 |
1.60e-92 |
|
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: 290.72 E-value: 1.60e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 5 IGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTQDGETLvGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQR 84
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSM-GVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 85 DVSIMPYKIVAADNGDAWLDV--KGTKT--APPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRI 160
Cdd:cd10228 80 ELKHLPYKVVKLPNGSVGIKVqyLGEEHvfTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 161 AGLEVKRIINEPTAAALAYGLDK------EVGNRTIAVYDLGGGTFDISIIEIDevdgEKTFEVLATNGDTHLGGEDFDT 234
Cdd:cd10228 160 AGLNCLRLLNDTTAVALAYGIYKqdlpaeEEKPRNVVFVDMGHSSLQVSVCAFN----KGKLKVLATAADPNLGGRDFDE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 235 RLINYLVDEFKKDQGIDLRNDPLAMQRLKEAAEKAKiELSSAQQTDV--NLPYITADatgpKHMNIKVTRAKLESLVEDL 312
Cdd:cd10228 236 LLVEHFAEEFKTKYKIDVKSKPRALLRLLTECEKLK-KLMSANATELplNIECFMDD----KDVSGKMKRAEFEELCAPL 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2005139737 313 VNRSIEPLKVALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQ 378
Cdd:cd10228 311 FARVEVPLRSALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVFGKEPSTTLNQDEAVARGCALQ 376
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
5-383 |
1.57e-85 |
|
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: 272.71 E-value: 1.57e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 5 IGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTQDGETLvGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQR 84
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYL-GEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 85 DVSIMPYKIVAAdNGDAWLDV----KGTKTAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRI 160
Cdd:cd24094 80 EEKYFTAKLVDA-NGEVGAEVnylgEKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 161 AGLEVKRIINEPTAAALAYGLDK------EVGNRTIAVYDLGGGTFDISIIEIdeVDGEktFEVLATNGDTHLGGEDFDT 234
Cdd:cd24094 159 AGLNPLRLMNDTTAAALGYGITKtdlpepEEKPRIVAFVDIGHSSYTVSIVAF--KKGQ--LTVKGTAYDRHFGGRDFDK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 235 RLINYLVDEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADatgpKHMNIKVTRAKLESLVEDLVN 314
Cdd:cd24094 235 ALTDHFADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMND----IDVSSMLKREEFEELIAPLLE 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2005139737 315 RSIEPLKVALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLT 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; ... |
4-379 |
1.44e-84 |
|
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: 268.98 E-value: 1.44e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 4 IIGIDLGTTNSCVAIM-DGTTARVLENAEGDRTTPSIIAYTqDGETLVGQPAKRQAVTNPQNTLFAIKRLIGrrFQDEEv 82
Cdd:cd10230 2 VLGIDLGSEFIKVALVkPGVPFEIVLNEESKRKTPSAVAFR-NGERLFGDDALALATRFPENTFSYLKDLLG--YSVEE- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 83 qrdvsimpykivaadngdawldvkgtktappqISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAG 162
Cdd:cd10230 78 --------------------------------LVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIAG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 163 LEVKRIINEPTAAALAYGLDKEVGN---RTIAVYDLGGGTFDISIIEIDEVDGEK--------TFEVLATNGDTHLGGED 231
Cdd:cd10230 126 LNVLSLINDNTAAALNYGIDRRFENnepQNVLFYDMGASSTSATVVEFSSVKEKDkgknktvpQVEVLGVGWDRTLGGLE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 232 FDTRLINYLVDEFKKDQGI--DLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADatgpKHMNIKVTRAKLESLV 309
Cdd:cd10230 206 FDLRLADHLADEFNEKHKKdkDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDD----IDFRTKITREEFEELC 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2005139737 310 EDLVNRSIEPLKVALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEP-RKDVNPDEAVAIGAAVQG 379
Cdd:cd10230 282 ADLFERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKElGKHLNADEAAALGAAFYA 352
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
4-378 |
3.05e-77 |
|
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: 251.01 E-value: 3.05e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 4 IIGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTQDGETlVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQ 83
Cdd:cd11737 2 VVGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRS-IGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 84 RDVSIMPYKIVAADNGDAWLDVKGTKT----APPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGR 159
Cdd:cd11737 81 AEKPSLAYELVQLPTGTTGIKVMYMEEernfTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 160 IAGLEVKRIINEPTAAALAYGLDK------EVGNRTIAVYDLGGGTFDISIIEIDevdgEKTFEVLATNGDTHLGGEDFD 233
Cdd:cd11737 161 IAGLNCLRLMNETTAVALAYGIYKqdlpapEEKPRNVVFVDMGHSAYQVSVCAFN----KGKLKVLATAFDPTLGGRKFD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 234 TRLINYLVDEFKKDQGIDLRNDPLAMQRLKEAAEKAKiELSSAQQTD--VNLPYITADATGPKHMNikvtRAKLESLVED 311
Cdd:cd11737 237 EVLVNHFCEEFGKKYKLDIKSKIRALLRLFQECEKLK-KLMSANASDlpLNIECFMNDIDVSGTMN----RGQFEEMCAD 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2005139737 312 LVNRSIEPLKVALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQ 378
Cdd:cd11737 312 LLARVEPPLRSVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFFGKEVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
