|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
43-648 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 918.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 43 IGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDTERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDPDVQRD 122
Cdd:PTZ00009 7 IGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDSVVQSD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 123 IKFLPYKVVNK-DGKPYIQVKVKGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGAIA 201
Cdd:PTZ00009 87 MKHWPFKVTTGgDDKPMIEVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAGTIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 202 GLNVVRIINEPTGAAIAYGLDKKG-GESNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDYFIKLV 280
Cdd:PTZ00009 167 GLNVLRIINEPTAAAIAYGLDKKGdGEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEFCVQDF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 281 KKKYN-KDISKDHKALGKLRRECELAKRSLSNQHQVRVEIESLFDGVDFSEPLTRARFEELNMDLFKKTMEPVKKALKDA 359
Cdd:PTZ00009 247 KRKNRgKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPVEKVLKDA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 360 GLKKSDIDEIVLVGGSTRIPKVQQMLKDFFDGKEPSKGTNPDEAVAYGAAVQGGVLSGEGGEETQNILLLDVAPLSLGIE 439
Cdd:PTZ00009 327 GMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGEQSSQVQDLLLLDVTPLSLGLE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 440 TVGGVMTNIIPRNTVIPTKKSQVFTTYQDQQTTVTINVYEGERSMTKDNRELGKFDLTGILPAPRGVPQIEVTFEVDANG 519
Cdd:PTZ00009 407 TAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTFDIDANG 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 520 ILQVKAEDKVAKTSQSITITNDKGRLTEEEIEEMIREAEEFAEEDKIMKEKIDARNKLETYVYNMKSTVADkEKLAKKIS 599
Cdd:PTZ00009 487 ILNVSAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQD-EKVKGKLS 565
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 334182408 600 DEDKEKMEGVLKEALEWLEENVNAEKEDYDEKLKEVELVCDPVIKSVYE 648
Cdd:PTZ00009 566 DSDKATIEKAIDEALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMYQ 614
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
42-648 |
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: 892.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 42 VIGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDTERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDPDVQR 121
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 122 DIKFLPYKVVNKD-GKPYIQVKVKGEekLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGAI 200
Cdd:pfam00012 81 DIKHLPYKVVKLPnGDAGVEVRYLGE--TFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 201 AGLNVVRIINEPTGAAIAYGLDKKGGESNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDYFIKLV 280
Cdd:pfam00012 159 AGLNVLRIVNEPTAAALAYGLDKTDKERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEEF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 281 KKKYNKDISKDHKALGKLRRECELAKRSLS-NQHQVRVEIESLF-DGVDFSEPLTRARFEELNMDLFKKTMEPVKKALKD 358
Cdd:pfam00012 239 KKKYGIDLSKDKRALQRLREAAEKAKIELSsNQTNINLPFITAMaDGKDVSGTLTRAKFEELVADLFERTLEPVEKALKD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 359 AGLKKSDIDEIVLVGGSTRIPKVQQMLKDFFdGKEPSKGTNPDEAVAYGAAVQGGVLSGEggEETQNILLLDVAPLSLGI 438
Cdd:pfam00012 319 AGLSKSEIDEVVLVGGSTRIPAVQELVKEFF-GKEPSKGVNPDEAVAIGAAVQAGVLSGT--FDVKDFLLLDVTPLSLGI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 439 ETVGGVMTNIIPRNTVIPTKKSQVFTTYQDQQTTVTINVYEGERSMTKDNRELGKFDLTGILPAPRGVPQIEVTFEVDAN 518
Cdd:pfam00012 396 ETLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDAN 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 519 GILQVKAEDKVAKTSQSITITNDKGrLTEEEIEEMIREAEEFAEEDKIMKEKIDARNKLETYVYNMKSTVADKeklAKKI 598
Cdd:pfam00012 476 GILTVSAKDKGTGKEQEITIEASEG-LSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEE---GDKV 551
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 334182408 599 SDEDKEKmegvLKEALEWLEENV-NAEKEDYDEKLKEVELVCDPVIKSVYE 648
Cdd:pfam00012 552 PEAEKSK----VESAIEWLKDELeGDDKEEIEAKTEELAQVSQKIGERMYQ 598
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
40-415 |
0e+00 |
|
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; This subfamily includes human BiP (also known as HSP70 family protein 5 /HSPA5; 70-kDa heat shock protein 5; glucose-regulated protein 78/GRP78; immunoglobulin heavy chain-binding protein), Sacchaormyces cerevisiae BiP (also known as Grp78p), Arabidopsis thaliana BiP1-3 (also known as luminal-binding protein 1-3) and related proteins. BiP plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. It plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). BiP may function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. It appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. BiP may also play a role in apoptosis and cell proliferation. Plant BiP may be required for pollen development and pollen tube growth. This subfamily belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466837 [Multi-domain] Cd Length: 376 Bit Score: 841.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 40 GTVIGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDTERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDPDV 119
Cdd:cd10241 1 GTVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 120 QRDIKFLPYKVVNKDGKPYIQVKVKGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGA 199
Cdd:cd10241 81 QKDIKLLPFKIVNKNGKPYIQVEVKGEKKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 200 IAGLNVVRIINEPTGAAIAYGLDKKGGESNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDYFIKL 279
Cdd:cd10241 161 IAGLNVLRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFIKL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 280 VKKKYNKDISKDHKALGKLRRECELAKRSLSNQHQVRVEIESLFDGVDFSEPLTRARFEELNMDLFKKTMEPVKKALKDA 359
Cdd:cd10241 241 FKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGEDFSETLTRAKFEELNMDLFRKTLKPVQKVLEDA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 334182408 360 GLKKSDIDEIVLVGGSTRIPKVQQMLKDFFDGKEPSKGTNPDEAVAYGAAVQGGVL 415
Cdd:cd10241 321 GLKKSDIDEIVLVGGSTRIPKVQQLLKDFFNGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
40-649 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 822.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 40 GTVIGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDT-ERLIGEAAKNQAAKNPERTIFDPKRLIGRKfdDPD 118
Cdd:PRK00290 2 GKIIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRLMGRR--DEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 119 VQRDIKFLPYKVVNKDGKPYIqVKVKGeeKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAG 198
Cdd:PRK00290 80 VQKDIKLVPYKIVKADNGDAW-VEIDG--KKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 199 AIAGLNVVRIINEPTGAAIAYGLDKKGGEsNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDYFIK 278
Cdd:PRK00290 157 KIAGLEVLRIINEPTAAALAYGLDKKGDE-KILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLAD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 279 LVKKKYNKDISKDHKALGKLRRECELAKRSLSNQHQVrvEIESLFDGVDFSEP------LTRARFEELNMDLFKKTMEPV 352
Cdd:PRK00290 236 EFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQT--EINLPFITADASGPkhleikLTRAKFEELTEDLVERTIEPC 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 353 KKALKDAGLKKSDIDEIVLVGGSTRIPKVQQMLKDFFdGKEPSKGTNPDEAVAYGAAVQGGVLSGEggeeTQNILLLDVA 432
Cdd:PRK00290 314 KQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLAGD----VKDVLLLDVT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 433 PLSLGIETVGGVMTNIIPRNTVIPTKKSQVFTTYQDQQTTVTINVYEGERSMTKDNRELGKFDLTGILPAPRGVPQIEVT 512
Cdd:PRK00290 389 PLSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 513 FEVDANGILQVKAEDKVAKTSQSITITNDKGrLTEEEIEEMIREAEEFAEEDKIMKEKIDARNKLETYVYNMKSTVADke 592
Cdd:PRK00290 469 FDIDANGIVHVSAKDKGTGKEQSITITASSG-LSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKE-- 545
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 334182408 593 kLAKKISDEDKEKMEGVLKEALEWLEENvnaEKEDYDEKLKEVELVCDPVIKSVYEK 649
Cdd:PRK00290 546 -LGDKVPADEKEKIEAAIKELKEALKGE---DKEAIKAKTEELTQASQKLGEAMYQQ 598
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
42-635 |
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: 763.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 42 VIGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDT-ERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDpdVQ 120
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNgERLVGQPAKRQAVTNPENTIYSIKRFMGRRFDE--VT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 121 RDIKFLPYKVVNKDGkpyiQVKVKGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGAI 200
Cdd:TIGR02350 80 EEAKRVPYKVVGDGG----DVRVKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 201 AGLNVVRIINEPTGAAIAYGLDKKGGESNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDYFIKLV 280
Cdd:TIGR02350 156 AGLEVLRIINEPTAAALAYGLDKSKKDEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADEF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 281 KKKYNKDISKDHKALGKLRRECELAKRSLSNQHQvrVEIESLFDGVDFSEP------LTRARFEELNMDLFKKTMEPVKK 354
Cdd:TIGR02350 236 KKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLS--TEINLPFITADASGPkhlemtLTRAKFEELTADLVERTKEPVRQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 355 ALKDAGLKKSDIDEIVLVGGSTRIPKVQQMLKDFFdGKEPSKGTNPDEAVAYGAAVQGGVLSGeggeETQNILLLDVAPL 434
Cdd:TIGR02350 314 ALKDAGLSASDIDEVILVGGSTRIPAVQELVKDFF-GKEPNKSVNPDEVVAIGAAIQGGVLKG----DVKDVLLLDVTPL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 435 SLGIETVGGVMTNIIPRNTVIPTKKSQVFTTYQDQQTTVTINVYEGERSMTKDNRELGKFDLTGILPAPRGVPQIEVTFE 514
Cdd:TIGR02350 389 SLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFD 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 515 VDANGILQVKAEDKVAKTSQSITITNDKGrLTEEEIEEMIREAEEFAEEDKIMKEKIDARNKLETYVYNMKSTVADkekL 594
Cdd:TIGR02350 469 IDANGILHVSAKDKGTGKEQSITITASSG-LSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKE---A 544
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 334182408 595 AKKISDEDKEKMEGVLKEALEWLEENVNAEKEDYDEKLKEV 635
Cdd:TIGR02350 545 GDKLPAEEKEKIEKAVAELKEALKGEDVEEIKAKTEELQQA 585
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
43-415 |
0e+00 |
|
