|
Name |
Accession |
Description |
Interval |
E-value |
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
1-615 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 1074.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 1 MALLQIAEPGQSSAPHEHRIAIGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYGNDVTHYGEEAKPFIIADPKN 80
Cdd:PRK05183 1 MALLQISEPGQSAAPHQRRLAVGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 81 TIVSVKRFMGRSKADIK---FQHPYELVGSENEMPAFETRSGRKTPVEISAEILKQLKERAESSLQNPVNGAVITVPAYF 157
Cdd:PRK05183 81 TISSVKRFMGRSLADIQqryPHLPYQFVASENGMPLIRTAQGLKSPVEVSAEILKALRQRAEETLGGELDGAVITVPAYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 158 DEAQRQATRDAAQLAGLNVLRLLNEPTAAAVAYGLDQetnlATDHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTAL 237
Cdd:PRK05183 161 DDAQRQATKDAARLAGLNVLRLLNEPTAAAIAYGLDS----GQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 238 GGDDLDRLIVKWAKKQLNIDT-LSDENYAVFIVAARQAKEQLSTQESVQLKLLENVLTLDRSTFESIIQVALDKTISVCK 316
Cdd:PRK05183 237 GGDDFDHLLADWILEQAGLSPrLDPEDQRLLLDAARAAKEALSDADSVEVSVALWQGEITREQFNALIAPLVKRTLLACR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 317 RVLRDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASITANQLIGN-SQDGSLLLDVTPLSL 395
Cdd:PRK05183 317 RALRDAGVEADEVKEVVMVGGSTRVPLVREAVGEFFGRTPLTSIDPDKVVAIGAAIQADILAGNkPDSDMLLLDVIPLSL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 396 GLETMGGLVERLISRNTAIPVARRQEFTTYQDGQTAMLIHVVQGERDLVEHCRSLGRFVLHGIPPMTAGQARIEVTFQVD 475
Cdd:PRK05183 397 GLETMGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVD 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 476 ADGLLTVSARETTSGVQAQIDIKPSYGLSESDTERLLIEGFQHAEEDKNLRHLKETKVEAQRELEALEQALKVDADLLNA 555
Cdd:PRK05183 477 ADGLLSVTAMEKSTGVEASIQVKPSYGLTDDEIARMLKDSMSHAEEDMQARALAEQKVEAERVLEALQAALAADGDLLSA 556
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 556 EQLEALKTAENMLKVQLDGNDIQAIEKSVEQLKVHSDAFAALRMNRHIDHALKGTKLEDW 615
Cdd:PRK05183 557 AERAAIDAAMAALREVAQGDDADAIEAAIKALDKATQEFAARRMDRSIRRALAGHSVDEI 616
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
21-614 |
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: 936.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 21 AIGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYGNDVT-HYGEEAKPFIIADPKNTIVSVKRFMGRSKADIK-- 97
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYLKDGGvEVGKEALAAAAEDPKNTISSVKRLMGRSIEDIKtf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 98 FQHPYELVGSENEMPAFETRSGRKTPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLAGLNVL 177
Cdd:TIGR01991 81 SILPYRFVDGPGEMVRLRTVQGTVTPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARLAGLNVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 178 RLLNEPTAAAVAYGLDQetnlATDHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKWAKKQLNID 257
Cdd:TIGR01991 161 RLLNEPTAAAVAYGLDK----ASEGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWILKQLGIS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 258 T-LSDENYAVFIVAARQAKEQLSTQESVQLKLLEN----VLTLDRSTFESIIQVALDKTISVCKRVLRDAKLELSDIQNV 332
Cdd:TIGR01991 237 AdLNPEDQRLLLQAARAAKEALTDAESVEVDFTLDgkdfKGKLTRDEFEALIQPLVQKTLSICRRALRDAGLSVEEIKGV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 333 VLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASITANQLIGNSQDG-SLLLDVTPLSLGLETMGGLVERLISRN 411
Cdd:TIGR01991 317 VLVGGSTRMPLVRRAVAELFGQEPLTDIDPDQVVALGAAIQADLLAGNRIGNdLLLLDVTPLSLGIETMGGLVEKIIPRN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 412 TAIPVARRQEFTTYQDGQTAMLIHVVQGERDLVEHCRSLGRFVLHGIPPMTAGQARIEVTFQVDADGLLTVSARETTSGV 491
Cdd:TIGR01991 397 TPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDADGLLTVSAQEQSTGV 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 492 QAQIDIKPSYGLSESDTERLLIEGFQHAEEDKNLRHLKETKVEAQRELEALEQALKVDADLLNAEQLEALKTAENMLKVQ 571
Cdd:TIGR01991 477 EQSIQVKPSYGLSDEEIERMLKDSFKHAEEDMYARALAEQKVEAERILEALQAALAADGDLLSEDERAAIDAAMEALQKA 556
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 488046570 572 LDGNDIQAIEKSVEQLKVHSDAFAALRMNRHIDHALKGTKLED 614
Cdd:TIGR01991 557 LQGDDADAIKAAIEALEEATDNFAARRMDRGIRKALAGRSLDE 599
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
21-498 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 615.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 21 AIGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYGNDVTH-YGEEAKPFIIADPKNTIVSVKRFMGRSKADIkfq 99
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPKDGEVlVGEAAKRQAVTNPGRTIRSIKRLLGRSLFDE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 100 hpyelvgsenempAFETRSGRKTPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLAGLNVLRL 179
Cdd:COG0443 78 -------------ATEVGGKRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARIAGLEVLRL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 180 LNEPTAAAVAYGLDQETnlaTDHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKWAKKQLNIDT- 258
Cdd:COG0443 145 LNEPTAAALAYGLDKGK---EEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPEFGKEEg 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 259 --LSDENYAVFIV--AARQAKEQLSTQESVQLKLLEN-----VLTLDRSTFESIIQVALDKTISVCKRVLRDAKLELSDI 329
Cdd:COG0443 222 idLRLDPAALQRLreAAEKAKIELSSADEAEINLPFSggkhlDVELTRAEFEELIAPLVERTLDPVRQALADAGLSPSDI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 330 QNVVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASITANQLIGNSQDgsllLDVTPLSLGLETMGGLVERLIS 409
Cdd:COG0443 302 DAVLLVGGSTRMPAVRERVKELFGKEPLKGVDPDEAVALGAAIQAGVLAGDVKD----LDVTPLSLGIETLGGVFTKLIP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 410 RNTAIPVARRQEFTTYQDGQTAMLIHVVQGERDLVEHCRSLGRFVLHGIPPMTAGQARIEVTFQVDADGLLTVSARETTS 489
Cdd:COG0443 378 RNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGILSVSAKDLGT 457
|
....*....
gi 488046570 490 GVQAQIDIK 498
Cdd:COG0443 458 GKEQSITIK 466
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
21-599 |
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: 598.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 21 AIGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYGNDVTHYGEEAKPFIIADPKNTIVSVKRFMGRSKADIKFQH 100
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 101 -----PYELVGSENEMPAFETRSGRK--TPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLAG 173
Cdd:pfam00012 81 dikhlPYKVVKLPNGDAGVEVRYLGEtfTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 174 LNVLRLLNEPTAAAVAYGLDQETnlaTDHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKW---- 249
Cdd:pfam00012 161 LNVLRIVNEPTAAALAYGLDKTD---KERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHlaee 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 250 AKKQLNIDtLSDENYAV--FIVAARQAKEQLS-TQESVQLKL-------LENVLTLDRSTFESIIQVALDKTISVCKRVL 319
Cdd:pfam00012 238 FKKKYGID-LSKDKRALqrLREAAEKAKIELSsNQTNINLPFitamadgKDVSGTLTRAKFEELVADLFERTLEPVEKAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 320 RDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASITANQLIGNSQ-DGSLLLDVTPLSLGLE 398
Cdd:pfam00012 317 KDAGLSKSEIDEVVLVGGSTRIPAVQELVKEFFGKEPSKGVNPDEAVAIGAAVQAGVLSGTFDvKDFLLLDVTPLSLGIE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 399 TMGGLVERLISRNTAIPVARRQEFTTYQDGQTAMLIHVVQGERDLVEHCRSLGRFVLHGIPPMTAGQARIEVTFQVDADG 478
Cdd:pfam00012 397 TLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDANG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 479 LLTVSARETTSGVQAQIDIKPSYGLSESDTERLLIEGFQHAEEDKNLRHLKETKVEAQRELEALEQALKVDADLLNAEQL 558
Cdd:pfam00012 477 ILTVSAKDKGTGKEQEITIEASEGLSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGDKVPEAEK 556
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 488046570 559 EALKTAENMLKVQLDGNDIQAIEKSVEQLKVHSDAFAALRM 599
Cdd:pfam00012 557 SKVESAIEWLKDELEGDDKEEIEAKTEELAQVSQKIGERMY 597
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
18-379 |
0e+00 |
|
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: 595.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 18 HRIAIGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYG-NDVTHYGEEAKPFIIADPKNTIVSVKRFMGRSKADI 96
Cdd:cd10236 1 HRLAVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGeDGKITVGEKAKENAITDPENTISSVKRLMGRSLADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 97 KF---QHPYELVGSENEMPAFETRSGRKTPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLAG 173
Cdd:cd10236 81 KEelpLLPYRLVGDENELPRFRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 174 LNVLRLLNEPTAAAVAYGLDQEtnlaTDHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKWAKKQ 253
Cdd:cd10236 161 LNVLRLLNEPTAAALAYGLDQK----KEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWILKQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 254 LNID-TLSDENYAVFIVAARQAKEQLSTQESVQLKLLENVL----TLDRSTFESIIQVALDKTISVCKRVLRDAKLELSD 328
Cdd:cd10236 237 IGIDaRLDPAVQQALLQAARRAKEALSDADSASIEVEVEGKdwerEITREEFEELIQPLVKRTLEPCRRALKDAGLEPAD 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 488046570 329 IQNVVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASITANQLIG 379
Cdd:cd10236 317 IDEVVLVGGSTRIPLVRQRVAEFFGREPLTSINPDEVVALGAAIQADILAG 367
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
21-596 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 590.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 21 AIGIDLGTTHSLVATVLSGKPKVL-NDEKERrLLPSIVHYGND----VthyGEEAKPFIIADPKNTIVSVKRFMGRS--- 92
Cdd:PRK00290 4 IIGIDLGTTNSCVAVMEGGEPKVIeNAEGAR-TTPSVVAFTKDgerlV---GQPAKRQAVTNPENTIFSIKRLMGRRdee 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 93 -KADIKfQHPYELVGSENEMPAFETRsGRK-TPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQ 170
