|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
6-575 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 821.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 6 FQGAIGIDLGTTYSCVATYES-SVEIIANEQGNRVTPSFVAFTPQERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDES 84
Cdd:PTZ00009 3 KGPAIGIDLGTTYSCVGVWKNeNVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDSV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 85 VQKDMKTWPFKVID-VDGNPVIEVQYLEETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDA 163
Cdd:PTZ00009 83 VQSDMKHWPFKVTTgGDDKPMIEVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 164 GAISGLNVLRIINEPTAAAIAYGLGAgKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEH 243
Cdd:PTZ00009 163 GTIAGLNVLRIINEPTAAAIAYGLDK-KGDGEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 244 FKAEFKKKT-GLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSLTRARFEDLNAALFKSTLEPVEQ 322
Cdd:PTZ00009 242 CVQDFKRKNrGKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPVEK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 323 VLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAILTGQsTSDETKDLLLLDVAP 402
Cdd:PTZ00009 322 VLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGE-QSSQVQDLLLLDVTP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 403 LSLGVGMQGDIFGIVVPRNTTVPTIKRRTFTTVSDNQTTVQFPVYQGERVNCKENTLLGEFDLKNIPMMPAGEPVLEAIF 482
Cdd:PTZ00009 401 LSLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 483 EVDANGILKVTAVEKSTGKSSNITISNAVGRLSSEEIEKMVNQAEEFKAADEAFAKKHEARQRLESYVASIEQTVTDPVL 562
Cdd:PTZ00009 481 DIDANGILNVSAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDEKV 560
|
570
....*....|...
gi 6324120 563 SSKLKRGSKSKIE 575
Cdd:PTZ00009 561 KGKLSDSDKATIE 573
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
9-613 |
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: 778.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 9 AIGIDLGTTYSCVATYES-SVEIIANEQGNRVTPSFVAFTPQERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 87
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGgGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 88 DMKTWPFKVI-DVDGNPVIEVQYLEETktFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 166
Cdd:pfam00012 81 DIKHLPYKVVkLPNGDAGVEVRYLGET--FTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 167 SGLNVLRIINEPTAAAIAYGLgaGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKA 246
Cdd:pfam00012 159 AGLNVLRIVNEPTAAALAYGL--DKTDKERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 247 EFKKKTGLDISDDARALRRLRTAAERAKRTLSSV-TQTTVEVDSLF-DGEDFESSLTRARFEDLNAALFKSTLEPVEQVL 324
Cdd:pfam00012 237 EFKKKYGIDLSKDKRALQRLREAAEKAKIELSSNqTNINLPFITAMaDGKDVSGTLTRAKFEELVADLFERTLEPVEKAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 325 KDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAILTGQStsdETKDLLLLDVAPLS 404
Cdd:pfam00012 317 KDAGLSKSEIDEVVLVGGSTRIPAVQELVKEFF-GKEPSKGVNPDEAVAIGAAVQAGVLSGTF---DVKDFLLLDVTPLS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 405 LGVGMQGDIFGIVVPRNTTVPTIKRRTFTTVSDNQTTVQFPVYQGERVNCKENTLLGEFDLKNIPMMPAGEPVLEAIFEV 484
Cdd:pfam00012 393 LGIETLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDI 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 485 DANGILKVTAVEKSTGKSSNITISNAvGRLSSEEIEKMVNQAEEFKAADEAFAKKHEARQRLESYVASIEQTVTDpvLSS 564
Cdd:pfam00012 473 DANGILTVSAKDKGTGKEQEITIEAS-EGLSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEE--EGD 549
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 6324120 565 KLKRGSKSKIEAALSDALAAlqIEDPSADELRKAEVGLKRVVTKAMSSR 613
Cdd:pfam00012 550 KVPEAEKSKVESAIEWLKDE--LEGDDKEEIEAKTEELAQVSQKIGERM 596
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
9-383 |
0e+00 |
|
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar proteins; Ssb is ribosome-bound, Hsp70-type chaperone that assists in the co-translational folding of newly synthesized proteins in the cytosol. It stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Saccharmoyces cerevisiae Ssb are encoded by two genes, SSB1 and SSB2. Ssb1p is also known as cold-inducible protein YG101. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466943 [Multi-domain] Cd Length: 375 Bit Score: 770.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 9 AIGIDLGTTYSCVATYESSVEIIANEQGNRVTPSFVAFTPQERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQKD 88
Cdd:cd24093 1 AIGIDLGTTYSCVATYESSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 89 MKTWPFKVIDVDGNPVIEVQYLEETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAISG 168