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; This subfamily includes human HSPA1A (70-kDa heat shock protein 1A, also known as HSP72; HSPA1; HSP70I; HSPA1B; HSP70-1; HSP70-1A), HSPA1B (70-kDa heat shock protein 1B, also known as HSPA1A; HSP70-2; HSP70-1B), and HSPA1L (70-kDa heat shock protein 1-like, also known as HSP70T; hum70t; HSP70-1L; HSP70-HOM), HSPA2 (70-kDa heat shock protein 2, also known as HSP70-2; HSP70-3), HSPA6 (also known as heat shock 70kDa protein 6; HSP70B'), HSPA7 (heat shock 70kDa protein 7 , also known as HSP70B), and HSPA8 (heat shock 70kDa protein 8, also known as Lipopolysaccharide-associated protein 1/LAP1; HSC70; HSP73; HSPA10). They are molecular chaperones implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. They play pivotal roles in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The subfamily also includes Saccharomyces cerevisiae heat shock protein Ssa1-4, which may play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. This subfamily belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466831 [Multi-domain] Cd Length: 375 Bit Score: 722.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 43 IGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDTERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDPDVQRD 122
Cdd:cd10233 2 IGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 123 IKFLPYKVVNKDGKPYIQVKVKGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGAIAG 202
Cdd:cd10233 82 MKHWPFKVVSGGDKPKIQVEYKGETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIAG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 203 LNVVRIINEPTGAAIAYGLDKKG-GESNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDYFIKLVK 281
Cdd:cd10233 162 LNVLRIINEPTAAAIAYGLDKKGkGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEFK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 282 KKYNKDISKDHKALGKLRRECELAKRSLSNQHQVRVEIESLFDGVDFSEPLTRARFEELNMDLFKKTMEPVKKALKDAGL 361
Cdd:cd10233 242 RKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELCADLFRSTLEPVEKVLRDAKL 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 334182408 362 KKSDIDEIVLVGGSTRIPKVQQMLKDFFDGKEPSKGTNPDEAVAYGAAVQGGVL 415
Cdd:cd10233 322 DKSQIHEIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
42-415 |
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: 687.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 42 VIGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDTERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDPDVQR 121
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 122 DIKFLPYKVVNK-DGKPYIQVKVKGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGAI 200
Cdd:cd24028 81 DIKHWPFKVVEDeDGKPKIEVTYKGEEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAATI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 201 AGLNVVRIINEPTGAAIAYGLDKK-GGESNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDYFIKL 279
Cdd:cd24028 161 AGLNVLRIINEPTAAALAYGLDKKsSGERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLVEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 280 VKKKYNKDISKDHKALGKLRRECELAKRSLSNQHQVRVEIESLFDGVDFSEPLTRARFEELNMDLFKKTMEPVKKALKDA 359
Cdd:cd24028 241 FKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGIDFETTITRAKFEELCEDLFKKCLEPVEKVLKDA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 334182408 360 GLKKSDIDEIVLVGGSTRIPKVQQMLKDFFDGKEPSKGTNPDEAVAYGAAVQGGVL 415
Cdd:cd24028 321 KLSKDDIDEVVLVGGSTRIPKIQELLSEFFGGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
42-541 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 686.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 42 VIGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFT-DTERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDpdvq 120
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPkDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 121 rdikflpykvvnkdgkpyIQVKVKGEEklFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGAI 200
Cdd:COG0443 77 ------------------EATEVGGKR--YSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 201 AGLNVVRIINEPTGAAIAYGLDKKGGESNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDYFIKLV 280
Cdd:COG0443 137 AGLEVLRLLNEPTAAALAYGLDKGKEEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPEF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 281 KKKYNKDISKDHKALGKLRRECELAKRSLSNQHQVRVEIeSLFDGVDFSEPLTRARFEELNMDLFKKTMEPVKKALKDAG 360
Cdd:COG0443 217 GKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINL-PFSGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADAG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 361 LKKSDIDEIVLVGGSTRIPKVQQMLKDFFdGKEPSKGTNPDEAVAYGAAVQGGVLSGEGGEetqnillLDVAPLSLGIET 440
Cdd:COG0443 296 LSPSDIDAVLLVGGSTRMPAVRERVKELF-GKEPLKGVDPDEAVALGAAIQAGVLAGDVKD-------LDVTPLSLGIET 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 441 VGGVMTNIIPRNTVIPTKKSQVFTTYQDQQTTVTINVYEGERSMTKDNRELGKFDLTGILPAPRGVPQIEVTFEVDANGI 520
Cdd:COG0443 368 LGGVFTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGI 447
|
490 500
....*....|....*....|.
gi 334182408 521 LQVKAEDKVAKTSQSITITND 541
Cdd:COG0443 448 LSVSAKDLGTGKEQSITIKEE 468
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
39-634 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 667.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 39 LGTVIGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDT-ERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDP 117
Cdd:PRK13411 1 MGKVIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSgDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 118 DVQRdiKFLPYKVV-NKDGKpyIQVKVKGeeKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKD 196
Cdd:PRK13411 81 EEER--SRVPYTCVkGRDDT--VNVQIRG--RNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 197 AGAIAGLNVVRIINEPTGAAIAYGLDKKGGESNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDYF 276
Cdd:PRK13411 155 AGTIAGLEVLRIINEPTAAALAYGLDKQDQEQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 277 IKLVKKKYNKDISKDHKALGKLRRECELAKRSLSNqhQVRVEIESLFDGVDFSEP------LTRARFEELNMDLFKKTME 350
Cdd:PRK13411 235 VENFQQQEGIDLSQDKMALQRLREAAEKAKIELSS--MLTTSINLPFITADETGPkhlemeLTRAKFEELTKDLVEATIE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 351 PVKKALKDAGLKKSDIDEIVLVGGSTRIPKVQQMLKDFFDGKEPSKGTNPDEAVAYGAAVQGGVLSGeggeETQNILLLD 430
Cdd:PRK13411 313 PMQQALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFGGKQPDRSVNPDEAVALGAAIQAGVLGG----EVKDLLLLD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 431 VAPLSLGIETVGGVMTNIIPRNTVIPTKKSQVFTTYQDQQTTVTINVYEGERSMTKDNRELGKFDLTGILPAPRGVPQIE 510
Cdd:PRK13411 389 VTPLSLGIETLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 511 VTFEVDANGILQVKAEDKVAKTSQSITITNdKGRLTEEEIEEMIREAEEFAEEDKIMKEKIDARNKLETYVYNMKSTVAD 590
Cdd:PRK13411 469 VSFEIDVNGILKVSAQDQGTGREQSIRITN-TGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKE 547
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 334182408 591 KEKLakkISDEDKEKMEGVlKEALEWLEENVNAEKEDYDEKLKE 634
Cdd:PRK13411 548 NGEL---ISEELKQRAEQK-VEQLEAALTDPNISLEELKQQLEE 587
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
40-636 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 658.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 40 GTVIGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDT-ERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDPD 118
Cdd:PTZ00400 41 GDIVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDgQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEDA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 119 VQRDIKFLPYKVV-NKDGKPYIQvkvkGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDA 197
Cdd:PTZ00400 121 TKKEQKILPYKIVrASNGDAWIE----AQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 198 GAIAGLNVVRIINEPTGAAIAYGLDKKGGESnILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDYFI 277
Cdd:PTZ00400 197 GKIAGLDVLRIINEPTAAALAFGMDKNDGKT-IAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYLI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 278 KLVKKKYNKDISKDHKALGKLRRECELAKRSLSNQHQVrvEIESLFDGVDFSEP------LTRARFEELNMDLFKKTMEP 351
Cdd:PTZ00400 276 AEFKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQT--EINLPFITADQSGPkhlqikLSRAKLEELTHDLLKKTIEP 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 352 VKKALKDAGLKKSDIDEIVLVGGSTRIPKVQQMLKDFFdGKEPSKGTNPDEAVAYGAAVQGGVLSGEggeeTQNILLLDV 431
Cdd:PTZ00400 354 CEKCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIF-GKEPSKGVNPDEAVAMGAAIQAGVLKGE----IKDLLLLDV 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 432 APLSLGIETVGGVMTNIIPRNTVIPTKKSQVFTTYQDQQTTVTINVYEGERSMTKDNRELGKFDLTGILPAPRGVPQIEV 511
Cdd:PTZ00400 429 TPLSLGIETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEV 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 512 TFEVDANGILQVKAEDKVAKTSQSITITNDKGrLTEEEIEEMIREAEEFAEEDKIMKEKIDARNKLETYVYNMKSTVADk 591
Cdd:PTZ00400 509 TFDVDANGIMNISAVDKSTGKKQEITIQSSGG-LSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSD- 586
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 334182408 592 ekLAKKISDEDKEKmegvLKEALEWLEENVNAEK-EDYDEKLKEVE 636
Cdd:PTZ00400 587 --LKDKISDADKDE----LKQKITKLRSTLSSEDvDSIKDKTKQLQ 626
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
39-650 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 657.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 39 LGTVIGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDT-ERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDp 117
Cdd:CHL00094 1 MGKVVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKgDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 118 dVQRDIKFLPYKVVNkDGKPYIQVKVKGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDA 197
Cdd:CHL00094 80 -ISEEAKQVSYKVKT-DSNGNIKIECPALNKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 198 GAIAGLNVVRIINEPTGAAIAYGLDKKGGESnILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDYFI 277
Cdd:CHL00094 158 GKIAGLEVLRIINEPTAASLAYGLDKKNNET-ILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 278 KLVKKKYNKDISKDHKALGKLRRECELAKRSLSNQHQVrvEIESLFDGVDFSEP------LTRARFEELNMDLFKKTMEP 351