4-383 |
3.57e-74 |
|
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: 242.90 E-value: 3.57e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 4 IIGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTQDGETlVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQ 83
Cdd:cd11738 2 VVGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRA-IGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 84 RDVSIMPYKIVAADNGDAWLDVKGTKTAPP----QISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGR 159
Cdd:cd11738 81 AEKIKLPYELQKMPNGSTGVKVRYLDEERVfaieQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 160 IAGLEVKRIINEPTAAALAYGLDK------EVGNRTIAVYDLGGGTFDISIIEIDevdgEKTFEVLATNGDTHLGGEDFD 233
Cdd:cd11738 161 IAGLNCLRLMNETTAVALAYGIYKqdlpalEEKPRNVVFVDMGHSAYQVSICAFN----KGKLKVLATTFDPYLGGRNFD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 234 TRLINYLVDEFKKDQGIDLRNDPLAMQRLKEAAEKAKiELSSAQQTD--VNLPYITADATGPKHMNikvtRAKLESLVED 311
Cdd:cd11738 237 EVLVDYFCEEFKTKYKLNVKENIRALLRLYQECEKLK-KLMSANASDlpLNIECFMNDIDVSSKMN----RAQFEELCAS 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2005139737 312 LVNRSIEPLKVALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLT 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 ... |
4-378 |
1.76e-71 |
|
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: 235.91 E-value: 1.76e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 4 IIGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTQDGETlVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQ 83
Cdd:cd11739 2 VVGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRT-IGVAAKNQQITNANNTVSNFKRFHGRAFNDPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 84 RDVSIMPYKIVAADNGDAWLDVKGTKT----APPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGR 159
Cdd:cd11739 81 KEKENLSYDLVPLKNGGVGVKVMYLDEehhfSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 160 IAGLEVKRIINEPTAAALAYGLDK------EVGNRTIAVYDLGGGTFDISIIEIDevdgEKTFEVLATNGDTHLGGEDFD 233
Cdd:cd11739 161 IVGLNCLRLMNDMTAVALNYGIYKqdlpapDEKPRIVVFVDMGHSAFQVSACAFN----KGKLKVLGTAFDPYLGGRNFD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 234 TRLINYLVDEFKKDQGIDLRNDPLAMQRLKEAAEKAKiELSSAQQTDV--NLPYITADATGPKHMNikvtRAKLESLVED 311
Cdd:cd11739 237 EKLVEHFCAEFKTKYKLDVKSKIRALLRLYQECEKLK-KLMSSNSTDLplNIECFMNDKDVSGKMN----RSQFEELCAD 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2005139737 312 LVNRSIEPLKVALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQ 378
Cdd:cd11739 312 LLQRIEVPLYSLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFFGKDVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
4-382 |
3.11e-69 |
|
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: 228.79 E-value: 3.11e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 4 IIGIDLGTTNSCVAIMD-GTTARVLENAEGDRTTPSIIAYTqDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRrfqdeev 82
Cdd:cd10232 2 VIGISFGNSNSSIAIINkDGRAEVIANEDGDRQIPSILAYH-GDEEYHGSQAKAQLVRNPKNTVANFRDLLGT------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 83 qrdvsimpyKIVAADNgdawldvkgtktappqISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAG 162
Cdd:cd10232 74 ---------TTLTVSE----------------VTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAAAAG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 163 LEVKRIINEPTAAALAYGLDKEVG-----NRTIAVYDLGGGTFDISIIEIDevdgEKTFEVLATNGDTHLGGEDFDTRLI 237
Cdd:cd10232 129 LEVLQLIPEPAAAALAYDLRAETSgdtikDKTVVVADLGGTRSDVTVVAVR----GGLYTILATVHDYELGGVALDDVLV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 238 NYLVDEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQ--QTDVNLPYITADATGpkhmniKVTRAKLESLVEDLVNR 315
Cdd:cd10232 205 GHFAKEFKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTsaPCSVESLADGIDFHS------SINRTRYELLASKVFQQ 278
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2005139737 316 SIEPLKVALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRK----DVNPDEAVAIGAAVQGGVL 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 |
3.80e-57 |
|
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: 196.17 E-value: 3.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 5 IGIDLGTTNSCVAIMDGTTARVLE---------NAEGDRTTPSIIaytqdgetlvgqpakrqavtnpqntlfaikrligr 75
Cdd:cd10170 1 VGIDFGTTYSGVAYALLGPGEPPLvvlqlpwpgGDGGSSKVPSVL----------------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 76 rfqdeevqrdvsimpykivaadngdawldvkgtktappQISAEVLKKMKKTAEDYLGE-------PVTEAVITVPAYFND 148
Cdd:cd10170 46 --------------------------------------EVVADFLRALLEHAKAELGDriwelekAPIEVVITVPAGWSD 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 149 AQRQATKDAGRIAGLEVK----RIINEPTAAALAYGLDKEVG-----NRTIAVYDLGGGTFDISIIEIDEVDGEKTFEVl 219
Cdd:cd10170 88 AAREALREAARAAGFGSDsdnvRLVSEPEAAALYALEDKGDLlplkpGDVVLVCDAGGGTVDLSLYEVTSGSPLLLEEV- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 220 ATNGDTHLGGEDFDTRLINYLVDEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATgPKHMNIK 299
Cdd:cd10170 167 APGGGALLGGTDIDEAFEKLLREKLGDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGL-PELGLEK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 300 VTRAKLESLVEDLVNRSIEPLKVALQDAGLSVS--DIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDV----NPDEAVAI 373
Cdd:cd10170 246 GTLLLTEEEIRDLFDPVIDKILELIEEQLEAKSgtPPDAVVLVGGFSRSPYLRERLRERFGSAGIIIVlrsdDPDTAVAR 325
|
....