Cdd:cd24093 81 MKTWPFKVIDVNGNPVIEVQYLGETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 169 LNVLRIINEPTAAAIAYGLGAGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAEF 248
Cdd:cd24093 161 LNVLRIINEPTAAAIAYGLGAGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 249 KKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSLTRARFEDLNAALFKSTLEPVEQVLKDAK 328
Cdd:cd24093 241 KKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSITRARFEDLNAALFKSTLEPVEQVLKDAK 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 6324120 329 ISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 383
Cdd:cd24093 321 ISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
9-383 |
0e+00 |
|
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; This subfamily includes human HSPA1A (70-kDa heat shock protein 1A, also known as HSP72; HSPA1; HSP70I; HSPA1B; HSP70-1; HSP70-1A), HSPA1B (70-kDa heat shock protein 1B, also known as HSPA1A; HSP70-2; HSP70-1B), and HSPA1L (70-kDa heat shock protein 1-like, also known as HSP70T; hum70t; HSP70-1L; HSP70-HOM), HSPA2 (70-kDa heat shock protein 2, also known as HSP70-2; HSP70-3), HSPA6 (also known as heat shock 70kDa protein 6; HSP70B'), HSPA7 (heat shock 70kDa protein 7 , also known as HSP70B), and HSPA8 (heat shock 70kDa protein 8, also known as Lipopolysaccharide-associated protein 1/LAP1; HSC70; HSP73; HSPA10). They are molecular chaperones implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. They play pivotal roles in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The subfamily also includes Saccharomyces cerevisiae heat shock protein Ssa1-4, which may play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. This subfamily belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466831 [Multi-domain] Cd Length: 375 Bit Score: 732.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 9 AIGIDLGTTYSCVATYES-SVEIIANEQGNRVTPSFVAFTPQERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 87
Cdd:cd10233 1 AIGIDLGTTYSCVGVWQNdKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 88 DMKTWPFKVIDVDGNPVIEVQYLEETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIS 167
Cdd:cd10233 81 DMKHWPFKVVSGGDKPKIQVEYKGETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 168 GLNVLRIINEPTAAAIAYGLGAgKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAE 247
Cdd:cd10233 161 GLNVLRIINEPTAAAIAYGLDK-KGKGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 248 FKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSLTRARFEDLNAALFKSTLEPVEQVLKDA 327
Cdd:cd10233 240 FKRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELCADLFRSTLEPVEKVLRDA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 6324120 328 KISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 383
Cdd:cd10233 320 KLDKSQIHEIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
9-575 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 727.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 9 AIGIDLGTTYSCVATYE-SSVEIIANEQGNRVTPSFVAFTP-QERLIGDAAKNQAALNPRNTVFDAKRLIGRRfdDESVQ 86
Cdd:PRK00290 4 IIGIDLGTTNSCVAVMEgGEPKVIENAEGARTTPSVVAFTKdGERLVGQPAKRQAVTNPENTIFSIKRLMGRR--DEEVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 87 KDMKTWPFKVIDVD-GNPVIEVqyleETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGA 165
Cdd:PRK00290 82 KDIKLVPYKIVKADnGDAWVEI----DGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDAGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 166 ISGLNVLRIINEPTAAAIAYGLGAGKSEKerhVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFK 245
Cdd:PRK00290 158 IAGLEVLRIINEPTAAALAYGLDKKGDEK---ILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 246 AEFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVE-----VDSlfDG-EDFESSLTRARFEDLNAALFKSTLEP 319
Cdd:PRK00290 235 DEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEINlpfitADA--SGpKHLEIKLTRAKFEELTEDLVERTIEP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 320 VEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAILTGqstsdETKDLLLLD 399
Cdd:PRK00290 313 CKQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLAG-----DVKDVLLLD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 400 VAPLSLGVGMQGDIFGIVVPRNTTVPTIKRRTFTTVSDNQTTVQFPVYQGERVNCKENTLLGEFDLKNIPMMPAGEPVLE 479
Cdd:PRK00290 387 VTPLSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 480 AIFEVDANGILKVTAVEKSTGKSSNITISNAVGrLSSEEIEKMVNQAEEFKAADEAFAKKHEARQRLESYVASIEQTVTD 559
Cdd:PRK00290 467 VTFDIDANGIVHVSAKDKGTGKEQSITITASSG-LSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKE 545
|
570
....*....|....*.