Cdd:CHL00094 237 KEFKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQT--EINLPFITATQTGPkhiektLTRAKFEELCSDLINRCRIP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 352 VKKALKDAGLKKSDIDEIVLVGGSTRIPKVQQMLKDFFdGKEPSKGTNPDEAVAYGAAVQGGVLSGEggeeTQNILLLDV 431
Cdd:CHL00094 315 VENALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLL-GKKPNQSVNPDEVVAIGAAVQAGVLAGE----VKDILLLDV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 432 APLSLGIETVGGVMTNIIPRNTVIPTKKSQVFTTYQDQQTTVTINVYEGERSMTKDNRELGKFDLTGILPAPRGVPQIEV 511
Cdd:CHL00094 390 TPLSLGVETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 512 TFEVDANGILQVKAEDKVAKTSQSITITNdKGRLTEEEIEEMIREAEEFAEEDKIMKEKIDARNKLETYVYNMKSTVadk 591
Cdd:CHL00094 470 TFDIDANGILSVTAKDKGTGKEQSITIQG-ASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQL--- 545
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334182408 592 EKLAKKISDEDKEKMEGVLKEalewLEENVnaEKEDYD---EKLKEVELVCDPVIKSVYEKT 650
Cdd:CHL00094 546 KELKDKISEEKKEKIENLIKK----LRQAL--QNDNYEsikSLLEELQKALMEIGKEVYSST 601
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
39-581 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 617.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 39 LGTVIGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFT-DTERLIGEAAKNQAAKNPERTIFDPKRLIGRKFD-- 115
Cdd:PRK13410 1 MGRIVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTkDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 116 DPDVQRdikfLPYkVVNKDGKPYIQVKVKGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATK 195
Cdd:PRK13410 81 DPESKR----VPY-TIRRNEQGNVRIKCPRLEREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 196 DAGAIAGLNVVRIINEPTGAAIAYGLDKkGGESNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDY 275
Cdd:PRK13410 156 DAGRIAGLEVERILNEPTAAALAYGLDR-SSSQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 276 FIKLVKKKYNKDISKDHKALGKLRRECELAKRSLSNQHQVRVE---IESLFDGVDFSEP-LTRARFEELNMDLFKKTMEP 351
Cdd:PRK13410 235 LAEQFLEKEGIDLRRDRQALQRLTEAAEKAKIELSGVSVTDISlpfITATEDGPKHIETrLDRKQFESLCGDLLDRLLRP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 352 VKKALKDAGLKKSDIDEIVLVGGSTRIPKVQQMLKDFFDgKEPSKGTNPDEAVAYGAAVQGGVLSGEggeeTQNILLLDV 431
Cdd:PRK13410 315 VKRALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLIP-REPNQNVNPDEVVAVGAAIQAGILAGE----LKDLLLLDV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 432 APLSLGIETVGGVMTNIIPRNTVIPTKKSQVFTTYQDQQTTVTINVYEGERSMTKDNRELGKFDLTGILPAPRGVPQIEV 511
Cdd:PRK13410 390 TPLSLGLETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQV 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 512 TFEVDANGILQVKAEDKVAKTSQSITITNdKGRLTEEEIEEMIREAEEFAEEDKIMKEKIDARNKLETYV 581
Cdd:PRK13410 470 AFDIDANGILQVSATDRTTGREQSVTIQG-ASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLI 538
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
35-639 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 614.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 35 EEQKL-GTVIGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDTERLIGEAAKNQAAKNPERTIFDPKRLIGRK 113
Cdd:PTZ00186 21 ESQKVqGDVIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 114 FDDPDVQRDIKFLPYKVVNK-DGKPYIQvkvKGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQ 192
Cdd:PTZ00186 101 FEDEHIQKDIKNVPYKIVRAgNGDAWVQ---DGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 193 ATKDAGAIAGLNVVRIINEPTGAAIAYGLDKKGgESNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRV 272
Cdd:PTZ00186 178 ATKDAGTIAGLNVIRVVNEPTAAALAYGMDKTK-DSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLAL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 273 MDYFIKLVKKKYNKDISKDHKALGKLRRECELAKRSLSNQHQVRVEIESLFDGVDFSE----PLTRARFEELNMDLFKKT 348
Cdd:PTZ00186 257 SDYILEEFRKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADGAQhiqmHISRSKFEGITQRLIERS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 349 MEPVKKALKDAGLKKSDIDEIVLVGGSTRIPKVQQMLKDFFdGKEPSKGTNPDEAVAYGAAVQGGVLSGEggeeTQNILL 428
Cdd:PTZ00186 337 IAPCKQCMKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFF-QKDPFRGVNPDEAVALGAATLGGVLRGD----VKGLVL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 429 LDVAPLSLGIETVGGVMTNIIPRNTVIPTKKSQVFTTYQDQQTTVTINVYEGERSMTKDNRELGKFDLTGILPAPRGVPQ 508
Cdd:PTZ00186 412 LDVTPLSLGIETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQ 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 509 IEVTFEVDANGILQVKAEDKVAKTSQSITITNDKGrLTEEEIEEMIREAEEFAEEDKIMKEKIDARNKLETyvynmKSTV 588
Cdd:PTZ00186 492 IEVTFDIDANGICHVTAKDKATGKTQNITITANGG-LSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAET-----QLTT 565
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 334182408 589 ADKEKLA-KKISDEDKEKMEGVLKEaLEWLEENVNAEKEDYD---EKLKEVELVC 639
Cdd:PTZ00186 566 AERQLGEwKYVSDAEKENVKTLVAE-LRKAMENPNVAKDDLAaatDKLQKAVMEC 619
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
42-634 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 585.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 42 VIGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDT-ERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDpdVQ 120
Cdd:PLN03184 41 VVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNgDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSE--VD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 121 RDIKFLPYKVVnKDGKPYIQVKVKGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGAI 200
Cdd:PLN03184 119 EESKQVSYRVV-RDENGNVKLDCPAIGKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 201 AGLNVVRIINEPTGAAIAYGLDKKGGESnILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDYFIKLV 280
Cdd:PLN03184 198 AGLEVLRIINEPTAASLAYGFEKKSNET-ILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLASNF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 281 KKKYNKDISKDHKALGKLRRECELAKRSLSNQHQVRVE---IESLFDGVDFSEP-LTRARFEELNMDLFKKTMEPVKKAL 356
Cdd:PLN03184 277 KKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISlpfITATADGPKHIDTtLTRAKFEELCSDLLDRCKTPVENAL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 357 KDAGLKKSDIDEIVLVGGSTRIPKVQQMLKDFfDGKEPSKGTNPDEAVAYGAAVQGGVLSGEggeeTQNILLLDVAPLSL 436
Cdd:PLN03184 357 RDAKLSFKDIDEVILVGGSTRIPAVQELVKKL-TGKDPNVTVNPDEVVALGAAVQAGVLAGE----VSDIVLLDVTPLSL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 437 GIETVGGVMTNIIPRNTVIPTKKSQVFTTYQDQQTTVTINVYEGERSMTKDNRELGKFDLTGILPAPRGVPQIEVTFEVD 516
Cdd:PLN03184 432 GLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFDID 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 517 ANGILQVKAEDKVAKTSQSITITNdKGRLTEEEIEEMIREAEEFAEEDKIMKEKIDARNKLETYVYNMKSTVadkEKLAK 596
Cdd:PLN03184 512 ANGILSVSATDKGTGKKQDITITG-ASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQL---KELGD 587
|
570 580 590
....*....|....*....|....*....|....*...
gi 334182408 597 KISDEDKEKMEGVLKEALEWLEENVNAEKEDYDEKLKE 634
Cdd:PLN03184 588 KVPADVKEKVEAKLKELKDAIASGSTQKMKDAMAALNQ 625
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
43-415 |
0e+00 |
|
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar proteins; Ssb is ribosome-bound, Hsp70-type chaperone that assists in the co-translational folding of newly synthesized proteins in the cytosol. It stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Saccharmoyces cerevisiae Ssb are encoded by two genes, SSB1 and SSB2. Ssb1p is also known as cold-inducible protein YG101. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466943 [Multi-domain] Cd Length: 375 Bit Score: 572.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 43 IGIDLGTTYSCVGVYHNkHVEIIANDQGNRITPSWVAFTDTERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDPDVQRD 122
Cdd:cd24093 2 IGIDLGTTYSCVATYES-SVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 123 IKFLPYKVVNKDGKPYIQVKVKGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGAIAG 202
Cdd:cd24093 81 MKTWPFKVIDVNGNPVIEVQYLGETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 203 LNVVRIINEPTGAAIAYGLDKKGG--ESNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDYFIKLV 280
Cdd:cd24093 161 LNVLRIINEPTAAAIAYGLGAGKSekERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 281 KKKYNKDISKDHKALGKLRRECELAKRSLSNQHQVRVEIESLFDGVDFSEPLTRARFEELNMDLFKKTMEPVKKALKDAG 360
Cdd:cd24093 241 KKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSITRARFEDLNAALFKSTLEPVEQVLKDAK 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 334182408 361 LKKSDIDEIVLVGGSTRIPKVQQMLKDFFDGKEPSKGTNPDEAVAYGAAVQGGVL 415
Cdd:cd24093 321 ISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
42-416 |
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: 557.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 42 VIGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDT-ERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDPDVQ 120
Cdd:cd10234 1 IIGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 121 RDIKflPYKVVNKDGkpyIQVKVKGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGAI 200
Cdd:cd10234 81 RKQV--PYPVVSAGN---GDAWVEIGGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 201 AGLNVVRIINEPTGAAIAYGLDKKGGEsNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDYFIKLV 280
Cdd:cd10234 156 AGLEVLRIINEPTAAALAYGLDKKKDE-KILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 281 KKKYNKDISKDHKALGKLRRECELAKRSLSNQHQvrVEIESLFDGVDFSEP------LTRARFEELNMDLFKKTMEPVKK 354
Cdd:cd10234 235 KKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLE--TEINLPFITADASGPkhlemkLTRAKFEELTEDLVERTIEPVEQ 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334182408 355 ALKDAGLKKSDIDEIVLVGGSTRIPKVQQMLKDFFdGKEPSKGTNPDEAVAYGAAVQGGVLS 416
Cdd:cd10234 313 ALKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
43-581 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 548.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 43 IGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDTERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDpdVQRD 122
Cdd:PRK05183 22 VGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKNTISSVKRFMGRSLAD--IQQR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 123 IKFLPYK-VVNKDGKPYIQVkVKGeekLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGAIA 201
Cdd:PRK05183 100 YPHLPYQfVASENGMPLIRT-AQG---LKSPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 202 GLNVVRIINEPTGAAIAYGLDKkGGESNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDYfiklVK 281