gi 2005139737 374 GAAV 377
Cdd:cd10170 326 GAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
5-377 |
1.01e-47 |
|
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: 172.84 E-value: 1.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 5 IGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIAYTQDGE-----TLVGQPAKRQAVTNPQNTLF--AIKRLIGRRF 77
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREEegaesIYFGNDAIDAYLNDPEEGRLikSVKSFLGSSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 78 QDEEVqrdvsimpykivaadngdawldVKGTKTAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQAT--- 154
Cdd:cd10231 81 FDETT----------------------IFGRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDDaqa 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 155 ----KDAGRIAGLEVKRIINEPTAAALAY--GLDKEvgnRTIAVYDLGGGTFDISIIEIDEVDGEKTFEVLATNGDtHLG 228
Cdd:cd10231 139 esrlRDAARRAGFRNVEFQYEPIAAALDYeqRLDRE---ELVLVVDFGGGTSDFSVLRLGPNRTDRRADILATSGV-GIG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 229 GEDFDTRLINYLV-----------------------------------------------------DEFKKDQGIDLRND 255
Cdd:cd10231 215 GDDFDRELALKKVmphlgrgstyvsgdkglpvpawlyadlsnwhaisllytkktlrllldlrrdaaDPEKIERLLSLVED 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 256 PLAmQRLKEAAEKAKIELSSAQQTDVNLPYItadatgPKHMNIKVTRAKLESLVEDLVNRSIEPLKVALQDAGLSVSDIQ 335
Cdd:cd10231 295 QLG-HRLFRAVEQAKIALSSADEATLSFDFI------EISIKVTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVD 367
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2005139737 336 DVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAV 377
Cdd:cd10231 368 RVFLTGGSSQSPAVRQALASLFGQARLVEGDEFGSVAAGLAL 409
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
4-384 |
3.36e-25 |
|
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: 107.75 E-value: 3.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 4 IIGIDLGTTNSCVAIM---DGTTARVLENAEGD------RTTPSIIAYTQDGEtLV--GQPAKRQAVTNPQNtlfaikrl 72
Cdd:cd10229 2 VVAIDFGTTYSGYAYSfitDPGDIHTMYNWWGAptgvssPKTPTCLLLNPDGE-FHsfGYEAREKYSDLAED-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 73 iGRRFQDEEVQRDVSIMPYKIVAADngDAWLDVKGTKTAPPQISAEVLKKMKKTAEDYL----GEPVTEA----VITVPA 144
Cdd:cd10229 73 -EEHQWLYFFKFKMMLLSEKELTRD--TKVKAVNGKSMPALEVFAEALRYLKDHALKELrdrsGSSLDEDdirwVLTVPA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 145 YFNDAQRQATKDAGRIAGLEVK------RIINEPTAAALAYGLDKEVGNRTIA-------VYDLGGGTFDISIIEIDEVD 211
Cdd:cd10229 150 IWSDAAKQFMREAAVKAGLISEenseqlIIALEPEAAALYCQKLLAEGEEKELkpgdkylVVDCGGGTVDITVHEVLEDG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 212 GEKtfEVLATNGDtHLGGEDFDTRLINYLVDEFKKD--QGIdLRNDPLAMQRLKEAAEKAKielssaqqtdvnlpyitad 289
Cdd:cd10229 230 KLE--ELLKASGG-PWGSTSVDEEFEELLEEIFGDDfmEAF-KQKYPSDYLDLLQAFERKK------------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 290 atgpKHMNIKVTRAKLESLVEDLVNRSIEPLKVALQdaGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDE 369
Cdd:cd10229 287 ----RSFKLRLSPELMKSLFDPVVKKIIEHIKELLE--KPELKGVDYIFLVGGFAESPYLQKAVKEAFSTKVKIIIPPEP 360
|
410
....*....|....*