gi 6324120 560 pvLSSKLKRGSKSKIE 575
Cdd:PRK00290 546 --LGDKVPADEKEKIE 559
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
9-383 |
0e+00 |
|
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The HSPA1-like family includes human HSPA1A (70-kDa heat shock protein 1A, also known as HSP72; HSPA1; HSP70I; HSPA1B; HSP70-1; HSP70-1A), HSPA1B (70-kDa heat shock protein 1B, also known as HSPA1A; HSP70-2; HSP70-1B), and HSPA1L (70-kDa heat shock protein 1-like, also known as HSP70T; hum70t; HSP70-1L; HSP70-HOM), HSPA2 (70-kDa heat shock protein 2, also known as HSP70-2; HSP70-3), BiP (also known as HSP70 family protein 5 /HSPA5; 70-kDa heat shock protein 5; glucose-regulated protein 78/GRP78; immunoglobulin heavy chain-binding protein), HSPA6 (also known as heat shock 70kDa protein 6; HSP70B'), HSPA7 (heat shock 70kDa protein 7 , also known as HSP70B), HSPA8 (heat shock 70kDa protein 8, also known as Lipopolysaccharide-associated protein 1/LAP1; HSC70; HSP73; HSPA10), HSPA13 (also known as 70-kDa heat shock protein 13; STCH; microsomal stress-70 protein ATPase core; stress-70 protein chaperone microsome-associated 60 kDa protein), as well as Saccharmoyces cerevisiae Hsp70 chaperone Ssb1-2 and heat shock protein Ssa1-4. HSPA1A/1B, HSPA1L, HSPA2 and HSPA6-8 are molecular chaperones implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. They play pivotal roles in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. BiP plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. It plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). HSPA13 has peptide-independent ATPase activity. All family members belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466878 [Multi-domain] Cd Length: 376 Bit Score: 696.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 9 AIGIDLGTTYSCVATYESS-VEIIANEQGNRVTPSFVAFTPQERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 87
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGkVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 88 DMKTWPFKVI-DVDGNPVIEVQYLEETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 166
Cdd:cd24028 81 DIKHWPFKVVeDEDGKPKIEVTYKGEEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAATI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 167 SGLNVLRIINEPTAAAIAYGLGAgKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKA 246
Cdd:cd24028 161 AGLNVLRIINEPTAAALAYGLDK-KSSGERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 247 EFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSLTRARFEDLNAALFKSTLEPVEQVLKD 326
Cdd:cd24028 240 EFKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGIDFETTITRAKFEELCEDLFKKCLEPVEKVLKD 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 6324120 327 AKISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 383
Cdd:cd24028 320 AKLSKDDIDEVVLVGGSTRIPKIQELLSEFFGGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
10-383 |
0e+00 |
|
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; This subfamily includes human BiP (also known as HSP70 family protein 5 /HSPA5; 70-kDa heat shock protein 5; glucose-regulated protein 78/GRP78; immunoglobulin heavy chain-binding protein), Sacchaormyces cerevisiae BiP (also known as Grp78p), Arabidopsis thaliana BiP1-3 (also known as luminal-binding protein 1-3) and related proteins. BiP plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. It plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). BiP may function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. It appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. BiP may also play a role in apoptosis and cell proliferation. Plant BiP may be required for pollen development and pollen tube growth. This subfamily belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466837 [Multi-domain] Cd Length: 376 Bit Score: 690.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVATYESS-VEIIANEQGNRVTPSFVAFTPQERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQKD 88
Cdd:cd10241 4 IGIDLGTTYSCVGVFKNGrVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKEVQKD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 89 MKTWPFKVIDVDGNPVIEVQYLEETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAISG 168