Cdd:PRK05183 176 GLNVLRLLNEPTAAAIAYGLDS-GQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADW----IL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 282 KKYNKDISKDHKALGKLRRECELAKRSLSNQHQVRVEIEsLFDGVdfsepLTRARFEELNMDLFKKTMEPVKKALKDAGL 361
Cdd:PRK05183 251 EQAGLSPRLDPEDQRLLLDAARAAKEALSDADSVEVSVA-LWQGE-----ITREQFNALIAPLVKRTLLACRRALRDAGV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 362 KKSDIDEIVLVGGSTRIPKVQQMLKDFFdGKEPSKGTNPDEAVAYGAAVQGGVLSGEGGEEtqNILLLDVAPLSLGIETV 441
Cdd:PRK05183 325 EADEVKEVVMVGGSTRVPLVREAVGEFF-GRTPLTSIDPDKVVAIGAAIQADILAGNKPDS--DMLLLDVIPLSLGLETM 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 442 GGVMTNIIPRNTVIPTKKSQVFTTYQDQQTTVTINVYEGERSMTKDNRELGKFDLTGILPAPRGVPQIEVTFEVDANGIL 521
Cdd:PRK05183 402 GGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADGLL 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 522 QVKAEDKVAKTSQSITITNDKGrLTEEEIEEMIREAEEFAEEDkimkekIDARNKLETYV 581
Cdd:PRK05183 482 SVTAMEKSTGVEASIQVKPSYG-LTDDEIARMLKDSMSHAEED------MQARALAEQKV 534
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
42-574 |
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: 535.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 42 VIGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAF-TDTERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDPdvq 120
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYlKDGGVEVGKEALAAAAEDPKNTISSVKRLMGRSIEDI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 121 RDIKFLPYKVV-NKDGKPYIQVkVKGEEklfSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGA 199
Cdd:TIGR01991 78 KTFSILPYRFVdGPGEMVRLRT-VQGTV---TPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 200 IAGLNVVRIINEPTGAAIAYGLDKkGGESNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDYFIKl 279
Cdd:TIGR01991 154 LAGLNVLRLLNEPTAAAVAYGLDK-ASEGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWILK- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 280 vKKKYNKDISKDHKALgkLRRECELAKRSLSNQHQVRVEIEslFDGVDFSEPLTRARFEELNMDLFKKTMEPVKKALKDA 359
Cdd:TIGR01991 232 -QLGISADLNPEDQRL--LLQAARAAKEALTDAESVEVDFT--LDGKDFKGKLTRDEFEALIQPLVQKTLSICRRALRDA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 360 GLKKSDIDEIVLVGGSTRIPKVQQMLKDFFdGKEPSKGTNPDEAVAYGAAVQGGVLSGEGGEEtqNILLLDVAPLSLGIE 439
Cdd:TIGR01991 307 GLSVEEIKGVVLVGGSTRMPLVRRAVAELF-GQEPLTDIDPDQVVALGAAIQADLLAGNRIGN--DLLLLDVTPLSLGIE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 440 TVGGVMTNIIPRNTVIPTKKSQVFTTYQDQQTTVTINVYEGERSMTKDNRELGKFDLTGILPAPRGVPQIEVTFEVDANG 519
Cdd:TIGR01991 384 TMGGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDADG 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 334182408 520 ILQVKAEDKVAKTSQSITITNDKGrLTEEEIEEMIREAEEFAEEDKIMKEKIDAR 574
Cdd:TIGR01991 464 LLTVSAQEQSTGVEQSIQVKPSYG-LSDEEIERMLKDSFKHAEEDMYARALAEQK 517
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
40-415 |
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: 518.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 40 GTVIGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFT-DTERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDPD 118
Cdd:cd11733 1 GDVIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 119 VQRDIKFLPYKVV---NKDGKpyiqvkVKGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATK 195
Cdd:cd11733 81 VQKDIKMVPYKIVkasNGDAW------VEAHGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 196 DAGAIAGLNVVRIINEPTGAAIAYGLDKKGGESnILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDY 275
Cdd:cd11733 155 DAGQIAGLNVLRIINEPTAAALAYGLDKKDDKI-IAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 276 FIKLVKKKYNKDISKDHKALGKLRRECELAKRSLSNQHQvrVEIESLFDGVDFSEP------LTRARFEELNMDLFKKTM 349
Cdd:cd11733 234 LVAEFKKEQGIDLSKDNLALQRLREAAEKAKIELSSSLQ--TDINLPFITADASGPkhlnmkLTRAKFESLVGDLIKRTV 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334182408 350 EPVKKALKDAGLKKSDIDEIVLVGGSTRIPKVQQMLKDFFdGKEPSKGTNPDEAVAYGAAVQGGVL 415
Cdd:cd11733 312 EPCKKCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIF-GKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
40-417 |
2.87e-166 |
|
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: 480.79 E-value: 2.87e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 40 GTVIGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFT-DTERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDPD 118
Cdd:cd11734 1 GPVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTkDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 119 VQRDIKFLPYKVV-NKDGKPYIQVKvkgeEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDA 197
Cdd:cd11734 81 VQRDIKEVPYKIVkHSNGDAWVEAR----GQKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 198 GAIAGLNVVRIINEPTGAAIAYGLDKKgGESNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDYFI 277
Cdd:cd11734 157 GQIAGLNVLRVINEPTAAALAYGLDKS-GDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 278 KLVKKKYNKDISKDHKALGKLRRECELAKRSLSNQHQvrVEIESLFDGVDFSEP------LTRARFEELNMDLFKKTMEP 351
Cdd:cd11734 236 SEFKKESGIDLSKDRMAIQRIREAAEKAKIELSSTLQ--TDINLPFITADASGPkhinmkLTRAQFESLVKPLVDRTVEP 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334182408 352 VKKALKDAGLKKSDIDEIVLVGGSTRIPKVQQMLKDFFdGKEPSKGTNPDEAVAYGAAVQGGVLSG 417
Cdd:cd11734 314 CKKALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIF-GREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
42-417 |
3.57e-157 |
|
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: 457.45 E-value: 3.57e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 42 VIGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDTERLI-GEAAKNQAAKNPERTIFDPKRLIGRKFDDpdVQ 120
Cdd:cd10236 4 AVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITvGEKAKENAITDPENTISSVKRLMGRSLAD--VK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 121 RDIKFLPYKVVNKDGkpyIQVKVKGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGAI 200
Cdd:cd10236 82 EELPLLPYRLVGDEN---ELPRFRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 201 AGLNVVRIINEPTGAAIAYGLDKKgGESNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDYFIklv 280
Cdd:cd10236 159 AGLNVLRLLNEPTAAALAYGLDQK-KEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWIL--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 281 kKKYNKDISKDHKALGKLRRECELAKRSLSNQHQVRveIESLFDGVDFSEPLTRARFEELNMDLFKKTMEPVKKALKDAG 360
Cdd:cd10236 235 -KQIGIDARLDPAVQQALLQAARRAKEALSDADSAS--IEVEVEGKDWEREITREEFEELIQPLVKRTLEPCRRALKDAG 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 334182408 361 LKKSDIDEIVLVGGSTRIPKVQQMLKDFFdGKEPSKGTNPDEAVAYGAAVQGGVLSG 417
Cdd:cd10236 312 LEPADIDEVVLVGGSTRIPLVRQRVAEFF-GREPLTSINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
41-417 |
3.82e-153 |
|
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: 448.71 E-value: 3.82e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 41 TVIGIDLGTTYSCVGVYH--NKHVEIIANDQGNRITPSWVAFTDTER-LIGEAAKNQAAKNPERTIFDPKRLIGRKFDDP 117
Cdd:cd10237 23 KIVGIDLGTTYSCVGVYHavTGEVEVIPDDDGHKSIPSVVAFTPDGGvLVGYDALAQAEHNPSNTIYDAKRFIGKTFTKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 118 DVQRDIKFLPYKVVN-KDGKPYIQVKVKGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKD 196
Cdd:cd10237 103 ELEEEAKRYPFKVVNdNIGSAFFEVPLNGSTLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 197 AGAIAGLNVVRIINEPTGAAIAYGLDKKGGESNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDYF 276
Cdd:cd10237 183 AANLAGLEVLRVINEPTAAAMAYGLHKKSDVNNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQYL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 277 IKLVKKKYNKDIsKDHKALGKLRRECELAKRSLSNQHQVRVEIE-----SLFDGVDFSEPLTRARFEELNMDLFKKTMEP 351
Cdd:cd10237 263 IDRIAKKFGKTL-TDKEDIQRLRQAVEEVKLNLTNHNSASLSLPlqislPSAFKVKFKEEITRDLFETLNEDLFQRVLEP 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334182408 352 VKKALKDAGLKKSDIDEIVLVGGSTRIPKVQQMLKDFFdGKEPSKGTNPDEAVAYGAAVQGGVLSG 417
Cdd:cd10237 342 IRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFF-GKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
43-416 |
8.67e-143 |
|
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: 420.06 E-value: 8.67e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 43 IGIDLGTTYSCVGVYHNKHVEIIA-NDQGNRITPSWVAFT-DTERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDpdvq 120
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAEVIIeNSEGKRTTPSVVYFDkDGEVLVGEEAKNQALLDPENTIYSVKRLMGRDTKD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 121 rdikflpykvvnkdgkpyiqvKVKGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGAI 200
Cdd:cd24029 77 ---------------------KEEIGGKEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 201 AGLNVVRIINEPTGAAIAYGLDKKGGESNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDYFIKLV 280
Cdd:cd24029 136 AGLNVLRLINEPTAAALAYGLDKEGKDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEKI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 281 KKKYNK-DISKDHKALGKLRRECELAKRSLSNQHQVRVEIESLFDGVDFSEPLTRARFEELNMDLFKKTMEPVKKALKDA 359
Cdd:cd24029 216 GIETGIlDDKEDERARARLREAAEEAKIELSSSDSTDILILDDGKGGELEIEITREEFEELIAPLIERTIDLLEKALKDA 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 334182408 360 GLKKSDIDEIVLVGGSTRIPKVQQMLKDFFdGKEPSKGTNPDEAVAYGAAVQGGVLS 416
Cdd:cd24029 296 KLSPEDIDRVLLVGGSSRIPLVREMLEEYF-GREPISSVDPDEAVAKGAAIYAASLA 351
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
41-415 |
7.48e-142 |
|
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: 418.57 E-value: 7.48e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 41 TVIGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDTERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDPDVQ 120
Cdd:cd10238 1 AAFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 121 RDIKFLPYKVVNKDGKPYIQVKVKGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGAI 200
Cdd:cd10238 81 ELKKESKCKIIEKDGKPGYEIELEEKKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 201 AGLNVVRIINEPTGAAIAYGL--DKKGGESNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDYFIK 278
Cdd:cd10238 161 AGFNVLRVISEPSAAALAYGIgqDDPTENSNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHLAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 279 LVKKKYNKDISKDHKALGKLRRECELAKRSLSNQHQVRVEIESLFDGVDFSEPLTRARFEELNMDLFKKTMEPVKKALKD 358