gi 2005139737 370 AVAIgaaVQGGVLTG 384
Cdd:cd10229 361 GLAV---VKGAVLFG 372
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
5-355 |
4.71e-18 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 87.22 E-value: 4.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 5 IGIDLGTTNSCVAIMDGTTARVLENAEGDRTTPSIIaYTQDGETLVGQPAKRQAVTNP----QNTLfaiKRLI-GRRFQD 79
Cdd:PRK11678 3 IGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTL-CAPTREAVSEWLYRHLDVPAYdderQALL---RRAIrYNREED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 80 EEVQRDvSIMpykiVAADNGDAWLD-------VKGTKT-------APPQIS------AEVLKKMKKTAEDYLGEPVTEAV 139
Cdd:PRK11678 79 IDVTAQ-SVF----FGLAALAQYLEdpeevyfVKSPKSflgasglKPQQVAlfedlvCAMMLHIKQQAEAQLQAAITQAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 140 ITVPAYFN-----DAQRQA----TKDAGRiAGLEVKRIINEPTAAalayGLDKEVG---NRTIAVYDLGGGTFDISIIE- 206
Cdd:PRK11678 154 IGRPVNFQglggeEANRQAegilERAAKR-AGFKDVEFQFEPVAA----GLDFEATlteEKRVLVVDIGGGTTDCSMLLm 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 207 ----IDEVDGEKTFevLATNGdTHLGGEDFDTRLINY-------LVDEFKKdqGI------------------------- 250
Cdd:PRK11678 229 gpswRGRADRSASL--LGHSG-QRIGGNDLDIALAFKqlmpllgMGSETEK--GIalpslpfwnavaindvpaqsdfysl 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 251 -------DLRND---PLAMQRLKE------------AAEKAKIELSSAQQTDVNLPYITADATgpkhmnIKVTRAKLESL 308
Cdd:PRK11678 304 angrllnDLIRDarePEKVARLLKvwrqrlsyrlvrSAEEAKIALSDQAETRASLDFISDGLA------TEISQQGLEEA 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2005139737 309 VEDLVNRSIEPLKVALQDAGLSvsdiQDVI-LVGGQTRMPMVQKKVAE 355
Cdd:PRK11678 378 ISQPLARILELVQLALDQAQVK----PDVIyLTGGSARSPLIRAALAQ 421
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
1-376 |
9.20e-12 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 66.70 E-value: 9.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 1 MGKIIGIDLGTTNSCVAIMD-GTtarVLENaegdrttPSIIAY-TQDGETL-VGQPAKRqavtnpqntlfaikrLIGRrf 77
Cdd:PRK13930 7 FSKDIGIDLGTANTLVYVKGkGI---VLNE-------PSVVAIdTKTGKVLaVGEEAKE---------------MLGR-- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 78 qdeevqrdvsiMPYKIVA---------ADngdawldvkgtktapPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFND 148
Cdd:PRK13930 60 -----------TPGNIEAirplkdgviAD---------------FEATEAMLRYFIKKARGRRFFRKPRIVICVPSGITE 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 149 AQRQATKDAGRIAGLEVKRIINEPTAAALAYGLD--KEVGNrtiAVYDLGGGTFDISIIEIDEVDGEKTFEVlatngdth 226
Cdd:PRK13930 114 VERRAVREAAEHAGAREVYLIEEPMAAAIGAGLPvtEPVGN---MVVDIGGGTTEVAVISLGGIVYSESIRV-------- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 227 lGGEDFDTRLINYLVDEFKKDQGIDlrndplamqrlkeAAEKAKIELSSAQQTDVNLpyiTADATG-------PKhmNIK 299
Cdd:PRK13930 183 -AGDEMDEAIVQYVRRKYNLLIGER-------------TAEEIKIEIGSAYPLDEEE---SMEVRGrdlvtglPK--TIE 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 300 VTRAKLESLVEDLVNRSIEPLKVALQD--AGLSvSDIQD--VILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGA 375
Cdd:PRK13930 244 ISSEEVREALAEPLQQIVEAVKSVLEKtpPELA-ADIIDrgIVLTGGGALLRGLDKLLSEETGLPVHIAEDPLTCVARGT 322
|
.