Cdd:PRK00290 80 vQKDIK-LVPYKIVKADNGDAWVEID-GKKyTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDAGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 171 LAGLNVLRLLNEPTAAAVAYGLDQETnlatDHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKWA 250
Cdd:PRK00290 158 IAGLEVLRIINEPTAAALAYGLDKKG----DEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 251 ----KKQLNIDtLSDENYAV--FIVAARQAKEQLSTQESVQLKL----------LENVLTLDRSTFESIIQVALDKTISV 314
Cdd:PRK00290 234 adefKKENGID-LRKDKMALqrLKEAAEKAKIELSSAQQTEINLpfitadasgpKHLEIKLTRAKFEELTEDLVERTIEP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 315 CKRVLRDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASITANQLIGNSQDgSLLLDVTPLS 394
Cdd:PRK00290 313 CKQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLAGDVKD-VLLLDVTPLS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 395 LGLETMGGLVERLISRNTAIPVARRQEFTTYQDGQTAMLIHVVQGERDLVEHCRSLGRFVLHGIPPMTAGQARIEVTFQV 474
Cdd:PRK00290 392 LGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDI 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 475 DADGLLTVSARETTSGVQAQIDIKPSYGLSESDTERLLIEGFQHAEEDKNLRHLKETKVEAQRELEALEQALKVDADLLN 554
Cdd:PRK00290 472 DANGIVHVSAKDKGTGKEQSITITASSGLSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKELGDKVP 551
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 488046570 555 AEQLEALKTAENMLKVQLDGNDIQAIEKSVEQLKVHSDAFAA 596
Cdd:PRK00290 552 ADEKEKIEAAIKELKEALKGEDKEAIKAKTEELTQASQKLGE 593
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
21-595 |
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: 566.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 21 AIGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYGNDV-THYGEEAKPFIIADPKNTIVSVKRFMGRSKADIK-- 97
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNGeRLVGQPAKRQAVTNPENTIYSIKRFMGRRFDEVTee 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 98 -FQHPYELVGSeNEMPAFETRSGRKTPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLAGLNV 176
Cdd:TIGR02350 82 aKRVPYKVVGD-GGDVRVKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAGLEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 177 LRLLNEPTAAAVAYGLDQETNlatDHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKWA----KK 252
Cdd:TIGR02350 161 LRIINEPTAAALAYGLDKSKK---DEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLadefKK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 253 QLNIDtLSDENYAV--FIVAARQAKEQLSTQESVQLKL------------LEnvLTLDRSTFESIIQVALDKTISVCKRV 318
Cdd:TIGR02350 238 EEGID-LSKDKMALqrLKEAAEKAKIELSSVLSTEINLpfitadasgpkhLE--MTLTRAKFEELTADLVERTKEPVRQA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 319 LRDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASITANQLIGNSQDgSLLLDVTPLSLGLE 398
Cdd:TIGR02350 315 LKDAGLSASDIDEVILVGGSTRIPAVQELVKDFFGKEPNKSVNPDEVVAIGAAIQGGVLKGDVKD-VLLLDVTPLSLGIE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 399 TMGGLVERLISRNTAIPVARRQEFTTYQDGQTAMLIHVVQGERDLVEHCRSLGRFVLHGIPPMTAGQARIEVTFQVDADG 478
Cdd:TIGR02350 394 TLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDANG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 479 LLTVSARETTSGVQAQIDIKPSYGLSESDTERLLIEGFQHAEEDKNLRHLKETKVEAQRELEALEQALKVDADLLNAEQL 558
Cdd:TIGR02350 474 ILHVSAKDKGTGKEQSITITASSGLSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAGDKLPAEEK 553
|
570 580 590
....*....|....*....|....*....|....*..
gi 488046570 559 EALKTAENMLKVQLDGNDIQAIEKSVEQLKVHSDAFA 595
Cdd:TIGR02350 554 EKIEKAVAELKEALKGEDVEEIKAKTEELQQALQKLA 590
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
22-594 |
5.05e-169 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 496.58 E-value: 5.05e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYG-NDVTHYGEEAKPFIIADPKNTIVSVKRFMGRSKADIKFQH 100
Cdd:PRK13411 5 IGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGkSGDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDDTEEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 101 ---PYELVGSENEMPAFETRSGRKTPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLAGLNVL 177
Cdd:PRK13411 85 srvPYTCVKGRDDTVNVQIRGRNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAGTIAGLEVL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 178 RLLNEPTAAAVAYGLDQETnlaTDHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKWA----KKQ 253
Cdd:PRK13411 165 RIINEPTAAALAYGLDKQD---QEQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWLvenfQQQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 254 LNIDtLSDENYAVFIV--AARQAKEQLSTQESVQLKL------------LENVLTldRSTFESIIQVALDKTISVCKRVL 319
Cdd:PRK13411 242 EGID-LSQDKMALQRLreAAEKAKIELSSMLTTSINLpfitadetgpkhLEMELT--RAKFEELTKDLVEATIEPMQQAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 320 RDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFN-QEPLCTINPDEVVAIGASITANQLIGNSQDgSLLLDVTPLSLGLE 398
Cdd:PRK13411 319 KDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFGgKQPDRSVNPDEAVALGAAIQAGVLGGEVKD-LLLLDVTPLSLGIE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 399 TMGGLVERLISRNTAIPVARRQEFTTYQDGQTAMLIHVVQGERDLVEHCRSLGRFVLHGIPPMTAGQARIEVTFQVDADG 478
Cdd:PRK13411 398 TLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSFEIDVNG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 479 LLTVSARETTSGVQAQIDIKPSYGLSESDTERLLIEGFQHAEEDKNLRHLKETKVEAQRELEALEQALKVDADLLNAEQL 558
Cdd:PRK13411 478 ILKVSAQDQGTGREQSIRITNTGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKENGELISEELK 557
|
570 580 590
....*....|....*....|....*....|....*.
gi 488046570 559 EALKTAENMLKVQLDGNDIqaiekSVEQLKVHSDAF 594
Cdd:PRK13411 558 QRAEQKVEQLEAALTDPNI-----SLEELKQQLEEF 588
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
22-588 |
3.24e-167 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 490.78 E-value: 3.24e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYG-NDVTHYGEEAKPFIIADPKNTIVSVKRFMGRSKADIK--- 97
Cdd:CHL00094 5 VGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTkKGDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSEISeea 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 98 FQHPYELVGSENEMPAFETRSGRK--TPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLAGLN 175
Cdd:CHL00094 85 KQVSYKVKTDSNGNIKIECPALNKdfSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAGKIAGLE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 176 VLRLLNEPTAAAVAYGLDQETNlatdHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKWA----K 251
Cdd:CHL00094 165 VLRIINEPTAASLAYGLDKKNN----ETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLikefK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 252 KQLNIDtLSDENYAV--FIVAARQAKEQLS--TQESVQL----------KLLENVLTldRSTFESIIQVALDKTISVCKR 317
Cdd:CHL00094 241 KKEGID-LSKDRQALqrLTEAAEKAKIELSnlTQTEINLpfitatqtgpKHIEKTLT--RAKFEELCSDLINRCRIPVEN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 318 VLRDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASITANQLIGNSQDgSLLLDVTPLSLGL 397
Cdd:CHL00094 318 ALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLLGKKPNQSVNPDEVVAIGAAVQAGVLAGEVKD-ILLLDVTPLSLGV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 398 ETMGGLVERLISRNTAIPVARRQEFTTYQDGQTAMLIHVVQGERDLVEHCRSLGRFVLHGIPPMTAGQARIEVTFQVDAD 477
Cdd:CHL00094 397 ETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDIDAN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 478 GLLTVSARETTSGVQAQIDIKPSYGLSESDTERLLIEGFQHAEEDKNLRHLKETKVEAQRELEALEQALKVDADLLNAEQ 557
Cdd:CHL00094 477 GILSVTAKDKGTGKEQSITIQGASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKELKDKISEEK 556
|
570 580 590
....*....|....*....|....*....|.
gi 488046570 558 LEALKTAENMLKVQLDGNDIQAIEKSVEQLK 588
Cdd:CHL00094 557 KEKIENLIKKLRQALQNDNYESIKSLLEELQ 587
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
22-587 |
3.02e-166 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 489.91 E-value: 3.02e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYGND----VthyGEEAKPFIIADPKNTIVSVKRFMGRSKADIK 97
Cdd:PRK13410 5 VGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTKDgellV---GQLARRQLVLNPQNTFYNLKRFIGRRYDELD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 98 ---FQHPYELvgSENEMPAFETRSGRK----TPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQ 170
Cdd:PRK13410 82 pesKRVPYTI--RRNEQGNVRIKCPRLerefAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDAGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 171 LAGLNVLRLLNEPTAAAVAYGLDQETNlatdHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKWA 250
Cdd:PRK13410 160 IAGLEVERILNEPTAAALAYGLDRSSS----QTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 251 KKQL----NIDTLSD-ENYAVFIVAARQAKEQLSTQESVQLKL------------LENvlTLDRSTFESIIQVALDKTIS 313
Cdd:PRK13410 236 AEQFlekeGIDLRRDrQALQRLTEAAEKAKIELSGVSVTDISLpfitatedgpkhIET--RLDRKQFESLCGDLLDRLLR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 314 VCKRVLRDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASITANQLIGNSQDgSLLLDVTPL 393
Cdd:PRK13410 314 PVKRALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLIPREPNQNVNPDEVVAVGAAIQAGILAGELKD-LLLLDVTPL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 394 SLGLETMGGLVERLISRNTAIPVARRQEFTTYQDGQTAMLIHVVQGERDLVEHCRSLGRFVLHGIPPMTAGQARIEVTFQ 473
Cdd:PRK13410 393 SLGLETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 474 VDADGLLTVSARETTSGVQAQIDIKPSYGLSESDTERLLIEGFQHAEEDKNLRHLKETKVEAQRELEALEQALKvDADL- 552
Cdd:PRK13410 473 IDANGILQVSATDRTTGREQSVTIQGASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERRLR-DAALe 551
|
570 580 590
....*....|....*....|....*....|....*....
