|
Name |
Accession |
Description |
Interval |
E-value |
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
1-616 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 1132.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 1 MALLQISEPGQTAAPHQHKLAVGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAETEKTVGIEAFAKAALDPKN 80
Cdd:PRK05183 1 MALLQISEPGQSAAPHQRRLAVGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 81 TVISAKRLIGRSLADVQQRYQNLPYQFVASENGLPLIQTAQGNKSPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYF 160
Cdd:PRK05183 81 TISSVKRFMGRSLADIQQRYPHLPYQFVASENGMPLIRTAQGLKSPVEVSAEILKALRQRAEETLGGELDGAVITVPAYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 161 DDAQRQSTKDAARLAGLNVLRLLNEPTAAAIAYGLESGQEGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDD 240
Cdd:PRK05183 161 DDAQRQATKDAARLAGLNVLRLLNEPTAAAIAYGLDSGQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 241 FDHLLAEWIAEQANYKPQ-TASEQRELLTLATQTKVALSQAVEFEVKFANWTGVVSRSQFNELIQPLVKRSLMTCRRALK 319
Cdd:PRK05183 241 FDHLLADWILEQAGLSPRlDPEDQRLLLDAARAAKEALSDADSVEVSVALWQGEITREQFNALIAPLVKRTLLACRRALR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 320 DAGVEAEEVREVVMVGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQADILVGNKPDSDMLLLDVVPLSLGIET 399
Cdd:PRK05183 321 DAGVEADEVKEVVMVGGSTRVPLVREAVGEFFGRTPLTSIDPDKVVAIGAAIQADILAGNKPDSDMLLLDVIPLSLGLET 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 400 MGGLVEKIIPRNTTIPVARAQEFTTGKDGQTAMTIHVLQGERELVEDCRSLGKITLRGIPAMAAGVAQVRVTYQVDADGL 479
Cdd:PRK05183 401 MGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADGL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 480 LNVTAMEKSTKVQASIQIKPSYGLTDEEVTQMIKSSMANAKEDMEARQLVEQRVEADRVIDSVVTALKEDGsAVLSVEEF 559
Cdd:PRK05183 481 LSVTAMEKSTGVEASIQVKPSYGLTDDEIARMLKDSMSHAEEDMQARALAEQKVEAERVLEALQAALAADG-DLLSAAER 559
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1721624176 560 QAIEAQLARLIELKEGTARFAIQQGIKEVDLATQEFAARRMNLSIQKALAGKKMDDL 616
Cdd:PRK05183 560 AAIDAAMAALREVAQGDDADAIEAAIKALDKATQEFAARRMDRSIRRALAGHSVDEI 616
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
21-615 |
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: 869.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 21 AVGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAETEK-TVGIEAFAKAALDPKNTVISAKRLIGRSLADVQQR 99
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYLKDGGvEVGKEALAAAAEDPKNTISSVKRLMGRSIEDIKTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 100 yQNLPYQFVASENGLPLIQTAQGNKSPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAGLNV 179
Cdd:TIGR01991 81 -SILPYRFVDGPGEMVRLRTVQGTVTPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARLAGLNV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 180 LRLLNEPTAAAIAYGLESGQEGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEWIAEQANYKPQ- 258
Cdd:TIGR01991 160 LRLLNEPTAAAVAYGLDKASEGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWILKQLGISADl 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 259 TASEQRELLTLATQTKVALSQA----VEFEVKFANWTGVVSRSQFNELIQPLVKRSLMTCRRALKDAGVEAEEVREVVMV 334
Cdd:TIGR01991 240 NPEDQRLLLQAARAAKEALTDAesveVDFTLDGKDFKGKLTRDEFEALIQPLVQKTLSICRRALRDAGLSVEEIKGVVLV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 335 GGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQADILVGNKPDSDMLLLDVVPLSLGIETMGGLVEKIIPRNTTI 414
Cdd:TIGR01991 320 GGSTRMPLVRRAVAELFGQEPLTDIDPDQVVALGAAIQADLLAGNRIGNDLLLLDVTPLSLGIETMGGLVEKIIPRNTPI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 415 PVARAQEFTTGKDGQTAMTIHVLQGERELVEDCRSLGKITLRGIPAMAAGVAQVRVTYQVDADGLLNVTAMEKSTKVQAS 494
Cdd:TIGR01991 400 PVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDADGLLTVSAQEQSTGVEQS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 495 IQIKPSYGLTDEEVTQMIKSSMANAKEDMEARQLVEQRVEADRVIDSVVTALKEDGsAVLSVEEFQAIEAQLARLIELKE 574
Cdd:TIGR01991 480 IQVKPSYGLSDEEIERMLKDSFKHAEEDMYARALAEQKVEAERILEALQAALAADG-DLLSEDERAAIDAAMEALQKALQ 558
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1721624176 575 GTARFAIQQGIKEVDLATQEFAARRMNLSIQKALAGKKMDD 615
Cdd:TIGR01991 559 GDDADAIKAAIEALEEATDNFAARRMDRGIRKALAGRSLDE 599
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
21-600 |
0e+00 |
|
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region.
Pssm-ID: 394970 [Multi-domain] Cd Length: 598 Bit Score: 658.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 21 AVGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAETEKTVGIEAFAKAALDPKNTVISAKRLIGRSLAD--VQQ 98
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDpvVQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 99 RYQNLPYQFVASENGLPLIQTAQGNK--SPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAG 176
Cdd:pfam00012 81 DIKHLPYKVVKLPNGDAGVEVRYLGEtfTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 177 LNVLRLLNEPTAAAIAYGLESGQ-EGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEWIAEQA-- 253
Cdd:pfam00012 161 LNVLRIVNEPTAAALAYGLDKTDkERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEEFkk 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 254 NYKPQTASEQR---ELLTLATQTKVALSQA-----VEFEVKFAN---WTGVVSRSQFNELIQPLVKRSLMTCRRALKDAG 322
Cdd:pfam00012 241 KYGIDLSKDKRalqRLREAAEKAKIELSSNqtninLPFITAMADgkdVSGTLTRAKFEELVADLFERTLEPVEKALKDAG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 323 VEAEEVREVVMVGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQADILVGNKPDSDMLLLDVVPLSLGIETMGG 402
Cdd:pfam00012 321 LSKSEIDEVVLVGGSTRIPAVQELVKEFFGKEPSKGVNPDEAVAIGAAVQAGVLSGTFDVKDFLLLDVTPLSLGIETLGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 403 LVEKIIPRNTTIPVARAQEFTTGKDGQTAMTIHVLQGERELVEDCRSLGKITLRGIPAMAAGVAQVRVTYQVDADGLLNV 482
Cdd:pfam00012 401 VMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDANGILTV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 483 TAMEKSTKVQASIQIKPSYGLTDEEVTQMIKSSMANAKEDMEARQLVEQRVEADRVIDSVVTALKEDGSAVLSvEEFQAI 562
Cdd:pfam00012 481 SAKDKGTGKEQEITIEASEGLSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGDKVPE-AEKSKV 559
|
570 580 590
....*....|....*....|....*....|....*...
gi 1721624176 563 EAQLARLIELKEGTARFAIQQGIKEVDLATQEFAARRM 600
Cdd:pfam00012 560 ESAIEWLKDELEGDDKEEIEAKTEELAQVSQKIGERMY 597
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
21-512 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 600.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 21 AVGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAETEKT-VGIEAFAKAALDPKNTVISAKRLIGRSLADVQqr 99
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPKDGEVlVGEAAKRQAVTNPGRTIRSIKRLLGRSLFDEA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 100 yqnlpyqfvasenglplIQTAQGNKSPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAGLNV 179
Cdd:COG0443 79 -----------------TEVGGKRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARIAGLEV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 180 LRLLNEPTAAAIAYGLESGQ-EGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEWIAEQANYK-- 256
Cdd:COG0443 142 LRLLNEPTAAALAYGLDKGKeEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPEFGKEeg 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 257 ---PQTASEQRELLTLATQTKVALSQAVEFEVKFA-----NWTGVVSRSQFNELIQPLVKRSLMTCRRALKDAGVEAEEV 328
Cdd:COG0443 222 idlRLDPAALQRLREAAEKAKIELSSADEAEINLPfsggkHLDVELTRAEFEELIAPLVERTLDPVRQALADAGLSPSDI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 329 REVVMVGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQADILVGNKPDsdmllLDVVPLSLGIETMGGLVEKII 408
Cdd:COG0443 302 DAVLLVGGSTRMPAVRERVKELFGKEPLKGVDPDEAVALGAAIQAGVLAGDVKD-----LDVTPLSLGIETLGGVFTKLI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 409 PRNTTIPVARAQEFTTGKDGQTAMTIHVLQGERELVEDCRSLGKITLRGIPAMAAGVAQVRVTYQVDADGLLNVTAMEKS 488
Cdd:COG0443 377 PRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGILSVSAKDLG 456
|
490 500
....*....|....*....|....