gi 2005139737 376 A 376
Cdd:PRK13930 323 G 323
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
117-399 |
1.66e-11 |
|
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: 65.39 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 117 AEVLKKMKKTAEDYLGEPVTEAVITVP----AYFNDAQRqatkdagriAGLEVKRIINEPTAAALAYGLDKEVgNRTIAV 192
Cdd:cd24004 49 AESIKELLKELEEKLGSKLKDVVIAIAkvveSLLNVLEK---------AGLEPVGLTLEPFAAANLLIPYDMR-DLNIAL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 193 YDLGGGTFDISIIEIDEVDGEKTFevlatngdtHLGGEDFDTRLInylvDEFKkdqgIDLrndplamqrlkEAAEKAKIE 272
Cdd:cd24004 119 VDIGAGTTDIALIRNGGIEAYRMV---------PLGGDDFTKAIA----EGFL----ISF-----------EEAEKIKRT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 273 LSSAqqtDVNLPYITADATGPKHMNIKVTRAKLESLVEDLVNRSIEPLKVALQdaglsvsdIQDVILVGGQTRMPMVQKK 352
Cdd:cd24004 171 YGIF---LLIEAKDQLGFTINKKEVYDIIKPVLEELASGIANAIEEYNGKFKL--------PDAVYLVGGGSKLPGLNEA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2005139737 353 VAEFFGkeprKDVNPDEAVAIGAAVQGGVLTGEVKDVLLldVTPLSL 399
Cdd:cd24004 240 LAEKLG----LPVERIAPRNIGAISDITDETSKAKGPEF--VTPLGI 280
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
5-377 |
2.62e-11 |
|
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: 65.19 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 5 IGIDLGTTNSCVAImdgttarvlenaEGDRTT---PSIIAY-TQDGETL-VGQPAKRqavtnpqntlfaikrLIGRrfqd 79
Cdd:cd10225 2 IGIDLGTANTLVYV------------KGKGIVlnePSVVAVdKNTGKVLaVGEEAKK---------------MLGR---- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 80 eeVQRDVSIM-PYKI-VAADngdawldvkgtktapPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDA 157
Cdd:cd10225 51 --TPGNIVAIrPLRDgVIAD---------------FEATEAMLRYFIRKAHRRRGFLRPRVVIGVPSGITEVERRAVKEA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 158 GRIAGL-EVkRIINEPTAAALAYGLDKE--VGNrtiAVYDLGGGTFDISIIEIDEVDGEKTFEVlatngdthlGGEDFDT 234
Cdd:cd10225 114 AEHAGArEV-YLIEEPMAAAIGAGLPIEepRGS---MVVDIGGGTTEIAVISLGGIVTSRSVRV---------AGDEMDE 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 235 RLINYLVDEFKKDQGIdlrndplamqrlkEAAEKAKIELSSAQQTDVNLPYITA--D-ATG-PKhmNIKVTRAKLESLVE 310
Cdd:cd10225 181 AIINYVRRKYNLLIGE-------------RTAERIKIEIGSAYPLDEELSMEVRgrDlVTGlPR--TIEITSEEVREALE 245
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 311 DLVNRSIEPLKVALQDAGLS-VSDIQD--VILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAV 377
Cdd:cd10225 246 EPVNAIVEAVRSTLERTPPElAADIVDrgIVLTGGGALLRGLDELLREETGLPVHVADDPLTCVAKGAGK 315
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
1-376 |
2.12e-10 |
|
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: 62.40 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 1 MGKIIGIDLGTTNSCVAI-MDGTtarVLEnaEgdrttPSIIAYTQDGETL--VGQPAKRqavtnpqntlfaikrLIGRrf 77
Cdd:COG1077 6 FSKDIGIDLGTANTLVYVkGKGI---VLN--E-----PSVVAIDKKTGKVlaVGEEAKE---------------MLGR-- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 78 qdeevqrdvsiMPYKIVA---------ADngdawldvkgtktapPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFND 148
Cdd:COG1077 59 -----------TPGNIVAirplkdgviAD---------------FEVTEAMLKYFIKKVHGRRSFFRPRVVICVPSGITE 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 149 AQRQATKDAGRIAGL-EVkRIINEPTAAALAYGLD--KEVGNrtiAVYDLGGGTFDISIIEIDEVdgektfeVLATNgdT 225
Cdd:COG1077 113 VERRAVRDAAEQAGArEV-YLIEEPMAAAIGAGLPieEPTGN---MVVDIGGGTTEVAVISLGGI-------VVSRS--I 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 226 HLGGEDFDTRLINYLvdefKKDQG--IDLRndplamqrlkeAAEKAKIELSSAQQTDVNLpyiTADATG-------PKhm 296
Cdd:COG1077 180 RVAGDELDEAIIQYV----RKKYNllIGER-----------TAEEIKIEIGSAYPLEEEL---TMEVRGrdlvtglPK-- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 297 NIKVTRAKLESLVEDLVNRSIEPLKVALQD--AGLSvSDIQD--VILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVA 372
Cdd:COG1077 240 TITITSEEIREALEEPLNAIVEAIKSVLEKtpPELA-ADIVDrgIVLTGGGALLRGLDKLLSEETGLPVHVAEDPLTCVA 318
|
....
gi 2005139737 373 IGAA 376
Cdd:COG1077 319 RGTG 322
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
117-227 |
1.04e-09 |
|
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: 59.20 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 117 AEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGLEVKRIINEPTAAALAYGLdkevgnRTIAVYDLG 196
Cdd:cd24047 46 IRIVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGI------RDGAVVDIG 119
|
90 100 110
....*....|....*....|....*....|.