Cdd:cd10238 241 EFKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATCSVESLYDGMDFQCNVSRARFESLCSSLFQQCLEPIQEVLNS 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 334182408 359 AGLKKSDIDEIVLVGGSTRIPKVQQMLKDFFDGKEPSKGTNPDEAVAYGAAVQGGVL 415
Cdd:cd10238 321 AGLTKEDIDKVILCGGSSRIPKLQQLIKDLFPSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
43-411 |
4.03e-131 |
|
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: 391.15 E-value: 4.03e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 43 IGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDTERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDPDVQRD 122
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 123 IKFLPYKVVN-KDGKPYIQVKVKGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGAIA 201
Cdd:cd11732 81 IKLLPFKLVElEDGKVGIEVSYNGEEVVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 202 GLNVVRIINEPTGAAIAYGL---DKKGGES---NILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDY 275
Cdd:cd11732 161 GLNCLRLINETTAAALDYGIyksDLLESEEkprIVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 276 FIKLVKKKYNKDISKDHKALGKLRRECELAKRSLSNQHQVRVEIESLFDGVDFSEPLTRARFEELNMDLFKKTMEPVKKA 355
Cdd:cd11732 241 FAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEDIDFSGQIKREEFEELIQPLLARLEAPIKKA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 334182408 356 LKDAGLKKSDIDEIVLVGGSTRIPKVQQMLKDFFdGKEPSKGTNPDEAVAYGAAVQ 411
Cdd:cd11732 321 LAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVF-GKDLSTTLNADEAVARGCALQ 375
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
43-413 |
5.63e-131 |
|
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: 389.30 E-value: 5.63e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 43 IGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAF-TDTERLIGEAAKNQAAKNPERTIFDPKRLIGRkfddpDVQR 121
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVdEDGSILVGRAAKERLVTHPDRTAASFKRFMGT-----DKQY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 122 DIkflpykvvnkdGKpyiqvkvkgeeKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGAIA 201
Cdd:cd10235 76 RL-----------GN-----------HTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 202 GLNVVRIINEPTGAAIAYGLDKKGGESNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDYFIKLVK 281
Cdd:cd10235 134 GLKVERLINEPTAAALAYGLHKREDETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFLKKHR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 282 KKYNkdiSKDHKALGKLRRECELAKRSLSNQHqvRVEIESLFDGVDFSEPLTRARFEELNMDLFKKTMEPVKKALKDAGL 361
Cdd:cd10235 214 LDFT---SLSPSELAALRKRAEQAKRQLSSQD--SAEIRLTYRGEELEIELTREEFEELCAPLLERLRQPIERALRDAGL 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 334182408 362 KKSDIDEIVLVGGSTRIPKVQQMLKDFFdGKEPSKGTNPDEAVAYGAAVQGG 413
Cdd:cd10235 289 KPSDIDAVILVGGATRMPLVRQLIARLF-GRLPLSSLDPDEAVALGAAIQAA 339
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
43-411 |
1.60e-129 |
|
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; This subgroup includes the human proteins, HSPA4 (also known as 70-kDa heat shock protein 4; APG-2; HS24/P52; hsp70 RY; HSPH2), HSPA4L (also known as 70-kDa heat shock protein 4-like; APG-1; HSPH3; OSP94), and HSPH1 (also known as heat shock 105kDa/110kDa protein 1; HSP105; HSP105A; HSP105B; NY-CO-25). They belong to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family, and includes proteins believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466826 [Multi-domain] Cd Length: 378 Bit Score: 387.02 E-value: 1.60e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 43 IGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDTERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDPDVQRD 122
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 123 IKFLPYKVVN-KDGKPYIQVKVKGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGAIA 201
Cdd:cd10228 81 LKHLPYKVVKlPNGSVGIKVQYLGEEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 202 GLNVVRIINEPTGAAIAYGLDKK----GGES--NILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDY 275
Cdd:cd10228 161 GLNCLRLLNDTTAVALAYGIYKQdlpaEEEKprNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 276 FIKLVKKKYNKDISKDHKALGKLRRECELAKRSLS-NQHQVRVEIESLFDGVDFSEPLTRARFEELNMDLFKKTMEPVKK 354
Cdd:cd10228 241 FAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSaNATELPLNIECFMDDKDVSGKMKRAEFEELCAPLFARVEVPLRS 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 334182408 355 ALKDAGLKKSDIDEIVLVGGSTRIPKVQQMLKDFFdGKEPSKGTNPDEAVAYGAAVQ 411
Cdd:cd10228 321 ALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVF-GKEPSTTLNQDEAVARGCALQ 376
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
42-416 |
2.64e-123 |
|
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: 371.26 E-value: 2.64e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 42 VIGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDTERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDPDVQR 121
Cdd:cd24095 3 VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEVQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 122 DIKFLPYKVVN-KDGKPYIQVKVKGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGAI 200
Cdd:cd24095 83 DLKLFPFKVTEgPDGEIGINVNYLGEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAAQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 201 AGLNVVRIINEPTGAAIAYGLDK----KGGESNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDYF 276
Cdd:cd24095 163 AGLNCLRLMNETTATALAYGIYKtdlpETDPTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFDHF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 277 IKLVKKKYNKDISKDHKALGKLRRECELAKRSLSNQHQVRVEIESLFDGVDFSEPLTRARFEELNMDLFKKTMEPVKKAL 356
Cdd:cd24095 243 AAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMEDKDVKGMITREEFEELAAPLLERLLEPLEKAL 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 357 KDAGLKKSDIDEIVLVGGSTRIPKVQQMLKDFFdGKEPSKGTNPDEAVAYGAAVQGGVLS 416
Cdd:cd24095 323 ADSGLTVDQIHSVEVVGSGSRIPAILKILTKFF-GKEPSRTMNASECVARGCALQCAMLS 381
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
41-412 |
2.23e-112 |
|
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: 341.78 E-value: 2.23e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 41 TVIGIDLGTTYSCVGVYH-NKHVEIIANDQGNRITPSWVAFTDTERLIGEAAKNQAAKNPERTIFDPKRLIGrkfddpdv 119
Cdd:cd10230 1 AVLGIDLGSEFIKVALVKpGVPFEIVLNEESKRKTPSAVAFRNGERLFGDDALALATRFPENTFSYLKDLLG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 120 qrdikflpykvvnkdgkpyiqvkvkgeeklFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGA 199
Cdd:cd10230 73 ------------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 200 IAGLNVVRIINEPTGAAIAYGLDKKGGES---NILVYDLGGGTFDVSILTID------------NGVFEVLSTSGDTHLG 264
Cdd:cd10230 123 IAGLNVLSLINDNTAAALNYGIDRRFENNepqNVLFYDMGASSTSATVVEFSsvkekdkgknktVPQVEVLGVGWDRTLG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 265 GEDFDHRVMDYFIKLVKKKYNK--DISKDHKALGKLRRECELAKRSLS--NQHQVRveIESLFDGVDFSEPLTRARFEEL 340
Cdd:cd10230 203 GLEFDLRLADHLADEFNEKHKKdkDVRTNPRAMAKLLKEANRVKEVLSanTEAPAS--IESLYDDIDFRTKITREEFEEL 280
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334182408 341 NMDLFKKTMEPVKKALKDAGLKKSDIDEIVLVGGSTRIPKVQQMLKDFFDGKEPSKGTNPDEAVAYGAAVQG 412
Cdd:cd10230 281 CADLFERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELGKHLNADEAAALGAAFYA 352
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
43-416 |
2.66e-110 |
|
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: 337.81 E-value: 2.66e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 43 IGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDTERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDPDVQRD 122
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 123 IKFLPYKVVNKDGKPYIQVKVKGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGAIAG 202
Cdd:cd24094 81 EKYFTAKLVDANGEVGAEVNYLGEKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 203 LNVVRIINEPTGAAIAYG---LDKKGGES---NILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVMDYF 276
Cdd:cd24094 161 LNPLRLMNDTTAAALGYGitkTDLPEPEEkprIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDHF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 277 IKLVKKKYNKDISKDHKALGKLRRECELAKRSLSNQHQVRVEIESLFDGVDFSEPLTRARFEELNMDLFKKTMEPVKKAL 356
Cdd:cd24094 241 ADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVSSMLKREEFEELIAPLLERVTAPLEKAL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 357 KDAGLKKSDIDEIVLVGGSTRIPKVQQMLKDFFdGKEPSKGTNPDEAVAYGAAVQGGVLS 416
Cdd:cd24094 321 AQAGLTKDEIDFVELVGGTTRVPALKESISAFF-GKPLSTTLNQDEAVARGAAFACAILS 379
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
36-543 |
4.56e-106 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 334.13 E-value: 4.56e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 36 EQKLGTVIGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDTERLIGeaaknqaAKNPERTIfdpKRLIGRKFD 115
Cdd:PRK01433 15 KQERQIAVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIG-------NNKGLRSI---KRLFGKTLK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 116 D----PDVQRDIKflPYKVVNKDgkpyiQVKVKGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQR 191
Cdd:PRK01433 85 EilntPALFSLVK--DYLDVNSS-----ELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 192 QATKDAGAIAGLNVVRIINEPTGAAIAYGLDKkGGESNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHR 271
Cdd:PRK01433 158 GEVMLAAKIAGFEVLRLIAEPTAAAYAYGLNK-NQKGCYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 272 VMDYFIklvkkkyNK-DISKDHKALgklrRECELAKRSLSNQHQVRVEIESLfdgvdfseplTRARFEELNMDLFKKTME 350
Cdd:PRK01433 237 ITQYLC-------NKfDLPNSIDTL----QLAKKAKETLTYKDSFNNDNISI----------NKQTLEQLILPLVERTIN 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 351 PVKKALKDAGlkKSDIDEIVLVGGSTRIPKVQQMLKDFFDGKEPSKgTNPDEAVAYGAAVQGGVLSGEggeeTQNILLLD 430
Cdd:PRK01433 296 IAQECLEQAG--NPNIDGVILVGGATRIPLIKDELYKAFKVDILSD-IDPDKAVVWGAALQAENLIAP----HTNSLLID 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 431 VAPLSLGIETVGGVMTNIIPRNTVIPTKKSQVFTTYQDQQTTVTINVYEGERSMTKDNRELGKFDLTGILPAPRGVPQIE 510
Cdd:PRK01433 369 VVPLSLGMELYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAE 448
|
490 500 510
....*....|....*....|....*....|...
