|
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: 1184.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 1 MALLQIAEPGQAAAPHQHRLAVGIDLGTTNSLVASVRSGQSVILNDEQERSLVPSVVHYGVEEKKVGLEAFEQASLDPKN 80
Cdd:PRK05183 1 MALLQISEPGQSAAPHQRRLAVGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 81 TVISVKRLIGRSLPDVQSRYSSLPYEFVASENGLPLIITAQGPKSPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYF 160
Cdd:PRK05183 81 TISSVKRFMGRSLADIQQRYPHLPYQFVASENGMPLIRTAQGLKSPVEVSAEILKALRQRAEETLGGELDGAVITVPAYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 161 DDAQRQSTKDAARLAGLNVLRLLNEPTAAALAYGLDSGQEGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDD 240
Cdd:PRK05183 161 DDAQRQATKDAARLAGLNVLRLLNEPTAAAIAYGLDSGQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 241 FDHLIADWVIEQTKLKPQ-TANQQRELITLANQAKITLTNEKSAVISWQDFSVEISREQFNELIYPLVKRSLLTCRRALK 319
Cdd:PRK05183 241 FDHLLADWILEQAGLSPRlDPEDQRLLLDAARAAKEALSDADSVEVSVALWQGEITREQFNALIAPLVKRTLLACRRALR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 320 DANVESEEVQAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQADILVGNKTDSDMLLLDVVPLSLGIET 399
Cdd:PRK05183 321 DAGVEADEVKEVVMVGGSTRVPLVREAVGEFFGRTPLTSIDPDKVVAIGAAIQADILAGNKPDSDMLLLDVIPLSLGLET 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 400 MGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMSVHVLQGERELVDDCRSLGRFTLRGIPPMAAGAAHIRVTYQVDADGL 479
Cdd:PRK05183 401 MGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADGL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 480 LSVTAMEKSTKVQASIQIKPSYGLTDEEVTAMIKSSFDNAQEDLQARELAEQRVEADRVIESVIVALQADGAeLLSTDEF 559
Cdd:PRK05183 481 LSVTAMEKSTGVEASIQVKPSYGLTDDEIARMLKDSMSHAEEDMQARALAEQKVEAERVLEALQAALAADGD-LLSAAER 559
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720137003 560 HHIETVLKQLMDVKQGSDRDAIAQGIKALDTATQEFAARRMNASINKALTGKNLSDI 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: 911.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 21 AVGIDLGTTNSLVASVRSGQSVILNDEQERSLVPSVVHYGVEEK-KVGLEAFEQASLDPKNTVISVKRLIGRSLPDVQSR 99
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYLKDGGvEVGKEALAAAAEDPKNTISSVKRLMGRSIEDIKTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 100 ySSLPYEFVASENGLPLIITAQGPKSPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLAGLNV 179
Cdd:TIGR01991 81 -SILPYRFVDGPGEMVRLRTVQGTVTPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARLAGLNV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 180 LRLLNEPTAAALAYGLDSGQEGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADWVIEQTKLKPQ- 258
Cdd:TIGR01991 160 LRLLNEPTAAAVAYGLDKASEGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWILKQLGISADl 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 259 TANQQRELITLANQAKITLTNEKSA----VISWQDFSVEISREQFNELIYPLVKRSLLTCRRALKDANVESEEVQAVVMV 334
Cdd:TIGR01991 240 NPEDQRLLLQAARAAKEALTDAESVevdfTLDGKDFKGKLTRDEFEALIQPLVQKTLSICRRALRDAGLSVEEIKGVVLV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 335 GGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQADILVGNKTDSDMLLLDVVPLSLGIETMGGLVEKIIPRNTTI 414
Cdd:TIGR01991 320 GGSTRMPLVRRAVAELFGQEPLTDIDPDQVVALGAAIQADLLAGNRIGNDLLLLDVTPLSLGIETMGGLVEKIIPRNTPI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 415 PVARAQEFTTFKDGQTAMSVHVLQGERELVDDCRSLGRFTLRGIPPMAAGAAHIRVTYQVDADGLLSVTAMEKSTKVQAS 494
Cdd:TIGR01991 400 PVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDADGLLTVSAQEQSTGVEQS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 495 IQIKPSYGLTDEEVTAMIKSSFDNAQEDLQARELAEQRVEADRVIESVIVALQADGaELLSTDEFHHIETVLKQLMDVKQ 574
Cdd:TIGR01991 480 IQVKPSYGLSDEEIERMLKDSFKHAEEDMYARALAEQKVEAERILEALQAALAADG-DLLSEDERAAIDAAMEALQKALQ 558
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1720137003 575 GSDRDAIAQGIKALDTATQEFAARRMNASINKALTGKNLSD 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: 683.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 21 AVGIDLGTTNSLVASVRSGQ-SVILNDEQERSLvPSVVHYGVEEKKVGLEAFEQASLDPKNTVISVKRLIGRSL--PDVQ 97
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGpEVIANAEGNRTT-PSVVAFTPKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFsdPVVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 98 SRYSSLPYEFVASENGLPLIITAQGPK--SPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLA 175
Cdd:pfam00012 80 RDIKHLPYKVVKLPNGDAGVEVRYLGEtfTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 176 GLNVLRLLNEPTAAALAYGLDSGQ-EGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADWVIEQ-- 252
Cdd:pfam00012 160 GLNVLRIVNEPTAAALAYGLDKTDkERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEEfk 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 253 TKLKPQTANQQR---ELITLANQAKITL-TNEKSAVISW-------QDFSVEISREQFNELIYPLVKRSLLTCRRALKDA 321
Cdd:pfam00012 240 KKYGIDLSKDKRalqRLREAAEKAKIELsSNQTNINLPFitamadgKDVSGTLTRAKFEELVADLFERTLEPVEKALKDA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 322 NVESEEVQAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQADILVGNKTDSDMLLLDVVPLSLGIETMG 401
Cdd:pfam00012 320 GLSKSEIDEVVLVGGSTRIPAVQELVKEFFGKEPSKGVNPDEAVAIGAAVQAGVLSGTFDVKDFLLLDVTPLSLGIETLG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 402 GLVEKIIPRNTTIPVARAQEFTTFKDGQTAMSVHVLQGERELVDDCRSLGRFTLRGIPPMAAGAAHIRVTYQVDADGLLS 481
Cdd:pfam00012 400 GVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDANGILT 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 482 VTAMEKSTKVQASIQIKPSYGLTDEEVTAMIKSSFDNAQEDLQARELAEQRVEADRVIESVIVALqADGAELLSTDEFHH 561
Cdd:pfam00012 480 VSAKDKGTGKEQEITIEASEGLSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSL-EEEGDKVPEAEKSK 558
|
570 580 590
....*....|....*....|....*....|....*....
gi 1720137003 562 IETVLKQLMDVKQGSDRDAIAQGIKALDTATQEFAARRM 600
Cdd:pfam00012 559 VESAIEWLKDELEGDDKEEIEAKTEELAQVSQKIGERMY 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: 644.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 21 AVGIDLGTTNSLVASVRSGQSVILNDEQERSLVPSVVHYGVE-EKKVGLEAFEQASLDPKNTVISVKRLIGRSLPDVQSR 99
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPKDgEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFDEATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 100 ysslpyefvasenglpliiTAQGPKSPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLAGLNV 179
Cdd:COG0443 81 -------------------VGGKRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARIAGLEV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 180 LRLLNEPTAAALAYGLDSGQ-EGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADWVIEQTKLK-- 256
Cdd:COG0443 142 LRLLNEPTAAALAYGLDKGKeEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPEFGKEeg 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 257 ---PQTANQQRELITLANQAKITLTNEKSAVISW-----QDFSVEISREQFNELIYPLVKRSLLTCRRALKDANVESEEV 328
Cdd:COG0443 222 idlRLDPAALQRLREAAEKAKIELSSADEAEINLpfsggKHLDVELTRAEFEELIAPLVERTLDPVRQALADAGLSPSDI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 329 QAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQADILVGNKTDsdmllLDVVPLSLGIETMGGLVEKII 408
Cdd:COG0443 302 DAVLLVGGSTRMPAVRERVKELFGKEPLKGVDPDEAVALGAAIQAGVLAGDVKD-----LDVTPLSLGIETLGGVFTKLI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 409 PRNTTIPVARAQEFTTFKDGQTAMSVHVLQGERELVDDCRSLGRFTLRGIPPMAAGAAHIRVTYQVDADGLLSVTAMEKS 488
Cdd:COG0443 377 PRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGILSVSAKDLG 456
|
490 500
....*....|....*....|....
gi 1720137003 489 TKVQASIQIKpsygltdEEVTAMI 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: 607.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 21 AVGIDLGTTNSLVASVRSGQS-VILNDEQERSlVPSVVHYGVE-EKKVGLEAFEQASLDPKNTVISVKRLIGRSLPDVQS 98
Cdd:PRK00290 4 IIGIDLGTTNSCVAVMEGGEPkVIENAEGART-TPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRLMGRRDEEVQK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 99 RYSSLPYEFVASENGLPlIITAQGPK-SPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLAGL 177
Cdd:PRK00290 83 DIKLVPYKIVKADNGDA-WVEIDGKKyTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 178 NVLRLLNEPTAAALAYGLDSGQEGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADWVIEQTK--- 254
Cdd:PRK00290 162 EVLRIINEPTAAALAYGLDKKGDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEFKken 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 255 ---LKPQTANQQReLITLANQAKITLTNEKSAVISWQ----------DFSVEISREQFNELIYPLVKRSLLTCRRALKDA 321
Cdd:PRK00290 242 gidLRKDKMALQR-LKEAAEKAKIELSSAQQTEINLPfitadasgpkHLEIKLTRAKFEELTEDLVERTIEPCKQALKDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 322 NVESEEVQAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQADILVGNKTdsDMLLLDVVPLSLGIETMG 401
Cdd:PRK00290 321 GLSVSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLAGDVK--DVLLLDVTPLSLGIETLG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 402 GLVEKIIPRNTTIPVARAQEFTTFKDGQTAMSVHVLQGERELVDDCRSLGRFTLRGIPPMAAGAAHIRVTYQVDADGLLS 481
Cdd:PRK00290 399 GVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDIDANGIVH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 482 VTAMEKSTKVQASIQIKPSYGLTDEEVTAMIKSSFDNAQEDLQARELAEQRVEADRVIESVIVALqADGAELLSTDEFHH 561
Cdd:PRK00290 479 VSAKDKGTGKEQSITITASSGLSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTL-KELGDKVPADEKEK 557
|
570 580 590
....*....|....*....|....*....|....*.