gi 2005139737 197 GGTFDISIIEidevDGEKTFEVLATNGDTHL 227
Cdd:cd24047 120 GGTTGIAVLK----DGKVVYTADEPTGGTHL 146
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
116-227 |
4.47e-09 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 57.92 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 116 SAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGLEVKRIINEPTAAALAYGLDKEvgnrtiAVYDL 195
Cdd:PRK15080 69 AVTIVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGIDNG------AVVDI 142
|
90 100 110
....*....|....*....|....*....|..
gi 2005139737 196 GGGTFDISIIEidevDGEKTFEVLATNGDTHL 227
Cdd:PRK15080 143 GGGTTGISILK----DGKVVYSADEPTGGTHM 170
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
138-375 |
6.57e-09 |
|
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: 57.95 E-value: 6.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 138 AVITVPAYFNDAQRQATKDAGRIAGLEVKRIINEPTAAALAYGLDKE--VGNrtiAVYDLGGGTFDISIIEIDEVDGEKT 215
Cdd:pfam06723 96 VVICVPSGITEVERRAVKEAAKNAGAREVFLIEEPMAAAIGAGLPVEepTGN---MVVDIGGGTTEVAVISLGGIVTSKS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 216 FEVlatngdthlGGEDFDTRLINYLVDEFKKDQGIdlrndplamqrlkEAAEKAKIELSSAQQTDVNLpyiTADATG--- 292
Cdd:pfam06723 173 VRV---------AGDEFDEAIIKYIRKKYNLLIGE-------------RTAERIKIEIGSAYPTEEEE---KMEIRGrdl 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 293 ----PKhmNIKVTRAKLESLVEDLVNRSIEPLKVALQD--AGLSvSDIQD--VILVGGQTRMPMVQKKVAEFFGKEPRKD 364
Cdd:pfam06723 228 vtglPK--TIEISSEEVREALKEPVSAIVEAVKEVLEKtpPELA-ADIVDrgIVLTGGGALLRGLDKLLSDETGLPVHIA 304
|
250
....*....|.
gi 2005139737 365 VNPDEAVAIGA 375
Cdd:pfam06723 305 EDPLTCVALGT 315
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
5-374 |
6.40e-08 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 54.91 E-value: 6.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 5 IGIDLGTTNscvaimdgttarvlenaegdrttpsIIAYTQDGETLVGQPAKrQAVTNPQNTLFAI----KRLIGRrfqde 80
Cdd:PRK13929 7 IGIDLGTAN-------------------------ILVYSKNKGIILNEPSV-VAVDTETKAVLAIgteaKNMIGK----- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 81 evqrdvsiMPYKIVAADngdawlDVKGTKTAPPQISAEVLKKMKKTAEDYLGEPVTE--AVITVPAYFNDAQRQATKDAG 158
Cdd:PRK13929 56 --------TPGKIVAVR------PMKDGVIADYDMTTDLLKQIMKKAGKNIGMTFRKpnVVVCTPSGSTAVERRAISDAV 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 159 RIAGLEVKRIINEPTAAALAYGL--DKEVGNrtiAVYDLGGGTFDISIIeidevdgekTFEVLATNGDTHLGGEDFDTRL 236
Cdd:PRK13929 122 KNCGAKNVHLIEEPVAAAIGADLpvDEPVAN---VVVDIGGGTTEVAII---------SFGGVVSCHSIRIGGDQLDEDI 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 237 INYLVDEFKKDQGidlrndplamqrlKEAAEKAKIELSSA--QQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDLVN 314
Cdd:PRK13929 190 VSFVRKKYNLLIG-------------ERTAEQVKMEIGYAliEHEPETMEVRGRDLVTGLPKTITLESKEIQGAMRESLL 256
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2005139737 315 RSIEPLKVALQDAGLSVS-DIQD--VILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIG 374
Cdd:PRK13929 257 HILEAIRATLEDCPPELSgDIVDrgVILTGGGALLNGIKEWLSEEIVVPVHVAANPLESVAIG 319
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
139-342 |
1.82e-06 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 50.29 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 139 VITVPAYFNDAQRQATKDAGRIAGLEVKRIINEPTAAALAYGLD--KEVGNrtiAVYDLGGGTFDISIIEIDEVDGEKTF 216
Cdd:PRK13928 99 MICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLDisQPSGN---MVVDIGGGTTDIAVLSLGGIVTSSSI 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 217 EVlatngdthlGGEDFDTRLINYLVDEFKKDQGidlrndplamqrlKEAAEKAKIELSSAQQTDVNLpyiTADATG---- 292
Cdd:PRK13928 176 KV---------AGDKFDEAIIRYIRKKYKLLIG-------------ERTAEEIKIKIGTAFPGAREE---EMEIRGrdlv 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2005139737 293 ---PKhmNIKVTRAKLESLVEDLVNRSIEPLKVALQDAG--LSvSDIQD--VILVGG 342
Cdd:PRK13928 231 tglPK--TITVTSEEIREALKEPVSAIVQAVKSVLERTPpeLS-ADIIDrgIIMTGG 284
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
120-384 |
9.39e-06 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar proteins; HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. HSPA12B belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12B.