Cdd:cd10241 84 IKLLPFKIVNKNGKPYIQVEVKGEKKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 169 LNVLRIINEPTAAAIAYGLgaGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAEF 248
Cdd:cd10241 164 LNVLRIINEPTAAAIAYGL--DKKGGEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFIKLF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 249 KKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSLTRARFEDLNAALFKSTLEPVEQVLKDAK 328
Cdd:cd10241 242 KKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGEDFSETLTRAKFEELNMDLFRKTLKPVQKVLEDAG 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 6324120 329 ISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 383
Cdd:cd10241 322 LKKSDIDEIVLVGGSTRIPKVQQLLKDFFNGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
9-612 |
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: 686.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 9 AIGIDLGTTYSCVATYESS-VEIIANEQGNRVTPSFVAFTPQ-ERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDesVQ 86
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGePVVIPNAEGARTTPSVVAFTKNgERLVGQPAKRQAVTNPENTIYSIKRFMGRRFDE--VT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 87 KDMKTWPFKVIDVDGNPVIEVqyleETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 166
Cdd:TIGR02350 80 EEAKRVPYKVVGDGGDVRVKV----DGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 167 SGLNVLRIINEPTAAAIAYGLgaGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKA 246
Cdd:TIGR02350 156 AGLEVLRIINEPTAAALAYGL--DKSKKDEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLAD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 247 EFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGED----FESSLTRARFEDLNAALFKSTLEPVEQ 322
Cdd:TIGR02350 234 EFKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINLPFITADASgpkhLEMTLTRAKFEELTADLVERTKEPVRQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 323 VLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAILTGqstsdETKDLLLLDVAP 402
Cdd:TIGR02350 314 ALKDAGLSASDIDEVILVGGSTRIPAVQELVKDFF-GKEPNKSVNPDEVVAIGAAIQGGVLKG-----DVKDVLLLDVTP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 403 LSLGVGMQGDIFGIVVPRNTTVPTIKRRTFTTVSDNQTTVQFPVYQGERVNCKENTLLGEFDLKNIPMMPAGEPVLEAIF 482
Cdd:TIGR02350 388 LSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTF 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 483 EVDANGILKVTAVEKSTGKSSNITISNAVGrLSSEEIEKMVNQAEEFKAADEAFAKKHEARQRLESYVASIEQTVTDPvl 562
Cdd:TIGR02350 468 DIDANGILHVSAKDKGTGKEQSITITASSG-LSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEA-- 544
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 6324120 563 SSKLKRGSKSKIEAALSDALAALQIEDPsaDELRKAEVGLKRVVTKAMSS 612
Cdd:TIGR02350 545 GDKLPAEEKEKIEKAVAELKEALKGEDV--EEIKAKTEELQQALQKLAEA 592
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
9-523 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 616.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 9 AIGIDLGTTYSCVATYES-SVEIIANEQGNRVTPSFVAFTPQ-ERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVq 86
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGgEPQVIPNAEGRRTLPSVVAFPKDgEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFDEAT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 87 kdmktwpfkviDVDGnpvievqyleetKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 166
Cdd:COG0443 80 -----------EVGG------------KRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 167 SGLNVLRIINEPTAAAIAYGLgaGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKA 246
Cdd:COG0443 137 AGLEVLRLLNEPTAAALAYGL--DKGKEEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 247 EFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDsLFDGEDFESSLTRARFEDLNAALFKSTLEPVEQVLKD 326
Cdd:COG0443 215 EFGKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINLP-FSGGKHLDVELTRAEFEELIAPLVERTLDPVRQALAD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 327 AKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAILTGqstsdETKDlllLDVAPLSLG 406
Cdd:COG0443 294 AGLSPSDIDAVLLVGGSTRMPAVRERVKELF-GKEPLKGVDPDEAVALGAAIQAGVLAG-----DVKD---LDVTPLSLG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 407 VGMQGDIFGIVVPRNTTVPTIKRRTFTTVSDNQTTVQFPVYQGERVNCKENTLLGEFDLKNIPMMPAGEPVLEAIFEVDA 486
Cdd:COG0443 365 IETLGGVFTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDA 444
|
490 500 510
....*....|....*....|....*....|....*..