gi 1721624176 489 TKVQASIQIKpsygltdEEVTQMI 512
Cdd:COG0443 457 TGKEQSITIK-------EEIERML 473
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
21-597 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 580.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 21 AVGIDLGTTNSLVATVRSGQTQVLLD-EQERAlVPSVVHYAET-EKTVGIEAFAKAALDPKNTVISAKRLIGRSLADVQQ 98
Cdd:PRK00290 4 IIGIDLGTTNSCVAVMEGGEPKVIENaEGART-TPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRLMGRRDEEVQK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 99 RYQNLPYQFVASENGLPLIqTAQGNK-SPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAGL 177
Cdd:PRK00290 83 DIKLVPYKIVKADNGDAWV-EIDGKKyTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 178 NVLRLLNEPTAAAIAYGLESGQEGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEWIAEQanYKP 257
Cdd:PRK00290 162 EVLRIINEPTAAALAYGLDKKGDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADE--FKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 258 QTASE--------QReLLTLATQTKVALSQAVEFEV------------KFANWTgvVSRSQFNELIQPLVKRSLMTCRRA 317
Cdd:PRK00290 240 ENGIDlrkdkmalQR-LKEAAEKAKIELSSAQQTEInlpfitadasgpKHLEIK--LTRAKFEELTEDLVERTIEPCKQA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 318 LKDAGVEAEEVREVVMVGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQADILVGNKpdSDMLLLDVVPLSLGI 397
Cdd:PRK00290 317 LKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLAGDV--KDVLLLDVTPLSLGI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 398 ETMGGLVEKIIPRNTTIPVARAQEFTTGKDGQTAMTIHVLQGERELVEDCRSLGKITLRGIPAMAAGVAQVRVTYQVDAD 477
Cdd:PRK00290 395 ETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDIDAN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 478 GLLNVTAMEKSTKVQASIQIKPSYGLTDEEVTQMIKSSMANAKEDMEARQLVEQRVEADRVIDSVVTALKEDGSAVlSVE 557
Cdd:PRK00290 475 GIVHVSAKDKGTGKEQSITITASSGLSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKELGDKV-PAD 553
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1721624176 558 EFQAIEAQLARLIELKEGTARFAIQQGIKEVDLATQEFAA 597
Cdd:PRK00290 554 EKEKIEAAIKELKEALKGEDKEAIKAKTEELTQASQKLGE 593
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
18-378 |
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: 562.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 18 HKLAVGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAETEK-TVGIEAFAKAALDPKNTVISAKRLIGRSLADV 96
Cdd:cd10236 1 HRLAVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKiTVGEKAKENAITDPENTISSVKRLMGRSLADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 97 QQRYQNLPYQFVASENGLPLIQTAQGNKSPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAG 176
Cdd:cd10236 81 KEELPLLPYRLVGDENELPRFRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 177 LNVLRLLNEPTAAAIAYGLESGQEGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEWIAEQANYK 256
Cdd:cd10236 161 LNVLRLLNEPTAAALAYGLDQKKEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWILKQIGID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 257 PQ-TASEQRELLTLATQTKVALSQA----VEFEVKFANWTGVVSRSQFNELIQPLVKRSLMTCRRALKDAGVEAEEVREV 331
Cdd:cd10236 241 ARlDPAVQQALLQAARRAKEALSDAdsasIEVEVEGKDWEREITREEFEELIQPLVKRTLEPCRRALKDAGLEPADIDEV 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1721624176 332 VMVGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQADILVG 378
Cdd:cd10236 321 VLVGGSTRIPLVRQRVAEFFGREPLTSINPDEVVALGAAIQADILAG 367
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
21-598 |
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: 553.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 21 AVGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAET-EKTVGIEAFAKAALDPKNTVISAKRLIGRSLADVQQR 99
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNgERLVGQPAKRQAVTNPENTIYSIKRFMGRRFDEVTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 100 YQNLPYQFVASeNGLPLIQTAQGNKSPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAGLNV 179
Cdd:TIGR02350 82 AKRVPYKVVGD-GGDVRVKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAGLEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 180 LRLLNEPTAAAIAYGLE-SGQEGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEWIAEqaNYKPQ 258
Cdd:TIGR02350 161 LRIINEPTAAALAYGLDkSKKDEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLAD--EFKKE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 259 TASE--------QReLLTLATQTKVALSQAVEFEVKF----ANWTG------VVSRSQFNELIQPLVKRSLMTCRRALKD 320
Cdd:TIGR02350 239 EGIDlskdkmalQR-LKEAAEKAKIELSSVLSTEINLpfitADASGpkhlemTLTRAKFEELTADLVERTKEPVRQALKD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 321 AGVEAEEVREVVMVGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQADILVGNKpdSDMLLLDVVPLSLGIETM 400
Cdd:TIGR02350 318 AGLSASDIDEVILVGGSTRIPAVQELVKDFFGKEPNKSVNPDEVVAIGAAIQGGVLKGDV--KDVLLLDVTPLSLGIETL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 401 GGLVEKIIPRNTTIPVARAQEFTTGKDGQTAMTIHVLQGERELVEDCRSLGKITLRGIPAMAAGVAQVRVTYQVDADGLL 480
Cdd:TIGR02350 396 GGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDANGIL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 481 NVTAMEKSTKVQASIQIKPSYGLTDEEVTQMIKSSMANAKEDMEARQLVEQRVEADRVIDSVVTALKEDGsAVLSVEEFQ 560
Cdd:TIGR02350 476 HVSAKDKGTGKEQSITITASSGLSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAG-DKLPAEEKE 554
|
570 580 590
....*....|....*....|....*....|....*...
gi 1721624176 561 AIEAQLARLIELKEGTARFAIQQGIKEVDLATQEFAAR 598
Cdd:TIGR02350 555 KIEKAVAELKEALKGEDVEEIKAKTEELQQALQKLAEA 592
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
22-616 |
2.83e-168 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 493.48 E-value: 2.83e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAET-EKTVGIEAFAKAALDPKNTVISAKRLIGRSLADVQQRY 100
Cdd:CHL00094 5 VGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKgDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSEISEEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 101 QNLPYQFVASENGLPLIQTAQGNK--SPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAGLN 178
Cdd:CHL00094 85 KQVSYKVKTDSNGNIKIECPALNKdfSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAGKIAGLE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 179 VLRLLNEPTAAAIAYGLESGQEGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEWI------AEQ 252
Cdd:CHL00094 165 VLRIINEPTAASLAYGLDKKNNETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLikefkkKEG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 253 ANYKPQTASEQReLLTLATQTKVALSQAVEFEVKF----ANWTG------VVSRSQFNELIQPLVKRSLMTCRRALKDAG 322
Cdd:CHL00094 245 IDLSKDRQALQR-LTEAAEKAKIELSNLTQTEINLpfitATQTGpkhiekTLTRAKFEELCSDLINRCRIPVENALKDAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 323 VEAEEVREVVMVGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQADILVGNKpdSDMLLLDVVPLSLGIETMGG 402
Cdd:CHL00094 324 LDKSDIDEVVLVGGSTRIPAIQELVKKLLGKKPNQSVNPDEVVAIGAAVQAGVLAGEV--KDILLLDVTPLSLGVETLGG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 403 LVEKIIPRNTTIPVARAQEFTTGKDGQTAMTIHVLQGERELVEDCRSLGKITLRGIPAMAAGVAQVRVTYQVDADGLLNV 482
Cdd:CHL00094 402 VMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDIDANGILSV 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 483 TAMEKSTKVQASIQIKPSYGLTDEEVTQMIKSSMANAKEDMEARQLVEQRVEADRVIDSVVTALKEDGSAVlSVEEFQAI 562
Cdd:CHL00094 482 TAKDKGTGKEQSITIQGASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKELKDKI-SEEKKEKI 560
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1721624176 563 EAQLARLIELKEGTARFAIQQGIKEVDLATQEFAARRMNlSIQKALAGKKMDDL 616
Cdd:CHL00094 561 ENLIKKLRQALQNDNYESIKSLLEELQKALMEIGKEVYS-STSTTDPASNDDDV 613
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
22-548 |
1.38e-166 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 490.68 E-value: 1.38e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYA-ETEKTVGIEAFAKAALDPKNTVISAKRLIGRSLADVQQRY 100
Cdd:PRK13410 5 VGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTkDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDELDPES 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 101 QNLPYQFVASENGLPLIQTAQGNK--SPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAGLN 178
Cdd:PRK13410 85 KRVPYTIRRNEQGNVRIKCPRLERefAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDAGRIAGLE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 179 VLRLLNEPTAAAIAYGLESGQEGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEWIAEQ------ 252
Cdd:PRK13410 165 VERILNEPTAAALAYGLDRSSSQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWLAEQflekeg 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 253 ANYKPQTASEQReLLTLATQTKVALSQAVEFEVKF----ANWTG------VVSRSQFNELIQPLVKRSLMTCRRALKDAG 322
Cdd:PRK13410 245 IDLRRDRQALQR-LTEAAEKAKIELSGVSVTDISLpfitATEDGpkhietRLDRKQFESLCGDLLDRLLRPVKRALKDAG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 323 VEAEEVREVVMVGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQADILVGNKpdSDMLLLDVVPLSLGIETMGG 402
Cdd:PRK13410 324 LSPEDIDEVVLVGGSTRMPMVQQLVRTLIPREPNQNVNPDEVVAVGAAIQAGILAGEL--KDLLLLDVTPLSLGLETIGG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 403 LVEKIIPRNTTIPVARAQEFTTGKDGQTAMTIHVLQGERELVEDCRSLGKITLRGIPAMAAGVAQVRVTYQVDADGLLNV 482
Cdd:PRK13410 402 VMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFDIDANGILQV 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721624176 483 TAMEKSTKVQASIQIKPSYGLTDEEVTQMIKSSMANAKEDMEARQLVEQRVEADRVIDSVVTALKE 548
Cdd:PRK13410 482 SATDRTTGREQSVTIQGASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERRLRD 547
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
22-569 |
7.19e-157 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 465.38 E-value: 7.19e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAET-EKTVGIEAFAKAALDPKNTVISAKRLIGRSLADVQQRY 100
Cdd:PRK13411 5 IGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSgDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDDTEEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 101 QNLPYQFVASENGLPLIQTAQGNKSPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAGLNVL 180
Cdd:PRK13411 85 SRVPYTCVKGRDDTVNVQIRGRNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAGTIAGLEVL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 181 RLLNEPTAAAIAYGLES-GQEGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEWIAEqaNYKPQT 259
Cdd:PRK13411 165 RIINEPTAAALAYGLDKqDQEQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWLVE--NFQQQE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 260 ASE--------QReLLTLATQTKVALSQAVEFEVKF----ANWTGV------VSRSQFNELIQPLVKRSLMTCRRALKDA 321
Cdd:PRK13411 243 GIDlsqdkmalQR-LREAAEKAKIELSSMLTTSINLpfitADETGPkhlemeLTRAKFEELTKDLVEATIEPMQQALKDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 322 GVEAEEVREVVMVGGSTRVPFVREQVGEFF-GKTPLTSIDPDKVVAIGAAVQADILVGNKpdSDMLLLDVVPLSLGIETM 400
Cdd:PRK13411 322 GLKPEDIDRVILVGGSTRIPAVQEAIQKFFgGKQPDRSVNPDEAVALGAAIQAGVLGGEV--KDLLLLDVTPLSLGIETL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 401 GGLVEKIIPRNTTIPVARAQEFTTGKDGQTAMTIHVLQGERELVEDCRSLGKITLRGIPAMAAGVAQVRVTYQVDADGLL 480
Cdd:PRK13411 400 GEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSFEIDVNGIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 481 NVTAMEKSTKVQASIQIKPSYGLTDEEVTQMIKSSMANAKEDMEARQLVEQRVEADRVIDSVVTALKEDGSaVLSVEEFQ 560
Cdd:PRK13411 480 KVSAQDQGTGREQSIRITNTGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKENGE-LISEELKQ 558
|
....*....