gi 334182408 511 VTFEVDANGILQVKAEDKVAKTSQSITITNDKG 543
Cdd:PRK01433 449 VTFAIDADGILSVSAYEKISNTSHAIEVKPNHG 481
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
41-411 |
7.72e-94 |
|
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: 294.92 E-value: 7.72e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 41 TVIGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDTERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDPDVQ 120
Cdd:cd11737 1 SVVGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 121 RDIKFLPYKVVN-KDGKPYIQVKVKGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGA 199
Cdd:cd11737 81 AEKPSLAYELVQlPTGTTGIKVMYMEEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 200 IAGLNVVRIINEPTGAAIAYGLDKKG------GESNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVM 273
Cdd:cd11737 161 IAGLNCLRLMNETTAVALAYGIYKQDlpapeeKPRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 274 DYFIKLVKKKYNKDISKDHKALGKLRRECELAKRSLS-NQHQVRVEIESLFDGVDFSEPLTRARFEELNMDLFKKTMEPV 352
Cdd:cd11737 241 NHFCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSaNASDLPLNIECFMNDIDVSGTMNRGQFEEMCADLLARVEPPL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 334182408 353 KKALKDAGLKKSDIDEIVLVGGSTRIPKVQQMLKDFFdGKEPSKGTNPDEAVAYGAAVQ 411
Cdd:cd11737 321 RSVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFF-GKEVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
41-415 |
4.83e-93 |
|
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: 291.96 E-value: 4.83e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 41 TVIGIDLGTTYSCVGvYHNKH--VEIIANDQGNRITPSWVAFTDTERLIGEAAKNQAAKNPERTIFDPKRLIGrkfddpd 118
Cdd:cd10232 1 VVIGISFGNSNSSIA-IINKDgrAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPKNTVANFRDLLG------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 119 vqrdikflpykvvnkdgkpyiqvkvkgeEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAG 198
Cdd:cd10232 73 ----------------------------TTTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 199 AIAGLNVVRIINEPTGAAIAYGLDK-----KGGESNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVM 273
Cdd:cd10232 125 AAAGLEVLQLIPEPAAAALAYDLRAetsgdTIKDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 274 DYFIKLVKKKYNKDISKDHKALGKLRRECELAKRSLSNQHQVRVEIESLFDGVDFSEPLTRARFEELNMDLFKKTMEPVK 353
Cdd:cd10232 205 GHFAKEFKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTSAPCSVESLADGIDFHSSINRTRYELLASKVFQQFADLVT 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334182408 354 KALKDAGLKKSDIDEIVLVGGSTRIPKVQQMLKDFFDGKEPSKGT---NPDEAVAYGAAVQGGVL 415
Cdd:cd10232 285 DAIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLFPESTIIRAPtqiNPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
41-411 |
3.73e-91 |
|
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: 287.91 E-value: 3.73e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 41 TVIGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDTERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDPDVQ 120
Cdd:cd11739 1 SVVGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 121 RDIKFLPYKVVN-KDGKPYIQVKVKGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGA 199
Cdd:cd11739 81 KEKENLSYDLVPlKNGGVGVKVMYLDEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 200 IAGLNVVRIINEPTGAAIAYGLDKK---GGESN--ILVY-DLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVM 273
Cdd:cd11739 161 IVGLNCLRLMNDMTAVALNYGIYKQdlpAPDEKprIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 274 DYFIKLVKKKYNKDISKDHKALGKLRRECELAKRSLS-NQHQVRVEIESLFDGVDFSEPLTRARFEELNMDLFKKTMEPV 352
Cdd:cd11739 241 EHFCAEFKTKYKLDVKSKIRALLRLYQECEKLKKLMSsNSTDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEVPL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 334182408 353 KKALKDAGLKKSDIDEIVLVGGSTRIPKVQQMLKDFFdGKEPSKGTNPDEAVAYGAAVQ 411
Cdd:cd11739 321 YSLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFF-GKDVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
41-416 |
1.34e-90 |
|
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: 286.81 E-value: 1.34e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 41 TVIGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDTERLIGEAAKNQAAKNPERTIFDPKRLIGRKFDDPDVQ 120
Cdd:cd11738 1 SVVGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 121 RDIKFLPYKVVN-KDGKPYIQVKVKGEEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGA 199
Cdd:cd11738 81 AEKIKLPYELQKmPNGSTGVKVRYLDEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 200 IAGLNVVRIINEPTGAAIAYGLDKKG------GESNILVYDLGGGTFDVSILTIDNGVFEVLSTSGDTHLGGEDFDHRVM 273
Cdd:cd11738 161 IAGLNCLRLMNETTAVALAYGIYKQDlpaleeKPRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 274 DYFIKLVKKKYNKDISKDHKALGKLRRECELAKRSLS-NQHQVRVEIESLFDGVDFSEPLTRARFEELNMDLFKKTMEPV 352
Cdd:cd11738 241 DYFCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSaNASDLPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEPPL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334182408 353 KKALKDAGLKKSDIDEIVLVGGSTRIPKVQQMLKDFFdGKEPSKGTNPDEAVAYGAAVQGGVLS 416
Cdd:cd11738 321 KAVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCAILS 383
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
43-410 |
5.71e-59 |
|
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: 201.56 E-value: 5.71e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 43 IGIDLGTTYSCVGVYHNKHVEIIANDqgnrITPSWVAFTDTERLIgeaaknqaaknpertifdPKRLigrkfddpdvqrd 122
Cdd:cd10170 1 VGIDFGTTYSGVAYALLGPGEPPLVV----LQLPWPGGDGGSSKV------------------PSVL------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 123 ikflpykvvnkdgkpyiqvkvkgeeklfspeEISAMILTKMKETAEAFLGKKIK-------DAVITVPAYFNDAQRQATK 195
Cdd:cd10170 46 -------------------------------EVVADFLRALLEHAKAELGDRIWelekapiEVVITVPAGWSDAAREALR 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 196 DAGAIAGL----NVVRIINEPTGAAIAYGLDKKGGE-----SNILVYDLGGGTFDVSILTIDNG---VFEVLSTSGDTHL 263
Cdd:cd10170 95 EAARAAGFgsdsDNVRLVSEPEAAALYALEDKGDLLplkpgDVVLVCDAGGGTVDLSLYEVTSGsplLLEEVAPGGGALL 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 264 GGEDFDHRVMDYFIKLVKKKYNKDISKDHKALGKLRRECELAKRSLSNQHQVRVEIESLFDGVD---FSEPLTRARFEEL 340
Cdd:cd10170 175 GGTDIDEAFEKLLREKLGDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGLpelGLEKGTLLLTEEE 254
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334182408 341 NMDLFKKTMEPVKKALKDAGLKKS--DIDEIVLVGGSTRIPKVQQMLKDFFDGKEP---SKGTNPDEAVAYGAAV 410
Cdd:cd10170 255 IRDLFDPVIDKILELIEEQLEAKSgtPPDAVVLVGGFSRSPYLRERLRERFGSAGIiivLRSDDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
43-410 |
5.79e-38 |
|
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: 145.88 E-value: 5.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 43 IGIDLGTTYSCVGVYHNKHVEIIANDQGNRITPSWVAFTDTE------RLIGEAAKNQAAKNPE--RTIFDPKRLIGrkf 114
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREeegaesIYFGNDAIDAYLNDPEegRLIKSVKSFLG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 115 ddpdvqrdIKFLPYKVVNkdgkpyiqvkvkgeEKLFSPEEISAMILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQAT 194
Cdd:cd10231 78 --------SSLFDETTIF--------------GRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 195 -------KDAGAIAGLNVVRIINEPTGAAIAY--GLDKkggESNILVYDLGGGTFDVSILTID----NGVFEVLSTSGDt 261
Cdd:cd10231 136 aqaesrlRDAARRAGFRNVEFQYEPIAAALDYeqRLDR---EELVLVVDFGGGTSDFSVLRLGpnrtDRRADILATSGV- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 262 HLGGEDFD-----HRVMDYF----------------------------IKLVKKKYN----KDISKDHKALGKLRR---- 300
Cdd:cd10231 212 GIGGDDFDrelalKKVMPHLgrgstyvsgdkglpvpawlyadlsnwhaISLLYTKKTlrllLDLRRDAADPEKIERllsl 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 301 -----------ECELAKRSLSNQHQVRVEIEslFDGVDFSEPLTRARFEELNMDLFKKTMEPVKKALKDAGLKKSDIDEI 369
Cdd:cd10231 292 vedqlghrlfrAVEQAKIALSSADEATLSFD--FIEISIKVTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRV 369
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 334182408 370 VLVGGSTRIPKVQQMLKDFFdGKEPSKGTNPDEAVAYGAAV 410
Cdd:cd10231 370 FLTGGSSQSPAVRQALASLF-GQARLVEGDEFGSVAAGLAL 409
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
42-409 |
2.28e-22 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar proteins; The family includes heat shock 70 kDa proteins HSPA12A and HSPA12B. HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. Both HSPA12A and HSPA12B belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A and HSPA12B.