gi 6324120 487 NGILKVTAVEKSTGKSSNITIsnavgrlsSEEIEKMV 523
Cdd:COG0443 445 NGILSVSAKDLGTGKEQSITI--------KEEIERML 473
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
10-592 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 603.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVATYESSV-EIIANEQGNRVTPSFVAFTPQ-ERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 87
Cdd:PTZ00400 44 VGIDLGTTNSCVAIMEGSQpKVIENSEGMRTTPSVVAFTEDgQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEDATKK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 88 DMKTWPFKVI-DVDGNPVIEVQyleeTKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 166
Cdd:PTZ00400 124 EQKILPYKIVrASNGDAWIEAQ----GKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAGKI 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 167 SGLNVLRIINEPTAAAIAYGL--GAGKSekerhVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHF 244
Cdd:PTZ00400 200 AGLDVLRIINEPTAAALAFGMdkNDGKT-----IAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 245 KAEFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTtvEVDSLFDGED------FESSLTRARFEDLNAALFKSTLE 318
Cdd:PTZ00400 275 IAEFKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQT--EINLPFITADqsgpkhLQIKLSRAKLEELTHDLLKKTIE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 319 PVEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAILTGqstsdETKDLLLL 398
Cdd:PTZ00400 353 PCEKCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIF-GKEPSKGVNPDEAVAMGAAIQAGVLKG-----EIKDLLLL 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 399 DVAPLSLGVGMQGDIFGIVVPRNTTVPTIKRRTFTTVSDNQTTVQFPVYQGERVNCKENTLLGEFDLKNIPMMPAGEPVL 478
Cdd:PTZ00400 427 DVTPLSLGIETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQI 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 479 EAIFEVDANGILKVTAVEKSTGKSSNITISNAvGRLSSEEIEKMVNQAEEFKAADEAFAKKHEARQRLESYVASIEQTVT 558
Cdd:PTZ00400 507 EVTFDVDANGIMNISAVDKSTGKKQEITIQSS-GGLSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLS 585
|
570 580 590
....*....|....*....|....*....|....
gi 6324120 559 DpvLSSKLKRGSKSKIEAALSDALAALQIEDPSA 592
Cdd:PTZ00400 586 D--LKDKISDADKDELKQKITKLRSTLSSEDVDS 617
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
10-575 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 595.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVATYESSVEI-IANEQGNRVTPSFVAFTP-QERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 87
Cdd:PRK13411 5 IGIDLGTTNSCVAVLEGGKPIvIPNSEGGRTTPSIVGFGKsGDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDDTEEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 88 DMKtwPFKVIDVDGNPViEVQYleETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIS 167
Cdd:PRK13411 85 SRV--PYTCVKGRDDTV-NVQI--RGRNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAGTIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 168 GLNVLRIINEPTAAAIAYGLGagKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAE 247
Cdd:PRK13411 160 GLEVLRIINEPTAAALAYGLD--KQDQEQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWLVEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 248 FKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGED----FESSLTRARFEDLNAALFKSTLEPVEQV 323
Cdd:PRK13411 238 FQQQEGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINLPFITADETgpkhLEMELTRAKFEELTKDLVEATIEPMQQA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 324 LKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAILTGqstsdETKDLLLLDVAPL 403
Cdd:PRK13411 318 LKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFGGKQPDRSVNPDEAVALGAAIQAGVLGG-----EVKDLLLLDVTPL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 404 SLGVGMQGDIFGIVVPRNTTVPTIKRRTFTTVSDNQTTVQFPVYQGERVNCKENTLLGEFDLKNIPMMPAGEPVLEAIFE 483
Cdd:PRK13411 393 SLGIETLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSFE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 484 VDANGILKVTAVEKSTGKSSNITISNAvGRLSSEEIEKMVNQAEEFKAADEAFAKKHEARQRLESYVASIEQTVTD--PV 561
Cdd:PRK13411 473 IDVNGILKVSAQDQGTGREQSIRITNT-GGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKEngEL 551
|
570
....*....|....
gi 6324120 562 LSSKLKRGSKSKIE 575
Cdd:PRK13411 552 ISEELKQRAEQKVE 565
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
10-589 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 584.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVATYESSV-EIIANEQGNRVTPSFVAFTP-QERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDesVQK 87
Cdd:CHL00094 5 VGIDLGTTNSVVAVMEGGKpTVIPNAEGFRTTPSIVAYTKkGDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSE--ISE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 88 DMKTWPFKVI-DVDGNPVIEVQYLEetKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 166
Cdd:CHL00094 83 EAKQVSYKVKtDSNGNIKIECPALN--KDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAGKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 167 SGLNVLRIINEPTAAAIAYGLGAGKSEKerhVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKA 246
Cdd:CHL00094 161 AGLEVLRIINEPTAASLAYGLDKKNNET---ILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLIK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 247 EFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGED----FESSLTRARFEDLNAALFKSTLEPVEQ 322
Cdd:CHL00094 238 EFKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINLPFITATQTgpkhIEKTLTRAKFEELCSDLINRCRIPVEN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 323 VLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAILTGqstsdETKDLLLLDVAP 402
Cdd:CHL00094 318 ALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLL-GKKPNQSVNPDEVVAIGAAVQAGVLAG-----EVKDILLLDVTP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 403 LSLGVGMQGDIFGIVVPRNTTVPTIKRRTFTTVSDNQTTVQFPVYQGERVNCKENTLLGEFDLKNIPMMPAGEPVLEAIF 482
Cdd:CHL00094 392 LSLGVETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 483 EVDANGILKVTAVEKSTGKSSNITISNAvGRLSSEEIEKMVNQAEEFKAADEAFAKKHEARQRLESYVASIEQTVTDpvL 562
Cdd:CHL00094 472 DIDANGILSVTAKDKGTGKEQSITIQGA-STLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKE--L 548
|
570 580
....*....|....*....|....*..