gi 1720137003 562 IETVLKQLMDVKQGSDRDAIAQGIKALDTATQEFAA 597
Cdd:PRK00290 558 IEAAIKELKEALKGEDKEAIKAKTEELTQASQKLGE 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: 586.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 18 HRLAVGIDLGTTNSLVASVRSGQSVILNDEQERSLVPSVVHYGVEEK-KVGLEAFEQASLDPKNTVISVKRLIGRSLPDV 96
Cdd:cd10236 1 HRLAVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKiTVGEKAKENAITDPENTISSVKRLMGRSLADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 97 QSRYSSLPYEFVASENGLPLIITAQGPKSPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLAG 176
Cdd:cd10236 81 KEELPLLPYRLVGDENELPRFRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 177 LNVLRLLNEPTAAALAYGLDSGQEGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADWVIEQTKLK 256
Cdd:cd10236 161 LNVLRLLNEPTAAALAYGLDQKKEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWILKQIGID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 257 PQ-TANQQRELITLANQAKITLTNEKSAVI----SWQDFSVEISREQFNELIYPLVKRSLLTCRRALKDANVESEEVQAV 331
Cdd:cd10236 241 ARlDPAVQQALLQAARRAKEALSDADSASIevevEGKDWEREITREEFEELIQPLVKRTLEPCRRALKDAGLEPADIDEV 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1720137003 332 VMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQADILVG 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: 572.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 21 AVGIDLGTTNSLVASVRSGQSVILNDEQERSLVPSVVHYGVE-EKKVGLEAFEQASLDPKNTVISVKRLIGRSLPDVQSR 99
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNgERLVGQPAKRQAVTNPENTIYSIKRFMGRRFDEVTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 100 YSSLPYEFVASENglPLIITAQGPK-SPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLAGLN 178
Cdd:TIGR02350 82 AKRVPYKVVGDGG--DVRVKVDGKEyTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAGLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 179 VLRLLNEPTAAALAYGLD-SGQEGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADWVIEQTK--- 254
Cdd:TIGR02350 160 VLRIINEPTAAALAYGLDkSKKDEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADEFKkee 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 255 ---LKPQTANQQReLITLANQAKITLTNEKSAVISWQ----------DFSVEISREQFNELIYPLVKRSLLTCRRALKDA 321
Cdd:TIGR02350 240 gidLSKDKMALQR-LKEAAEKAKIELSSVLSTEINLPfitadasgpkHLEMTLTRAKFEELTADLVERTKEPVRQALKDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 322 NVESEEVQAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQADILVGNKTdsDMLLLDVVPLSLGIETMG 401
Cdd:TIGR02350 319 GLSASDIDEVILVGGSTRIPAVQELVKDFFGKEPNKSVNPDEVVAIGAAIQGGVLKGDVK--DVLLLDVTPLSLGIETLG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 402 GLVEKIIPRNTTIPVARAQEFTTFKDGQTAMSVHVLQGERELVDDCRSLGRFTLRGIPPMAAGAAHIRVTYQVDADGLLS 481
Cdd:TIGR02350 397 GVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDANGILH 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 482 VTAMEKSTKVQASIQIKPSYGLTDEEVTAMIKSSFDNAQEDLQARELAEQRVEADRVIESVIVALqADGAELLSTDEFHH 561
Cdd:TIGR02350 477 VSAKDKGTGKEQSITITASSGLSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTL-KEAGDKLPAEEKEK 555
|
570 580 590
....*....|....*....|....*....|....*..
gi 1720137003 562 IETVLKQLMDVKQGSDRDAIAQGIKALDTATQEFAAR 598
Cdd:TIGR02350 556 IEKAVAELKEALKGEDVEEIKAKTEELQQALQKLAEA 592
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
22-616 |
1.08e-179 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 522.75 E-value: 1.08e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASVRSGQ-SVILNDEQERSlVPSVVHYG-VEEKKVGLEAFEQASLDPKNTVISVKRLIGRSLPDVQSR 99
Cdd:CHL00094 5 VGIDLGTTNSVVAVMEGGKpTVIPNAEGFRT-TPSIVAYTkKGDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSEISEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 100 YSSLPYEFVASENGLPLIITAQGPK--SPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLAGL 177
Cdd:CHL00094 84 AKQVSYKVKTDSNGNIKIECPALNKdfSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAGKIAGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 178 NVLRLLNEPTAAALAYGLDSGQEGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADWVIEQTK--- 254
Cdd:CHL00094 164 EVLRIINEPTAASLAYGLDKKNNETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLIKEFKkke 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 255 ---LKPQTANQQReLITLANQAKITLTNEKSAVISW----------QDFSVEISREQFNELIYPLVKRSLLTCRRALKDA 321
Cdd:CHL00094 244 gidLSKDRQALQR-LTEAAEKAKIELSNLTQTEINLpfitatqtgpKHIEKTLTRAKFEELCSDLINRCRIPVENALKDA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 322 NVESEEVQAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQADILVGNKTdsDMLLLDVVPLSLGIETMG 401
Cdd:CHL00094 323 KLDKSDIDEVVLVGGSTRIPAIQELVKKLLGKKPNQSVNPDEVVAIGAAVQAGVLAGEVK--DILLLDVTPLSLGVETLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 402 GLVEKIIPRNTTIPVARAQEFTTFKDGQTAMSVHVLQGERELVDDCRSLGRFTLRGIPPMAAGAAHIRVTYQVDADGLLS 481
Cdd:CHL00094 401 GVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDIDANGILS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 482 VTAMEKSTKVQASIQIKPSYGLTDEEVTAMIKSSFDNAQEDLQARELAEQRVEADRVIESVIVALQaDGAELLSTDEFHH 561
Cdd:CHL00094 481 VTAKDKGTGKEQSITIQGASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLK-ELKDKISEEKKEK 559
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1720137003 562 IETVLKQLMDVKQGSDRDAIAQGIKALDTATQEFAARRMNASiNKALTGKNLSDI 616
Cdd:CHL00094 560 IENLIKKLRQALQNDNYESIKSLLEELQKALMEIGKEVYSST-STTDPASNDDDV 613
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
22-599 |
1.03e-173 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 509.17 E-value: 1.03e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASVRSGQS-VILNDEQERSlVPSVVHYGVE-EKKVGLEAFEQASLDPKNTVISVKRLIGRSLPDVQSR 99
Cdd:PRK13410 5 VGIDLGTTNSVVAVMEGGKPvVIANAEGMRT-TPSVVGFTKDgELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDELDPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 100 YSSLPYEFVASENGLPLIITAQGPK--SPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLAGL 177
Cdd:PRK13410 84 SKRVPYTIRRNEQGNVRIKCPRLERefAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDAGRIAGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 178 NVLRLLNEPTAAALAYGLDSGQEGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADWVIEQTK--- 254
Cdd:PRK13410 164 EVERILNEPTAAALAYGLDRSSSQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWLAEQFLeke 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 255 ---LKPQTANQQReLITLANQAKITLTNEKSAVISW----------QDFSVEISREQFNELIYPLVKRSLLTCRRALKDA 321
Cdd:PRK13410 244 gidLRRDRQALQR-LTEAAEKAKIELSGVSVTDISLpfitatedgpKHIETRLDRKQFESLCGDLLDRLLRPVKRALKDA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 322 NVESEEVQAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQADILVGNKtdSDMLLLDVVPLSLGIETMG 401
Cdd:PRK13410 323 GLSPEDIDEVVLVGGSTRMPMVQQLVRTLIPREPNQNVNPDEVVAVGAAIQAGILAGEL--KDLLLLDVTPLSLGLETIG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 402 GLVEKIIPRNTTIPVARAQEFTTFKDGQTAMSVHVLQGERELVDDCRSLGRFTLRGIPPMAAGAAHIRVTYQVDADGLLS 481
Cdd:PRK13410 401 GVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFDIDANGILQ 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 482 VTAMEKSTKVQASIQIKPSYGLTDEEVTAMIKSSFDNAQEDLQARELAEQR-------VEADRVIESVIVALQADGAELL 554
Cdd:PRK13410 481 VSATDRTTGREQSVTIQGASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRnraltliAQAERRLRDAALEFGPYFAERQ 560
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1720137003 555 StdefHHIETVLKQLMDVKQGSDRDAIAQGIKALDTA----TQEFAARR 599
Cdd:PRK13410 561 R----RAVESAMRDVQDSLEQDDDRELDLAVADLQEAlyglNREVRAEY 605
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
1-617 |
2.45e-168 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 492.83 E-value: 2.45e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 1 MALLQIAEPGQAAAPHQHRLAVGIDLGTTNSLVASVRSGQSVILNDEQERSLVPSVVHYGVEEKKVGleafeqasldPKN 80
Cdd:PRK01433 1 MQIIEIREPEQADFKQERQIAVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIG----------NNK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 81 TVISVKRLIGRSLPDV--QSRYSSLPYEFVASENGLPLIITAQGPKSPIEVSSDILSRLNHIAEQRLGGELSGVVITVPA 158
Cdd:PRK01433 71 GLRSIKRLFGKTLKEIlnTPALFSLVKDYLDVNSSELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 159 YFDDAQRQSTKDAARLAGLNVLRLLNEPTAAALAYGLDSGQEGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGG 238
Cdd:PRK01433 151 HFNDAARGEVMLAAKIAGFEVLRLIAEPTAAAYAYGLNKNQKGCYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 239 DDFDHLIADWVIEQTKLkpqtaNQQRELITLANQAKITLTNEKSavisWQDFSVEISREQFNELIYPLVKRSLLTCRRAL 318
Cdd:PRK01433 231 NDIDVVITQYLCNKFDL-----PNSIDTLQLAKKAKETLTYKDS----FNNDNISINKQTLEQLILPLVERTINIAQECL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 319 KDANveSEEVQAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQADILVGNKTDSdmLLLDVVPLSLGIE 398
Cdd:PRK01433 302 EQAG--NPNIDGVILVGGATRIPLIKDELYKAFKVDILSDIDPDKAVVWGAALQAENLIAPHTNS--LLIDVVPLSLGME 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 399 TMGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMSVHVLQGERELVDDCRSLGRFTLRGIPPMAAGAAHIRVTYQVDADG 478
Cdd:PRK01433 378 LYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDADG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 479 LLSVTAMEKSTKVQASIQIKPSYGLTDEEVTAMIKSSFDNAQEDLQARELAEQRVEADRVIESvIVALQADGAELLSTDE 558
Cdd:PRK01433 458 ILSVSAYEKISNTSHAIEVKPNHGIDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFN-IERAIAELTTLLSESE 536
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720137003 559 FHHIETVLKQLMDVKQGSDRDAIAQGIKALDTATQEFAARRMNASINKALTGKNLSDIE 617
Cdd:PRK01433 537 ISIINSLLDNIKEAVHARDIILINNSIKEFKSKIKKSMDTKLNIIINDLLKGKNINQIK 595
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
22-569 |
2.52e-167 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 492.35 E-value: 2.52e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASVRSGQS-VILNDEQERSlVPSVVHYG-VEEKKVGLEAFEQASLDPKNTVISVKRLIGRSLPDVQSR 99
Cdd:PRK13411 5 IGIDLGTTNSCVAVLEGGKPiVIPNSEGGRT-TPSIVGFGkSGDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDDTEEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 100 YSSLPYEFVASENGLpLIITAQGPK-SPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLAGLN 178
Cdd:PRK13411 84 RSRVPYTCVKGRDDT-VNVQIRGRNyTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAGTIAGLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 179 VLRLLNEPTAAALAYGLDS-GQEGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADWVIEQTK--- 254
Cdd:PRK13411 163 VLRIINEPTAAALAYGLDKqDQEQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWLVENFQqqe 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 255 ---LKPQTANQQReLITLANQAKITLTNEKSAVISW----------QDFSVEISREQFNELIYPLVKRSLLTCRRALKDA 321
Cdd:PRK13411 243 gidLSQDKMALQR-LREAAEKAKIELSSMLTTSINLpfitadetgpKHLEMELTRAKFEELTKDLVEATIEPMQQALKDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 322 NVESEEVQAVVMVGGSTRVPYVREQVGEFF-GKTPLTSIDPDKVVALGAAIQADILVGNKtdSDMLLLDVVPLSLGIETM 400
Cdd:PRK13411 322 GLKPEDIDRVILVGGSTRIPAVQEAIQKFFgGKQPDRSVNPDEAVALGAAIQAGVLGGEV--KDLLLLDVTPLSLGIETL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 401 GGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMSVHVLQGERELVDDCRSLGRFTLRGIPPMAAGAAHIRVTYQVDADGLL 480
Cdd:PRK13411 400 GEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSFEIDVNGIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 481 SVTAMEKSTKVQASIQIKPSYGLTDEEVTAMIKSSFDNAQEDLQARELAEQRVEADRVIESVIVALQaDGAELLSTDEFH 560
Cdd:PRK13411 480 KVSAQDQGTGREQSIRITNTGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLK-ENGELISEELKQ 558
|
....*....