gi 488046570 553 ----LNAEQLEALKTAENMLKVQLDGNDIQAIEKSVEQL 587
Cdd:PRK13410 552 fgpyFAERQRRAVESAMRDVQDSLEQDDDRELDLAVADL 590
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
1-609 |
4.72e-151 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 448.53 E-value: 4.72e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 1 MALLQIAEPGQSSAPHEHRIAIGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVhygnDVTHYGeeakpFIIADpKN 80
Cdd:PRK01433 1 MQIIEIREPEQADFKQERQIAVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTI----DFTSNN-----FTIGN-NK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 81 TIVSVKRFMGRSKADIK-----FQHPYELVGSENEMPAFETRSGRKTPVEISAEILKQLKERAESSLQNPVNGAVITVPA 155
Cdd:PRK01433 71 GLRSIKRLFGKTLKEILntpalFSLVKDYLDVNSSELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 156 YFDEAQRQATRDAAQLAGLNVLRLLNEPTAAAVAYGLDQETNlatdHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHT 235
Cdd:PRK01433 151 HFNDAARGEVMLAAKIAGFEVLRLIAEPTAAAYAYGLNKNQK----GCYLVYDLGGGTFDVSILNIQEGIFQVIATNGDN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 236 ALGGDDLDRLIVKWA--KKQLNIDTLSDEnyavfivAARQAKEQLSTQESVQlkllENVLTLDRSTFESIIQVALDKTIS 313
Cdd:PRK01433 227 MLGGNDIDVVITQYLcnKFDLPNSIDTLQ-------LAKKAKETLTYKDSFN----NDNISINKQTLEQLILPLVERTIN 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 314 VCKRVLRDAKLElsDIQNVVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASITANQLIGNSQDgSLLLDVTPL 393
Cdd:PRK01433 296 IAQECLEQAGNP--NIDGVILVGGATRIPLIKDELYKAFKVDILSDIDPDKAVVWGAALQAENLIAPHTN-SLLIDVVPL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 394 SLGLETMGGLVERLISRNTAIPVARRQEFTTYQDGQTAMLIHVVQGERDLVEHCRSLGRFVLHGIPPMTAGQARIEVTFQ 473
Cdd:PRK01433 373 SLGMELYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFA 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 474 VDADGLLTVSARETTSGVQAQIDIKPSYGLSESDTERLLIEGFQHAEEDKNLRHLKETKVEAQRELEALEQALKVDADLL 553
Cdd:PRK01433 453 IDADGILSVSAYEKISNTSHAIEVKPNHGIDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAIAELTTLL 532
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 488046570 554 NAEQLEALKTAENMLKVQLDGNDIQAIEKSVEQLKVHSDAFAALRMNRHIDHALKG 609
Cdd:PRK01433 533 SESEISIINSLLDNIKEAVHARDIILINNSIKEFKSKIKKSMDTKLNIIINDLLKG 588
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
22-588 |
9.02e-151 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 450.46 E-value: 9.02e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYG-NDVTHYGEEAKPFIIADPKNTIVSVKRFMGRSKADI---K 97
Cdd:PLN03184 42 VGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTkNGDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSEVdeeS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 98 FQHPYELVGSENEMPAFETRSGRKT--PVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLAGLN 175
Cdd:PLN03184 122 KQVSYRVVRDENGNVKLDCPAIGKQfaAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRIAGLE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 176 VLRLLNEPTAAAVAYGLDQETNlatdHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKWA----K 251
Cdd:PLN03184 202 VLRIINEPTAASLAYGFEKKSN----ETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLasnfK 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 252 KQLNIDTLSDENYAVFIV-AARQAKEQLS--TQESVQLKLLENV--------LTLDRSTFESIIQVALDKTISVCKRVLR 320
Cdd:PLN03184 278 KDEGIDLLKDKQALQRLTeAAEKAKIELSslTQTSISLPFITATadgpkhidTTLTRAKFEELCSDLLDRCKTPVENALR 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 321 DAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASITANQLIGNSQDgSLLLDVTPLSLGLETM 400
Cdd:PLN03184 358 DAKLSFKDIDEVILVGGSTRIPAVQELVKKLTGKDPNVTVNPDEVVALGAAVQAGVLAGEVSD-IVLLDVTPLSLGLETL 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 401 GGLVERLISRNTAIPVARRQEFTTYQDGQTAMLIHVVQGERDLVEHCRSLGRFVLHGIPPMTAGQARIEVTFQVDADGLL 480
Cdd:PLN03184 437 GGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFDIDANGIL 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 481 TVSARETTSGVQAQIDIKPSYGLSESDTERLLIEGFQHAEEDKNLRHLKETKVEAQRELEALEQALKVDADLLNAEQLEA 560
Cdd:PLN03184 517 SVSATDKGTGKKQDITITGASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKELGDKVPADVKEK 596
|
570 580
....*....|....*....|....*...
gi 488046570 561 LKTAENMLKVQLDGNDIQAIEKSVEQLK 588
Cdd:PLN03184 597 VEAKLKELKDAIASGSTQKMKDAMAALN 624
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
22-588 |
1.25e-150 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 449.66 E-value: 1.25e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYGNDVTHY-GEEAKPFIIADPKNTIVSVKRFMGR------SKA 94
Cdd:PTZ00400 44 VGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDGQRLvGIVAKRQAVTNPENTVFATKRLIGRrydedaTKK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 95 DiKFQHPYELVGSENEMPAFETRSGRKTPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLAGL 174
Cdd:PTZ00400 124 E-QKILPYKIVRASNGDAWIEAQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAGKIAGL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 175 NVLRLLNEPTAAAVAYGLDQetnlATDHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKWA---- 250
Cdd:PTZ00400 203 DVLRIINEPTAAALAFGMDK----NDGKTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYLiaef 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 251 KKQLNIDtLSDENYAV--FIVAARQAKEQLS--TQESVQL----------KLLEnvLTLDRSTFESIIQVALDKTISVCK 316
Cdd:PTZ00400 279 KKQQGID-LKKDKLALqrLREAAETAKIELSskTQTEINLpfitadqsgpKHLQ--IKLSRAKLEELTHDLLKKTIEPCE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 317 RVLRDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASITANQLIGNSQDgSLLLDVTPLSLG 396
Cdd:PTZ00400 356 KCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIFGKEPSKGVNPDEAVAMGAAIQAGVLKGEIKD-LLLLDVTPLSLG 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 397 LETMGGLVERLISRNTAIPVARRQEFTTYQDGQTAMLIHVVQGERDLVEHCRSLGRFVLHGIPPMTAGQARIEVTFQVDA 476
Cdd:PTZ00400 435 IETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTFDVDA 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 477 DGLLTVSARETTSGVQAQIDIKPSYGLSESDTERLLIEGFQHAEEDKNLRHLKETKVEAQRELEALEQALKVDADLLNAE 556
Cdd:PTZ00400 515 NGIMNISAVDKSTGKKQEITIQSSGGLSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSDLKDKISDA 594
|
570 580 590
....*....|....*....|....*....|..
gi 488046570 557 QLEALKTAENMLKVQLDGNDIQAIEKSVEQLK 588
Cdd:PTZ00400 595 DKDELKQKITKLRSTLSSEDVDSIKDKTKQLQ 626
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
22-566 |
1.15e-145 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 436.81 E-value: 1.15e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYGNDVTHYGEEAKPFIIADPKNTIVSVKRFMGRSKADIKFQH- 100
Cdd:PTZ00186 30 IGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEHIQKd 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 101 ----PYELVGSENEMPAFETRSGRK-TPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLAGLN 175
Cdd:PTZ00186 110 iknvPYKIVRAGNGDAWVQDGNGKQySPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTIAGLN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 176 VLRLLNEPTAAAVAYGLDQetnlATDHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLD----RLIVKWAK 251
Cdd:PTZ00186 190 VIRVVNEPTAAALAYGMDK----TKDSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDlalsDYILEEFR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 252 KQLNIDtLSDENYAVFIV--AARQAKEQLSTQESVQLKL---------LENV-LTLDRSTFESIIQVALDKTISVCKRVL 319
Cdd:PTZ00186 266 KTSGID-LSKERMALQRVreAAEKAKCELSSAMETEVNLpfitanadgAQHIqMHISRSKFEGITQRLIERSIAPCKQCM 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 320 RDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASITANQLIGNSQdGSLLLDVTPLSLGLET 399
Cdd:PTZ00186 345 KDAGVELKEINDVVLVGGMTRMPKVVEEVKKFFQKDPFRGVNPDEAVALGAATLGGVLRGDVK-GLVLLDVTPLSLGIET 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 400 MGGLVERLISRNTAIPVARRQEFTTYQDGQTAMLIHVVQGERDLVEHCRSLGRFVLHGIPPMTAGQARIEVTFQVDADGL 479
Cdd:PTZ00186 424 LGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDIDANGI 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 480 LTVSARETTSGVQAQIDIKPSYGLSESDTERLLIEGFQHAEEDKNLRHLKETKVEAQRELEALEQALK-----VDADLLN 554
Cdd:PTZ00186 504 CHVTAKDKATGKTQNITITANGGLSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGewkyvSDAEKEN 583
|
570
....*....|....
gi 488046570 555 AEQL--EALKTAEN 566
Cdd:PTZ00186 584 VKTLvaELRKAMEN 597
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
21-586 |
3.88e-139 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 419.97 E-value: 3.88e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 21 AIGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYGNDVTHYGEEAKPFIIADPKNTIVSVKRFMGRSKADIKFQH 100
Cdd:PTZ00009 6 AIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDSVVQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 101 -----PYELVGSENEMPAFE-TRSGRK---TPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQL 171
Cdd:PTZ00009 86 dmkhwPFKVTTGGDDKPMIEvTYQGEKktfHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAGTI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 172 AGLNVLRLLNEPTAAAVAYGLDQETNlaTDHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKWA- 250
Cdd:PTZ00009 166 AGLNVLRIINEPTAAAIAYGLDKKGD--GEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEFCv 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 251 ---KKQLNIDTLSDENYAV--FIVAARQAKEQLS--TQESVQL-KLLENV---LTLDRSTFESIIQVALDKTISVCKRVL 319
Cdd:PTZ00009 244 qdfKRKNRGKDLSSNQRALrrLRTQCERAKRTLSssTQATIEIdSLFEGIdynVTISRARFEELCGDYFRNTLQPVEKVL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 320 RDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFN-QEPLCTINPDEVVAIGASITANQLIGNSQ---DGSLLLDVTPLSL 395
Cdd:PTZ00009 324 KDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNgKEPCKSINPDEAVAYGAAVQAAILTGEQSsqvQDLLLLDVTPLSL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 396 GLETMGGLVERLISRNTAIPVARRQEFTTYQDGQTAMLIHVVQGERDLVEHCRSLGRFVLHGIPPMTAGQARIEVTFQVD 475
Cdd:PTZ00009 404 GLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTFDID 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 476 ADGLLTVSARETTSGVQAQIDIKPSYG-LSESDTERLLIEGFQHAEEDKNLRHlketKVEAQRELEALEQALKvdaDLLN 554
Cdd:PTZ00009 484 ANGILNVSAEDKSTGKSNKITITNDKGrLSKADIDRMVNEAEKYKAEDEANRE----RVEAKNGLENYCYSMK---NTLQ 556
|
570 580 590
....*....|....*....|....*....|..