Pssm-ID: 466842 [Multi-domain] Cd Length: 361 Bit Score: 48.42 E-value: 9.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 120 LKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGL------EVKRIINEPTAAAL-AYGLDKEVgnrtiaV 192
Cdd:cd11736 125 LQELKDQSPSLPEKDAVRWVLTVPAIWKQPAKQFMREAAYLAGLvspenpEQLLIALEPEAASIyCRKLDRYI------V 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 193 YDLGGGTFDISIIEIDEVDGEKTFEVLATNGDTHLGGED--FDTRLINY----LVDEFKKDQGIDLRNDPLAMQRLKEAa 266
Cdd:cd11736 199 ADCGGGTVDLTVHQIEQPQGTLKELYKASGGPYGAVGVDlaFEKLLCQIfgedFIATFKAKRPAAWVDLTIAFEARKRT- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 267 ekAKIELSSAQQTDVNLPYITADAtgpKHmnikvtrakleslVEDLVNRSieplkvalqdaglSVSDIQDVILVGGQTRM 346
Cdd:cd11736 278 --AALRMSSEAMNELFQPTISQII---QH-------------IDDLMKKP-------------EVKGIKFLFLVGGFAES 326
|
250 260 270
....*....|....*....|....*....|....*...
gi 2005139737 347 PMVQKKVAEFFGKEPRKDVNPDEAVAIgaaVQGGVLTG 384
Cdd:cd11736 327 PMLQRAVQAAFGNICRVIIPQDVGLTI---LKGAVLFG 361
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
138-199 |
1.54e-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: 42.07 E-value: 1.54e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2005139737 138 AVITVPAYFNDAQRQAT-----------KDAGRIAGLEVKRIINEPTAAALAYGLDKevGNRTIAVYDLGGGT 199
Cdd:cd00012 16 IVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGALLTL--GPEGLLVVDLGGGT 86
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
5-375 |
1.07e-03 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 41.61 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 5 IGIDLGTTNSCVaIMDGTTARVLEnaegdrttPSIIAYTQDGETL--VGQPAKRqavtnpqntlfaikrLIGRrfqdeev 82
Cdd:PRK13927 8 LGIDLGTANTLV-YVKGKGIVLNE--------PSVVAIRTDTKKVlaVGEEAKQ---------------MLGR------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 83 qrdvsiMPYKIVA---------ADngdawldvkgtktappqisAEVLKKM-----KKTAEDYLGEPvtEAVITVPAYFND 148
Cdd:PRK13927 57 ------TPGNIVAirpmkdgviAD-------------------FDVTEKMlkyfiKKVHKNFRPSP--RVVICVPSGITE 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 149 AQRQATKDAGRIAGL-EVkRIINEPTAAALAYGLDKE--VGNrtiAVYDLGGGTFDISIIEIDevdGektfevLATNGDT 225
Cdd:PRK13927 110 VERRAVRESALGAGArEV-YLIEEPMAAAIGAGLPVTepTGS---MVVDIGGGTTEVAVISLG---G------IVYSKSV 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 226 HLGGEDFDTRLINYLvdefKKDQGIdlrndpLAMQRlkeAAEKAKIELSSAQQTDVNLPYIT--AD-ATG-PKHMNIKvT 301
Cdd:PRK13927 177 RVGGDKFDEAIINYV----RRNYNL------LIGER---TAERIKIEIGSAYPGDEVLEMEVrgRDlVTGlPKTITIS-S 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 302 RAKLESLVEdLVNRSIEPLKVALQDAG--LSvSDIQD--VILVGG-------------QTRMPMVqkkVAEffgkeprkd 364
Cdd:PRK13927 243 NEIREALQE-PLSAIVEAVKVALEQTPpeLA-ADIVDrgIVLTGGgallrgldkllseETGLPVH---VAE--------- 308
|
410
....*....|.