gi 1720137003 561 HIETVLKQL 569
Cdd:PRK13411 559 RAEQKVEQL 567
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
22-592 |
2.56e-159 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 472.00 E-value: 2.56e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASVRSGQ-SVILNDEQERSlVPSVVHYGVE-EKKVGLEAFEQASLDPKNTVISVKRLIGRSL--PDVQ 97
Cdd:PTZ00400 44 VGIDLGTTNSCVAIMEGSQpKVIENSEGMRT-TPSVVAFTEDgQRLVGIVAKRQAVTNPENTVFATKRLIGRRYdeDATK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 98 SRYSSLPYEFVASENGlPLIITAQGPK-SPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLAG 176
Cdd:PTZ00400 123 KEQKILPYKIVRASNG-DAWIEAQGKKySPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAGKIAG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 177 LNVLRLLNEPTAAALAYGLDSGQEGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADWVIEQTKlK 256
Cdd:PTZ00400 202 LDVLRIINEPTAAALAFGMDKNDGKTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYLIAEFK-K 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 257 PQTANQQRELITL------ANQAKITLTNEKSAVISW----------QDFSVEISREQFNELIYPLVKRSLLTCRRALKD 320
Cdd:PTZ00400 281 QQGIDLKKDKLALqrlreaAETAKIELSSKTQTEINLpfitadqsgpKHLQIKLSRAKLEELTHDLLKKTIEPCEKCIKD 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 321 ANVESEEVQAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQADILVGNKtdSDMLLLDVVPLSLGIETM 400
Cdd:PTZ00400 361 AGVKKDELNDVILVGGMTRMPKVSETVKKIFGKEPSKGVNPDEAVAMGAAIQAGVLKGEI--KDLLLLDVTPLSLGIETL 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 401 GGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMSVHVLQGERELVDDCRSLGRFTLRGIPPMAAGAAHIRVTYQVDADGLL 480
Cdd:PTZ00400 439 GGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTFDVDANGIM 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 481 SVTAMEKSTKVQASIQIKPSYGLTDEEVTAMIKSSFDNAQEDLQARELAEQRVEADRVIESVIVALqADGAELLSTDEFH 560
Cdd:PTZ00400 519 NISAVDKSTGKKQEITIQSSGGLSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQL-SDLKDKISDADKD 597
|
570 580 590
....*....|....*....|....*....|..
gi 1720137003 561 HIETVLKQLMDVKQGSDRDAIAQGIKALDTAT 592
Cdd:PTZ00400 598 ELKQKITKLRSTLSSEDVDSIKDKTKQLQEAS 629
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
22-594 |
4.49e-158 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 468.78 E-value: 4.49e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASVRSGQSVILNDEQERSLVPSVVHYGVEEKKVGLEAFEQASLDPKNTVISVKRLIGRSLPD--VQSR 99
Cdd:PTZ00186 30 IGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDehIQKD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 100 YSSLPYEFVASENGLPLIITAQGPK-SPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLAGLN 178
Cdd:PTZ00186 110 IKNVPYKIVRAGNGDAWVQDGNGKQySPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTIAGLN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 179 VLRLLNEPTAAALAYGLDSGQEGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADWVIEQTKlKPQ 258
Cdd:PTZ00186 190 VIRVVNEPTAAALAYGMDKTKDSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYILEEFR-KTS 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 259 TANQQRELITL------ANQAKITLTNEKSAVISW----------QDFSVEISREQFNELIYPLVKRSLLTCRRALKDAN 322
Cdd:PTZ00186 269 GIDLSKERMALqrvreaAEKAKCELSSAMETEVNLpfitanadgaQHIQMHISRSKFEGITQRLIERSIAPCKQCMKDAG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 323 VESEEVQAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQADILVGNKtdSDMLLLDVVPLSLGIETMGG 402
Cdd:PTZ00186 349 VELKEINDVVLVGGMTRMPKVVEEVKKFFQKDPFRGVNPDEAVALGAATLGGVLRGDV--KGLVLLDVTPLSLGIETLGG 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 403 LVEKIIPRNTTIPVARAQEFTTFKDGQTAMSVHVLQGERELVDDCRSLGRFTLRGIPPMAAGAAHIRVTYQVDADGLLSV 482
Cdd:PTZ00186 427 VFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDIDANGICHV 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 483 TAMEKSTKVQASIQIKPSYGLTDEEVTAMIKSSFDNAQEDLQARELAEQRVEADrvIESVIVALQADGAELLSTDEFHHI 562
Cdd:PTZ00186 507 TAKDKATGKTQNITITANGGLSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAE--TQLTTAERQLGEWKYVSDAEKENV 584
|
570 580 590
....*....|....*....|....*....|....
gi 1720137003 563 ETVLKQLMDVKQGSD--RDAIAQGIKALDTATQE 594
Cdd:PTZ00186 585 KTLVAELRKAMENPNvaKDDLAAATDKLQKAVME 618
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
22-590 |
1.91e-154 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 460.09 E-value: 1.91e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASVRSGQ-SVILNDEQERSlVPSVVHYGVE-EKKVGLEAFEQASLDPKNTVISVKRLIGRSLPDVQSR 99
Cdd:PLN03184 42 VGIDLGTTNSAVAAMEGGKpTIVTNAEGQRT-TPSVVAYTKNgDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSEVDEE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 100 YSSLPYEFVASENG-LPLIITAQGPK-SPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLAGL 177
Cdd:PLN03184 121 SKQVSYRVVRDENGnVKLDCPAIGKQfAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRIAGL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 178 NVLRLLNEPTAAALAYGLDSGQEGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADWVIEQTK--- 254
Cdd:PLN03184 201 EVLRIINEPTAASLAYGFEKKSNETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLASNFKkde 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 255 ----LKPQTANQQreLITLANQAKITLTNEKSAVISW----------QDFSVEISREQFNELIYPLVKRSLLTCRRALKD 320
Cdd:PLN03184 281 gidlLKDKQALQR--LTEAAEKAKIELSSLTQTSISLpfitatadgpKHIDTTLTRAKFEELCSDLLDRCKTPVENALRD 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 321 ANVESEEVQAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQADILVGNKtdSDMLLLDVVPLSLGIETM 400
Cdd:PLN03184 359 AKLSFKDIDEVILVGGSTRIPAVQELVKKLTGKDPNVTVNPDEVVALGAAVQAGVLAGEV--SDIVLLDVTPLSLGLETL 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 401 GGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMSVHVLQGERELVDDCRSLGRFTLRGIPPMAAGAAHIRVTYQVDADGLL 480
Cdd:PLN03184 437 GGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFDIDANGIL 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 481 SVTAMEKSTKVQASIQIKPSYGLTDEEVTAMIKSSFDNAQEDLQARELAEQRVEADRVIESVIVALQADGaELLSTDEFH 560
Cdd:PLN03184 517 SVSATDKGTGKKQDITITGASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKELG-DKVPADVKE 595
|
570 580 590
....*....|....*....|....*....|
gi 1720137003 561 HIETVLKQLMDVKQGSDRDAIAQGIKALDT 590
Cdd:PLN03184 596 KVEAKLKELKDAIASGSTQKMKDAMAALNQ 625
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
21-540 |
6.22e-152 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 452.71 E-value: 6.22e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 21 AVGIDLGTTNSLVASVRSGQSVILNDEQERSLVPSVVHYGVEEKKVGLEAFEQASLDPKNTVISVKRLIGRSLPD--VQS 98
Cdd:PTZ00009 6 AIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDsvVQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 99 RYSSLPYEFVASENGLPLI-ITAQGPK---SPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARL 174
Cdd:PTZ00009 86 DMKHWPFKVTTGGDDKPMIeVTYQGEKktfHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAGTI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 175 AGLNVLRLLNEPTAAALAYGLDSGQEGI--IAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADWVIEQ 252
Cdd:PTZ00009 166 AGLNVLRIINEPTAAAIAYGLDKKGDGEknVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEFCVQD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 253 TKLKPQ----TANQQ--RELITLANQAKITLTNEKSAVISWQ------DFSVEISREQFNELIYPLVKRSLLTCRRALKD 320
Cdd:PTZ00009 246 FKRKNRgkdlSSNQRalRRLRTQCERAKRTLSSSTQATIEIDslfegiDYNVTISRARFEELCGDYFRNTLQPVEKVLKD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 321 ANVESEEVQAVVMVGGSTRVPYVREQVGEFF-GKTPLTSIDPDKVVALGAAIQADILVGNKTDS--DMLLLDVVPLSLGI 397
Cdd:PTZ00009 326 AGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFnGKEPCKSINPDEAVAYGAAVQAAILTGEQSSQvqDLLLLDVTPLSLGL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 398 ETMGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMSVHVLQGERELVDDCRSLGRFTLRGIPPMAAGAAHIRVTYQVDAD 477
Cdd:PTZ00009 406 ETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTFDIDAN 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720137003 478 GLLSVTAMEKSTKVQASIQIKPSYG-LTDEEVTAMIKSSFDNAQEDLQARElaeqRVEADRVIE 540
Cdd:PTZ00009 486 GILNVSAEDKSTGKSNKITITNDKGrLSKADIDRMVNEAEKYKAEDEANRE----RVEAKNGLE 545
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
21-376 |
9.15e-140 |
|
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: 411.52 E-value: 9.15e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 21 AVGIDLGTTNSLVASVRSGQSVILNDEQERSLVPSVVHYGVEEKKVGLEAFEQASLDPKNTVISVKRLIGRSL--PDVQS 98
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPENTIFDVKRLIGRKFddPSVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 99 RYSSLPYEFVASENGLPLIITAQGPK----SPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARL 174
Cdd:cd24028 81 DIKHWPFKVVEDEDGKPKIEVTYKGEektfSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAATI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 175 AGLNVLRLLNEPTAAALAYGLD--SGQEGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADWVIEQ 252
Cdd:cd24028 161 AGLNVLRIINEPTAAALAYGLDkkSSGERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLVEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 253 TKLK-----PQTANQQRELITLANQAKITLTNEKSAVISW------QDFSVEISREQFNELIYPLVKRSLLTCRRALKDA 321