gi 6324120 563 SSKLKRGSKSKIEAALSDALAALQIED 589
Cdd:CHL00094 549 KDKISEEKKEKIENLIKKLRQALQNDN 575
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
10-559 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 555.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVATYESS-VEIIANEQGNRVTPSFVAFTPQERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQKD 88
Cdd:PTZ00186 30 IGVDLGTTYSCVATMDGDkARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEHIQKD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 89 MKTWPFKVIDVdGNPVIEVQYlEETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAISG 168
Cdd:PTZ00186 110 IKNVPYKIVRA-GNGDAWVQD-GNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTIAG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 169 LNVLRIINEPTAAAIAYGLgagKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAEF 248
Cdd:PTZ00186 188 LNVIRVVNEPTAAALAYGM---DKTKDSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYILEEF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 249 KKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGED----FESSLTRARFEDLNAALFKSTLEPVEQVL 324
Cdd:PTZ00186 265 RKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADgaqhIQMHISRSKFEGITQRLIERSIAPCKQCM 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 325 KDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAILTGqstsdETKDLLLLDVAPLS 404
Cdd:PTZ00186 345 KDAGVELKEINDVVLVGGMTRMPKVVEEVKKFF-QKDPFRGVNPDEAVALGAATLGGVLRG-----DVKGLVLLDVTPLS 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 405 LGVGMQGDIFGIVVPRNTTVPTIKRRTFTTVSDNQTTVQFPVYQGERVNCKENTLLGEFDLKNIPMMPAGEPVLEAIFEV 484
Cdd:PTZ00186 419 LGIETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDI 498
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324120 485 DANGILKVTAVEKSTGKSSNITISnAVGRLSSEEIEKMVNQAEEFKAADEAFAKKHEARQRLESYVASIEQTVTD 559
Cdd:PTZ00186 499 DANGICHVTAKDKATGKTQNITIT-ANGGLSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGE 572
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
10-562 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 553.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVATYESSVEI-IANEQGNRVTPSFVAFTP-QERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDesVQK 87
Cdd:PRK13410 5 VGIDLGTTNSVVAVMEGGKPVvIANAEGMRTTPSVVGFTKdGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDE--LDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 88 DMKTWPFKV-IDVDGNPVIEVQYLEetKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 166
Cdd:PRK13410 83 ESKRVPYTIrRNEQGNVRIKCPRLE--REFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDAGRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 167 SGLNVLRIINEPTAAAIAYGLGAGKSEKerhVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKA 246
Cdd:PRK13410 161 AGLEVERILNEPTAAALAYGLDRSSSQT---VLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWLAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 247 EFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGED----FESSLTRARFEDLNAALFKSTLEPVEQ 322
Cdd:PRK13410 238 QFLEKEGIDLRRDRQALQRLTEAAEKAKIELSGVSVTDISLPFITATEDgpkhIETRLDRKQFESLCGDLLDRLLRPVKR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 323 VLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFDgKQLEKSINPDEAVAYGAAVQGAILTGqstsdETKDLLLLDVAP 402
Cdd:PRK13410 318 ALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLIP-REPNQNVNPDEVVAVGAAIQAGILAG-----ELKDLLLLDVTP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 403 LSLGVGMQGDIFGIVVPRNTTVPTIKRRTFTTVSDNQTTVQFPVYQGERVNCKENTLLGEFDLKNIPMMPAGEPVLEAIF 482
Cdd:PRK13410 392 LSLGLETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 483 EVDANGILKVTAVEKSTGKSSNITISNAvGRLSSEEIEKMVNQAEEFKAADEAFAKKHEARQRLESYVASIEQTVTDPVL 562
Cdd:PRK13410 472 DIDANGILQVSATDRTTGREQSVTIQGA-STLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERRLRDAAL 550
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
10-384 |
0e+00 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar proteins; This subfamily includes Escherichia coli chaperone protein DnaK (also known as heat shock 70 kDa protein/HSP70), human mitochondrial heat shock 70 kDa protein HSPA9 (also known as mitochondrial stress-70 protein; mortalin; 75 kDa glucose-regulated protein/GRP-75; HSPA9B; MOT; peptide-binding protein 74/PBP74), Saccharomyces cerevisiae stress-seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and Ssc3p (also called extracellular mutant protein 10/Ecm10), and Saccharomyces cerevisiae Stress-seventy subfamily Q protein 1/Ssq1p (also called Ssc2p; Ssh1p; mtHSP70 homolog). They all belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs); for Escherichia coli DnaK, these are the DnaJ and GrpE, respectively.