gi 1721624176 561 AIEAQLARL 569
Cdd:PRK13411 559 RAEQKVEQL 567
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
22-584 |
5.84e-152 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 453.13 E-value: 5.84e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAET-EKTVGIEAFAKAALDPKNTVISAKRLIGRSLAD--VQQ 98
Cdd:PTZ00400 44 VGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDgQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEdaTKK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 99 RYQNLPYQFVASENGLPLIQtAQGNK-SPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAGL 177
Cdd:PTZ00400 124 EQKILPYKIVRASNGDAWIE-AQGKKySPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAGKIAGL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 178 NVLRLLNEPTAAAIAYGLESGQEGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFD-----HLLAEWIAEQ 252
Cdd:PTZ00400 203 DVLRIINEPTAAALAFGMDKNDGKTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDqrilnYLIAEFKKQQ 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 253 A-NYKPQTASEQReLLTLATQTKVALSQAVEFEVKF----ANWTG------VVSRSQFNELIQPLVKRSLMTCRRALKDA 321
Cdd:PTZ00400 283 GiDLKKDKLALQR-LREAAETAKIELSSKTQTEINLpfitADQSGpkhlqiKLSRAKLEELTHDLLKKTIEPCEKCIKDA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 322 GVEAEEVREVVMVGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQADILVGNKpdSDMLLLDVVPLSLGIETMG 401
Cdd:PTZ00400 362 GVKKDELNDVILVGGMTRMPKVSETVKKIFGKEPSKGVNPDEAVAMGAAIQAGVLKGEI--KDLLLLDVTPLSLGIETLG 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 402 GLVEKIIPRNTTIPVARAQEFTTGKDGQTAMTIHVLQGERELVEDCRSLGKITLRGIPAMAAGVAQVRVTYQVDADGLLN 481
Cdd:PTZ00400 440 GVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTFDVDANGIMN 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 482 VTAMEKSTKVQASIQIKPSYGLTDEEVTQMIKSSMANAKEDMEARQLVEQRVEADRVIDSV---VTALKEDGS------- 551
Cdd:PTZ00400 520 ISAVDKSTGKKQEITIQSSGGLSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVekqLSDLKDKISdadkdel 599
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1721624176 552 --------AVLSVEEFQAIEAQLARLIELKEGTARFAIQQG 584
Cdd:PTZ00400 600 kqkitklrSTLSSEDVDSIKDKTKQLQEASWKISQQAYKQG 640
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
22-548 |
8.94e-152 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 452.60 E-value: 8.94e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAETEKTVGIEAFAKAALDPKNTVISAKRLIGRSLAD--VQQR 99
Cdd:PTZ00186 30 IGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDehIQKD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 100 YQNLPYQFVASENGLPLIQTAQGNK-SPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAGLN 178
Cdd:PTZ00186 110 IKNVPYKIVRAGNGDAWVQDGNGKQySPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTIAGLN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 179 VLRLLNEPTAAAIAYGLESGQEGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEWIAEQanYKPQ 258
Cdd:PTZ00186 190 VIRVVNEPTAAALAYGMDKTKDSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYILEE--FRKT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 259 TA---SEQRELLT----LATQTKVALSQAVEFEVKF----ANWTGV------VSRSQFNELIQPLVKRSLMTCRRALKDA 321
Cdd:PTZ00186 268 SGidlSKERMALQrvreAAEKAKCELSSAMETEVNLpfitANADGAqhiqmhISRSKFEGITQRLIERSIAPCKQCMKDA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 322 GVEAEEVREVVMVGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQADILVGNKpdSDMLLLDVVPLSLGIETMG 401
Cdd:PTZ00186 348 GVELKEINDVVLVGGMTRMPKVVEEVKKFFQKDPFRGVNPDEAVALGAATLGGVLRGDV--KGLVLLDVTPLSLGIETLG 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 402 GLVEKIIPRNTTIPVARAQEFTTGKDGQTAMTIHVLQGERELVEDCRSLGKITLRGIPAMAAGVAQVRVTYQVDADGLLN 481
Cdd:PTZ00186 426 GVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDIDANGICH 505
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721624176 482 VTAMEKSTKVQASIQIKPSYGLTDEEVTQMIKSSMANAKEDMEARQLVEQRVEADRVIDSVVTALKE 548
Cdd:PTZ00186 506 VTAKDKATGKTQNITITANGGLSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGE 572
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
1-616 |
3.88e-151 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 448.53 E-value: 3.88e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 1 MALLQISEPGQTAAPHQHKLAVGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAETEKTVGieafakaaldPKN 80
Cdd:PRK01433 1 MQIIEIREPEQADFKQERQIAVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIG----------NNK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 81 TVISAKRLIGRSLADVQQR---YQNLPYQFVASENGLPLiQTAQGNKSPIEVSADILSHLAQFAEKRLAGELSGVVITVP 157
Cdd:PRK01433 71 GLRSIKRLFGKTLKEILNTpalFSLVKDYLDVNSSELKL-NFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 158 AYFDDAQRQSTKDAARLAGLNVLRLLNEPTAAAIAYGLESGQEGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALG 237
Cdd:PRK01433 150 AHFNDAARGEVMLAAKIAGFEVLRLIAEPTAAAYAYGLNKNQKGCYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 238 GDDFDHLLAEWIAEQAnykpqTASEQRELLTLATQTKVALSqaveFEVKFANWTGVVSRSQFNELIQPLVKRSLMTCRRA 317
Cdd:PRK01433 230 GNDIDVVITQYLCNKF-----DLPNSIDTLQLAKKAKETLT----YKDSFNNDNISINKQTLEQLILPLVERTINIAQEC 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 318 LKDAGVEAEEVREVVmvGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQADILVGnkPDSDMLLLDVVPLSLGI 397
Cdd:PRK01433 301 LEQAGNPNIDGVILV--GGATRIPLIKDELYKAFKVDILSDIDPDKAVVWGAALQAENLIA--PHTNSLLIDVVPLSLGM 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 398 ETMGGLVEKIIPRNTTIPVARAQEFTTGKDGQTAMTIHVLQGERELVEDCRSLGKITLRGIPAMAAGVAQVRVTYQVDAD 477
Cdd:PRK01433 377 ELYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDAD 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 478 GLLNVTAMEKSTKVQASIQIKPSYGLTDEEVTQMIKSSMANAKEDMEARQLVEQRVEADRVIDSVVTALKEDgSAVLSVE 557
Cdd:PRK01433 457 GILSVSAYEKISNTSHAIEVKPNHGIDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAIAEL-TTLLSES 535
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1721624176 558 EFQAIEAQLARLIELKEGTARFAIQQGIKEVDLATQEFAARRMNLSIQKALAGKKMDDL 616
Cdd:PRK01433 536 EISIINSLLDNIKEAVHARDIILINNSIKEFKSKIKKSMDTKLNIIINDLLKGKNINQI 594
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
22-577 |
1.62e-147 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 441.98 E-value: 1.62e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAET-EKTVGIEAFAKAALDPKNTVISAKRLIGRSLADVQQRY 100
Cdd:PLN03184 42 VGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNgDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSEVDEES 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 101 QNLPYQFVASENGLPLIQTAQGNK--SPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAGLN 178
Cdd:PLN03184 122 KQVSYRVVRDENGNVKLDCPAIGKqfAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRIAGLE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 179 VLRLLNEPTAAAIAYGLESGQEGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEWIA-------- 250
Cdd:PLN03184 202 VLRIINEPTAASLAYGFEKKSNETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLAsnfkkdeg 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 251 ------EQANYKPQTASEQREL-LTLATQTKVALS--QAVEFEVKFANWTgvVSRSQFNELIQPLVKRSLMTCRRALKDA 321
Cdd:PLN03184 282 idllkdKQALQRLTEAAEKAKIeLSSLTQTSISLPfiTATADGPKHIDTT--LTRAKFEELCSDLLDRCKTPVENALRDA 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 322 GVEAEEVREVVMVGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQADILVGNKpdSDMLLLDVVPLSLGIETMG 401
Cdd:PLN03184 360 KLSFKDIDEVILVGGSTRIPAVQELVKKLTGKDPNVTVNPDEVVALGAAVQAGVLAGEV--SDIVLLDVTPLSLGLETLG 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 402 GLVEKIIPRNTTIPVARAQEFTTGKDGQTAMTIHVLQGERELVEDCRSLGKITLRGIPAMAAGVAQVRVTYQVDADGLLN 481
Cdd:PLN03184 438 GVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFDIDANGILS 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 482 VTAMEKSTKVQASIQIKPSYGLTDEEVTQMIKSSMANAKEDMEARQLVEQRVEADRVIDSVVTALKEDGSAVLSveefQA 561
Cdd:PLN03184 518 VSATDKGTGKKQDITITGASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKELGDKVPA----DV 593
|
570
....*....|....*.