gi 488046570 555 AEQlealktaenmLKVQLDGNDIQAIEKSVEQ 586
Cdd:PTZ00009 557 DEK----------VKGKLSDSDKATIEKAIDE 578
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
22-374 |
1.51e-130 |
|
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: 386.93 E-value: 1.51e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVATVLSGKPKVL-NDEKERRLLPSIVHYGND-VTHYGEEAKPFIIADPKNTIVSVKRFMGRSkadikFQ 99
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAEVIiENSEGKRTTPSVVYFDKDgEVLVGEEAKNQALLDPENTIYSVKRLMGRD-----TK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 100 HPYELVGSEnempafetrsgrKTPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLAGLNVLRL 179
Cdd:cd24029 76 DKEEIGGKE------------YTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAELAGLNVLRL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 180 LNEPTAAAVAYGLDQETNlatDHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKWAKKQLNIDT- 258
Cdd:cd24029 144 INEPTAAALAYGLDKEGK---DGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEKIGIETg 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 259 -----LSDENYAVFIVAARQAKEQLSTQESVQLKLLENV------LTLDRSTFESIIQVALDKTISVCKRVLRDAKLELS 327
Cdd:cd24029 221 ilddkEDERARARLREAAEEAKIELSSSDSTDILILDDGkggeleIEITREEFEELIAPLIERTIDLLEKALKDAKLSPE 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 488046570 328 DIQNVVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASITA 374
Cdd:cd24029 301 DIDRVLLVGGSSRIPLVREMLEEYFGREPISSVDPDEAVAKGAAIYA 347
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
21-377 |
3.24e-130 |
|
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: 387.25 E-value: 3.24e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 21 AIGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYGNDVTHYGEEAKPFIIADPKNTIVSVKRFMGRSKADIKFQH 100
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 101 -----PYELVGSENEMPAFE-TRSGRK---TPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQL 171
Cdd:cd24028 81 dikhwPFKVVEDEDGKPKIEvTYKGEEktfSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAATI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 172 AGLNVLRLLNEPTAAAVAYGLDQETnlATDHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKWA- 250
Cdd:cd24028 161 AGLNVLRIINEPTAAALAYGLDKKS--SGERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLv 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 251 ---KKQLNIDtLSDENYAVFI--VAARQAKEQLSTQES--VQLKLLENV----LTLDRSTFESIIQVALDKTISVCKRVL 319
Cdd:cd24028 239 eefKKKHGKD-LRENPRAMRRlrSACERAKRTLSTSTSatIEIDSLYDGidfeTTITRAKFEELCEDLFKKCLEPVEKVL 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 488046570 320 RDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFNQEPLC-TINPDEVVAIGASITANQL 377
Cdd:cd24028 318 KDAKLSKDDIDEVVLVGGSTRIPKIQELLSEFFGGKELCkSINPDEAVAYGAAIQAAIL 376
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
22-377 |
6.87e-127 |
|
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: 378.36 E-value: 6.87e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVATVLSGKPKVL-NDEKERrLLPSIVHYGND----VthyGEEAKPFIIADPKNTIVSVKRFMGRSKADI 96
Cdd:cd10234 2 IGIDLGTTNSCVAVMEGGKPTVIpNAEGGR-TTPSVVAFTKDgerlV---GQPAKRQAVTNPENTIFSIKRFMGRRYKEV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 97 KFQH---PYELVGSENEMPAFETRSGRKTPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLAG 173
Cdd:cd10234 78 EVERkqvPYPVVSAGNGDAWVEIGGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 174 LNVLRLLNEPTAAAVAYGLDQETNlatdHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKWA--- 250
Cdd:cd10234 158 LEVLRIINEPTAAALAYGLDKKKD----EKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLade 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 251 -KKQLNIDtLSDENYAV--FIVAARQAKEQLSTQESVQLKL------------LEnvLTLDRSTFESIIQVALDKTISVC 315
Cdd:cd10234 234 fKKEEGID-LSKDKMALqrLKEAAEKAKIELSSVLETEINLpfitadasgpkhLE--MKLTRAKFEELTEDLVERTIEPV 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488046570 316 KRVLRDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASITANQL 377
Cdd:cd10234 311 EQALKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVL 372
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
22-372 |
9.34e-109 |
|
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: 331.92 E-value: 9.34e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVAtVLSGK-PKVLNDEKERRLLPSIVHYGNDvthyGEE-----AKPFIIADPKNTIVSVKRFMGRS--- 92
Cdd:cd11733 4 IGIDLGTTNSCVA-VMEGKtPKVIENAEGARTTPSVVAFTAD----GERlvgmpAKRQAVTNPENTLYATKRLIGRRfdd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 93 ---KADIKFQhPYELVGSENEMPAFETRSGRKTPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAA 169
Cdd:cd11733 79 pevQKDIKMV-PYKIVKASNGDAWVEAHGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 170 QLAGLNVLRLLNEPTAAAVAYGLDQetnlATDHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKW 249
Cdd:cd11733 158 QIAGLNVLRIINEPTAAALAYGLDK----KDDKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 250 A----KKQLNIDtLSDENYAVFIV--AARQAKEQLS--TQESVQLKLLEN--------VLTLDRSTFESIIQVALDKTIS 313
Cdd:cd11733 234 LvaefKKEQGID-LSKDNLALQRLreAAEKAKIELSssLQTDINLPFITAdasgpkhlNMKLTRAKFESLVGDLIKRTVE 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 488046570 314 VCKRVLRDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASI 372
Cdd:cd11733 313 PCKKCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIFGKAPSKGVNPDEAVAMGAAI 371
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
22-374 |
6.72e-108 |
|
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: 329.94 E-value: 6.72e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYGNDVTHYGEEAKPFIIADPKNTIVSVKRFMGRS------KAD 95
Cdd:cd10241 4 IGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTVFDVKRLIGRKfddkevQKD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 96 IKFqHPYELVgSENEMPAFE--TRSGRKT--PVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQL 171
Cdd:cd10241 84 IKL-LPFKIV-NKNGKPYIQveVKGEKKTfaPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 172 AGLNVLRLLNEPTAAAVAYGLDQETNlatDHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLI----V 247
Cdd:cd10241 162 AGLNVLRIINEPTAAAIAYGLDKKGG---EKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVmdhfI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 248 KWAKKQLNIDtLSDENYAV--FIVAARQAKEQLSTQESVQLKlLENVL-------TLDRSTFESIIQVALDKTISVCKRV 318
Cdd:cd10241 239 KLFKKKTGKD-ISKDKRAVqkLRREVEKAKRALSSQHQARIE-IESLFdgedfseTLTRAKFEELNMDLFRKTLKPVQKV 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 488046570 319 LRDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFN-QEPLCTINPDEVVAIGASITA 374
Cdd:cd10241 317 LEDAGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFNgKEPSRGINPDEAVAYGAAVQA 373
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
22-374 |
7.82e-103 |
|
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: 315.34 E-value: 7.82e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYGNDVTHY-GEEAKPFIIADPKNTIVSVKRFMGRSKadikfqh 100
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVDEDGSILvGRAAKERLVTHPDRTAASFKRFMGTDK------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 101 PYELvgsenempafetrsGRKT--PVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLAGLNVLR 178
Cdd:cd10235 74 QYRL--------------GNHTfrAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELAGLKVER 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 179 LLNEPTAAAVAYGLDQEtnlATDHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKWA--KKQLNI 256
Cdd:cd10235 140 LINEPTAAALAYGLHKR---EDETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFlkKHRLDF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 257 DTLSDENYAVFIVAARQAKEQLSTQESVQLKLL----ENVLTLDRSTFESIIQVALDKTISVCKRVLRDAKLELSDIQNV 332
Cdd:cd10235 217 TSLSPSELAALRKRAEQAKRQLSSQDSAEIRLTyrgeELEIELTREEFEELCAPLLERLRQPIERALRDAGLKPSDIDAV 296
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 488046570 333 VLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASITA 374
Cdd:cd10235 297 ILVGGATRMPLVRQLIARLFGRLPLSSLDPDEAVALGAAIQA 338
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
21-379 |
6.93e-99 |
|
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: 306.68 E-value: 6.93e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 21 AIGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYGNDVTHY-GEEAKPFIIADPKNTIVSVKRFMGRS------K 93
Cdd:cd11734 3 VIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTKDGERLvGVPAKRQAVVNPENTLFATKRLIGRKfddaevQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 94 ADIKfQHPYELVGSENEMPAFETRSGRKTPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLAG 173
Cdd:cd11734 83 RDIK-EVPYKIVKHSNGDAWVEARGQKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAGQIAG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 174 LNVLRLLNEPTAAAVAYGLDQEtnlaTDHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLD----RLIVKW 249
Cdd:cd11734 162 LNVLRVINEPTAAALAYGLDKS----GDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDialvRHIVSE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 250 AKKQLNIDtLSDENYAVFIV--AARQAKEQLST--QESVQLKLLEN--------VLTLDRSTFESIIQVALDKTISVCKR 317
Cdd:cd11734 238 FKKESGID-LSKDRMAIQRIreAAEKAKIELSStlQTDINLPFITAdasgpkhiNMKLTRAQFESLVKPLVDRTVEPCKK 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488046570 318 VLRDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASITANQLIG 379
Cdd:cd11734 317 ALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIFGREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
21-374 |
6.67e-96 |
|
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: 298.77 E-value: 6.67e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 21 AIGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYGNDVTHYGEEAKPFIIADPKNTIVSVKRFMGRSKADIKFQH 100