Pssm-ID: 466832 [Multi-domain] Cd Length: 373 Bit Score: 525.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVATYES-SVEIIANEQGNRVTPSFVAFTPQ-ERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 87
Cdd:cd10234 2 IGIDLGTTNSCVAVMEGgKPTVIPNAEGGRTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 88 DMKTWPFkVIDVDGNPVIEVQyleeTKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIS 167
Cdd:cd10234 82 KQVPYPV-VSAGNGDAWVEIG----GKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 168 GLNVLRIINEPTAAAIAYGLGAGKSEKerhVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAE 247
Cdd:cd10234 157 GLEVLRIINEPTAAALAYGLDKKKDEK---ILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 248 FKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGED----FESSLTRARFEDLNAALFKSTLEPVEQV 323
Cdd:cd10234 234 FKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLETEINLPFITADASgpkhLEMKLTRAKFEELTEDLVERTIEPVEQA 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6324120 324 LKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAILT 384
Cdd:cd10234 314 LKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
10-575 |
4.13e-178 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 520.18 E-value: 4.13e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVATYES-SVEIIANEQGNRVTPSFVAFTPQ-ERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDesVQK 87
Cdd:PLN03184 42 VGIDLGTTNSAVAAMEGgKPTIVTNAEGQRTTPSVVAYTKNgDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSE--VDE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 88 DMKTWPFKVI-DVDGNPVIEVQYLeeTKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 166
Cdd:PLN03184 120 ESKQVSYRVVrDENGNVKLDCPAI--GKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 167 SGLNVLRIINEPTAAAIAYGLGAGKSEKerhVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKA 246
Cdd:PLN03184 198 AGLEVLRIINEPTAASLAYGFEKKSNET---ILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLAS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 247 EFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVE---VDSLFDG-EDFESSLTRARFEDLNAALFKSTLEPVEQ 322
Cdd:PLN03184 275 NFKKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISlpfITATADGpKHIDTTLTRAKFEELCSDLLDRCKTPVEN 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 323 VLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFfDGKQLEKSINPDEAVAYGAAVQGAILTGqstsdETKDLLLLDVAP 402
Cdd:PLN03184 355 ALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKL-TGKDPNVTVNPDEVVALGAAVQAGVLAG-----EVSDIVLLDVTP 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 403 LSLGVGMQGDIFGIVVPRNTTVPTIKRRTFTTVSDNQTTVQFPVYQGERVNCKENTLLGEFDLKNIPMMPAGEPVLEAIF 482
Cdd:PLN03184 429 LSLGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKF 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 483 EVDANGILKVTAVEKSTGKSSNITISNAvGRLSSEEIEKMVNQAEEFKAADEAFAKKHEARQRLESYVASIEQTVTDpvL 562
Cdd:PLN03184 509 DIDANGILSVSATDKGTGKKQDITITGA-STLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKE--L 585
|
570
....*....|...