Pssm-ID: 466827 [Multi-domain] Cd Length: 372 Bit Score: 99.27 E-value: 2.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 42 VIGIDLGTTYSCVGV-----YHNKHVEIIANDQGNRI----TPSWVAFTDTERL--IGEAAKNQAAKNPERtifdpkrli 110
Cdd:cd10229 2 VVAIDFGTTYSGYAYsfitdPGDIHTMYNWWGAPTGVsspkTPTCLLLNPDGEFhsFGYEAREKYSDLAED--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 111 GRKFDDPDVQRDIKFLPYKVVNKDGKPYIqvkVKGeeKLFSPEEISAMILTKMKETAEAFLGKKIKDA--------VITV 182
Cdd:cd10229 73 EEHQWLYFFKFKMMLLSEKELTRDTKVKA---VNG--KSMPALEVFAEALRYLKDHALKELRDRSGSSldeddirwVLTV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 183 PAYFNDAQ----RQATKDAGAIAGLN--VVRIINEPTGAAIAYGLDKKGGESNI-------LVYDLGGGTFDVSILTI-- 247
Cdd:cd10229 148 PAIWSDAAkqfmREAAVKAGLISEENseQLIIALEPEAAALYCQKLLAEGEEKElkpgdkyLVVDCGGGTVDITVHEVle 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 248 DNGVFEVLSTSGDtHLGGEDFDhrvmDYFIKLVKKKynkdiskdhkaLGKLRRECELAKRSLsnqhqVRVEIESLFDG-- 325
Cdd:cd10229 228 DGKLEELLKASGG-PWGSTSVD----EEFEELLEEI-----------FGDDFMEAFKQKYPS-----DYLDLLQAFERkk 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 326 VDFSEPLTRARFEElnmdLFKKTMEPVKKALKD--AGLKKSDIDEIVLVGGSTRIPKVQQMLKDFFDGK----EPskgTN 399
Cdd:cd10229 287 RSFKLRLSPELMKS----LFDPVVKKIIEHIKEllEKPELKGVDYIFLVGGFAESPYLQKAVKEAFSTKvkiiIP---PE 359
|
410
....*....|
gi 334182408 400 PDEAVAYGAA 409
Cdd:cd10229 360 PGLAVVKGAV 369
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
43-410 |
9.94e-14 |
|
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: 72.51 E-value: 9.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 43 IGIDLGTTYSCVgvyHNKHVEIIANDqgnritPSWVAF-TDTERLI--GEAAKNQAAKNPERtifdpkrligrkfddpdv 119
Cdd:cd10225 2 IGIDLGTANTLV---YVKGKGIVLNE------PSVVAVdKNTGKVLavGEEAKKMLGRTPGN------------------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 120 qrdikflpYKVVN--KDGkpyiqvkVkgeeklfspeeISAMiltkmkETAEAFLGKKIK-----------DAVITVPAYF 186
Cdd:cd10225 55 --------IVAIRplRDG-------V-----------IADF------EATEAMLRYFIRkahrrrgflrpRVVIGVPSGI 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 187 NDAQRQATKDAGAIAGLNVVRIINEPTGAAIAYGLDKKGGESNILVyDLGGGTFDVSILTIdNGVfeVLSTSgdTHLGGE 266
Cdd:cd10225 103 TEVERRAVKEAAEHAGAREVYLIEEPMAAAIGAGLPIEEPRGSMVV-DIGGGTTEIAVISL-GGI--VTSRS--VRVAGD 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 267 DFDHRVMDYfiklVKKKYNKDISkdhkalgklRRECELAKRSLSNQH------QVRVEIESLFDGVDFSEPLTRARFEEL 340
Cdd:cd10225 177 EMDEAIINY----VRRKYNLLIG---------ERTAERIKIEIGSAYpldeelSMEVRGRDLVTGLPRTIEITSEEVREA 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 341 NMDLFKKTMEPVKKALKD-----AglkkSDIDE--IVLVGGSTRIpkvqQMLKDFFdgkepSKGT--------NPDEAVA 405
Cdd:cd10225 244 LEEPVNAIVEAVRSTLERtppelA----ADIVDrgIVLTGGGALL----RGLDELL-----REETglpvhvadDPLTCVA 310
|
....*
gi 334182408 406 YGAAV 410
Cdd:cd10225 311 KGAGK 315
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
43-285 |
1.20e-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: 63.56 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 43 IGIDLGTTYSCVGVyhnKHVEIIANDqgnritPSWVAF-TDTERLI--GEAAKNQAAKNPE--RTIFdPKRligrkfD-- 115
Cdd:COG1077 10 IGIDLGTANTLVYV---KGKGIVLNE------PSVVAIdKKTGKVLavGEEAKEMLGRTPGniVAIR-PLK------Dgv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 116 --DPDVQRdiKFLPYkvvnkdgkpYIQvKVKGEEKLFSPEeisamiltkmketaeaflgkkikdAVITVPAYFNDAQRQA 193
Cdd:COG1077 74 iaDFEVTE--AMLKY---------FIK-KVHGRRSFFRPR------------------------VVICVPSGITEVERRA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 194 TKDAGAIAGLNVVRIINEPTGAAIAYGLDKKGGESNILVyDLGGGTFDVSILTIdNGVfeVLSTSgdTHLGGEDFDHRVM 273
Cdd:COG1077 118 VRDAAEQAGAREVYLIEEPMAAAIGAGLPIEEPTGNMVV-DIGGGTTEVAVISL-GGI--VVSRS--IRVAGDELDEAII 191
|
250
....*....|..
gi 334182408 274 DYfiklVKKKYN 285
Cdd:COG1077 192 QY----VRKKYN 199
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
157-387 |
4.73e-10 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 62.19 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 157 AMILtKMKETAEAFLGKKIKDAVITVPAYFN-----DAQRQAT---KDAGAIAGLNVVRIINEPTGAAIAY--GLDKkgg 226
Cdd:PRK11678 132 AMML-HIKQQAEAQLQAAITQAVIGRPVNFQglggeEANRQAEgilERAAKRAGFKDVEFQFEPVAAGLDFeaTLTE--- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 227 ESNILVYDLGGGTFDVSILTI-------DNGVFEVLSTSGdTHLGGEDFD-----HRVMDYF---IKLVKKK-------Y 284
Cdd:PRK11678 208 EKRVLVVDIGGGTTDCSMLLMgpswrgrADRSASLLGHSG-QRIGGNDLDialafKQLMPLLgmgSETEKGIalpslpfW 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 285 N----------------------KDISKD--------------HKALG-KLRRECELAKRSLSNQHQVRVEIESLFDGVd 327
Cdd:PRK11678 287 NavaindvpaqsdfyslangrllNDLIRDarepekvarllkvwRQRLSyRLVRSAEEAKIALSDQAETRASLDFISDGL- 365
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334182408 328 fSEPLTRARFEELNMDLFKKTMEPVKKALKDAGLKKsdiDEIVLVGGSTRIP----KVQQMLKD 387
Cdd:PRK11678 366 -ATEISQQGLEEAISQPLARILELVQLALDQAQVKP---DVIYLTGGSARSPliraALAQQLPG 425
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
165-285 |
6.03e-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: 6.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 165 ETAEAFL---GKKIKDA--------VITVPAYFNDAQRQATKDAGAIAGLNVVRIINEPTGAAIAYGLDKKGGESNiLVY 233
Cdd:pfam06723 72 EVTEAMLkyfIKKVHGRrsfskprvVICVPSGITEVERRAVKEAAKNAGAREVFLIEEPMAAAIGAGLPVEEPTGN-MVV 150
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 334182408 234 DLGGGTFDVSILTIdNGVfeVLSTSgdTHLGGEDFDHRVmdyfIKLVKKKYN 285
Cdd:pfam06723 151 DIGGGTTEVAVISL-GGI--VTSKS--VRVAGDEFDEAI----IKYIRKKYN 193
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
39-285 |
1.15e-08 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 57.45 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 39 LGTVIGIDLGTTYSCVGVyhnKHVEIIANDqgnritPSWVAF-TDTERL--IGEAAKnqaaknpertifdpkRLIGRKFD 115
Cdd:PRK13930 7 FSKDIGIDLGTANTLVYV---KGKGIVLNE------PSVVAIdTKTGKVlaVGEEAK---------------EMLGRTPG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 116 DPDVQRDIKflpykvvnkDGkpyiqVKVkgeeklfSPEEISAMILTKMKETAEAFLGKKIKdAVITVPAYFNDAQRQATK 195
Cdd:PRK13930 63 NIEAIRPLK---------DG-----VIA-------DFEATEAMLRYFIKKARGRRFFRKPR-IVICVPSGITEVERRAVR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 196 DAGAIAGLNVVRIINEPTGAAIAYGLDKKGGESNILVyDLGGGTFDVSILTIdNGVfeVLSTSgdTHLGGEDFDHRVMDY 275
Cdd:PRK13930 121 EAAEHAGAREVYLIEEPMAAAIGAGLPVTEPVGNMVV-DIGGGTTEVAVISL-GGI--VYSES--IRVAGDEMDEAIVQY 194
|
250
....*....|
gi 334182408 276 fiklVKKKYN 285
Cdd:PRK13930 195 ----VRRKYN 200
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
142-390 |
5.97e-08 |
|
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: 54.61 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 142 KVKGEEKLFSPEEIS-----AMILTKMKETAEAFLGKKIKDAVITVP----AYFNDAQRqatkdagaiAGLNVVRIINEP 212
Cdd:cd24004 29 SEEHPERAMGDGQIHdiskvAESIKELLKELEEKLGSKLKDVVIAIAkvveSLLNVLEK---------AGLEPVGLTLEP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 213 TgAAIAYGLDKKGGESNILVYDLGGGTFDVSIltIDNGVfevLSTSGDTHLGGEDFDHRVMDYFiklvkkkynkDISKDh 292
Cdd:cd24004 100 F-AAANLLIPYDMRDLNIALVDIGAGTTDIAL--IRNGG---IEAYRMVPLGGDDFTKAIAEGF----------LISFE- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 293 kalgklrrECELAKRSlsnqhqvrveiESLFDGVDFSEPLTRARFEELNMDLFKKTMEP----VKKALKDAGLKKSDIDE 368
Cdd:cd24004 163 --------EAEKIKRT-----------YGIFLLIEAKDQLGFTINKKEVYDIIKPVLEElasgIANAIEEYNGKFKLPDA 223
|
250 260
....*....|....*....|..
gi 334182408 369 IVLVGGSTRIPKVQQMLKDFFD 390
Cdd:cd24004 224 VYLVGGGSKLPGLNEALAEKLG 245
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
159-263 |
8.04e-08 |
|
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity.
Pssm-ID: 466897 [Multi-domain] Cd Length: 241 Bit Score: 53.81 E-value: 8.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 159 ILTKMKETAEAFLGKKIKDAVITVPAYFNDAQRQATKDAGAIAGLNVVRIINEPTGAAIAYGLDkkggesNILVYDLGGG 238
Cdd:cd24047 48 IVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGIR------DGAVVDIGGG 121
|
90 100
....*....|....*....|....*
gi 334182408 239 TFDVSILTIDNGVFEVLSTSGDTHL 263
Cdd:cd24047 122 TTGIAVLKDGKVVYTADEPTGGTHL 146
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
179-285 |
8.16e-08 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 54.52 E-value: 8.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 179 VITVPAYFNDAQRQATKDAGAIAGLNVVRIINEPTGAAIAYGLDKKGGESNILVyDLGGGTFDVSILTIDNGVfevlsTS 258
Cdd:PRK13928 99 MICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLDISQPSGNMVV-DIGGGTTDIAVLSLGGIV-----TS 172
|
90 100
....*....|....*....|....*..