gi 1721624176 562 IEAQLARLIELKEGTA 577
Cdd:PLN03184 594 KEKVEAKLKELKDAIA 609
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
21-532 |
1.77e-144 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 433.45 E-value: 1.77e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 21 AVGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAETEKTVGIEAFAKAALDPKNTVISAKRLIGRSLAD--VQQ 98
Cdd:PTZ00009 6 AIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDsvVQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 99 RYQNLPYQFVASENGLPLIQ-TAQGNKS---PIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARL 174
Cdd:PTZ00009 86 DMKHWPFKVTTGGDDKPMIEvTYQGEKKtfhPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAGTI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 175 AGLNVLRLLNEPTAAAIAYGLESGQEGV--IAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEWIAE- 251
Cdd:PTZ00009 166 AGLNVLRIINEPTAAAIAYGLDKKGDGEknVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEFCVQd 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 252 --QANYKPQTASEQRELLTLATQ---TKVALSQA----VEFEVKFAN--WTGVVSRSQFNELIQPLVKRSLMTCRRALKD 320
Cdd:PTZ00009 246 fkRKNRGKDLSSNQRALRRLRTQcerAKRTLSSStqatIEIDSLFEGidYNVTISRARFEELCGDYFRNTLQPVEKVLKD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 321 AGVEAEEVREVVMVGGSTRVPFVREQVGEFF-GKTPLTSIDPDKVVAIGAAVQADILVGNKPDS--DMLLLDVVPLSLGI 397
Cdd:PTZ00009 326 AGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFnGKEPCKSINPDEAVAYGAAVQAAILTGEQSSQvqDLLLLDVTPLSLGL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 398 ETMGGLVEKIIPRNTTIPVARAQEFTTGKDGQTAMTIHVLQGERELVEDCRSLGKITLRGIPAMAAGVAQVRVTYQVDAD 477
Cdd:PTZ00009 406 ETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTFDIDAN 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1721624176 478 GLLNVTAMEKSTKVQASIQIKPSYG-LTDEEVTQMIKSSMANAKEDMEARQLVEQR 532
Cdd:PTZ00009 486 GILNVSAEDKSTGKSNKITITNDKGrLSKADIDRMVNEAEKYKAEDEANRERVEAK 541
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
22-376 |
9.12e-122 |
|
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: 365.26 E-value: 9.12e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGQTQVLL-DEQERAlVPSVVHYAET-EKTVGIEAFAKAALDPKNTVISAKRLIGRSLADVQQR 99
Cdd:cd10234 2 IGIDLGTTNSCVAVMEGGKPTVIPnAEGGRT-TPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 100 YQNLPYQFVASENGLPLIQTAQGNKSPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAGLNV 179
Cdd:cd10234 81 RKQVPYPVVSAGNGDAWVEIGGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIAGLEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 180 LRLLNEPTAAAIAYGLESGQEGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEWIAEQanYKPQT 259
Cdd:cd10234 161 LRIINEPTAAALAYGLDKKKDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADE--FKKEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 260 ASE--------QReLLTLATQTKVALSQAVEFEVK----FANWTGV------VSRSQFNELIQPLVKRSLMTCRRALKDA 321
Cdd:cd10234 239 GIDlskdkmalQR-LKEAAEKAKIELSSVLETEINlpfiTADASGPkhlemkLTRAKFEELTEDLVERTIEPVEQALKDA 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1721624176 322 GVEAEEVREVVMVGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQADIL 376
Cdd:cd10234 318 KLSPSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVL 372
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
21-376 |
2.80e-121 |
|
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: 364.14 E-value: 2.80e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 21 AVGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAETEKTVGIEAFAKAALDPKNTVISAKRLIGRSLAD--VQQ 98
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDpsVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 99 RYQNLPYQFVASENGLPLIQTAQGNK----SPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARL 174
Cdd:cd24028 81 DIKHWPFKVVEDEDGKPKIEVTYKGEektfSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAATI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 175 AGLNVLRLLNEPTAAAIAYGLE--SGQEGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEWIAEQ 252
Cdd:cd24028 161 AGLNVLRIINEPTAAALAYGLDkkSSGERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLVEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 253 ANYK-----PQTASEQRELLTLATQTKVALS----QAVEFEVKFA--NWTGVVSRSQFNELIQPLVKRSLMTCRRALKDA 321
Cdd:cd24028 241 FKKKhgkdlRENPRAMRRLRSACERAKRTLStstsATIEIDSLYDgiDFETTITRAKFEELCEDLFKKCLEPVEKVLKDA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1721624176 322 GVEAEEVREVVMVGGSTRVPFVREQVGEFFGKTPL-TSIDPDKVVAIGAAVQADIL 376
Cdd:cd24028 321 KLSKDDIDEVVLVGGSTRIPKIQELLSEFFGGKELcKSINPDEAVAYGAAIQAAIL 376
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
22-377 |
1.88e-120 |
|
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: 361.12 E-value: 1.88e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGQTQVLL-DEQERALVPSVVHYAE-TEKTVGIEAFAKAALDPKNTVISAKRLIGRSladvqqr 99
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAEVIIeNSEGKRTTPSVVYFDKdGEVLVGEEAKNQALLDPENTIYSVKRLMGRD------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 100 yqnlpYQFVASENGlpliqtaqGNKSPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAGLNV 179
Cdd:cd24029 74 -----TKDKEEIGG--------KEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAELAGLNV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 180 LRLLNEPTAAAIAYGLES-GQEGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEWIAEQA--NYK 256
Cdd:cd24029 141 LRLINEPTAAALAYGLDKeGKDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEKIgiETG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 257 PQTASE----QRELLTLATQTKVALSQAVEFEVKFANWTGV------VSRSQFNELIQPLVKRSLMTCRRALKDAGVEAE 326
Cdd:cd24029 221 ILDDKEderaRARLREAAEEAKIELSSSDSTDILILDDGKGgeleieITREEFEELIAPLIERTIDLLEKALKDAKLSPE 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1721624176 327 EVREVVMVGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQADILV 377
Cdd:cd24029 301 DIDRVLLVGGSSRIPLVREMLEEYFGREPISSVDPDEAVAKGAAIYAASLA 351
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
22-376 |
8.92e-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: 8.92e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHY-AETEKTVGIEAFAKAALDPKNTVISAKRLIGRSLAD--VQQ 98
Cdd:cd11733 4 IGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFtADGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDpeVQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 99 RYQNLPYQFVASENGLPLIQTAQGNKSPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAGLN 178
Cdd:cd11733 84 DIKMVPYKIVKASNGDAWVEAHGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDAGQIAGLN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 179 VLRLLNEPTAAAIAYGLESGQEGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFD-----HLLAEWIAEQA 253
Cdd:cd11733 164 VLRIINEPTAAALAYGLDKKDDKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDnallnYLVAEFKKEQG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 254 -NYKPQTASEQReLLTLATQTKVALSQAVEFEVKF----ANWTG------VVSRSQFNELIQPLVKRSLMTCRRALKDAG 322
Cdd:cd11733 244 iDLSKDNLALQR-LREAAEKAKIELSSSLQTDINLpfitADASGpkhlnmKLTRAKFESLVGDLIKRTVEPCKKCLKDAG 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1721624176 323 VEAEEVREVVMVGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQADIL 376
Cdd:cd11733 323 VSKSDIGEVLLVGGMTRMPKVQETVQEIFGKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
22-376 |
8.38e-103 |
|
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: 316.46 E-value: 8.38e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAETEKTVGIEAFAKAALDPKNTVISAKRLIGRSLAD--VQQR 99
Cdd:cd10241 4 IGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDkeVQKD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 100 YQNLPYQfVASENGLPLIQTAQGNK----SPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLA 175
Cdd:cd10241 84 IKLLPFK-IVNKNGKPYIQVEVKGEkktfAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 176 GLNVLRLLNEPTAAAIAYGLES-GQEGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEWIAEQan 254
Cdd:cd10241 163 GLNVLRIINEPTAAAIAYGLDKkGGEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFIKL-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 255 YKPQT----ASEQRELLTL---ATQTKVALSQA----VEFEVKF--ANWTGVVSRSQFNELIQPLVKRSLMTCRRALKDA 321
Cdd:cd10241 241 FKKKTgkdiSKDKRAVQKLrreVEKAKRALSSQhqarIEIESLFdgEDFSETLTRAKFEELNMDLFRKTLKPVQKVLEDA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1721624176 322 GVEAEEVREVVMVGGSTRVPFVREQVGEFF-GKTPLTSIDPDKVVAIGAAVQADIL 376
Cdd:cd10241 321 GLKKSDIDEIVLVGGSTRIPKVQQLLKDFFnGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
21-378 |
3.23e-100 |
|
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: 310.15 E-value: 3.23e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 21 AVGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAET-EKTVGIEAFAKAALDPKNTVISAKRLIGRSLAD--VQ 97
Cdd:cd11734 3 VIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTKDgERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDaeVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 98 QRYQNLPYQFVASENGLPLIQTAQGNKSPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAGL 177
Cdd:cd11734 83 RDIKEVPYKIVKHSNGDAWVEARGQKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAGQIAGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 178 NVLRLLNEPTAAAIAYGLESGQEGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEWIAEQanYKP 257
Cdd:cd11734 163 NVLRVINEPTAAALAYGLDKSGDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHIVSE--FKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 258 QTASE--------QReLLTLATQTKVALSQAVEFEVKF----ANWTG------VVSRSQFNELIQPLVKRSLMTCRRALK 319
Cdd:cd11734 241 ESGIDlskdrmaiQR-IREAAEKAKIELSSTLQTDINLpfitADASGpkhinmKLTRAQFESLVKPLVDRTVEPCKKALK 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1721624176 320 DAGVEAEEVREVVMVGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQADILVG 378
Cdd:cd11734 320 DAGVKTSEINEVILVGGMSRMPKVQETVKSIFGREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
21-376 |
3.77e-99 |
|
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: 307.25 E-value: 3.77e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 21 AVGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAETEKTVGIEAFAKAALDPKNTVISAKRLIGRSLAD--VQQ 98