Cdd:cd10233 1 AIGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 101 -----PYELV-GSENEMPAFETRSGRKT--PVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLA 172
Cdd:cd10233 81 dmkhwPFKVVsGGDKPKIQVEYKGETKTftPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 173 GLNVLRLLNEPTAAAVAYGLDQetNLATDHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKWA-- 250
Cdd:cd10233 161 GLNVLRIINEPTAAAIAYGLDK--KGKGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFvq 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 251 --KKQLNIDtLSDENYAV--FIVAARQAKEQLS--TQESVQL-KLLENV---LTLDRSTFESIIQVALDKTISVCKRVLR 320
Cdd:cd10233 239 efKRKHKKD-ISGNPRALrrLRTACERAKRTLSssTQASIEIdSLFEGIdfyTSITRARFEELCADLFRSTLEPVEKVLR 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 488046570 321 DAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFNQEPLC-TINPDEVVAIGASITA 374
Cdd:cd10233 318 DAKLDKSQIHEIVLVGGSTRIPKVQKLLQDFFNGKELNkSINPDEAVAYGAAVQA 372
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
21-374 |
1.49e-86 |
|
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: 274.55 E-value: 1.49e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 21 AIGIDLGTTHSLVATvLSGKPKVLNDEKERRLLPSIVHYGNDVTHYGEEAKPFIIADPKNTIVSVKRFMGR------SKA 94
Cdd:cd24093 1 AIGIDLGTTYSCVAT-YESSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRrfddesVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 95 DIKfQHPYELVGSeNEMPAFETRS-GRK---TPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQ 170
Cdd:cd24093 80 DMK-TWPFKVIDV-NGNPVIEVQYlGETktfSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 171 LAGLNVLRLLNEPTAAAVAYGLDQEtNLATDHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKWA 250
Cdd:cd24093 158 IAGLNVLRIINEPTAAAIAYGLGAG-KSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 251 KKQLNIDT---LSDENYAV--FIVAARQAKEQLS--TQESVQLKLLEN----VLTLDRSTFESIIQVALDKTISVCKRVL 319
Cdd:cd24093 237 KAEFKKKTgldISDDARALrrLRTAAERAKRTLSsvTQTTVEVDSLFDgedfESSITRARFEDLNAALFKSTLEPVEQVL 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 488046570 320 RDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFNQEPL-CTINPDEVVAIGASITA 374
Cdd:cd24093 317 KDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLeKSINPDEAVAYGAAVQG 372
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
22-374 |
2.63e-86 |
|
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: 274.99 E-value: 2.63e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVAT--VLSGKPKVLNDEKERRLLPSIVHYGNDVTHY-GEEAKPFIIADPKNTIVSVKRFMGR-----SK 93
Cdd:cd10237 25 VGIDLGTTYSCVGVyhAVTGEVEVIPDDDGHKSIPSVVAFTPDGGVLvGYDALAQAEHNPSNTIYDAKRFIGKtftkeEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 94 ADIKFQHPYELVGSENEMPAFE--TRSGRK--TPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAA 169
Cdd:cd10237 105 EEEAKRYPFKVVNDNIGSAFFEvpLNGSTLvvSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRKAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 170 QLAGLNVLRLLNEPTAAAVAYGLDQETNLatdHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKW 249
Cdd:cd10237 185 NLAGLEVLRVINEPTAAAMAYGLHKKSDV---NNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 250 A----KKQLNIDTLSDENYAVFIVAARQAKEQLSTQESVQLKLLENV-----------LTLDRSTFESIIQVALDKTISV 314
Cdd:cd10237 262 LidriAKKFGKTLTDKEDIQRLRQAVEEVKLNLTNHNSASLSLPLQIslpsafkvkfkEEITRDLFETLNEDLFQRVLEP 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 315 CKRVLRDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASITA 374
Cdd:cd10237 342 IRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFFGKDPNTSVDPELAVVTGVAIQA 401
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
21-374 |
5.47e-77 |
|
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: 249.47 E-value: 5.47e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 21 AIGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYGNDVTHYGEEAKPFIIADPKNTIVSVKRFMGRSKADIKFQH 100
Cdd:cd10238 2 AFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAVQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 101 -----PYELVgSENEMPAFETRSGRK----TPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQL 171
Cdd:cd10238 82 lkkesKCKII-EKDGKPGYEIELEEKkklvSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 172 AGLNVLRLLNEPTAAAVAYGLDQETNLATDHNYViYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKWA- 250
Cdd:cd10238 161 AGFNVLRVISEPSAAALAYGIGQDDPTENSNVLV-YRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHLa 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 251 ---KKQLNIDtLSDENYAV--FIVAARQAKEQLSTQESVQ---------LKLLENVltlDRSTFESIIQVALDKTISVCK 316
Cdd:cd10238 240 sefKRQWKQD-VRENKRAMakLMNAAEVCKHVLSTLNTATcsveslydgMDFQCNV---SRARFESLCSSLFQQCLEPIQ 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 488046570 317 RVLRDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVF-NQEPLCTINPDEVVAIGASITA 374
Cdd:cd10238 316 EVLNSAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFpSAEVLSSIPPDEVIAIGAAKQA 374
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
22-374 |
6.25e-74 |
|
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: 241.69 E-value: 6.25e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYGNDVTHYGEEAKPFIIADPKNTIVSVKRFMGRSKADIKFQH- 100
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQKe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 101 ----PYELVGSENEMPAFE-TRSGRK---TPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLA 172
Cdd:cd11732 81 ikllPFKLVELEDGKVGIEvSYNGEEvvfSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 173 GLNVLRLLNEPTAAAVAYGL--DQETNLATDHNYVIY-DLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKW 249
Cdd:cd11732 161 GLNCLRLINETTAAALDYGIykSDLLESEEKPRIVAFvDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 250 A----KKQLNIDTLSDeNYAVF--IVAARQAKEQLSTQESVQLK---LLENV---LTLDRSTFESIIQVALDKTISVCKR 317
Cdd:cd11732 241 FaeefKKKYKIDPLEN-PKARLrlLDACEKLKKVLSANGEAPLNvecLMEDIdfsGQIKREEFEELIQPLLARLEAPIKK 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 488046570 318 VLRDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASITA 374
Cdd:cd11732 320 ALAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVFGKDLSTTLNADEAVARGCALQA 376
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
22-372 |
9.26e-67 |
|
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: 222.54 E-value: 9.26e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYGNDVTHYGEEAKPFIIADPKNTIVSVKRFMGRSKADIKFQH- 100
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQKe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 101 ----PYELVGSENEMPAFETR-SGRK---TPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLA 172
Cdd:cd10228 81 lkhlPYKVVKLPNGSVGIKVQyLGEEhvfTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 173 GLNVLRLLNEPTAAAVAYG-----LDQETnlATDHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIV 247
Cdd:cd10228 161 GLNCLRLLNDTTAVALAYGiykqdLPAEE--EKPRNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 248 KWAKKQLNidtlsdENYAVFIVAARQAKEQLsTQESVQLKLL------------ENVL-------TLDRSTFESIIQVAL 308
Cdd:cd10228 239 EHFAEEFK------TKYKIDVKSKPRALLRL-LTECEKLKKLmsanatelplniECFMddkdvsgKMKRAEFEELCAPLF 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488046570 309 DKTISVCKRVLRDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASI 372
Cdd:cd10228 312 ARVEVPLRSALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVFGKEPSTTLNQDEAVARGCAL 375
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
20-372 |
2.17e-65 |
|
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: 219.49 E-value: 2.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 20 IAIGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYGNDVTHYGEEAKPFIIADPKNTIVSVKRFMGRSKADIKFQ 99
Cdd:cd24095 2 SVVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 100 H-----PYELVGSENEMPAFETR-SGRK---TPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQ 170
Cdd:cd24095 82 RdlklfPFKVTEGPDGEIGINVNyLGEQkvfTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 171 LAGLNVLRLLNEPTAAAVAYGLDQETNLATD-HNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIV-- 247
Cdd:cd24095 162 IAGLNCLRLMNETTATALAYGIYKTDLPETDpTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFdh 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 248 ---KWAKKQlNIDTLSDENYAVFIVAA-RQAKEQLSTQESVQLK---LLENV---LTLDRSTFESIIQVALDKTISVCKR 317
Cdd:cd24095 242 faaEFKEKY-KIDVKSNKKASLRLRAAcEKVKKILSANPEAPLNiecLMEDKdvkGMITREEFEELAAPLLERLLEPLEK 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 488046570 318 VLRDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASI 372
Cdd:cd24095 321 ALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFFGKEPSRTMNASECVARGCAL 375
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
22-374 |
1.70e-64 |
|
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: 215.82 E-value: 1.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVATVLSGKPK--VLNDEKERRLlPSIVHYGNDVTHYGEEAKPFIIADPKNTIVSVKRFMGrskadikfq 99
Cdd:cd10230 3 LGIDLGSEFIKVALVKPGVPFeiVLNEESKRKT-PSAVAFRNGERLFGDDALALATRFPENTFSYLKDLLG--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 100 hpYelvgsenempafetrsgrkTPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLAGLNVLRL 179
Cdd:cd10230 73 --Y-------------------SVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIAGLNVLSL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 180 LNEPTAAAVAYGLDQETNLATDHNYVIYDLGGGTFDVSILRFSQ------------GVFEVLATGGHTALGGDDLDRLIV 247