Cdd:cd24028 241 FKKKhgkdlRENPRAMRRLRSACERAKRTLSTSTSATIEIdslydgIDFETTITRAKFEELCEDLFKKCLEPVEKVLKDA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720137003 322 NVESEEVQAVVMVGGSTRVPYVREQVGEFFGKTPL-TSIDPDKVVALGAAIQADIL 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 |
7.03e-138 |
|
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: 405.81 E-value: 7.03e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASVRSGQS-VILNDEQERSLVPSVVHYG-VEEKKVGLEAFEQASLDPKNTVISVKRLIGRSLPDVQSR 99
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAeVIIENSEGKRTTPSVVYFDkDGEVLVGEEAKNQALLDPENTIYSVKRLMGRDTKDKEEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 100 YSSLpyefvasenglpliitaqgpKSPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLAGLNV 179
Cdd:cd24029 81 GGKE--------------------YTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAELAGLNV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 180 LRLLNEPTAAALAYGLDS-GQEGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADWVIEQTKLKP- 257
Cdd:cd24029 141 LRLINEPTAAALAYGLDKeGKDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEKIGIETg 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 258 -----QTANQQRELITLANQAKITLTNEKSAVIS------WQDFSVEISREQFNELIYPLVKRSLLTCRRALKDANVESE 326
Cdd:cd24029 221 ilddkEDERARARLREAAEEAKIELSSSDSTDILilddgkGGELEIEITREEFEELIAPLIERTIDLLEKALKDAKLSPE 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1720137003 327 EVQAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQADILV 377
Cdd:cd24029 301 DIDRVLLVGGSSRIPLVREMLEEYFGREPISSVDPDEAVAKGAAIYAASLA 351
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
22-376 |
6.54e-136 |
|
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: 401.47 E-value: 6.54e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASVRSGQ-SVILNDEQERsLVPSVVHYGVE-EKKVGLEAFEQASLDPKNTVISVKRLIGRSLPDVQSR 99
Cdd:cd10234 2 IGIDLGTTNSCVAVMEGGKpTVIPNAEGGR-TTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 100 YSSLPYEFVASENGLPLIITAQGPKSPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLAGLNV 179
Cdd:cd10234 81 RKQVPYPVVSAGNGDAWVEIGGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIAGLEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 180 LRLLNEPTAAALAYGLDSGQEGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADWVIEQTK----- 254
Cdd:cd10234 161 LRIINEPTAAALAYGLDKKKDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEFKkeegi 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 255 --LKPQTANQQreLITLANQAKITLTNEKSAVISW----------QDFSVEISREQFNELIYPLVKRSLLTCRRALKDAN 322
Cdd:cd10234 241 dlSKDKMALQR--LKEAAEKAKIELSSVLETEINLpfitadasgpKHLEMKLTRAKFEELTEDLVERTIEPVEQALKDAK 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1720137003 323 VESEEVQAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQADIL 376
Cdd:cd10234 319 LSPSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVL 372
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
22-376 |
5.22e-120 |
|
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: 360.81 E-value: 5.22e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVAsVRSGQS--VILNDEQERSlVPSVVHYGVE-EKKVGLEAFEQASLDPKNTVISVKRLIGRSL--PDV 96
Cdd:cd11733 4 IGIDLGTTNSCVA-VMEGKTpkVIENAEGART-TPSVVAFTADgERLVGMPAKRQAVTNPENTLYATKRLIGRRFddPEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 97 QSRYSSLPYEFVASENGlPLIITAQGPK-SPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLA 175
Cdd:cd11733 82 QKDIKMVPYKIVKASNG-DAWVEAHGKKySPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDAGQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 176 GLNVLRLLNEPTAAALAYGLDSGQEGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADWVIEQTK- 254
Cdd:cd11733 161 GLNVLRIINEPTAAALAYGLDKKDDKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNYLVAEFKk 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 255 -----LKPQTANQQReLITLANQAKITLTNEKSAVISW----------QDFSVEISREQFNELIYPLVKRSLLTCRRALK 319
Cdd:cd11733 241 eqgidLSKDNLALQR-LREAAEKAKIELSSSLQTDINLpfitadasgpKHLNMKLTRAKFESLVGDLIKRTVEPCKKCLK 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720137003 320 DANVESEEVQAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQADIL 376
Cdd:cd11733 320 DAGVSKSDIGEVLLVGGMTRMPKVQETVQEIFGKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
22-376 |
1.45e-115 |
|
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: 349.59 E-value: 1.45e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASVRSGQSVILNDEQERSLVPSVVHYGVEEKKVGLEAFEQASLDPKNTVISVKRLIGRSL--PDVQSR 99
Cdd:cd10241 4 IGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTVFDVKRLIGRKFddKEVQKD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 100 YSSLPYEfVASENGLPLI-ITAQGPK---SPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLA 175
Cdd:cd10241 84 IKLLPFK-IVNKNGKPYIqVEVKGEKktfAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 176 GLNVLRLLNEPTAAALAYGLDS-GQEGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADWVIEQTK 254
Cdd:cd10241 163 GLNVLRIINEPTAAAIAYGLDKkGGEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFIKLFK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 255 LKPQT--ANQQRELITL---ANQAKITLTNEKSAVIS------WQDFSVEISREQFNELIYPLVKRSLLTCRRALKDANV 323
Cdd:cd10241 243 KKTGKdiSKDKRAVQKLrreVEKAKRALSSQHQARIEieslfdGEDFSETLTRAKFEELNMDLFRKTLKPVQKVLEDAGL 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1720137003 324 ESEEVQAVVMVGGSTRVPYVREQVGEFF-GKTPLTSIDPDKVVALGAAIQADIL 376
Cdd:cd10241 323 KKSDIDEIVLVGGSTRIPKVQQLLKDFFnGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
21-376 |
6.16e-108 |
|
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: 329.98 E-value: 6.16e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 21 AVGIDLGTTNSLVASVRSGQ-SVILNDEQERSlVPSVVHYGVEEKKVGLEAFEQASLDPKNTVISVKRLIGR--SLPDVQ 97
Cdd:cd10233 1 AIGIDLGTTYSCVGVWQNDKvEIIANDQGNRT-TPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRkfDDPVVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 98 SRYSSLPYEfVASENGLPLI-ITAQGPK---SPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAAR 173
Cdd:cd10233 80 SDMKHWPFK-VVSGGDKPKIqVEYKGETktfTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 174 LAGLNVLRLLNEPTAAALAYGLD--SGQEGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADWVIE 251
Cdd:cd10233 159 IAGLNVLRIINEPTAAAIAYGLDkkGKGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 252 QTKLKPQ---TANQQ--RELITLANQAKITLTNEKSAVISWQ------DFSVEISREQFNELIYPLVKRSLLTCRRALKD 320
Cdd:cd10233 239 EFKRKHKkdiSGNPRalRRLRTACERAKRTLSSSTQASIEIDslfegiDFYTSITRARFEELCADLFRSTLEPVEKVLRD 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720137003 321 ANVESEEVQAVVMVGGSTRVPYVREQVGEFF-GKTPLTSIDPDKVVALGAAIQADIL 376
Cdd:cd10233 319 AKLDKSQIHEIVLVGGSTRIPKVQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
21-378 |
2.19e-107 |
|
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: 328.64 E-value: 2.19e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 21 AVGIDLGTTNSLVAsVRSGQS--VILNDEQERSlVPSVVHYGVE-EKKVGLEAFEQASLDPKNTVISVKRLIGRSLPD-- 95
Cdd:cd11734 3 VIGIDLGTTNSCVA-VMEGKTprVIENAEGART-TPSVVAFTKDgERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDae 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 96 VQSRYSSLPYEFVASENGlPLIITAQGPK-SPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARL 174
Cdd:cd11734 81 VQRDIKEVPYKIVKHSNG-DAWVEARGQKySPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAGQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 175 AGLNVLRLLNEPTAAALAYGLDSGQEGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADWVIEQTK 254
Cdd:cd11734 160 AGLNVLRVINEPTAAALAYGLDKSGDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHIVSEFK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 255 -------LKPQTANQQ-RElitLANQAKITLTNEKSAVISW----------QDFSVEISREQFNELIYPLVKRSLLTCRR 316
Cdd:cd11734 240 kesgidlSKDRMAIQRiRE---AAEKAKIELSSTLQTDINLpfitadasgpKHINMKLTRAQFESLVKPLVDRTVEPCKK 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720137003 317 ALKDANVESEEVQAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQADILVG 378
Cdd:cd11734 317 ALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIFGREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
22-378 |
5.27e-106 |
|
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: 323.81 E-value: 5.27e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASVRSGQSVILNDEQERSLVPSVVhyGVEEKK---VGLEAFEQASLDPKNTVISVKRLIGrslpdvqs 98
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVV--SVDEDGsilVGRAAKERLVTHPDRTAASFKRFMG-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 99 rySSLPYEFvasenglpliitaqGPKS--PIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLAG 176
Cdd:cd10235 71 --TDKQYRL--------------GNHTfrAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELAG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 177 LNVLRLLNEPTAAALAYGL-DSGQEGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADWVIEQTKL 255
Cdd:cd10235 135 LKVERLINEPTAAALAYGLhKREDETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFLKKHRL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 256 K--PQTANQQRELITLANQAKITLTNEKSAVIS----WQDFSVEISREQFNELIYPLVKRSLLTCRRALKDANVESEEVQ 329
Cdd:cd10235 215 DftSLSPSELAALRKRAEQAKRQLSSQDSAEIRltyrGEELEIELTREEFEELCAPLLERLRQPIERALRDAGLKPSDID 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1720137003 330 AVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQADILVG 378
Cdd:cd10235 295 AVILVGGATRMPLVRQLIARLFGRLPLSSLDPDEAVALGAAIQAALKAR 343