Cdd:cd10233 1 AIGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDpvVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 99 RYQNLPYQfVASENGLPLIQ-TAQGNK---SPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARL 174
Cdd:cd10233 81 DMKHWPFK-VVSGGDKPKIQvEYKGETktfTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 175 AGLNVLRLLNEPTAAAIAYGLE--SGQEGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEWIAE- 251
Cdd:cd10233 160 AGLNVLRIINEPTAAAIAYGLDkkGKGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQe 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 252 -QANYKPQTASEQRELLTLATQ---TKVALSQAVE--------FE-VKFANwtgVVSRSQFNELIQPLVKRSLMTCRRAL 318
Cdd:cd10233 240 fKRKHKKDISGNPRALRRLRTAcerAKRTLSSSTQasieidslFEgIDFYT---SITRARFEELCADLFRSTLEPVEKVL 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1721624176 319 KDAGVEAEEVREVVMVGGSTRVPFVREQVGEFF-GKTPLTSIDPDKVVAIGAAVQADIL 376
Cdd:cd10233 317 RDAKLDKSQIHEIVLVGGSTRIPKVQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
22-378 |
2.32e-98 |
|
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: 303.78 E-value: 2.32e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAET-EKTVGIEAFAKAALDPKNTVISAKRLIGrsladvqqry 100
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVDEDgSILVGRAAKERLVTHPDRTAASFKRFMG---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 101 QNLPYQFvasenglpliqtaqGNKS--PIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAGLN 178
Cdd:cd10235 71 TDKQYRL--------------GNHTfrAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELAGLK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 179 VLRLLNEPTAAAIAYGL-ESGQEGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEWIAEQA--NY 255
Cdd:cd10235 137 VERLINEPTAAALAYGLhKREDETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFLKKHrlDF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 256 KPQTASEQRELLTLATQTKVALS--QAVEFEVKF--ANWTGVVSRSQFNELIQPLVKRSLMTCRRALKDAGVEAEEVREV 331
Cdd:cd10235 217 TSLSPSELAALRKRAEQAKRQLSsqDSAEIRLTYrgEELEIELTREEFEELCAPLLERLRQPIERALRDAGLKPSDIDAV 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1721624176 332 VMVGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQADILVG 378
Cdd:cd10235 297 ILVGGATRMPLVRQLIARLFGRLPLSSLDPDEAVALGAAIQAALKAR 343
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
21-376 |
1.20e-90 |
|
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: 285.34 E-value: 1.20e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 21 AVGIDLGTTNSLVATVRsGQTQVLLDEQERALVPSVVHYAETEKTVGIEAFAKAALDPKNTVISAKRLIGRSLAD--VQQ 98
Cdd:cd24093 1 AIGIDLGTTYSCVATYE-SSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDesVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 99 RYQNLPYQfVASENGLPLIQTAQ-GNK---SPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARL 174
Cdd:cd24093 80 DMKTWPFK-VIDVNGNPVIEVQYlGETktfSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 175 AGLNVLRLLNEPTAAAIAYGLESG---QEGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEWIAE 251
Cdd:cd24093 159 AGLNVLRIINEPTAAAIAYGLGAGkseKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 252 QANYKPQT-----ASEQRELLTLATQTKVALSQAVEFEVKF------ANWTGVVSRSQFNELIQPLVKRSLMTCRRALKD 320
Cdd:cd24093 239 EFKKKTGLdisddARALRRLRTAAERAKRTLSSVTQTTVEVdslfdgEDFESSITRARFEDLNAALFKSTLEPVEQVLKD 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1721624176 321 AGVEAEEVREVVMVGGSTRVPFVREQVGEFF-GKTPLTSIDPDKVVAIGAAVQADIL 376
Cdd:cd24093 319 AKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
22-381 |
8.13e-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: 273.83 E-value: 8.13e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVAT--VRSGQTQVLLDEQERALVPSVVHYAETEKT-VGIEAFAKAALDPKNTVISAKRLIGR-----SL 93
Cdd:cd10237 25 VGIDLGTTYSCVGVyhAVTGEVEVIPDDDGHKSIPSVVAFTPDGGVlVGYDALAQAEHNPSNTIYDAKRFIGKtftkeEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 94 ADVQQRYqnlPYQFVASENGLPLIQTAQGNK----SPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTK 169
Cdd:cd10237 105 EEEAKRY---PFKVVNDNIGSAFFEVPLNGStlvvSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 170 DAARLAGLNVLRLLNEPTAAAIAYGLESgQEGV--IAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAE 247
Cdd:cd10237 182 KAANLAGLEVLRVINEPTAAAMAYGLHK-KSDVnnVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQ 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 248 W----IAEQANYKPQTASEQRELLTLATQTKVALSQAVEFEVKF-----------ANWTGVVSRSQFNELIQPLVKRSLM 312
Cdd:cd10237 261 YlidrIAKKFGKTLTDKEDIQRLRQAVEEVKLNLTNHNSASLSLplqislpsafkVKFKEEITRDLFETLNEDLFQRVLE 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721624176 313 TCRRALKDAGVEAEEVREVVMVGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQADILVGNKP 381
Cdd:cd10237 341 PIRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFFGKDPNTSVDPELAVVTGVAIQAGIIGGMWP 409
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
22-373 |
5.30e-77 |
|
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: 249.40 E-value: 5.30e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAETEKTVGIEAFAKAALDPKNTVISAKRLIGRSLAD--VQQR 99
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDpeVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 100 YQNLPYQFVASENGLPLIQTAQGNK----SPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLA 175
Cdd:cd11732 81 IKLLPFKLVELEDGKVGIEVSYNGEevvfSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 176 GLNVLRLLNEPTAAAIAYG------LESGQEGVIAVY-DLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEW 248
Cdd:cd11732 161 GLNCLRLINETTAAALDYGiyksdlLESEEKPRIVAFvDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 249 IAEQ--ANYKPQTASEQR---ELLTLATQTKVALS--QAVEFEVKF----ANWTGVVSRSQFNELIQPLVKRSLMTCRRA 317
Cdd:cd11732 241 FAEEfkKKYKIDPLENPKarlRLLDACEKLKKVLSanGEAPLNVEClmedIDFSGQIKREEFEELIQPLLARLEAPIKKA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1721624176 318 LKDAGVEAEEVREVVMVGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQA 373
Cdd:cd11732 321 LAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVFGKDLSTTLNADEAVARGCALQA 376
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
21-376 |
4.49e-72 |
|
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: 237.21 E-value: 4.49e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 21 AVGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAETEKTVGIEAFAKAALDPKNTVISAKRLIGRSLAD--VQQ 98
Cdd:cd24095 3 VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDpeVQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 99 RYQNLPYQFVASENGLPLIQTAQGNK----SPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARL 174
Cdd:cd24095 83 DLKLFPFKVTEGPDGEIGINVNYLGEqkvfTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAAQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 175 AGLNVLRLLNEPTAAAIAYG-----LESGQEGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEWI 249
Cdd:cd24095 163 AGLNCLRLMNETTATALAYGiyktdLPETDPTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFDHF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 250 AE--QANYKPQTASEQRELLTLAT---QTKVALS---QAV--------EFEVKfanwtGVVSRSQFNELIQPLVKRSLMT 313
Cdd:cd24095 243 AAefKEKYKIDVKSNKKASLRLRAaceKVKKILSanpEAPlnieclmeDKDVK-----GMITREEFEELAAPLLERLLEP 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721624176 314 CRRALKDAGVEAEEVREVVMVGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQADIL 376
Cdd:cd24095 318 LEKALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFFGKEPSRTMNASECVARGCALQCAML 380
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
22-373 |
8.86e-72 |
|
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: 236.02 E-value: 8.86e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAETEKTVGIEAFAKAALDPKNTVISAKRLIGRSLAD--VQQR 99
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDpfVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 100 YQNLPYQFVASENGLPLIQTA----QGNKSPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLA 175
Cdd:cd10228 81 LKHLPYKVVKLPNGSVGIKVQylgeEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 176 GLNVLRLLNEPTAAAIAYGL-------ESGQEGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEW 248
Cdd:cd10228 161 GLNCLRLLNDTTAVALAYGIykqdlpaEEEKPRNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 249 IAE--QANYKPQTASEQRELLTL------------ATQTKVALSqaVEFEVKFANWTGVVSRSQFNELIQPLVKRSLMTC 314
Cdd:cd10228 241 FAEefKTKYKIDVKSKPRALLRLlteceklkklmsANATELPLN--IECFMDDKDVSGKMKRAEFEELCAPLFARVEVPL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1721624176 315 RRALKDAGVEAEEVREVVMVGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQA 373
Cdd:cd10228 319 RSALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVFGKEPSTTLNQDEAVARGCALQC 377
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
21-376 |
2.87e-70 |
|
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: 231.75 E-value: 2.87e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 21 AVGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAETEKTVGIEAFAKAALDPKNTVISAKRLIGRSLAD--VQQ 98
Cdd:cd10238 2 AFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDpaVQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 99 RYQNLPYQfVASENGLPLIQTAQGNK----SPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARL 174
Cdd:cd10238 82 LKKESKCK-IIEKDGKPGYEIELEEKkklvSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 175 AGLNVLRLLNEPTAAAIAYGLesGQE-----GVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEWI 249
Cdd:cd10238 161 AGFNVLRVISEPSAAALAYGI--GQDdptenSNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 250 AE--QANYKPQTASEQR---ELLTLATQTKVALSQ------AVEFEVKFANWTGVVSRSQFNELIQPLVKRSLMTCRRAL 318
Cdd:cd10238 239 ASefKRQWKQDVRENKRamaKLMNAAEVCKHVLSTlntatcSVESLYDGMDFQCNVSRARFESLCSSLFQQCLEPIQEVL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1721624176 319 KDAGVEAEEVREVVMVGGSTRVPFVREQVGEFF-GKTPLTSIDPDKVVAIGAAVQADIL 376
Cdd:cd10238 319 NSAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFpSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
22-376 |
6.10e-58 |
|
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: 199.52 E-value: 6.10e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAETEKTVGIEAFAKAALDPKNTVISAKRLIGRSLAD--VQQR 99