Cdd:cd10230 132 INDNTAAALNYGIDRRFENNEPQNVLFYDMGASSTSATVVEFSSvkekdkgknktvPQVEVLGVGWDRTLGGLEFDLRLA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 248 KWA----KKQLNIDTLSDEN---YAVFIVAARQAKEQLS--TQESVQLK-LLENV---LTLDRSTFESIIQVALDKTISV 314
Cdd:cd10230 212 DHLadefNEKHKKDKDVRTNpraMAKLLKEANRVKEVLSanTEAPASIEsLYDDIdfrTKITREEFEELCADLFERVVAP 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488046570 315 CKRVLRDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFNQEPLCT-INPDEVVAIGASITA 374
Cdd:cd10230 292 IEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELGKhLNADEAAALGAAFYA 352
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
20-377 |
2.47e-56 |
|
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: 194.12 E-value: 2.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 20 IAIGIDLGTTHSLVA-TVLSGKPKVLNDEKERRLLPSIVHYGNDVTHYGEEAKPFIIADPKNTIVSVKRFMGRSkadikf 98
Cdd:cd10232 1 VVIGISFGNSNSSIAiINKDGRAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPKNTVANFRDLLGTT------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 99 qhpyelvgsenempafetrsgRKTPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLAGLNVLR 178
Cdd:cd10232 75 ---------------------TLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAAAAGLEVLQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 179 LLNEPTAAAVAYGLDQETNLAT--DHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKWA----KK 252
Cdd:cd10232 134 LIPEPAAAALAYDLRAETSGDTikDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVGHFakefKK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 253 QLNIDTLSD-ENYAVFIVAARQAKEQLSTQESVQLKL------LENVLTLDRSTFESIIQVALDKTISVCKRVLRDAKLE 325
Cdd:cd10232 214 KTKTDPRKNaRSLAKLRNAAEITKRALSQGTSAPCSVesladgIDFHSSINRTRYELLASKVFQQFADLVTDAIEKAGLD 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 488046570 326 LSDIQNVVLVGGSTRSYAVQQAVRNVFNQE----PLCTINPDEVVAIGASITANQL 377
Cdd:cd10232 294 PLDIDEVLLAGGASRTPKLASNFEYLFPEStiirAPTQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
22-371 |
1.58e-55 |
|
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: 192.97 E-value: 1.58e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYGNDVTHYGEEAKPFIIADPKNTIVSVKRFMGRSKADIKFQ-- 99
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAee 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 100 ---HPYELVGSENEMPAFETRSGRKT---PVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLAG 173
Cdd:cd24094 81 ekyFTAKLVDANGEVGAEVNYLGEKHvfsATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 174 LNVLRLLNEPTAAAVAYGLDQeTNLATD----HNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKW 249
Cdd:cd24094 161 LNPLRLMNDTTAAALGYGITK-TDLPEPeekpRIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 250 AKKQLN----IDTLSDENyAVF--IVAARQAKEQLSTQESVQLKlLENVLT-------LDRSTFESIIQVALDKTISVCK 316
Cdd:cd24094 240 FADEFKekykIDVRSNPK-AYFrlLAAAEKLKKVLSANAQAPLN-VESLMNdidvssmLKREEFEELIAPLLERVTAPLE 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 488046570 317 RVLRDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGAS 371
Cdd:cd24094 318 KALAQAGLTKDEIDFVELVGGTTRVPALKESISAFFGKPLSTTLNQDEAVARGAA 372
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
22-372 |
1.93e-54 |
|
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: 190.15 E-value: 1.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYGNDVTHYGEEAKPFIIADPKNTIVSVKRFMGRSKADIKFQH- 100
Cdd:cd11737 3 VGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQAe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 101 ----PYELVgsenEMPAFETrsGRK----------TPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATR 166
Cdd:cd11737 83 kpslAYELV----QLPTGTT--GIKvmymeeernfTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 167 DAAQLAGLNVLRLLNEPTAAAVAYGLDQETNLATDH---NYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLD 243
Cdd:cd11737 157 DATQIAGLNCLRLMNETTAVALAYGIYKQDLPAPEEkprNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 244 RLIVKW----AKKQLNIDTLSDENYAVFIVAARQAKEQLSTQESVQLKL-LENVL-------TLDRSTFESIIQVALDKT 311
Cdd:cd11737 237 EVLVNHfceeFGKKYKLDIKSKIRALLRLFQECEKLKKLMSANASDLPLnIECFMndidvsgTMNRGQFEEMCADLLARV 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488046570 312 ISVCKRVLRDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASI 372
Cdd:cd11737 317 EPPLRSVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFFGKEVSTTLNADEAVARGCAL 377
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
22-372 |
8.29e-51 |
|
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: 180.11 E-value: 8.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYGNDVTHYGEEAKPFIIADPKNTIVSVKRFMGRSKADIKFQH- 100
Cdd:cd11738 3 VGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFVQAe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 101 ----PYELVGSENEMPAFETR---SGRKTPVE-ISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLA 172
Cdd:cd11738 83 kiklPYELQKMPNGSTGVKVRyldEERVFAIEqVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 173 GLNVLRLLNEPTAAAVAYGL---DQETNLATDHNYVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKW 249
Cdd:cd11738 163 GLNCLRLMNETTAVALAYGIykqDLPALEEKPRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVLVDY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 250 ------AKKQLNIdtlsDENYAVFIVAARQAK--EQLSTQESVQLKL--------LENVLTLDRSTFESIIQVALDKTIS 313
Cdd:cd11738 243 fceefkTKYKLNV----KENIRALLRLYQECEklKKLMSANASDLPLniecfmndIDVSSKMNRAQFEELCASLLARVEP 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 488046570 314 VCKRVLRDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASI 372
Cdd:cd11738 319 PLKAVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCAL 377
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
22-370 |
2.58e-49 |
|
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: 174.60 E-value: 2.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVATVLSGKPKVLNDekerrllpsivhygndvthygeeakpfiiadpkntivsvkrfmgrskadIKFQHP 101
Cdd:cd10170 1 VGIDFGTTYSGVAYALLGPGEPPLV-------------------------------------------------VLQLPW 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 102 YELVGSENEMPafetrsgrkTPVEISAEILKQLKERAESSLQNPVNGA-------VITVPAYFDEAQRQATRDAAQLAGL 174
Cdd:cd10170 32 PGGDGGSSKVP---------SVLEVVADFLRALLEHAKAELGDRIWELekapievVITVPAGWSDAAREALREAARAAGF 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 175 ----NVLRLLNEPTAAAVAYGLDQE--TNLATDHNYVIYDLGGGTFDVSILRFSQG---VFEVLATGGHTALGGDDLDRL 245
Cdd:cd10170 103 gsdsDNVRLVSEPEAAALYALEDKGdlLPLKPGDVVLVCDAGGGTVDLSLYEVTSGsplLLEEVAPGGGALLGGTDIDEA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 246 IVKWAKKQL-----NIDTLSDENYAVFIVAARQAKEQLSTQESVQLKLL---------ENVLTLDRSTFESIIQVALDKT 311
Cdd:cd10170 183 FEKLLREKLgdkgkDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPsllggglpeLGLEKGTLLLTEEEIRDLFDPV 262
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488046570 312 ISVCKRVLRDAKLELS--DIQNVVLVGGSTRSYAVQQAVRNVFNQEPLCTI----NPDEVVAIGA 370
Cdd:cd10170 263 IDKILELIEEQLEAKSgtPPDAVVLVGGFSRSPYLRERLRERFGSAGIIIVlrsdDPDTAVARGA 327
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
22-372 |
7.44e-45 |
|
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: 163.88 E-value: 7.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHYGNDVTHYGEEAKPFIIADPKNTIVSVKRFMGRSKADIKFQH- 100
Cdd:cd11739 3 VGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFVQKe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 101 ----PYELVGSENEMPAFETRSGRKTPV----EISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLA 172
Cdd:cd11739 83 kenlSYDLVPLKNGGVGVKVMYLDEEHHfsieQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 173 GLNVLRLLNEPTAAAVAYGLDQETNLATDHN---YVIYDLGGGTFDVSILRFSQGVFEVLATGGHTALGGDDLDRLIVKW 249
Cdd:cd11739 163 GLNCLRLMNDMTAVALNYGIYKQDLPAPDEKpriVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKLVEH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 250 ----AKKQLNIDTLSDENYAVFIVAARQAKEQLSTQESVQLKL--------LENVLTLDRSTFESIIQVALDKTISVCKR 317
Cdd:cd11739 243 fcaeFKTKYKLDVKSKIRALLRLYQECEKLKKLMSSNSTDLPLniecfmndKDVSGKMNRSQFEELCADLLQRIEVPLYS 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 488046570 318 VLRDAKLELSDIQNVVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASI 372
Cdd:cd11739 323 LMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFFGKDVSTTLNADEAVARGCAL 377
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
22-369 |
2.60e-36 |
|
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: 140.49 E-value: 2.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVATVLSGKPKVLNDEKERRLLPSIVHY------GNDVTHYGEEAKPFIIADPKNT--IVSVKRFMGRSK 93
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFprreeeGAESIYFGNDAIDAYLNDPEEGrlIKSVKSFLGSSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 94 ADIKFQHPYelvgsenempafetrsgRKTPVEISAEILKQLKERAESSLQNPVNGAVITVPAYF-------DEAQRQATR 166
Cdd:cd10231 81 FDETTIFGR-----------------RYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFsgvgaedDAQAESRLR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 167 DAAQLAGLNVLRLLNEPTAAAVAYgldqETNLATDHNYVIYDLGGGTFDVSILRFSQGVFE----VLATGGhTALGGDDL 242
Cdd:cd10231 144 DAARRAGFRNVEFQYEPIAAALDY----EQRLDREELVLVVDFGGGTSDFSVLRLGPNRTDrradILATSG-VGIGGDDF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 243 DRLIV--------------------------------KWAKKQL------------------------NIDTLSDENYAV 266
Cdd:cd10231 219 DRELAlkkvmphlgrgstyvsgdkglpvpawlyadlsNWHAISLlytkktlrllldlrrdaadpekieRLLSLVEDQLGH 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 267 FIV-AARQAKEQLSTQESVQLKL--LENVL--TLDRSTFESIIQVALDKTISVCKRVLRDAKLELSDIQNVVLVGGSTRS 341
Cdd:cd10231 299 RLFrAVEQAKIALSSADEATLSFdfIEISIkvTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRVFLTGGSSQS 378
|
410 420
....*....|....*....|....*...