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
21-376 |
4.15e-100 |
|
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: 309.61 E-value: 4.15e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 21 AVGIDLGTTNSLVASVRSGQSVILNDEQERSlVPSVVHYGVEEKKVGLEAFEQASLDPKNTVISVKRLIGRSL--PDVQS 98
Cdd:cd24093 1 AIGIDLGTTYSCVATYESSVEIIANEQGNRV-TPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFddESVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 99 RYSSLPYEfVASENGLPLI-ITAQGPK---SPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARL 174
Cdd:cd24093 80 DMKTWPFK-VIDVNGNPVIeVQYLGETktfSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 175 AGLNVLRLLNEPTAAALAYGLDSG---QEGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADWVIE 251
Cdd:cd24093 159 AGLNVLRIINEPTAAAIAYGLGAGkseKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 252 QTKLKPQT-----ANQQRELITLANQAKITL------TNEKSAVISWQDFSVEISREQFNELIYPLVKRSLLTCRRALKD 320
Cdd:cd24093 239 EFKKKTGLdisddARALRRLRTAAERAKRTLssvtqtTVEVDSLFDGEDFESSITRARFEDLNAALFKSTLEPVEQVLKD 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720137003 321 ANVESEEVQAVVMVGGSTRVPYVREQVGEFF-GKTPLTSIDPDKVVALGAAIQADIL 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; ... |
22-378 |
6.25e-97 |
|
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: 302.72 E-value: 6.25e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASVR--SGQSVILNDEQERSLVPSVVHYGVEEKK-VGLEAFEQASLDPKNTVISVKRLIGR-----SL 93
Cdd:cd10237 25 VGIDLGTTYSCVGVYHavTGEVEVIPDDDGHKSIPSVVAFTPDGGVlVGYDALAQAEHNPSNTIYDAKRFIGKtftkeEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 94 PDVQSRYsslPYEFVASENGLP-LIITAQGPK---SPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTK 169
Cdd:cd10237 105 EEEAKRY---PFKVVNDNIGSAfFEVPLNGSTlvvSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 170 DAARLAGLNVLRLLNEPTAAALAYGLDSgQEGI--IAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIAD 247
Cdd:cd10237 182 KAANLAGLEVLRVINEPTAAAMAYGLHK-KSDVnnVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQ 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 248 WVIEQTKLK-PQTANQQRELITL---ANQAKITLTNEKSAVISWQD-----------FSVEISREQFNELIYPLVKRSLL 312
Cdd:cd10237 261 YLIDRIAKKfGKTLTDKEDIQRLrqaVEEVKLNLTNHNSASLSLPLqislpsafkvkFKEEITRDLFETLNEDLFQRVLE 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720137003 313 TCRRALKDANVESEEVQAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQADILVG 378
Cdd:cd10237 341 PIRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFFGKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| 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 |
3.41e-82 |
|
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: 263.27 E-value: 3.41e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASVRSGQ-SVILNDEQERsLVPSVVHYGVEEKKVGLEAFEQASLDPKNTVISVKRLIGRSL--PDVQS 98
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGiDIVLNEVSNR-KTPTLVGFTEKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFddPEVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 99 RYSSLPYEFVASENGLPLIITAQGPK----SPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARL 174
Cdd:cd11732 80 EIKLLPFKLVELEDGKVGIEVSYNGEevvfSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 175 AGLNVLRLLNEPTAAALAYGL---------DSGQegIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLI 245
Cdd:cd11732 160 AGLNCLRLINETTAAALDYGIyksdlleseEKPR--IVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRAL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 246 ADWVIEQTKLKP-----QTANQQRELITLANQAKITLTNEKSAVISWQ------DFSVEISREQFNELIYPLVKRSLLTC 314
Cdd:cd11732 238 VEHFAEEFKKKYkidplENPKARLRLLDACEKLKKVLSANGEAPLNVEclmediDFSGQIKREEFEELIQPLLARLEAPI 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720137003 315 RRALKDANVESEEVQAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQA 373
Cdd:cd11732 318 KKALAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVFGKDLSTTLNADEAVARGCALQA 376
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
22-373 |
6.80e-79 |
|
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: 254.51 E-value: 6.80e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASVRSGQ-SVILNDEQERSlVPSVVHYGVEEKKVGLEAFEQASLDPKNTVISVKRLIGRSL--PDVQS 98
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGiETIANEYSDRC-TPSVVSFGEKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFddPFVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 99 RYSSLPYEFVASENGLPLI-ITAQGPK---SPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARL 174
Cdd:cd10228 80 ELKHLPYKVVKLPNGSVGIkVQYLGEEhvfTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 175 AGLNVLRLLNEPTAAALAYG-----LDSGQEG--IIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIAD 247
Cdd:cd10228 160 AGLNCLRLLNDTTAVALAYGiykqdLPAEEEKprNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 248 WVIE--QTKLKPQTANQQRELITL------------ANQAKITLTNEksAVISWQDFSVEISREQFNELIYPLVKRSLLT 313
Cdd:cd10228 240 HFAEefKTKYKIDVKSKPRALLRLlteceklkklmsANATELPLNIE--CFMDDKDVSGKMKRAEFEELCAPLFARVEVP 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 314 CRRALKDANVESEEVQAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQA 373
Cdd:cd10228 318 LRSALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVFGKEPSTTLNQDEAVARGCALQC 377
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
21-376 |
2.38e-78 |
|
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: 253.32 E-value: 2.38e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 21 AVGIDLGTTNSLVASVRSGQS-VILNDEQERSlVPSVVHYGVEEKKVGLEAFEQASLDPKNTVISVKRLIGRSL--PDVQ 97
Cdd:cd10238 2 AFGVHFGNTNACVAVYKDGRTdVVANDAGDRV-TPAVVAFTDNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFddPAVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 98 SRYSSLPYEfVASENGLPLI-ITAQGPK---SPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAAR 173
Cdd:cd10238 81 ELKKESKCK-IIEKDGKPGYeIELEEKKklvSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 174 LAGLNVLRLLNEPTAAALAYGLdsGQEGI-----IAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADW 248
Cdd:cd10238 160 KAGFNVLRVISEPSAAALAYGI--GQDDPtensnVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 249 VI----EQTKLKPQTanQQRELITL---ANQAKITLTNEKSAVISWQ------DFSVEISREQFNELIYPLVKRSLLTCR 315
Cdd:cd10238 238 LAsefkRQWKQDVRE--NKRAMAKLmnaAEVCKHVLSTLNTATCSVEslydgmDFQCNVSRARFESLCSSLFQQCLEPIQ 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720137003 316 RALKDANVESEEVQAVVMVGGSTRVPYVREQVGEFF-GKTPLTSIDPDKVVALGAAIQADIL 376
Cdd:cd10238 316 EVLNSAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFpSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
21-376 |
4.74e-77 |
|
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: 250.31 E-value: 4.74e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 21 AVGIDLGTTNSLVASVRS-GQSVILNDEQERsLVPSVVHYGVEEKKVGLEAFEQASLDPKNTVISVKRLIGRSL--PDVQ 97
Cdd:cd24095 3 VVGIDFGNENCVVAVARKgGIDVVLNEESNR-ETPSMVSFGEKQRFLGEAAAASILMNPKNTISQLKRLIGRKFddPEVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 98 SRYSSLPYEFVASENGLPLI-ITAQGPK---SPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAAR 173
Cdd:cd24095 82 RDLKLFPFKVTEGPDGEIGInVNYLGEQkvfTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 174 LAGLNVLRLLNEPTAAALAYG-----LDSGQEGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFD-----H 243
Cdd:cd24095 162 IAGLNCLRLMNETTATALAYGiyktdLPETDPTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDevlfdH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 244 LIADWvieQTKLKPQTANQQRELITL---ANQAKITLTNEKSAVISWQ------DFSVEISREQFNELIYPLVKRSLLTC 314
Cdd:cd24095 242 FAAEF---KEKYKIDVKSNKKASLRLraaCEKVKKILSANPEAPLNIEclmedkDVKGMITREEFEELAAPLLERLLEPL 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720137003 315 RRALKDANVESEEVQAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQADIL 376
Cdd:cd24095 319 EKALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFFGKEPSRTMNASECVARGCALQCAML 380
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
22-376 |
2.00e-68 |
|
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: 227.26 E-value: 2.00e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASVRS-GQSVILNDEQERSlVPSVVHYGVEEKKVGLEAFEQASLDPKNTVISVKRLIGRSL--PDVQS 98
Cdd:cd24094 1 VGLDLGNLNSVIAVARNrGIDIIVNEVSNRS-TPSLVGFGPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFsdPEVAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 99 RYSSLPYEFVASENGLPLIITAQGPK---SPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLA 175
Cdd:cd24094 80 EEKYFTAKLVDANGEVGAEVNYLGEKhvfSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 176 GLNVLRLLNEPTAAALAYG-----LDSGQEG--IIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADW 248
Cdd:cd24094 160 GLNPLRLMNDTTAAALGYGitktdLPEPEEKprIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 249 VIEQTKLK--------PQTANQqreLITLANQAKITLTNEKSAVISWQ------DFSVEISREQFNELIYPLVKRSLLTC 314
Cdd:cd24094 240 FADEFKEKykidvrsnPKAYFR---LLAAAEKLKKVLSANAQAPLNVEslmndiDVSSMLKREEFEELIAPLLERVTAPL 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720137003 315 RRALKDANVESEEVQAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQADIL 376
Cdd:cd24094 317 EKALAQAGLTKDEIDFVELVGGTTRVPALKESISAFFGKPLSTTLNQDEAVARGAAFACAIL 378
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
22-375 |
4.05e-62 |
|