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDpeVAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 100 YQNLPYQFVASENGLPLIQTAQGNK---SPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAG 176
Cdd:cd24094 81 EKYFTAKLVDANGEVGAEVNYLGEKhvfSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 177 LNVLRLLNEPTAAAIAYG-----LESGQEG--VIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEWI 249
Cdd:cd24094 161 LNPLRLMNDTTAAALGYGitktdLPEPEEKprIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDHF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 250 AEQ--ANYKPQTASEQRELLTLATQT----KV--ALSQA---VEFEVKFANWTGVVSRSQFNELIQPLVKRSLMTCRRAL 318
Cdd:cd24094 241 ADEfkEKYKIDVRSNPKAYFRLLAAAeklkKVlsANAQAplnVESLMNDIDVSSMLKREEFEELIAPLLERVTAPLEKAL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1721624176 319 KDAGVEAEEVREVVMVGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQADIL 376
Cdd:cd24094 321 AQAGLTKDEIDFVELVGGTTRVPALKESISAFFGKPLSTTLNQDEAVARGAAFACAIL 378
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
22-375 |
1.59e-57 |
|
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: 198.24 E-value: 1.59e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAETEKTVGIEAFAKAALDPKNTVISAKRLIGRSLAD--VQQR 99
Cdd:cd11737 3 VGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDpfVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 100 YQNLPYQFVASENGLPLIQTA----QGNKSPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLA 175
Cdd:cd11737 83 KPSLAYELVQLPTGTTGIKVMymeeERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 176 GLNVLRLLNEPTAAAIAYG--------LESGQEGVIAVyDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAE 247
Cdd:cd11737 163 GLNCLRLMNETTAVALAYGiykqdlpaPEEKPRNVVFV-DMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVLVN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 248 WIAEQ--ANYKPQTASEQRELLTLATQ----TKVALSQAVEFEVK---FAN---WTGVVSRSQFNELIQPLVKRSLMTCR 315
Cdd:cd11737 242 HFCEEfgKKYKLDIKSKIRALLRLFQEceklKKLMSANASDLPLNiecFMNdidVSGTMNRGQFEEMCADLLARVEPPLR 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 316 RALKDAGVEAEEVREVVMVGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQADI 375
Cdd:cd11737 322 SVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFFGKEVSTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
22-372 |
5.67e-57 |
|
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: 196.62 E-value: 5.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAETEKTVGIEAFAKAALDPKNTVISAKRLIGRSLAD--VQQR 99
Cdd:cd11739 3 VGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDpfVQKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 100 YQNLPYQFVASEN---GLPLIQTAQGNKSPIE-VSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLA 175
Cdd:cd11739 83 KENLSYDLVPLKNggvGVKVMYLDEEHHFSIEqITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 176 GLNVLRLLNEPTAAAIAYG-----LESGQEG--VIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEW 248
Cdd:cd11739 163 GLNCLRLMNDMTAVALNYGiykqdLPAPDEKprIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKLVEH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 249 I-AE-QANYKPQTASEQRELLTLATQ----TKVALSQAVEFEVK---FAN---WTGVVSRSQFNELIQPLVKRSLMTCRR 316
Cdd:cd11739 243 FcAEfKTKYKLDVKSKIRALLRLYQEceklKKLMSSNSTDLPLNiecFMNdkdVSGKMNRSQFEELCADLLQRIEVPLYS 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1721624176 317 ALKDAGVEAEEVREVVMVGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQ 372
Cdd:cd11739 323 LMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFFGKDVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
22-376 |
1.52e-53 |
|
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: 187.43 E-value: 1.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAETEKTVGIEAFAKAALDPKNTVISAKRLIGRSLAD--VQQR 99
Cdd:cd11738 3 VGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDpfVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 100 YQNLPYQFVASENGLPLIQTAQGNKSPI----EVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLA 175
Cdd:cd11738 83 KIKLPYELQKMPNGSTGVKVRYLDEERVfaieQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 176 GLNVLRLLNEPTAAAIAYG--------LESGQEGVIAVyDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAE 247
Cdd:cd11738 163 GLNCLRLMNETTAVALAYGiykqdlpaLEEKPRNVVFV-DMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVLVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 248 WIAEQ--ANYKPQTASEQRELLTLATQ----TKVALSQAVEFEVK---FAN---WTGVVSRSQFNELIQPLVKRSLMTCR 315
Cdd:cd11738 242 YFCEEfkTKYKLNVKENIRALLRLYQEceklKKLMSANASDLPLNiecFMNdidVSSKMNRAQFEELCASLLARVEPPLK 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721624176 316 RALKDAGVEAEEVREVVMVGGSTRVPFVREQVGEFFGKTPLTSIDPDKVVAIGAAVQADIL 376
Cdd:cd11738 322 AVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAIL 382
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
22-373 |
4.65e-52 |
|
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: 182.70 E-value: 4.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGQT-QVLLDEQERALVPSVVHYAETEKTVGIEAFAKAALDPKNTVISAKRLIGrsladvqqry 100
Cdd:cd10230 3 LGIDLGSEFIKVALVKPGVPfEIVLNEESKRKTPSAVAFRNGERLFGDDALALATRFPENTFSYLKDLLG---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 101 qnlpyqfVASEnglpliqtaqgnkspiEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAGLNVL 180
Cdd:cd10230 73 -------YSVE----------------ELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIAGLNVL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 181 RLLNEPTAAAIAYGL-----ESGQEGVIaVYDLGGGTFDLSILR------------LRKGVFEVLATAGDTALGGDDFDH 243
Cdd:cd10230 130 SLINDNTAAALNYGIdrrfeNNEPQNVL-FYDMGASSTSATVVEfssvkekdkgknKTVPQVEVLGVGWDRTLGGLEFDL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 244 LLAEWIAEQANYKPQTASEQRE-------LLTLATQTKVALSQAVEFEVK---------FanwTGVVSRSQFNELIQPLV 307
Cdd:cd10230 209 RLADHLADEFNEKHKKDKDVRTnpramakLLKEANRVKEVLSANTEAPASieslyddidF---RTKITREEFEELCADLF 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721624176 308 KRSLMTCRRALKDAGVEAEEVREVVMVGGSTRVPFVREQVGEFFGKTPL-TSIDPDKVVAIGAAVQA 373
Cdd:cd10230 286 ERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELgKHLNADEAAALGAAFYA 352
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
21-376 |
4.01e-48 |
|
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: 171.78 E-value: 4.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 21 AVGIDLGTTNSLVA-TVRSGQTQVLLDEQERALVPSVVHYAETEKTVGIEAFAKAALDPKNTVISAKRLIGrsladvqqr 99
Cdd:cd10232 2 VIGISFGNSNSSIAiINKDGRAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPKNTVANFRDLLG--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 100 yqnlpyqfvasenglPLIQTAQgnkspiEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAGLNV 179
Cdd:cd10232 73 ---------------TTTLTVS------EVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAAAAGLEV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 180 LRLLNEPTAAAIAYGL------ESGQEGVIAVYDLGGGTFDLSILRLRKGVFEVLATAGDTALGGDDFDHLLAEWIAEQA 253
Cdd:cd10232 132 LQLIPEPAAAALAYDLraetsgDTIKDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVGHFAKEF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 254 NYKPQTASEQ-----RELLTLATQTKVALSQA------VEFEVKFANWTGVVSRSQFNELIQPLVKRSLMTCRRALKDAG 322
Cdd:cd10232 212 KKKTKTDPRKnarslAKLRNAAEITKRALSQGtsapcsVESLADGIDFHSSINRTRYELLASKVFQQFADLVTDAIEKAG 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1721624176 323 VEAEEVREVVMVGGSTRVPFVREQVGEFFGKT----PLTSIDPDKVVAIGAAVQADIL 376
Cdd:cd10232 292 LDPLDIDEVLLAGGASRTPKLASNFEYLFPEStiirAPTQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
22-371 |
2.20e-39 |
|
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: 147.25 E-value: 2.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAETektvgieafakaaldpkntvisakrligrsladvqqryq 101
Cdd:cd10170 1 VGIDFGTTYSGVAYALLGPGEPPLVVLQLPWPGGDGGSSKV--------------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 102 nlpyqfvasenglPliqtaqgnkSPIEVSADILSHLAQFAEKRLAGELSG-------VVITVPAYFDDAQRQSTKDAARL 174
Cdd:cd10170 42 -------------P---------SVLEVVADFLRALLEHAKAELGDRIWElekapieVVITVPAGWSDAAREALREAARA 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 175 AGL----NVLRLLNEPTAAAIAYGLESGQEG------VIAVYDLGGGTFDLSILRLRKG---VFEVLATAGDTALGGDDF 241
Cdd:cd10170 100 AGFgsdsDNVRLVSEPEAAALYALEDKGDLLplkpgdVVLVCDAGGGTVDLSLYEVTSGsplLLEEVAPGGGALLGGTDI 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 242 DHLLAEWIAEQ-----ANYKPQTASEQRELLTLATQTKVALSQAVEFEVKFANWTGVVSRSQ---------FNELIQPLV 307
Cdd:cd10170 180 DEAFEKLLREKlgdkgKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGLPELglekgtlllTEEEIRDLF 259
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 308 KRSLMTCRRALKDAGVEAEEVREVV--MVGGSTRVPFVREQVGEFFGKTPL----TSIDPDKVVAIGAAV 371
Cdd:cd10170 260 DPVIDKILELIEEQLEAKSGTPPDAvvLVGGFSRSPYLRERLRERFGSAGIiivlRSDDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
22-371 |
2.28e-29 |
|
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: 120.46 E-value: 2.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVHYAETEKTVGIEA-FAKAALDPKNTVISAKRLIgRSladvqqry 100
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREEEGAESIyFGNDAIDAYLNDPEEGRLI-KS-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 101 qnlPYQFVASEnGLPLIQTAQGNKSPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYF------DDAQRQST-KDAAR 173
Cdd:cd10231 72 ---VKSFLGSS-LFDETTIFGRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFsgvgaeDDAQAESRlRDAAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 174 LAGLNVLRLLNEPTAAAIAYGLESGQEGVIAVYDLGGGTFDLSILRL----RKGVFEVLATAGDtALGGDDFDHLLAE-- 247
Cdd:cd10231 148 RAGFRNVEFQYEPIAAALDYEQRLDREELVLVVDFGGGTSDFSVLRLgpnrTDRRADILATSGV-GIGGDDFDRELALkk 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 248 ------------------------------WIAEQANYKPQTASEQRELLTLAT-------------------------Q 272
Cdd:cd10231 227 vmphlgrgstyvsgdkglpvpawlyadlsnWHAISLLYTKKTLRLLLDLRRDAAdpekierllslvedqlghrlfraveQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 273 TKVALSQAVEFEVKFA----NWTGVVSRSQFNELIQPLVKRSLMTCRRALKDAGVEAEEVREVVMVGGSTRVPFVREQVG 348
Cdd:cd10231 307 AKIALSSADEATLSFDfieiSIKVTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRVFLTGGSSQSPAVRQALA 386
|
410 420
....*....|....*....|...