gi 2005139737 365 vNPDEAVAIGA 375
Cdd:PRK13927 309 -DPLTCVARGT 318
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
290-389 |
1.13e-03 |
|
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: 41.74 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 290 ATGPKHMnikvTRAKLESLVEDLvNRSIEplkvALQDAGLsvsDIQDVILVGGQTRMPMVQKKVAEFFGKEPRKdVNPDE 369
Cdd:COG1070 364 SHTRAHL----ARAVLEGVAFAL-RDGLE----ALEEAGV---KIDRIRATGGGARSPLWRQILADVLGRPVEV-PEAEE 430
|
90 100
....*....|....*....|
gi 2005139737 370 AVAIGAAVQGGVLTGEVKDV 389
Cdd:COG1070 431 GGALGAALLAAVGLGLYDDL 450
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
161-388 |
1.84e-03 |
|
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: 40.98 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 161 AGLEVKRIINEPTAAALA--YGLDKEVGnrtIAVYDLGGGTFDISIIEIDEVDGEKTFEVlatngdthlGGEDFDtrlin 238
Cdd:cd24048 172 AGLEVDDIVLSPLASAEAvlTEDEKELG---VALIDIGGGTTDIAVFKNGSLRYTAVIPV---------GGNHIT----- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 239 ylvdefkkdqgidlrNDpLAMqRLK---EAAEKAKIELSSAQQTDV---NLPYITADATGPkhmNIKVTRAKLESLVEDL 312
Cdd:cd24048 235 ---------------ND-IAI-GLNtpfEEAERLKIKYGSALSEEAdedEIIEIPGVGGRE---PREVSRRELAEIIEAR 294
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2005139737 313 VNRSIEPLKVALQDAGLSVSDIQDVILVGGQTRMPMVQKKVAEFFGKeprkdvnpdeAVAIGAAVQGGVLTGEVKD 388
Cdd:cd24048 295 VEEILELVKKELKESGYEDLLPGGIVLTGGGSQLPGLVELAEEVFGM----------PVRIGRPKNIGGLPEEVND 360
|
|
| PRK06975 |
PRK06975 |
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed |
522-599 |
3.16e-03 |
|
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
Pssm-ID: 235899 [Multi-domain] Cd Length: 656 Bit Score: 40.47 E-value: 3.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2005139737 522 NAEADRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLpaddkTAIESALTALETSLkgedkADIEAKMQALAQASQKLM 599
Cdd:PRK06975 345 NRKVDRLDQELVQRQQANDAQTAELRVKTEQAQASV-----HQLDSQFAQLDGKL-----ADAQSAQQALEQQYQDLS 412
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
3-87 |
5.63e-03 |
|
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: 39.51 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 3 KIIGIDLGTTNSCVAIMDGTTARVLENAEgdRTTPSIIAYTQDGEtlvgqpakrqAVTNPQNTLFAIKRLIGRrfQDEEV 82
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLESGRILESVS--RPTPAPISSDDPGR----------SEQDPEKILEAVRNLIDE--LPREY 66
|
....*
gi 2005139737 83 QRDVS 87
Cdd:cd07777 67 LSDVT 71
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
161-377 |
6.54e-03 |
|
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.
Pssm-ID: 466899 [Multi-domain] Cd Length: 339 Bit Score: 39.18 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 161 AGLEVKRIINEPTAAALAYGLDK-EVGNRTIAVYDLGGGTFDISIIEIDEVDGEKTFEVlatngdthlGGEDFDTRLINY 239
Cdd:cd24049 148 AGLKPVAIDVESFALARALEYLLpDEEEETVALLDIGASSTTLVIVKNGKLLFTRSIPV---------GGNDITEAIAKA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 240 LvdefkkdqGIDLrndplamqrlkEAAEKAKIELSSAQQTDVNLPYITADATgpkhmnikvtRAKLESLVEDlVNRSIEP 319
Cdd:cd24049 219 L--------GLSF-----------EEAEELKREYGLLLEGEEGELKKVAEAL----------RPVLERLVSE-IRRSLDY 268
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2005139737 320 LKVALQDaglsvSDIQDVILVGGQTRMPMVQKKVAEFFGKE-----PRKDVNPDE-------------AVAIGAAV 377
Cdd:cd24049 269 YRSQNGG-----EPIDKIYLTGGGSLLPGLDEYLSERLGIPveilnPFSNIESKKsddeelkedaplfAVAIGLAL 339
|
|
| FtsA |
pfam14450 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
191-374 |
6.73e-03 |
|
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains. The FtsA protein contains two structurally related actin-like ATPase domains which are also structurally related to the ATPase domains of HSP70 (see PF00012). FtsA has a SHS2 domain PF02491 inserted in to the RnaseH fold PF02491.
Pssm-ID: 464177 [Multi-domain] Cd Length: 167 Bit Score: 37.70 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 191 AVYDLGGGTFDISIIEideVDGEKTFEVLATNGDthlggedfdtrlinylvdefkkdqgiDLRNDplAMQRLK---EAAE 267
Cdd:pfam14450 1 ALIDIGGGTTDIAVFE---DGALRHTRVIPVGGN--------------------------GITKD--IAIGLRtavEEAE 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2005139737 268 KAKIELSSAQQTDVNLPYITADATGPKHMN-----IKVTRAKLESLVEdLVNRSIEPLKVALQDAGLSVSDIQDVILVGG 342
Cdd:pfam14450 50 RLKIKYGSALASLADEDEVPGVGGREPREIsrkelAEIIEARVEEILE-LVRAELEDREVLPGEYVRLEVDVHGIVLTGG 128
|
170 180 190
....*....|....*....|....*....|....*....
gi 2005139737 343 QTRMPMVQKKVAEFFGKEPRKDV-------NPDEAVAIG 374
Cdd:pfam14450 129 GSALPGLVELAERALGLPVRIGSpdgiggrNPAYATALG 167
|
|
| |