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: 210.57 E-value: 4.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASVRSGQ-SVILNDEQERSlVPSVVHYGVEEKKVGLEAFEQASLDPKNTVISVKRLIGRSLPD--VQS 98
Cdd:cd11737 3 VGFDLGFQSCYVAVARAGGiETVANEYSDRS-TPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDpfVQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 99 RYSSLPYEFVASENGLPLI----ITAQGPKSPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARL 174
Cdd:cd11737 82 EKPSLAYELVQLPTGTTGIkvmyMEEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 175 AGLNVLRLLNEPTAAALAYG-----LDSGQEG--IIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIAD 247
Cdd:cd11737 162 AGLNCLRLMNETTAVALAYGiykqdLPAPEEKprNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVLVN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 248 WVIEQ--TKLKPQTANQQRELITLANQA----KITLTNEKSAVISWQ------DFSVEISREQFNELIYPLVKRSLLTCR 315
Cdd:cd11737 242 HFCEEfgKKYKLDIKSKIRALLRLFQECeklkKLMSANASDLPLNIEcfmndiDVSGTMNRGQFEEMCADLLARVEPPLR 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 316 RALKDANVESEEVQAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQADI 375
Cdd:cd11737 322 SVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFFGKEVSTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
22-373 |
1.55e-61 |
|
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: 208.12 E-value: 1.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASVRSGQ--SVILNDEQERSLvPSVVHYGVEEKKVGLEAFEQASLDPKNTVISVKRLIGrslpdvqsr 99
Cdd:cd10230 3 LGIDLGSEFIKVALVKPGVpfEIVLNEESKRKT-PSAVAFRNGERLFGDDALALATRFPENTFSYLKDLLG--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 100 YSslPYEFVASenglpliitaqgpkspievssdILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLAGLNV 179
Cdd:cd10230 73 YS--VEELVAM----------------------ILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIAGLNV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 180 LRLLNEPTAAALAYGLDSGQEG----IIAVYDLGGGTFDISILRLS------------KGIFEVLATGGDTALGGDDFDH 243
Cdd:cd10230 129 LSLINDNTAAALNYGIDRRFENnepqNVLFYDMGASSTSATVVEFSsvkekdkgknktVPQVEVLGVGWDRTLGGLEFDL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 244 LIADW----VIEQTKLKPQTANQQR---ELITLANQAKITLTNEKSAVISW------QDFSVEISREQFNELIYPLVKRS 310
Cdd:cd10230 209 RLADHladeFNEKHKKDKDVRTNPRamaKLLKEANRVKEVLSANTEAPASIeslyddIDFRTKITREEFEELCADLFERV 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720137003 311 LLTCRRALKDANVESEEVQAVVMVGGSTRVPYVREQVGEFFGKTPL-TSIDPDKVVALGAAIQA 373
Cdd:cd10230 289 VAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELgKHLNADEAAALGAAFYA 352
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
22-376 |
6.30e-60 |
|
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: 204.77 E-value: 6.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASVRSGQSVILNDEQERSLVPSVVHYGVEEKKVGLEAFEQASLDPKNTVISVKRLIGRSLPD--VQSR 99
Cdd:cd11738 3 VGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDpfVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 100 YSSLPYEFVASENGLPLI----ITAQGPKSPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLA 175
Cdd:cd11738 83 KIKLPYELQKMPNGSTGVkvryLDEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 176 GLNVLRLLNEPTAAALAYG--------LDSGQEGIIAVyDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIAD 247
Cdd:cd11738 163 GLNCLRLMNETTAVALAYGiykqdlpaLEEKPRNVVFV-DMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVLVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 248 WVIEQ--TKLKPQTANQQRELITL------------ANQAKITLTNEksAVISWQDFSVEISREQFNELIYPLVKRSLLT 313
Cdd:cd11738 242 YFCEEfkTKYKLNVKENIRALLRLyqeceklkklmsANASDLPLNIE--CFMNDIDVSSKMNRAQFEELCASLLARVEPP 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720137003 314 CRRALKDANVESEEVQAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQADIL 376
Cdd:cd11738 320 LKAVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAIL 382
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
22-372 |
1.28e-59 |
|
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: 203.94 E-value: 1.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASVRSGQSVILNDEQERSLVPSVVHYGVEEKKVGLEAFEQASLDPKNTVISVKRLIGRSLPD--VQSR 99
Cdd:cd11739 3 VGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDpfVQKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 100 YSSLPYEFVASEN---GLPLIITAQGPKSPIE-VSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLA 175
Cdd:cd11739 83 KENLSYDLVPLKNggvGVKVMYLDEEHHFSIEqITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 176 GLNVLRLLNEPTAAALAYG-----LDSGQEG--IIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADW 248
Cdd:cd11739 163 GLNCLRLMNDMTAVALNYGiykqdLPAPDEKprIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKLVEH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 249 VIEQ--TKLKPQTANQQRELITL------------ANQAKITLTNEksAVISWQDFSVEISREQFNELIYPLVKRSLLTC 314
Cdd:cd11739 243 FCAEfkTKYKLDVKSKIRALLRLyqeceklkklmsSNSTDLPLNIE--CFMNDKDVSGKMNRSQFEELCADLLQRIEVPL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720137003 315 RRALKDANVESEEVQAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAIQ 372
Cdd:cd11739 321 YSLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFFGKDVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
21-376 |
4.30e-57 |
|
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: 196.04 E-value: 4.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 21 AVGIDLGTTNSLVASVRSGQ--SVILNDEQERSlVPSVVHYGVEEKKVGLEAFEQASLDPKNTVISVKRLIGrslpdvqs 98
Cdd:cd10232 2 VIGISFGNSNSSIAIINKDGraEVIANEDGDRQ-IPSILAYHGDEEYHGSQAKAQLVRNPKNTVANFRDLLG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 99 rysslpyefvasenglPLIITAQgpkspiEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLAGLN 178
Cdd:cd10232 73 ----------------TTTLTVS------EVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAAAAGLE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 179 VLRLLNEPTAAALAYGL------DSGQEGIIAVYDLGGGTFDISILRLSKGIFEVLATGGDTALGGDDFDHLIADWVIEQ 252
Cdd:cd10232 131 VLQLIPEPAAAALAYDLraetsgDTIKDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVGHFAKE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 253 TKLKPQTA--NQQRELITLANQAKIT---LTNEKSAVISWQ------DFSVEISREQFNELIYPLVKRSLLTCRRALKDA 321
Cdd:cd10232 211 FKKKTKTDprKNARSLAKLRNAAEITkraLSQGTSAPCSVEsladgiDFHSSINRTRYELLASKVFQQFADLVTDAIEKA 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720137003 322 NVESEEVQAVVMVGGSTRVPYVREQVGEFFGKT----PLTSIDPDKVVALGAAIQADIL 376
Cdd:cd10232 291 GLDPLDIDEVLLAGGASRTPKLASNFEYLFPEStiirAPTQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
22-371 |
6.19e-46 |
|
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: 165.36 E-value: 6.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASVRSGQSVILNDEqerslvpsvvhygveekkvgleafeqasldpkntvisvkrlIGRSLPDVQSRYS 101
Cdd:cd10170 1 VGIDFGTTYSGVAYALLGPGEPPLVV-----------------------------------------LQLPWPGGDGGSS 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 102 SLPyefvasenglpliitaqgpkSPIEVSSDILSRLNHIAEQRLGGELSG-------VVITVPAYFDDAQRQSTKDAARL 174
Cdd:cd10170 40 KVP--------------------SVLEVVADFLRALLEHAKAELGDRIWElekapieVVITVPAGWSDAAREALREAARA 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 175 AGL----NVLRLLNEPTAAALAYGLDSGQEG------IIAVYDLGGGTFDISILRLSKGIFEVL---ATGGDTALGGDDF 241
Cdd:cd10170 100 AGFgsdsDNVRLVSEPEAAALYALEDKGDLLplkpgdVVLVCDAGGGTVDLSLYEVTSGSPLLLeevAPGGGALLGGTDI 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 242 DHLIADWVIEQ-----TKLKPQTANQQRELITLANQAKITLTNEKSAVISW---------QDFSVEISREQFNELIYPLV 307
Cdd:cd10170 180 DEAFEKLLREKlgdkgKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVpsllggglpELGLEKGTLLLTEEEIRDLF 259
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 308 KRSLLTCRRALKDA--NVESEEVQAVVMVGGSTRVPYVREQVGEFFGKTPL----TSIDPDKVVALGAAI 371
Cdd:cd10170 260 DPVIDKILELIEEQleAKSGTPPDAVVLVGGFSRSPYLRERLRERFGSAGIiivlRSDDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
22-370 |
1.52e-35 |
|
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: 138.56 E-value: 1.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASVRSGQSVILNDEQERSLVPSVVHYGVEEKKVGLEA-FEQASLDPKNTVISVKRLIgrslpdvQSRY 100
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREEEGAESIyFGNDAIDAYLNDPEEGRLI-------KSVK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 101 SSLPYEfvasenGLPLIITAQGPKSPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYF------DDAQRQST-KDAAR 173
Cdd:cd10231 74 SFLGSS------LFDETTIFGRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFsgvgaeDDAQAESRlRDAAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 174 LAGLNVLRLLNEPTAAALAYGLDSGQEGIIAVYDLGGGTFDISILRLSKGIFE----VLATGGDtALGGDDFDHLIADWV 249
Cdd:cd10231 148 RAGFRNVEFQYEPIAAALDYEQRLDREELVLVVDFGGGTSDFSVLRLGPNRTDrradILATSGV-GIGGDDFDRELALKK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 250 I----------------------------EQTKLK--------------PQTANQQRELITL---------------ANQ 272
Cdd:cd10231 227 VmphlgrgstyvsgdkglpvpawlyadlsNWHAISllytkktlrllldlRRDAADPEKIERLlslvedqlghrlfraVEQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 273 AKITLTNEKSAVISWQDFSVEI----SREQFNELIYPLVKRSLLTCRRALKDANVESEEVQAVVMVGGSTRVPYVREQVG 348
Cdd:cd10231 307 AKIALSSADEATLSFDFIEISIkvtiTRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRVFLTGGSSQSPAVRQALA 386
|
410 420
....*....|....*....|..