gi 1721624176 349 EFFGKTPLTSIDPDKVVAIGAAV 371
Cdd:cd10231 387 SLFGQARLVEGDEFGSVAAGLAL 409
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
20-309 |
1.48e-14 |
|
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: 75.78 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 20 LAVGIDLGTTNS--LVATVRSGQTQVLLDEQERAlvPSVVHYAETEKTVGieafakaaLDPKNTVIS----AKRLIGRSL 93
Cdd:cd10229 1 VVVAIDFGTTYSgyAYSFITDPGDIHTMYNWWGA--PTGVSSPKTPTCLL--------LNPDGEFHSfgyeAREKYSDLA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 94 ADVQQRYQNLPYQFVA----SENGLPLIQTAQGNKS--PIEVSADILSHLAQFAEKRLAGELSGV--------VITVPAY 159
Cdd:cd10229 71 EDEEHQWLYFFKFKMMllseKELTRDTKVKAVNGKSmpALEVFAEALRYLKDHALKELRDRSGSSldeddirwVLTVPAI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 160 FDDAQRQSTKDAARLAGL------NVLRLLNEPTAAAIAYGLESGQEGVIA--------VYDLGGGTFDLSILRL-RKGV 224
Cdd:cd10229 151 WSDAAKQFMREAAVKAGLiseensEQLIIALEPEAAALYCQKLLAEGEEKElkpgdkylVVDCGGGTVDITVHEVlEDGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 225 FEVLATAGDTALGG----DDFDHLLAEWIAEQA--NYKPQTASEQRELLTlatqtkvalsqavEFEVKFANWTGVVSRSQ 298
Cdd:cd10229 231 LEELLKASGGPWGStsvdEEFEELLEEIFGDDFmeAFKQKYPSDYLDLLQ-------------AFERKKRSFKLRLSPEL 297
|
330
....*....|.
gi 1721624176 299 FNELIQPLVKR 309
Cdd:cd10229 298 MKSLFDPVVKK 308
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
22-254 |
2.12e-09 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 59.53 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGqtqVLLDEqeralvPSVVHYAETEKTV---GIEAfakaaldpkntvisaKRLIGRSladvqq 98
Cdd:PRK13929 7 IGIDLGTANILVYSKNKG---IILNE------PSVVAVDTETKAVlaiGTEA---------------KNMIGKT------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 99 ryqnlPYQFVASEnglPLiqtAQGNKSPIEVSADILSHLAQFAEKRLAGELS--GVVITVPAYFDDAQRQSTKDAARLAG 176
Cdd:PRK13929 57 -----PGKIVAVR---PM---KDGVIADYDMTTDLLKQIMKKAGKNIGMTFRkpNVVVCTPSGSTAVERRAISDAVKNCG 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721624176 177 LNVLRLLNEPTAAAIAYGLESGQEGVIAVYDLGGGTFDLSILRlrkgvFEVLATAGDTALGGDDFDHLLAEWIAEQAN 254
Cdd:PRK13929 126 AKNVHLIEEPVAAAIGADLPVDEPVANVVVDIGGGTTEVAIIS-----FGGVVSCHSIRIGGDQLDEDIVSFVRKKYN 198
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
131-271 |
4.72e-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: 57.28 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 131 ADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAGLNVLRLLNEPTAAAIAYGLESGqegviAVYDLGG 210
Cdd:cd24047 46 IRIVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGIRDG-----AVVDIGG 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721624176 211 GTFDLSIlrLRKGvfEVLATAgDTALGGDDFDHLLAEW----IAEQANYKpQTASEQRELLTLAT 271
Cdd:cd24047 121 GTTGIAV--LKDG--KVVYTA-DEPTGGTHLSLVLAGNygisFEEAEIIK-RDPARHKELLPVVR 179
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
22-254 |
8.42e-09 |
|
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.
Pssm-ID: 399596 [Multi-domain] Cd Length: 327 Bit Score: 57.57 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGqtqVLLDEqeralvPSVVHYAETEKT---VGIEAfakaaldpkntvisaKRLIGRSladvqq 98
Cdd:pfam06723 4 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAINTKTKKvlaVGNEA---------------KKMLGRT------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 99 ryqnlPYQFVASEnglPLiqtAQGNKSPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAGLN 178
Cdd:pfam06723 54 -----PGNIVAVR---PL---KDGVIADFEVTEAMLKYFIKKVHGRRSFSKPRVVICVPSGITEVERRAVKEAAKNAGAR 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721624176 179 VLRLLNEPTAAAIAYGLESGQEGVIAVYDLGGGTFDLSILRLRKGVfevlaTAGDTALGGDDFDHLLAEWIAEQAN 254
Cdd:pfam06723 123 EVFLIEEPMAAAIGAGLPVEEPTGNMVVDIGGGTTEVAVISLGGIV-----TSKSVRVAGDEFDEAIIKYIRKKYN 193
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
130-246 |
1.17e-08 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 56.38 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 130 SADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAGLNVLRLLNEPTAAAIAYGLESGqegviAVYDLG 209
Cdd:PRK15080 69 AVTIVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGIDNG-----AVVDIG 143
|
90 100 110
....*....|....*....|....*....|....*..
gi 1721624176 210 GGTFDLSIlrLRKGvfEVLATAgDTALGGDDFDHLLA 246
Cdd:PRK15080 144 GGTTGISI--LKDG--KVVYSA-DEPTGGTHMSLVLA 175
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
22-256 |
1.22e-08 |
|
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: 56.71 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGqtqVLLDEqeralvPSVVHYAETEK---TVGIEAfakaaldpkntvisaKRLIGRSLADVQQ 98
Cdd:cd10225 2 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAVDKNTGkvlAVGEEA---------------KKMLGRTPGNIVA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 99 RYqnlpyqfvasenglPLiqtAQGNKSPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAGLN 178
Cdd:cd10225 58 IR--------------PL---RDGVIADFEATEAMLRYFIRKAHRRRGFLRPRVVIGVPSGITEVERRAVKEAAEHAGAR 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721624176 179 VLRLLNEPTAAAIAYGLESGQ-EGVIAVyDLGGGTFDLSILRLrKGVfeVLATAgdTALGGDDFDHLLAEWIaeQANYK 256
Cdd:cd10225 121 EVYLIEEPMAAAIGAGLPIEEpRGSMVV-DIGGGTTEIAVISL-GGI--VTSRS--VRVAGDEMDEAIINYV--RRKYN 191
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
22-254 |
5.40e-08 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 55.14 E-value: 5.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGqtqVLLDEqeralvPSVVhyaetektvgieAFAKAaldpKNTVIS----AKRLIGRSLADVQ 97
Cdd:PRK13930 11 IGIDLGTANTLVYVKGKG---IVLNE------PSVV------------AIDTK----TGKVLAvgeeAKEMLGRTPGNIE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 98 -QRyqnlpyqfvasenglPLiqtAQGNKSPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAG 176
Cdd:PRK13930 66 aIR---------------PL---KDGVIADFEATEAMLRYFIKKARGRRFFRKPRIVICVPSGITEVERRAVREAAEHAG 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721624176 177 LNVLRLLNEPTAAAIAYGLESGQ-EGVIAVyDLGGGTFDLSILRLRkGVfevlATAGDTALGGDDFDHLLAEWIAEQAN 254
Cdd:PRK13930 128 AREVYLIEEPMAAAIGAGLPVTEpVGNMVV-DIGGGTTEVAVISLG-GI----VYSESIRVAGDEMDEAIVQYVRRKYN 200
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
22-242 |
4.16e-07 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 52.21 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGqtqVLLDEqeralvPSVVhyaetektvgieafakaALDP-KNTVIS----AKRLIGRSladv 96
Cdd:PRK13928 6 IGIDLGTANVLVYVKGKG---IVLNE------PSVV-----------------AIDKnTNKVLAvgeeARRMVGRT---- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 97 qqryqnlPYQFVASEnglPLiqtAQGNKSPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAG 176
Cdd:PRK13928 56 -------PGNIVAIR---PL---RDGVIADYDVTEKMLKYFINKACGKRFFSKPRIMICIPTGITSVEKRAVREAAEQAG 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721624176 177 LNVLRLLNEPTAAAIAYGLESGQEGVIAVYDLGGGTFDLSILRLRKGVfevlaTAGDTALGGDDFD 242
Cdd:PRK13928 123 AKKVYLIEEPLAAAIGAGLDISQPSGNMVVDIGGGTTDIAVLSLGGIV-----TSSSIKVAGDKFD 183
|
|
| ASKHA_NBD_MamK |
cd24009 |
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ... |
19-252 |
4.31e-07 |
|
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called magnetosome cytoskeleton protein MamK, is a protein with ATPase activity which forms dynamic cytoplasmic filaments (probably with paralog MamK-like) that may organize magnetosomes into long chains running parallel to the long axis of the cell. Turnover of MamK filaments is probably promoted by MamK-like (e.g.. MamJ and/or LimJ), which provides a monomer pool. MamK forms twisted filaments in the presence of ATP or GTP. It serves to close gaps between magnetosomes in the chain. Interaction with MCP10 is involved in controlling the response to magnetic fields, possibly by controlling flagellar rotation. The MamK family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466859 [Multi-domain] Cd Length: 328 Bit Score: 52.21 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 19 KLAVGIDLGTTNSLVATvrsgqtqvllDEQERALVPSVVHYAE---TEKTVGIE-AFAKAALDpkntvisaKRLigrSLa 94
Cdd:cd24009 1 TLYIGIDLGTSRSAVVT----------SRGKRFSFRSVVGYPKdiiARKLLGKEvLFGDEALE--------NRL---AL- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 95 dvqqryqNLPYQFvasENGLpliqTAQGNKSPIEVSADILSHLAQFAEKRLAGELSGvVITVPAYFDDAQRQSTKDAARL 174
Cdd:cd24009 59 -------DLRRPL---EDGV----IKEGDDRDLEAARELLQHLIELALPGPDDEIYA-VIGVPARASAENKQALLEIARE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 175 AGLNVLrLLNEPTaaAIAYGLESGQEGVIAvyDLGGGTFDLSILrlrKGvfeVLATAGD---TALGGDDFDHLLAEWIAE 251
Cdd:cd24009 124 LVDGVM-VVSEPF--AVAYGLDRLDNSLIV--DIGAGTTDLCRM---KG---TIPTEEDqitLPKAGDYIDEELVDLIKE 192
|
.