gi 488046570 342 YAVQQAVRNVFNQEPLCTINPDEVVAIG 369
Cdd:cd10231 379 PAVRQALASLFGQARLVEGDEFGSVAAG 406
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
22-372 |
6.06e-23 |
|
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: 100.82 E-value: 6.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVATVLSGKPKvlnDEKERRLL---PSIVHYGNDVTH-----------YGEEAKPFIIADPKNTIVSVKR 87
Cdd:cd10229 3 VAIDFGTTYSGYAYSFITDPG---DIHTMYNWwgaPTGVSSPKTPTClllnpdgefhsFGYEAREKYSDLAEDEEHQWLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 88 FMGRskadiKFQHPYELVGSENEMPafETRSGRKTPV-EISAEILKQLKERAESSLQNPVNGA--------VITVPAYFD 158
Cdd:cd10229 80 FFKF-----KMMLLSEKELTRDTKV--KAVNGKSMPAlEVFAEALRYLKDHALKELRDRSGSSldeddirwVLTVPAIWS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 159 EAQRQATRDAAQLAGL------NVLRLLNEPTAAAVAYGL----DQETNLATDHNYVIYDLGGGTFDVSILRF--SQGVF 226
Cdd:cd10229 153 DAAKQFMREAAVKAGLiseensEQLIIALEPEAAALYCQKllaeGEEKELKPGDKYLVVDCGGGTVDITVHEVleDGKLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 227 EVL-ATGGHtaLGGDDLDRLIVKWakkqlnidtLSDenyaVFIVAARQAKEQLSTQESVQL-KLLENV-----LTLDRST 299
Cdd:cd10229 233 ELLkASGGP--WGSTSVDEEFEEL---------LEE----IFGDDFMEAFKQKYPSDYLDLlQAFERKkrsfkLRLSPEL 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488046570 300 FESIIQVALDKTISVCKRVLRdaKLELSDIQNVVLVGGSTRSYAVQQAVRNVFnqEPLCTI----NPDEVVAIGASI 372
Cdd:cd10229 298 MKSLFDPVVKKIIEHIKELLE--KPELKGVDYIFLVGGFAESPYLQKAVKEAF--STKVKIiippEPGLAVVKGAVL 370
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
22-338 |
3.74e-17 |
|
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins; MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466824 [Multi-domain] Cd Length: 317 Bit Score: 82.91 E-value: 3.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVATvlSGKPKVLNDekerrllPSIVHY---GNDVTHYGEEAKpfiiadpkntivsvkRFMGRSKADIKF 98
Cdd:cd10225 2 IGIDLGTANTLVYV--KGKGIVLNE-------PSVVAVdknTGKVLAVGEEAK---------------KMLGRTPGNIVA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 99 QHPYelvgsenempafetRSGRKTPVEISAEILKQLKERA--ESSLQNPVngAVITVPAYFDEAQRQATRDAAQLAGLNV 176
Cdd:cd10225 58 IRPL--------------RDGVIADFEATEAMLRYFIRKAhrRRGFLRPR--VVIGVPSGITEVERRAVKEAAEHAGARE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 177 LRLLNEPTAAAVAYGLDQETNLATdhnyVIYDLGGGTFDVSilrfsqgvfeVLATGG----HTA-LGGDDLDRLIVKWAK 251
Cdd:cd10225 122 VYLIEEPMAAAIGAGLPIEEPRGS----MVVDIGGGTTEIA----------VISLGGivtsRSVrVAGDEMDEAIINYVR 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 252 KQLNIdtLSDENyavfivAARQAKEQL----STQESVQLKL--------LENVLTLDRSTFESIIQVALDKTISVCKRVL 319
Cdd:cd10225 188 RKYNL--LIGER------TAERIKIEIgsayPLDEELSMEVrgrdlvtgLPRTIEITSEEVREALEEPVNAIVEAVRSTL 259
|
330 340
....*....|....*....|..
gi 488046570 320 RDAKLELS-DI--QNVVLVGGS 338
Cdd:cd10225 260 ERTPPELAaDIvdRGIVLTGGG 281
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
22-372 |
2.11e-15 |
|
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: 77.60 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVatVLSGKPKVLNDekerrllPSIVHY---GNDVTHYGEEAKPFIiadpkntivsvkrfmGRSKADIKF 98
Cdd:pfam06723 4 IGIDLGTANTLV--YVKGKGIVLNE-------PSVVAIntkTKKVLAVGNEAKKML---------------GRTPGNIVA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 99 QHPyelvgsenempafeTRSGRKTPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLAGLNVLR 178
Cdd:pfam06723 60 VRP--------------LKDGVIADFEVTEAMLKYFIKKVHGRRSFSKPRVVICVPSGITEVERRAVKEAAKNAGAREVF 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 179 LLNEPTAAAVAYGLDQETNLATdhnyVIYDLGGGTFDVSILRFSQGVfevlaTGGHTALGGDDLDRLIVKWAKKQLNIdt 258
Cdd:pfam06723 126 LIEEPMAAAIGAGLPVEEPTGN----MVVDIGGGTTEVAVISLGGIV-----TSKSVRVAGDEFDEAIIKYIRKKYNL-- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 259 lsdenyAVFIVAARQAKEQLST------QESVQLK---LLENV---LTLDRSTFESIIQVALDKTISVCKRVLRDAKLEL 326
Cdd:pfam06723 195 ------LIGERTAERIKIEIGSaypteeEEKMEIRgrdLVTGLpktIEISSEEVREALKEPVSAIVEAVKEVLEKTPPEL 268
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 488046570 327 S-DIQN--VVLVGGSTRSYAVQQAVRNVFNQEPLCTINPDEVVAIGASI 372
Cdd:pfam06723 269 AaDIVDrgIVLTGGGALLRGLDKLLSDETGLPVHIAEDPLTCVALGTGK 317
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
22-338 |
6.08e-14 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 73.24 E-value: 6.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVATvlSGKPKVLNDekerrllPSIVHY---GNDVTHYGEEAKpfiiadpkntivsvkRFMGRSKADIKF 98
Cdd:PRK13930 11 IGIDLGTANTLVYV--KGKGIVLNE-------PSVVAIdtkTGKVLAVGEEAK---------------EMLGRTPGNIEA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 99 QHPyelvgseneMpafetRSGRKTPVEISAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLAGLNVLR 178
Cdd:PRK13930 67 IRP---------L-----KDGVIADFEATEAMLRYFIKKARGRRFFRKPRIVICVPSGITEVERRAVREAAEHAGAREVY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 179 LLNEPTAAAVAYGLDQETNLATdhnyVIYDLGGGTFDVSILRFSqGVfevlATGGHTALGGDDLDRLIVKWAKKQLNIdt 258
Cdd:PRK13930 133 LIEEPMAAAIGAGLPVTEPVGN----MVVDIGGGTTEVAVISLG-GI----VYSESIRVAGDEMDEAIVQYVRRKYNL-- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 259 lsdenyAVFIVAARQAKEQL-STQESVQLKLLE----NVLT-------LDRSTFESIIQVALDKTISVCKRVLRDAKLEL 326
Cdd:PRK13930 202 ------LIGERTAEEIKIEIgSAYPLDEEESMEvrgrDLVTglpktieISSEEVREALAEPLQQIVEAVKSVLEKTPPEL 275
|
330
....*....|....*
gi 488046570 327 S-DIQN--VVLVGGS 338
Cdd:PRK13930 276 AaDIIDrgIVLTGGG 290
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
22-338 |
4.81e-13 |
|
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 440695 [Multi-domain] Cd Length: 339 Bit Score: 70.49 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVatVLSGKPKVLNDekerrllPSIV---HYGNDVTHYGEEAKpfiiadpkntivsvkRFMGRSKADIKF 98
Cdd:COG1077 10 IGIDLGTANTLV--YVKGKGIVLNE-------PSVVaidKKTGKVLAVGEEAK---------------EMLGRTPGNIVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 99 QHPYelvgsenempafetRSGRKTPVEISAEILKQLKERA--ESSLQNPvnGAVITVPAYFDEAQRQATRDAAQLAGLNV 176
Cdd:COG1077 66 IRPL--------------KDGVIADFEVTEAMLKYFIKKVhgRRSFFRP--RVVICVPSGITEVERRAVRDAAEQAGARE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 177 LRLLNEPTAAAVAYGLDQET---NLatdhnyvIYDLGGGTFDVSILRFSqGVfeVLATGghTALGGDDLDRLIVKWAKKQ 253
Cdd:COG1077 130 VYLIEEPMAAAIGAGLPIEEptgNM-------VVDIGGGTTEVAVISLG-GI--VVSRS--IRVAGDELDEAIIQYVRKK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 254 LNIdtLSDENyavfivAARQAKEQLST------QESVQLK---LLENV---LTLDRSTFESIIQVALDKTISVCKRVLRD 321
Cdd:COG1077 198 YNL--LIGER------TAEEIKIEIGSaypleeELTMEVRgrdLVTGLpktITITSEEIREALEEPLNAIVEAIKSVLEK 269
|
330 340
....*....|....*....|
gi 488046570 322 AKLELS-DIQN--VVLVGGS 338
Cdd:COG1077 270 TPPELAaDIVDrgIVLTGGG 289
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
22-369 |
1.96e-12 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 68.78 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVATvlSGKPKVLNDekerrllPSIVHYGN---DVTHYGEEAKPFIIADPKNtIVSVKRFmgrskadikf 98
Cdd:PRK13929 7 IGIDLGTANILVYS--KNKGIILNE-------PSVVAVDTetkAVLAIGTEAKNMIGKTPGK-IVAVRPM---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 99 qhpyelvgsenempafetRSGRKTPVEISAEILKQLKERAESSLQNPVN--GAVITVPAYFDEAQRQATRDAAQLAGLNV 176
Cdd:PRK13929 67 ------------------KDGVIADYDMTTDLLKQIMKKAGKNIGMTFRkpNVVVCTPSGSTAVERRAISDAVKNCGAKN 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 177 LRLLNEPTAAAVAYGLDQETNLATdhnyVIYDLGGGTFDVSILRFSqGVfevlATGGHTALGGDDLDRLIVKWAKKQLN- 255
Cdd:PRK13929 129 VHLIEEPVAAAIGADLPVDEPVAN----VVVDIGGGTTEVAIISFG-GV----VSCHSIRIGGDQLDEDIVSFVRKKYNl 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 256 -IDTLSDENYAVFIVAARQAKEQLSTQESVQ--LKLLENVLTLDRSTFESIIQVALDKTISVCKRVLRDAKLELS-DI-- 329
Cdd:PRK13929 200 lIGERTAEQVKMEIGYALIEHEPETMEVRGRdlVTGLPKTITLESKEIQGAMRESLLHILEAIRATLEDCPPELSgDIvd 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 488046570 330 QNVVLVGGStrsyAVQQAVRNVFNQEPLCTI----NPDEVVAIG 369
Cdd:PRK13929 280 RGVILTGGG----ALLNGIKEWLSEEIVVPVhvaaNPLESVAIG 319
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
135-357 |
2.45e-10 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 62.96 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 135 KERAESSLQNPVNGAVITVPAYF-----DEAQRQA----TRdAAQLAGLNVLRLLNEPTAAavayGLDQETNLATDHNYV 205
Cdd:PRK11678 138 KQQAEAQLQAAITQAVIGRPVNFqglggEEANRQAegilER-AAKRAGFKDVEFQFEPVAA----GLDFEATLTEEKRVL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 206 IYDLGGGTFDVSILRF----------SQGVFevlatgGHTA--LGGDDLD-RLIVK-----------------------W 249
Cdd:PRK11678 213 VVDIGGGTTDCSMLLMgpswrgradrSASLL------GHSGqrIGGNDLDiALAFKqlmpllgmgsetekgialpslpfW 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 250 ---------------------AKKQLNIDTLSDENYAVF-----------IV-AARQAKEQLSTQESVQ--LKLLENVL- 293
Cdd:PRK11678 287 navaindvpaqsdfyslangrLLNDLIRDAREPEKVARLlkvwrqrlsyrLVrSAEEAKIALSDQAETRasLDFISDGLa 366
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488046570 294 -TLDRSTFESIIQVALDKTISVCKRVLRDAKlELSDIqnVVLVGGSTRSYAVQQAVRNVFNQEPL 357
Cdd:PRK11678 367 tEISQQGLEEAISQPLARILELVQLALDQAQ-VKPDV--IYLTGGSARSPLIRAALAQQLPGIPI 428
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
127-234 |
4.15e-10 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 61.00 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 127 SAEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLAGLNVLRLLNEPTAAAVAYGLDqetnlatdhNYVI 206
Cdd:PRK15080 69 AVTIVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGID---------NGAV 139
|
90 100
....*....|....*....|....*....