gi 1720137003 349 EFFGKTPLTSIDPDKVVALGAA 370
Cdd:cd10231 387 SLFGQARLVEGDEFGSVAAGLA 408
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
20-371 |
8.08e-17 |
|
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: 82.71 E-value: 8.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 20 LAVGIDLGTTNSLVA-SVRSGQSVIlndeqerslvpsVVHYGVEEKKVGLEAFEQAS---LDPKNTVISvkrlIGRS--- 92
Cdd:cd10229 1 VVVAIDFGTTYSGYAySFITDPGDI------------HTMYNWWGAPTGVSSPKTPTcllLNPDGEFHS----FGYEare 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 93 -----LPDVQSRYSSLPYEFVA----SENGLPLIITAQGPKS--PIEVSSDILSRLNHIAEQRLGGELSGV--------V 153
Cdd:cd10229 65 kysdlAEDEEHQWLYFFKFKMMllseKELTRDTKVKAVNGKSmpALEVFAEALRYLKDHALKELRDRSGSSldeddirwV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 154 ITVPAYFDDAQRQSTKDAARLAGL------NVLRLLNEPTAAALAYG--LDSGQEGIIA------VYDLGGGTFDISILR 219
Cdd:cd10229 145 LTVPAIWSDAAKQFMREAAVKAGLiseensEQLIIALEPEAAALYCQklLAEGEEKELKpgdkylVVDCGGGTVDITVHE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 220 L-SKGIFEVLATGGDTALGG----DDFDHLIADwVIEQTKLKPQTANQQRELITLANQAKITLTNeksaviswqdFSVEI 294
Cdd:cd10229 225 VlEDGKLEELLKASGGPWGStsvdEEFEELLEE-IFGDDFMEAFKQKYPSDYLDLLQAFERKKRS----------FKLRL 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720137003 295 SREQFNELIYPLVKRsLLTCRRALKDaNVESEEVQAVVMVGGSTRVPYVREQVGEFFG--KTPLTSIDPDKVVALGAAI 371
Cdd:cd10229 294 SPELMKSLFDPVVKK-IIEHIKELLE-KPELKGVDYIFLVGGFAESPYLQKAVKEAFStkVKIIIPPEPGLAVVKGAVL 370
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
22-371 |
4.14e-12 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 67.85 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVAsvRSGQSVILNDeqerslvPSVVHYGVEEKK---VGLEAfeqasldpkntvisvKRLIGRSLPDVQS 98
Cdd:PRK13930 11 IGIDLGTANTLVY--VKGKGIVLNE-------PSVVAIDTKTGKvlaVGEEA---------------KEMLGRTPGNIEA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 99 RYsslpyefvasenglPLiitAQGPKSPIEVSSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLAGLN 178
Cdd:PRK13930 67 IR--------------PL---KDGVIADFEATEAMLRYFIKKARGRRFFRKPRIVICVPSGITEVERRAVREAAEHAGAR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 179 VLRLLNEPTAAALAYGLDSGQ-EG--IIavyDLGGGTFDISILRLSkGIfevlATGGDTALGGDDFDHLIADWVIEQTKL 255
Cdd:PRK13930 130 EVYLIEEPMAAAIGAGLPVTEpVGnmVV---DIGGGTTEVAVISLG-GI----VYSESIRVAGDEMDEAIVQYVRRKYNL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 256 kpqtanqqreLI--TLANQAKITL------TNEKSAVISWQDF------SVEISREQFNELIYPLVKRSLLTCRRALKDA 321
Cdd:PRK13930 202 ----------LIgeRTAEEIKIEIgsayplDEEESMEVRGRDLvtglpkTIEISSEEVREALAEPLQQIVEAVKSVLEKT 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720137003 322 nveSEEVQA------VVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAI 371
Cdd:PRK13930 272 ---PPELAAdiidrgIVLTGGGALLRGLDKLLSEETGLPVHIAEDPLTCVARGTGK 324
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
130-232 |
9.37e-12 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 65.62 E-value: 9.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 130 SSDILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLAGLNVLRLLNEPTAAALAYGLDSGqegiiAVYDLG 209
Cdd:PRK15080 69 AVTIVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGIDNG-----AVVDIG 143
|
90 100
....*....|....*....|....
gi 1720137003 210 GGTFDISILRLSKGIFEV-LATGG 232
Cdd:PRK15080 144 GGTTGISILKDGKVVYSAdEPTGG 167
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
22-371 |
1.76e-11 |
|
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins; MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466824 [Multi-domain] Cd Length: 317 Bit Score: 65.57 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASvrSGQSVILNDeqerslvPSVVHYGVEEKK---VGLEAfeqasldpkntvisvKRLIGRSLPDVQs 98
Cdd:cd10225 2 IGIDLGTANTLVYV--KGKGIVLNE-------PSVVAVDKNTGKvlaVGEEA---------------KKMLGRTPGNIV- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 99 rysslpyefvasenglplIITaqgpksPIE--VSSDI-LSR--LNHIAEQRLGGELSG---VVITVPAYFDDAQRQSTKD 170
Cdd:cd10225 57 ------------------AIR------PLRdgVIADFeATEamLRYFIRKAHRRRGFLrprVVIGVPSGITEVERRAVKE 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 171 AARLAGLNVLRLLNEPTAAALAYGLDSGQEGIIAVYDLGGGTFDISILRLSkGIfeVLATGgdTALGGDDFDHLIADWVI 250
Cdd:cd10225 113 AAEHAGAREVYLIEEPMAAAIGAGLPIEEPRGSMVVDIGGGTTEIAVISLG-GI--VTSRS--VRVAGDEMDEAIINYVR 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 251 EQTKLK--PQTAnqqrELITLANQAKITLTNEKSAVISWQDF------SVEISREQFNELIYPLVKRSLLTCRRALKDAn 322
Cdd:cd10225 188 RKYNLLigERTA----ERIKIEIGSAYPLDEELSMEVRGRDLvtglprTIEITSEEVREALEEPVNAIVEAVRSTLERT- 262
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 323 veSEEVQA------VVMVGGSTRVP----YVREQVGeffgkTPLT-SIDPDKVVALGAAI 371
Cdd:cd10225 263 --PPELAAdivdrgIVLTGGGALLRgldeLLREETG-----LPVHvADDPLTCVAKGAGK 315
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
22-371 |
3.59e-11 |
|
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: 64.88 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASvrSGQSVILNDeqerslvPSVVHYGVEEKK---VGLEAfeqasldpkntvisvKRLIGRSlpdvqs 98
Cdd:pfam06723 4 IGIDLGTANTLVYV--KGKGIVLNE-------PSVVAINTKTKKvlaVGNEA---------------KKMLGRT------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 99 rysslpyefvasenglPLIITAQGPK-----SPIEVSSDILsrlNHIAEQRLGGEL---SGVVITVPAYFDDAQRQSTKD 170
Cdd:pfam06723 54 ----------------PGNIVAVRPLkdgviADFEVTEAML---KYFIKKVHGRRSfskPRVVICVPSGITEVERRAVKE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 171 AARLAGLNVLRLLNEPTAAALAYGLDSGQEGIIAVYDLGGGTFDISILRLSkGIfevlATGGDTALGGDDFDHLIADWVI 250
Cdd:pfam06723 115 AAKNAGAREVFLIEEPMAAAIGAGLPVEEPTGNMVVDIGGGTTEVAVISLG-GI----VTSKSVRVAGDEFDEAIIKYIR 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 251 EQTKLK--PQTANQQRelITLANQAKitLTNEKSAVISWQDF------SVEISREQFNELIYPLVKRSLLTCRRALKDAN 322
Cdd:pfam06723 190 KKYNLLigERTAERIK--IEIGSAYP--TEEEEKMEIRGRDLvtglpkTIEISSEEVREALKEPVSAIVEAVKEVLEKTP 265
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1720137003 323 VE-SEEV--QAVVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAI 371
Cdd:pfam06723 266 PElAADIvdRGIVLTGGGALLRGLDKLLSDETGLPVHIAEDPLTCVALGTGK 317
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
22-371 |
1.21e-10 |
|
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 440695 [Multi-domain] Cd Length: 339 Bit Score: 63.17 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASvrSGQSVILNDeqerslvPSVVHYGVEEKK---VGLEAfeqasldpkntvisvKRLIGRslpdvqs 98
Cdd:COG1077 10 IGIDLGTANTLVYV--KGKGIVLNE-------PSVVAIDKKTGKvlaVGEEA---------------KEMLGR------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 99 ryssLPYEFVAS---ENGlpliitaqgpkspieVSSDIlsrlnHIAEQRL---------GGELSG--VVITVPAYFDDAQ 164
Cdd:COG1077 59 ----TPGNIVAIrplKDG---------------VIADF-----EVTEAMLkyfikkvhgRRSFFRprVVICVPSGITEVE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 165 RQSTKDAARLAGLNVLRLLNEPTAAALAYGLDSGQ-EGIIAVyDLGGGTFDISILRLSkGIfeVLATGgdTALGGDDFDH 243
Cdd:COG1077 115 RRAVRDAAEQAGAREVYLIEEPMAAAIGAGLPIEEpTGNMVV-DIGGGTTEVAVISLG-GI--VVSRS--IRVAGDELDE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 244 LIADWVIEQTKLK--PQTAnqqrELItlanqaKITL------TNEKSAVISWQDF------SVEISREQFNELIYPLVKR 309
Cdd:COG1077 189 AIIQYVRKKYNLLigERTA----EEI------KIEIgsayplEEELTMEVRGRDLvtglpkTITITSEEIREALEEPLNA 258
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720137003 310 SLLTCRRALKDAnveSEEVQA------VVMVGGSTRVPYVREQVGEFFGKTPLTSIDPDKVVALGAAI 371
Cdd:COG1077 259 IVEAIKSVLEKT---PPELAAdivdrgIVLTGGGALLRGLDKLLSEETGLPVHVAEDPLTCVARGTGK 323
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
132-246 |
2.53e-10 |
|
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity.
Pssm-ID: 466897 [Multi-domain] Cd Length: 241 Bit Score: 61.13 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 132 DILSRLNHIAEQRLGGELSGVVITVPAYFDDAQRQSTKDAARLAGLNVLRLLNEPTAAALAYGLDSGqegiiAVYDLGGG 211
Cdd:cd24047 47 RIVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGIRDG-----AVVDIGGG 121
|
90 100 110
....*....|....*....|....*....|....*
gi 1720137003 212 TFDISILRlsKGifEVLATgGDTALGGDDFDHLIA 246
Cdd:cd24047 122 TTGIAVLK--DG--KVVYT-ADEPTGGTHLSLVLA 151
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
123-367 |
1.46e-09 |
|
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466854 [Multi-domain] Cd Length: 282 Bit Score: 59.23 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 123 PKSPIEVSSDILSRLnhiaEQRLGGELSGVVITVPAYFDdaqrqSTKDAARLAGLNVLRLLNEPTAAALAYGLDSGQEGI 202
Cdd:cd24004 45 ISKVAESIKELLKEL----EEKLGSKLKDVVIAIAKVVE-----SLLNVLEKAGLEPVGLTLEPFAAANLLIPYDMRDLN 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 203 IAVYDLGGGTFDISILRlsKGifeVLATGGDTALGGDDFDHLIADwvieQTKLKPQTAnqqrELItlanqaKITLTNEKS 282
Cdd:cd24004 116 IALVDIGAGTTDIALIR--NG---GIEAYRMVPLGGDDFTKAIAE----GFLISFEEA----EKI------KRTYGIFLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 283 AVISwQDFSVEISREQFNELIYPLVKRSLLTCRRALKDANVESEEVQAVVMVGGSTRVPYVREQVGEFFGkTPLTSIDPD 362
Cdd:cd24004 177 IEAK-DQLGFTINKKEVYDIIKPVLEELASGIANAIEEYNGKFKLPDAVYLVGGGSKLPGLNEALAEKLG-LPVERIAPR 254
|
....*
gi 1720137003 363 KVVAL 367
Cdd:cd24004 255 NIGAI 259
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
22-280 |
7.94e-09 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 57.61 E-value: 7.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASVRSGqsVILNDeqerslvPSVVHYGVEEKKV---GLEAfeqasldpkntvisvKRLIGRSlpdvqs 98
Cdd:PRK13929 7 IGIDLGTANILVYSKNKG--IILNE-------PSVVAVDTETKAVlaiGTEA---------------KNMIGKT------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 99 rysslPYEFVASEnglPLiitAQGPKSPIEVSSDILSRLNHIAEQRLGGELS--GVVITVPAYFDDAQRQSTKDAARLAG 176
Cdd:PRK13929 57 -----PGKIVAVR---PM---KDGVIADYDMTTDLLKQIMKKAGKNIGMTFRkpNVVVCTPSGSTAVERRAISDAVKNCG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 177 LNVLRLLNEPTAAALAYGLDSGQEGIIAVYDLGGGTFDISILRlskgiFEVLATGGDTALGGDDFDHLIADWVIEQTKL- 255
Cdd:PRK13929 126 AKNVHLIEEPVAAAIGADLPVDEPVANVVVDIGGGTTEVAIIS-----FGGVVSCHSIRIGGDQLDEDIVSFVRKKYNLl 200
|
250 260
....*....|....*....|....*.