gi 334182408 259 GDTHLGGEDFDHRVMDYfiklVKKKYN 285
Cdd:PRK13928 173 SSIKVAGDKFDEAIIRY----IRKKYK 195
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
41-285 |
4.15e-07 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 52.60 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 41 TVIGIDLGTTYSCVgvyHNKHVEIIANDqgnritPSWVAFTDTER---LIGEAAKNQAAKNPERTIfdpkrligrkfddp 117
Cdd:PRK13929 5 TEIGIDLGTANILV---YSKNKGIILNE------PSVVAVDTETKavlAIGTEAKNMIGKTPGKIV-------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 118 dVQRDIKflpykvvnkDGkpyiqvkvkgeekLFSPEEISAMILTKMKETAEAFLGKKIK--DAVITVPAYFNDAQRQATK 195
Cdd:PRK13929 62 -AVRPMK---------DG-------------VIADYDMTTDLLKQIMKKAGKNIGMTFRkpNVVVCTPSGSTAVERRAIS 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 196 DAGAIAGLNVVRIINEPTGAAIAYGLDKKGGESNILVyDLGGGTFDVSILTidngvFEVLSTSGDTHLGGEDFDhrvmDY 275
Cdd:PRK13929 119 DAVKNCGAKNVHLIEEPVAAAIGADLPVDEPVANVVV-DIGGGTTEVAIIS-----FGGVVSCHSIRIGGDQLD----ED 188
|
250
....*....|
gi 334182408 276 FIKLVKKKYN 285
Cdd:PRK13929 189 IVSFVRKKYN 198
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
179-285 |
9.43e-07 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 51.24 E-value: 9.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 179 VITVPAYFNDAQRQATKDAGAIAGLNVVRIINEPTGAAIAYGLDKKGGESNILVyDLGGGTFDVSILTIdNGVfeVLSTS 258
Cdd:PRK13927 100 VICVPSGITEVERRAVRESALGAGAREVYLIEEPMAAAIGAGLPVTEPTGSMVV-DIGGGTTEVAVISL-GGI--VYSKS 175
|
90 100
....*....|....*....|....*..
gi 334182408 259 gdTHLGGEDFDHRVMDYfiklVKKKYN 285
Cdd:PRK13927 176 --VRVGGDKFDEAIINY----VRRNYN 196
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
159-245 |
3.32e-06 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 49.06 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 159 ILTKMKETAEAFLGKKIKDAVITVPAyfndaqrqAT--KDAGAI------AGLNVVRIINEPTGAAIAYGLDkkggesNI 230
Cdd:PRK15080 72 IVRRLKATLEEKLGRELTHAATAIPP--------GTseGDPRAIinvvesAGLEVTHVLDEPTAAAAVLGID------NG 137
|
90
....*....|....*
gi 334182408 231 LVYDLGGGTFDVSIL 245
Cdd:PRK15080 138 AVVDIGGGTTGISIL 152
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
43-293 |
1.05e-05 |
|
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466825 [Multi-domain] Cd Length: 263 Bit Score: 47.52 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 43 IGIDLGTTYSCVgVYHNKHVEII----------ANDQGNRITPSWVAFTDTERLIGEAAKNQAAKNPERTIFDPKR---- 108
Cdd:cd10227 1 IGIDIGNGNTKV-VTGGGKEFKFpsavaearesSLDDGLLEDDIIVEYNGKRYLVGELALREGGGGRSTGDDKKKSedal 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 109 -----LIGRKFDDPDVQRDIKF-LPYKVVNKDGKPYIQVKVKGEEKLfspeeisamiltkmketaeaflgkkikdavitv 182
Cdd:cd10227 80 llllaALALLGDDEEVDVNLVVgLPISEYKEEKKELKKKLLKGLHEF--------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 183 paYFNDAQRQATkdagaiagLNVVRIINEPTGAAIAYGLDKKGGES-NILVYDLGGGTfdVSILTIDNGvfEVLSTSGDT 261
Cdd:cd10227 127 --TFNGKERRIT--------INDVKVLPEGAGAYLDYLLDDDELEDgNVLVIDIGGGT--TDILTFENG--KPIEESSDT 192
|
250 260 270
....*....|....*....|....*....|..
gi 334182408 262 HLGGEDFDHRVMDYFIKLVKKKYNKDISKDHK 293
Cdd:cd10227 193 LPGGEEALEKYADDILNELLKKLGDELDSADK 224
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
177-286 |
2.68e-05 |
|
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: 44.38 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 177 DAVITVPAYFNDAQRQAT-----------KDAGAIAGLNVVRIINEPTGAAIAYGLDKkgGESNILVYDLGGGTfdvsil 245
Cdd:cd00012 15 PIVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGALLTL--GPEGLLVVDLGGGT------ 86
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 334182408 246 tidNGVFEVLSTSGDTHLggEDFDHRVMDYFIKLVKKKYNK 286
Cdd:cd00012 87 ---DISANVVLVGGGARN--NGLAKRLKELLLFRGGLKVVK 122
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
355-418 |
3.32e-05 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 46.75 E-value: 3.32e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334182408 355 ALKDAGLKksdIDEIVLVGGSTRIPKVQQMLKDFFDgkEPSKGTNPDEAVAYGAAVQGGVLSGE 418
Cdd:COG1070 388 ALEEAGVK---IDRIRATGGGARSPLWRQILADVLG--RPVEVPEAEEGGALGAALLAAVGLGL 446
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
355-417 |
4.33e-04 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 43.31 E-value: 4.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334182408 355 ALKDAGLKksdIDEIVLVGGSTRIPKVQQMLKDFFDgkEPSKGTNPDEAVAYGAAVQGGVLSG 417
Cdd:cd07809 386 ILRELGVE---IDEIRLIGGGSKSPVWRQILADVFG--VPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_ParM_R1-like |
cd24022 |
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and ... |
215-409 |
7.65e-04 |
|
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and similar proteins from ParM domain family; Type II plasmid partition systems utilize ParM NTPases in coordination with a centromere-binding protein called ParR to mediate accurate DNA segregation, a process critical for plasmid retention. The family corresponds to a group of uncharacterized proteins similar to Escherichia coli ParM, also called ParA locus 36 kDa protein, or protein StbA. It is a plasmid-encoded protein involved in the control of plasmid partition and required for accurate segregation of low-copy-number plasmid R1.
Pssm-ID: 466872 [Multi-domain] Cd Length: 324 Bit Score: 42.26 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 215 AAIAYGLDKKGGESN-------ILVYDLGGGTFDVSILTIDNGVfeVLSTSGDTHLGGEDfdhrVMDYFIKLVKKKYN-K 286
Cdd:cd24022 154 AYFDYLLDEDGNGTDeeeeegpVAVIDIGGTTTDIAVVSGGLSI--DHARSGTIELGVLD----VRDALKDALKKRFGlS 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 287 DISkdhkalgklRRECELAKRSLSNQHQVRVEieslfdgVDFSEPLTRARFEelnmdLFKKTMEPVKKALKDAglkkSDI 366
Cdd:cd24022 228 SIS---------DAELDRALRTGKFRLNGGKE-------VDVSDLVNEAIAE-----VAERILNEIKRRLGDA----SDL 282
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 334182408 367 DEIVLVGGSTRIpkVQQMLKDFFdGKEPSKGTNPDEAVAYGAA 409
Cdd:cd24022 283 DRVIFVGGGAEL--LEDELKEAL-GPNAIIVDEPEFANARGML 322
|
|
| ASKHA_NBD_ScArp9-like |
cd10208 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ... |
203-379 |
2.12e-03 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and similar proteins; Saccharomyces cerevisiae Arp9, also called actin-like protein 9, chromatin structure-remodeling complex protein ARP9, or SWI/SNF complex component ARP9, is a component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. It is also part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, which is required for the positive and negative regulation of gene expression of many genes. Arp9 forms a stable heterodimer with Arp7 protein in both the RSC and SWI/SNF chromatin-remodeling complexes. It has been suggested that this dimer functions as a module with DNA bending proteins, to achieve correct architecture and facilitate complex-complex interactions. Fission yeast SWI/SNF and RSC complexes do not contain Arp7 and Arp8, but instead contain Arp9 and Arp42.
Pssm-ID: 466814 Cd Length: 356 Bit Score: 40.75 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 203 LNV--VRIINEPTGAAIAYGLdkkggeSNILVYDLGGGTFDVSILtIDNGVfeVLSTSGDTHLGGEDFDhrvmDYFIKLV 280
Cdd:cd10208 97 LNVpaFAILEAPLAALYAAGA------TSGIVVDIGHEKTDITPI-VDSQV--VPHALVSIPIGGQDCT----AHLAQLL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 281 KKKYNKDISKDHKALGKLRRECELAKRSlsnqHQVRVEIES--LFDGVDFSEPLTRARFEElnmDLFKKTMEPVKKALKD 358
Cdd:cd10208 164 KSDEPELKSQAESGEEATLDLAEALKKS----PICEVLSDGadLASGTEITVGKERFRACE---PLFKPSSLRVDLLIAA 236
|
170 180 190
....*....|....*....|....*....|...
gi 334182408 359 AGL-----------KKSDI-DEIVLVGGSTRIP 379
Cdd:cd10208 237 IAGalvlnasdepdKRPALwENIIIVGGGSRIR 269
|
|
| ASKHA_NBD_ParM_Psk41-like |
cd24021 |
nucleotide-binding domain (NBD) of Staphylococcus aureus pSK41 actin-like ParM protein and ... |
206-407 |
2.84e-03 |
|
nucleotide-binding domain (NBD) of Staphylococcus aureus pSK41 actin-like ParM protein and similar proteins from the ParM domain family; Type II plasmid partition systems utilize ParM NTPases in coordination with a centromere-binding protein called ParR to mediate accurate DNA segregation, a process critical for plasmid retention. The family corresponds to a group of uncharacterized proteins similar to Staphylococcus aureus pSK41 actin-like ParM protein, which is functionally homologous to R1 ParM, a known actin homologue, suggesting that it may also form filaments to drive partition. However, pSK41 ParM shows the strongest structural homology to the archaeal actin-like protein Thermoplasma acidophilum Ta0583, but not R1 ParM.
Pssm-ID: 466871 [Multi-domain] Cd Length: 298 Bit Score: 40.35 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 206 VRIINEPTGAAIAYGLDKKGG-------ESNILVYDLGGGTFDVSIltIDNGVFEVLSTSGDThlggedfdhrVMDYFIK 278
Cdd:cd24021 150 VYVIPQPLGTLYNLLLDENGEvkneeleDSKVLIIDIGGGTTDVDV--INGLKIDENRFQIET----------GMKDVYD 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182408 279 LVKKKynkdiskdhkalgklrrecelakrslsnqhqvrveieslfdgvDFSEPLTRArfeelnmdlFKKTMEPVKKALKD 358
Cdd:cd24021 218 EIAKE-------------------------------------------DITEIVEKA---------IEEYAEEIVAEINN 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 334182408 359 AGLKKSDIDEIVLVGGSTRIpkVQQMLKDFFDGKEPSKGTNPDEAVAYG 407
Cdd:cd24021 246 AFKDLDSFDKVIFTGGGANI--LNKYLKEKLEGDNFVFVENPQTANVRG 292
|
|
| |