gi 1721624176 252 Q 252
Cdd:cd24009 193 R 193
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
22-254 |
1.43e-06 |
|
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: 50.46 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGqtqVLLDEqeralvPSVVhyaetektvgieafakaALDPK-NTVI----SAKRLIGRsladv 96
Cdd:COG1077 10 IGIDLGTANTLVYVKGKG---IVLNE------PSVV-----------------AIDKKtGKVLavgeEAKEMLGR----- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 97 qqryqnLPYQFVASEnglPLiqtAQGNKSPIEVSADILSHLAQFAEKRLAGELSGVVITVPAYFDDAQRQSTKDAARLAG 176
Cdd:COG1077 59 ------TPGNIVAIR---PL---KDGVIADFEVTEAMLKYFIKKVHGRRSFFRPRVVICVPSGITEVERRAVRDAAEQAG 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721624176 177 LNVLRLLNEPTAAAIAYGLESGQ-EGVIAVyDLGGGTFDLSILRLRkGVfeVLATAgdTALGGDDFDHLLAEWIAEQAN 254
Cdd:COG1077 127 AREVYLIEEPMAAAIGAGLPIEEpTGNMVV-DIGGGTTEVAVISLG-GI--VVSRS--IRVAGDELDEAIIQYVRKKYN 199
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
22-246 |
1.94e-06 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 50.63 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVATVRSGQTQVLLDEQERALVPSVVhYAETEKTVGiEAFAKAaLDPKNTVISAKRLIGRSLA------- 94
Cdd:PRK11678 3 IGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTL-CAPTREAVS-EWLYRH-LDVPAYDDERQALLRRAIRynreedi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 95 -----DVQ------QRYQNLPYQ--FVAS------ENGLPLIQTAQgnkspIE--VSADILsHLAQFAEKRLAGELSGVV 153
Cdd:PRK11678 80 dvtaqSVFfglaalAQYLEDPEEvyFVKSpksflgASGLKPQQVAL-----FEdlVCAMML-HIKQQAEAQLQAAITQAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 154 ITVPAYF-----DDAQRQST---KDAARLAGLNVLRLLNEPTAAAIAYglESG--QEGVIAVYDLGGGTFDLSILRL--- 220
Cdd:PRK11678 154 IGRPVNFqglggEEANRQAEgilERAAKRAGFKDVEFQFEPVAAGLDF--EATltEEKRVLVVDIGGGTTDCSMLLMgps 231
|
250 260 270
....*....|....*....|....*....|..
gi 1721624176 221 ------RKGVFevLATAGdTALGGDDFDHLLA 246
Cdd:PRK11678 232 wrgradRSASL--LGHSG-QRIGGNDLDIALA 260
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
126-241 |
3.24e-06 |
|
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: 49.21 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 126 PIEVSADILSHLAQfAEKRLAGELSGVVITVPAYFDdaqrqSTKDAARLAGLNVLRLLNEPTAAAIAYGLESGQEGVIAV 205
Cdd:cd24004 45 ISKVAESIKELLKE-LEEKLGSKLKDVVIAIAKVVE-----SLLNVLEKAGLEPVGLTLEPFAAANLLIPYDMRDLNIAL 118
|
90 100 110
....*....|....*....|....*....|....*.
gi 1721624176 206 YDLGGGTFDLSIlrLRKGVfeVLATaGDTALGGDDF 241
Cdd:cd24004 119 VDIGAGTTDIAL--IRNGG--IEAY-RMVPLGGDDF 149
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
117-308 |
1.58e-04 |
|
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: 44.19 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 117 IQTAQGNKSP-IEVSADILSHLAQFAEKRLAGELSGV--------VITVPAYFDDAQRQSTKDAARLAGL----NVLRLL 183
Cdd:cd11736 99 LEAVNGKKVQaLEVFAHALRFFKEHALQELKDQSPSLpekdavrwVLTVPAIWKQPAKQFMREAAYLAGLvspeNPEQLL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 184 N--EPTAAAIaYGLESGQegvIAVYDLGGGTFDLSILRLRK--GVFEVL--ATAGDTALGGDD--FDHLLAEWIAEQ--A 253
Cdd:cd11736 179 IalEPEAASI-YCRKLDR---YIVADCGGGTVDLTVHQIEQpqGTLKELykASGGPYGAVGVDlaFEKLLCQIFGEDfiA 254
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1721624176 254 NYKPQTASEQRELltlatqtkvalsqAVEFEVKFANWTGVVSRSQFNELIQPLVK 308
Cdd:cd11736 255 TFKAKRPAAWVDL-------------TIAFEARKRTAALRMSSEAMNELFQPTIS 296
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
22-242 |
2.43e-04 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 43.54 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 22 VGIDLGTTNSLVAtVRsGQTqVLLDEqeralvPSVVHYAETEKT---VGIEAfakaaldpkntvisaKRLIGRsladvqq 98
Cdd:PRK13927 8 LGIDLGTANTLVY-VK-GKG-IVLNE------PSVVAIRTDTKKvlaVGEEA---------------KQMLGR------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 99 ryqnlpyqfvASENglplIQTaqgnKSPIE--VSADI------LSHLAQFAEKRLAGELSgVVITVPAYFDDAQRQSTKD 170
Cdd:PRK13927 57 ----------TPGN----IVA----IRPMKdgVIADFdvtekmLKYFIKKVHKNFRPSPR-VVICVPSGITEVERRAVRE 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721624176 171 AARLAGLNVLRLLNEPTAAAIAYGL---ESgqEGVIAVyDLGGGTFDLSILRLRkGVfeVLATAgdTALGGDDFD 242
Cdd:PRK13927 118 SALGAGAREVYLIEEPMAAAIGAGLpvtEP--TGSMVV-DIGGGTTEVAVISLG-GI--VYSKS--VRVGGDKFD 184
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
153-251 |
2.28e-03 |
|
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: 40.76 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 153 VITVPAYFDDAQRQSTKDAARLAGLNV------LRLLNEPTAAAI-AYGLESGQEGVIAVYDLGGGTFDLSI--LRLRKG 223
Cdd:cd11735 144 VITVPAIWKQPAKQFMRQAAYKAGLASpenpeqLIIALEPEAASIyCRKLRLHQMDRYVVVDCGGGTVDLTVhqIRLPEG 223
|
90 100 110
....*....|....*....|....*....|..
gi 1721624176 224 VFEVL--ATAGD-TALGGD-DFDHLLAEWIAE 251
Cdd:cd11735 224 HLKELykASGGPyGSLGVDyEFEKLLCKIFGE 255
|
|
| RNB |
pfam00773 |
RNB domain; This domain is the catalytic domain of ribonuclease II. |
470-585 |
3.33e-03 |
|
RNB domain; This domain is the catalytic domain of ribonuclease II.
Pssm-ID: 459934 [Multi-domain] Cd Length: 314 Bit Score: 39.96 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624176 470 VTYQVDADGLLnvtameKSTKVQASIqIKPSYGLTDEEVTQMI-----KSSMANAKEDME-----ARQLVEQRVEADRV- 538
Cdd:pfam00773 96 VEITIDADGEV------TSYEIYPSV-IRSKARLTYEEVDDLLegkdaEKDKPDLAEDLRllyelAKILRAKRLQRGALd 168
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1721624176 539 IDSVVTALKEDGSAVLSVEEFQAIEAQlaRLIE---LK--EGTARFAIQQGI 585
Cdd:pfam00773 169 LDTPENKLILDEEGVIDILIQERTDAH--SLIEefmLLanEAVARHLQELGI 218
|
|
| |