gi 1720137003 256 -KPQTANQQRELITLANQAKITLTNE 280
Cdd:PRK13929 201 iGERTAEQVKMEIGYALIEHEPETME 226
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
22-360 |
7.37e-08 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 55.25 E-value: 7.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVASVRSGQSVILNDEQERSLVPSVV--------------HYGVEEkkvgLEAFEQASLdpkNTVISVKR 87
Cdd:PRK11678 3 IGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTLcaptreavsewlyrHLDVPA----YDDERQALL---RRAIRYNR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 88 L--IGRSLPDVQ------SRYSSLPYE--FVASenglpliitaqgPKS--------PIEVS--SDI----LSRLNHIAEQ 143
Cdd:PRK11678 76 EedIDVTAQSVFfglaalAQYLEDPEEvyFVKS------------PKSflgasglkPQQVAlfEDLvcamMLHIKQQAEA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 144 RLGGELSGVVITVPAYF-----DDAQRQST---KDAARLAGLNVLRLLNEPTAAALAYGLDSGQEGIIAVYDLGGGTFDI 215
Cdd:PRK11678 144 QLQAAITQAVIGRPVNFqglggEEANRQAEgilERAAKRAGFKDVEFQFEPVAAGLDFEATLTEEKRVLVVDIGGGTTDC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 216 SILRLS--------------------------------KGIFEVLATGGDTALG-------------------------- 237
Cdd:PRK11678 224 SMLLMGpswrgradrsasllghsgqriggndldialafKQLMPLLGMGSETEKGialpslpfwnavaindvpaqsdfysl 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 238 --GDDFDHLIADwVIEQTKLKP-QTANQQR---ELITLANQAKITLTNEKSAVISW----QDFSVEISREQFNELIYPLV 307
Cdd:PRK11678 304 anGRLLNDLIRD-AREPEKVARlLKVWRQRlsyRLVRSAEEAKIALSDQAETRASLdfisDGLATEISQQGLEEAISQPL 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1720137003 308 KRSLLTCRRALKDANVESEevqAVVMVGGSTRVPYVREQVGEFFGKTPLTSID 360
Cdd:PRK11678 383 ARILELVQLALDQAQVKPD---VIYLTGGSARSPLIRAALAQQLPGIPIVGGD 432
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
22-255 |
4.86e-07 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 52.21 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVasVRSGQSVILNDeqerslvPSVVhygveekkvgleAFEQASldpkNTVISV----KRLIGRSlpdvq 97
Cdd:PRK13928 6 IGIDLGTANVLV--YVKGKGIVLNE-------PSVV------------AIDKNT----NKVLAVgeeaRRMVGRT----- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 98 srysslPYEFVASEnglPLiitAQGPKSPIEVSSDILSR-LNHIAEQRLggeLSG--VVITVPAYFDDAQRQSTKDAARL 174
Cdd:PRK13928 56 ------PGNIVAIR---PL---RDGVIADYDVTEKMLKYfINKACGKRF---FSKprIMICIPTGITSVEKRAVREAAEQ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 175 AGLNVLRLLNEPTAAALAYGLDSGQEGIIAVYDLGGGTFDISILRLSkGIfeVLATggDTALGGDDFDHLIADWVIEQTK 254
Cdd:PRK13928 121 AGAKKVYLIEEPLAAAIGAGLDISQPSGNMVVDIGGGTTDIAVLSLG-GI--VTSS--SIKVAGDKFDEAIIRYIRKKYK 195
|
.
gi 1720137003 255 L 255
Cdd:PRK13928 196 L 196
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
22-249 |
5.40e-06 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 48.93 E-value: 5.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTNSLVaSVRsGQSVILNDeqerslvPSVVHYGVEEKK---VGLEAfeqasldpkntvisvKRLIGRslpdvqs 98
Cdd:PRK13927 8 LGIDLGTANTLV-YVK-GKGIVLNE-------PSVVAIRTDTKKvlaVGEEA---------------KQMLGR------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 99 rysslpyefvASENglpliITAqgpKSPIE--VSSDI---LSRLNHIAEQRLGGELSG--VVITVPAYFDDAQRQSTKDA 171
Cdd:PRK13927 57 ----------TPGN-----IVA---IRPMKdgVIADFdvtEKMLKYFIKKVHKNFRPSprVVICVPSGITEVERRAVRES 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720137003 172 ARLAGLNVLRLLNEPTAAALAYGLDSGQ-EGIIAVyDLGGGTFDISILRLSkGIfeVLATGgdTALGGDDFDHLIADWV 249
Cdd:PRK13927 119 ALGAGAREVYLIEEPMAAAIGAGLPVTEpTGSMVV-DIGGGTTEVAVISLG-GI--VYSKS--VRVGGDKFDEAIINYV 191
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
153-354 |
4.15e-05 |
|
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: 46.11 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 153 VITVPAYFDDAQRQSTKDAARLAGL----NVLRLLN--EPTAAAL-AYGLDSgqegiIAVYDLGGGTFDISILRLSK--G 223
Cdd:cd11736 144 VLTVPAIWKQPAKQFMREAAYLAGLvspeNPEQLLIalEPEAASIyCRKLDR-----YIVADCGGGTVDLTVHQIEQpqG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 224 IFEVL--ATGGDTALGGDDFD------HLIADWVIEQTKLKPQTANQQrelITLANQAKitltnEKSAviswqdfSVEIS 295
Cdd:cd11736 219 TLKELykASGGPYGAVGVDLAfekllcQIFGEDFIATFKAKRPAAWVD---LTIAFEAR-----KRTA-------ALRMS 283
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720137003 296 REQFNELIYPLVKRSLLTCRRALKDANVESeeVQAVVMVGGSTRVPYVREQVGEFFGKT 354
Cdd:cd11736 284 SEAMNELFQPTISQIIQHIDDLMKKPEVKG--IKFLFLVGGFAESPMLQRAVQAAFGNI 340
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
22-371 |
7.23e-05 |
|
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.
Pssm-ID: 466899 [Multi-domain] Cd Length: 339 Bit Score: 45.35 E-value: 7.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 22 VGIDLGTTN-SLVASVRSGQSVILNDEQERSLVPSVVHYGVEEKKVGL-----EAFEQASLDPKNTVISVkrligrSLPD 95
Cdd:cd24049 1 LGIDIGSSSiKAVELKRSGGGLVLVAFAIIPLPEGAIVDGEIADPEALaealkKLLKENKIKGKKVVVAL------PGSD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 96 VQSRYSSLPyefVASENGLPLIITAQ------GPKSPIEVSSDILSRlnhiaEQRLGGELSGVVITVPAyfDDAQRQstK 169
Cdd:cd24049 75 VIVRTIKLP---KMPEKELEEAIRFEaeqylpFPLEEVVLDYQILGE-----VEEGGEKLEVLVVAAPK--EIVESY--L 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 170 DAARLAGLNVLRLlnEPTAAALA----YGLDSGQEGIIAVYDLGGGTFDISILRlsKGIFeVLATggDTALGGDDFDHLI 245
Cdd:cd24049 143 ELLKEAGLKPVAI--DVESFALAraleYLLPDEEEETVALLDIGASSTTLVIVK--NGKL-LFTR--SIPVGGNDITEAI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 246 AdwviEQTKLKPQTanqqrelitlANQAKITLTNEKSAVISWQDFSVEISREQFNELIYpLVKRSLLTCRRALKDANVES 325
Cdd:cd24049 216 A----KALGLSFEE----------AEELKREYGLLLEGEEGELKKVAEALRPVLERLVS-EIRRSLDYYRSQNGGEPIDK 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720137003 326 eevqaVVMVGGSTRVPYVREQVGEFFGKT-----PLTSIDPDKV-------------VALGAAI 371
Cdd:cd24049 281 -----IYLTGGGSLLPGLDEYLSERLGIPveilnPFSNIESKKSddeelkedaplfaVAIGLAL 339
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
153-260 |
1.41e-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: 41.53 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 153 VITVPAYFDDAQRQSTKDAARLAGLNV------LRLLNEPTAAAL-AYGLDSGQEGIIAVYDLGGGTFDISI--LRLSKG 223
Cdd:cd11735 144 VITVPAIWKQPAKQFMRQAAYKAGLASpenpeqLIIALEPEAASIyCRKLRLHQMDRYVVVDCGGGTVDLTVhqIRLPEG 223
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1720137003 224 IFEVL--ATGGD-TALGGD-DFDHLI----ADWVIEQTKLKPQTA 260
Cdd:cd11735 224 HLKELykASGGPyGSLGVDyEFEKLLckifGEDFIDQFKIKRPAA 268
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
152-232 |
1.88e-03 |
|
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.
Pssm-ID: 466786 [Multi-domain] Cd Length: 135 Bit Score: 38.99 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720137003 152 VVITVPAYFDDAQRQST-----------KDAARLAGLNVLRLLNEPTAAALAYGLDSGQEGIIaVYDLGGGTfdisilrl 220
Cdd:cd00012 16 IVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGALLTLGPEGLL-VVDLGGGT-------- 86
|
90
....*....|..
gi 1720137003 221 sKGIFEVLATGG 232
Cdd:cd00012 87 -DISANVVLVGG 97
|
|
| |