gi 488046570 207 YDLGGGTFDVSILRFSQGVFEV-LATGGH 234
Cdd:PRK15080 140 VDIGGGTTGISILKDGKVVYSAdEPTGGT 168
|
|
| ASKHA_NBD_MamK |
cd24009 |
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ... |
22-340 |
5.19e-10 |
|
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called magnetosome cytoskeleton protein MamK, is a protein with ATPase activity which forms dynamic cytoplasmic filaments (probably with paralog MamK-like) that may organize magnetosomes into long chains running parallel to the long axis of the cell. Turnover of MamK filaments is probably promoted by MamK-like (e.g.. MamJ and/or LimJ), which provides a monomer pool. MamK forms twisted filaments in the presence of ATP or GTP. It serves to close gaps between magnetosomes in the chain. Interaction with MCP10 is involved in controlling the response to magnetic fields, possibly by controlling flagellar rotation. The MamK family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466859 [Multi-domain] Cd Length: 328 Bit Score: 61.07 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVATvlsgkpkvlnDEKERRLLPSIVHYGNDvthygeeakpfIIAdpkntivsvKRFMGRskadikfqhP 101
Cdd:cd24009 4 IGIDLGTSRSAVVT----------SRGKRFSFRSVVGYPKD-----------IIA---------RKLLGK---------E 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 102 YeLVGSEnempAFETRS---------------GRKTPVEISAEILKQLKERAESSLQNPVNgAVITVPAYFDEAQRQATR 166
Cdd:cd24009 45 V-LFGDE----ALENRLaldlrrpledgvikeGDDRDLEAARELLQHLIELALPGPDDEIY-AVIGVPARASAENKQALL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 167 DAAQLAGLNVLrLLNEPTaaAVAYGLDQetnlaTDHNYVIyDLGGGTFDVSILrfsQGVFEVLATGGHTALGGDDLDRLI 246
Cdd:cd24009 119 EIARELVDGVM-VVSEPF--AVAYGLDR-----LDNSLIV-DIGAGTTDLCRM---KGTIPTEEDQITLPKAGDYIDEEL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 247 V-----KWAKKQLNIDTlsdenyavfivaARQAKEQLS----TQESVQLKLLEN--VLTLD-----RSTFESIIqvalDK 310
Cdd:cd24009 187 VdlikeRYPEVQLTLNM------------ARRWKEKYGfvgdASEPVKVELPVDgkPVTYDiteelRIACESLV----PD 250
|
330 340 350
....*....|....*....|....*....|..
gi 488046570 311 TISVCKRVLRDAKLELSD--IQNVVLVGGSTR 340
Cdd:cd24009 251 IVEGIKKLIASFDPEFQEelRNNIVLAGGGSR 282
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
114-352 |
1.35e-09 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar proteins; HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. HSPA12B belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12B.
Pssm-ID: 466842 [Multi-domain] Cd Length: 361 Bit Score: 60.37 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 114 FETRSGRKTP-VEISAEILKQLKERAESSLQNPVNGA--------VITVPAYFDEAQRQATRDAAQLAGL----NVLRLL 180
Cdd:cd11736 99 LEAVNGKKVQaLEVFAHALRFFKEHALQELKDQSPSLpekdavrwVLTVPAIWKQPAKQFMREAAYLAGLvspeNPEQLL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 181 N--EPTAAAV-AYGLDQetnlatdhnYVIYDLGGGTFDVSILRFSQ--GVFEVL--ATGGHTALGGDDL--DRLIVKWAK 251
Cdd:cd11736 179 IalEPEAASIyCRKLDR---------YIVADCGGGTVDLTVHQIEQpqGTLKELykASGGPYGAVGVDLafEKLLCQIFG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 252 KQLnIDTLSDENYAVFI--VAARQAKEQlstqeSVQLKLLENVLT-LDRSTFESIIQvALDKTIsvckrvlrdAKLELSD 328
Cdd:cd11736 250 EDF-IATFKAKRPAAWVdlTIAFEARKR-----TAALRMSSEAMNeLFQPTISQIIQ-HIDDLM---------KKPEVKG 313
|
250 260
....*....|....*....|....
gi 488046570 329 IQNVVLVGGSTRSYAVQQAVRNVF 352
Cdd:cd11736 314 IKFLFLVGGFAESPMLQRAVQAAF 337
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
128-234 |
2.02e-09 |
|
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity.
Pssm-ID: 466897 [Multi-domain] Cd Length: 241 Bit Score: 58.43 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 128 AEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLAGLNVLRLLNEPTAAAVAYGLDqetnlatdhNYVIY 207
Cdd:cd24047 46 IRIVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGIR---------DGAVV 116
|
90 100
....*....|....*....|....*...
gi 488046570 208 DLGGGTFDVSILRFSQGVFEV-LATGGH 234
Cdd:cd24047 117 DIGGGTTGIAVLKDGKVVYTAdEPTGGT 144
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
22-256 |
6.06e-09 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 57.99 E-value: 6.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTthslvATVL---SGKPKVLNDekerrllPSIVHYGND---VTHYGEEAKPFIIADPKNtIVSVKRFMGRSKAD 95
Cdd:PRK13928 6 IGIDLGT-----ANVLvyvKGKGIVLNE-------PSVVAIDKNtnkVLAVGEEARRMVGRTPGN-IVAIRPLRDGVIAD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 96 ikfqhpYELvgSENEMPAFETRSGRKTPVeisaeilkqLKERAesslqnpvngaVITVPAYFDEAQRQATRDAAQLAGLN 175
Cdd:PRK13928 73 ------YDV--TEKMLKYFINKACGKRFF---------SKPRI-----------MICIPTGITSVEKRAVREAAEQAGAK 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 176 VLRLLNEPTAAAVAYGLD--QETNlatdhNYVIyDLGGGTFDVSilrfsqgvfeVLATGG---HTAL--GGDDLDRLIVK 248
Cdd:PRK13928 125 KVYLIEEPLAAAIGAGLDisQPSG-----NMVV-DIGGGTTDIA----------VLSLGGivtSSSIkvAGDKFDEAIIR 188
|
....*...
gi 488046570 249 WAKKQLNI 256
Cdd:PRK13928 189 YIRKKYKL 196
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
128-337 |
6.10e-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: 6.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 128 AEILKQLKERAESSLQNPVNGAVITVPAYFDEAQRqatrdAAQLAGLNVLRLLNEPTAAAVAYgldqETNLATDHNYVIY 207
Cdd:cd24004 49 AESIKELLKELEEKLGSKLKDVVIAIAKVVESLLN-----VLEKAGLEPVGLTLEPFAAANLL----IPYDMRDLNIALV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 208 DLGGGTFDVSILRfsQGVfeVLATgGHTALGGDDLDRLIVkwakKQLNIDtlsdenyavfIVAARQAKEQLSTQESVQLK 287
Cdd:cd24004 120 DIGAGTTDIALIR--NGG--IEAY-RMVPLGGDDFTKAIA----EGFLIS----------FEEAEKIKRTYGIFLLIEAK 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488046570 288 lLENVLTLDRSTFESIIQVALDKTISVCKRVLRDAKLELSDIQNVVLVGG 337
Cdd:cd24004 181 -DQLGFTINKKEVYDIIKPVLEELASGIANAIEEYNGKFKLPDAVYLVGG 229
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
22-256 |
1.17e-07 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 53.94 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 22 IGIDLGTTHSLVatVLSGKPKVLNDekerrllPSIVHYGND---VTHYGEEAKPFIIADPKNtIVSVkRFMgrsK----A 94
Cdd:PRK13927 8 LGIDLGTANTLV--YVKGKGIVLNE-------PSVVAIRTDtkkVLAVGEEAKQMLGRTPGN-IVAI-RPM---KdgviA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 95 DIkfqhpyelvgsenempafetrsgrktpvEISAEILKQLKERA-ESSLQNP-VngaVITVPAYFDEAQRQATRDAAQLA 172
Cdd:PRK13927 74 DF----------------------------DVTEKMLKYFIKKVhKNFRPSPrV---VICVPSGITEVERRAVRESALGA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 173 GLNVLRLLNEPTAAAVAYGLDQETnlATDHnyVIYDLGGGTFDVSILRFSqGVfeVLATGGHTalGGDDLDRLIVKWAKK 252
Cdd:PRK13927 123 GAREVYLIEEPMAAAIGAGLPVTE--PTGS--MVVDIGGGTTEVAVISLG-GI--VYSKSVRV--GGDKFDEAIINYVRR 193
|
....
gi 488046570 253 QLNI 256
Cdd:PRK13927 194 NYNL 197
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
131-355 |
2.82e-07 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar proteins; HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12A belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A.
Pssm-ID: 466841 [Multi-domain] Cd Length: 413 Bit Score: 53.09 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 131 LKQLKERAESSLQNPVNGAVITVPAYFDEAQRQATRDAAQLAGLNV------LRLLNEPTAAAVAYgldQETNLATDHNY 204
Cdd:cd11735 125 LKELSDQAGSEFDNSDVRWVITVPAIWKQPAKQFMRQAAYKAGLASpenpeqLIIALEPEAASIYC---RKLRLHQMDRY 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 205 VIYDLGGGTFDVSI--LRFSQGVFEVL--ATGG-HTALGGD-DLDRLIVKWAKKQLnIDTLSDENYAVFI--VAARQAKE 276
Cdd:cd11735 202 VVVDCGGGTVDLTVhqIRLPEGHLKELykASGGpYGSLGVDyEFEKLLCKIFGEDF-IDQFKIKRPAAWVdlMIAFESRK 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488046570 277 QLSTQE-----------------------SVQLKLLENVLTLDRSTFESIIQVALDK-------TISVCKRVLRD--AKL 324
Cdd:cd11735 281 RAAAPDrtnplnitlpfsfidyykkfrghSVEHALRKSNVDFVKWSSQGMLRMSPDAmnalfkpTIDHIIQHLTDlfQKP 360
|
250 260 270
....*....|....*....|....*....|.
gi 488046570 325 ELSDIQNVVLVGGSTRSYAVQQAVRNVFNQE 355
Cdd:cd11735 361 EVSGVKFLFLVGGFAESPLLQQAVQNAFGDQ 391
|
|
| |