gi 6324120 563 SSKLKRGSKSKIE 575
Cdd:PLN03184 586 GDKVPADVKEKVE 598
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
9-548 |
5.74e-173 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 505.10 E-value: 5.74e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 9 AIGIDLGTTYSCVATYESSV-EIIANEQGNRVTPSFVAFTPQERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDesVQK 87
Cdd:PRK05183 21 AVGIDLGTTNSLVATVRSGQaEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKNTISSVKRFMGRSLAD--IQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 88 DMKTWPFKVID-VDGNPVIEVqyleETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 166
Cdd:PRK05183 99 RYPHLPYQFVAsENGMPLIRT----AQGLKSPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 167 SGLNVLRIINEPTAAAIAYGLgagKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHfka 246
Cdd:PRK05183 175 AGLNVLRLLNEPTAAAIAYGL---DSGQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADW--- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 247 eFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVdSLFDGEdfessLTRARFEDLNAALFKSTLEPVEQVLKD 326
Cdd:PRK05183 249 -ILEQAGLSPRLDPEDQRLLLDAARAAKEALSDADSVEVSV-ALWQGE-----ITREQFNALIAPLVKRTLLACRRALRD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 327 AKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAILTGQSTSDetkDLLLLDVAPLSLG 406
Cdd:PRK05183 322 AGVEADEVKEVVMVGGSTRVPLVREAVGEFF-GRTPLTSIDPDKVVAIGAAIQADILAGNKPDS---DMLLLDVIPLSLG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 407 VGMQGDIFGIVVPRNTTVPTIKRRTFTTVSDNQTTVQFPVYQGERVNCKENTLLGEFDLKNIPMMPAGEPVLEAIFEVDA 486
Cdd:PRK05183 398 LETMGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDA 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6324120 487 NGILKVTAVEKSTGKSSNITISNAVGrLSSEEIEKMVnqAEEFKAADEAFAKKHEARQRLES 548
Cdd:PRK05183 478 DGLLSVTAMEKSTGVEASIQVKPSYG-LTDDEIARML--KDSMSHAEEDMQARALAEQKVEA 536
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
10-383 |
8.05e-171 |
|
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: 490.62 E-value: 8.05e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVATYE-SSVEIIANEQGNRVTPSFVAFTPQ-ERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 87
Cdd:cd11733 4 IGIDLGTTNSCVAVMEgKTPKVIENAEGARTTPSVVAFTADgERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDPEVQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 88 DMKTWPFKVIDVD-GNPVIEVQyleeTKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 166
Cdd:cd11733 84 DIKMVPYKIVKASnGDAWVEAH----GKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDAGQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 167 SGLNVLRIINEPTAAAIAYGLgaGKSEkERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKA 246
Cdd:cd11733 160 AGLNVLRIINEPTAAALAYGL--DKKD-DKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNYLVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 247 EFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTtvEVDSLFDGED------FESSLTRARFEDLNAALFKSTLEPV 320
Cdd:cd11733 237 EFKKEQGIDLSKDNLALQRLREAAEKAKIELSSSLQT--DINLPFITADasgpkhLNMKLTRAKFESLVGDLIKRTVEPC 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324120 321 EQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAIL 383
Cdd:cd11733 315 KKCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIF-GKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
9-548 |
4.36e-166 |
|
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: 486.78 E-value: 4.36e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 9 AIGIDLGTTYSCVATY-ESSVEIIANEQGNRVTPSFVAFTPQ-ERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDesvQ 86
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVrSGVPEVLPDAEGRVLLPSVVRYLKDgGVEVGKEALAAAAEDPKNTISSVKRLMGRSIED---I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 87 KDMKTWPFKVIDVDG-NPVIEVQyleeTKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGA 165
Cdd:TIGR01991 78 KTFSILPYRFVDGPGeMVRLRTV----QGTVTPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 166 ISGLNVLRIINEPTAAAIAYGLGAGKsekERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFK 245
Cdd:TIGR01991 154 LAGLNVLRLLNEPTAAAVAYGLDKAS---EGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWIL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 246 aefkKKTGLDISDDARALRRLRTAAERAKRTLSSVTQttVEVDSLFDGEDFESSLTRARFEDLNAALFKSTLEPVEQVLK 325
Cdd:TIGR01991 231 ----KQLGISADLNPEDQRLLLQAARAAKEALTDAES--VEVDFTLDGKDFKGKLTRDEFEALIQPLVQKTLSICRRALR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 326 DAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAILTGQSTSDetkDLLLLDVAPLSL 405
Cdd:TIGR01991 305 DAGLSVEEIKGVVLVGGSTRMPLVRRAVAELF-GQEPLTDIDPDQVVALGAAIQADLLAGNRIGN---DLLLLDVTPLSL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 406 GVGMQGDIFGIVVPRNTTVPTIKRRTFTTVSDNQTTVQFPVYQGERVNCKENTLLGEFDLKNIPMMPAGEPVLEAIFEVD 485
Cdd:TIGR01991 381 GIETMGGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVD 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324120 486 ANGILKVTAVEKSTGKSSNITISNAVGrLSSEEIEKMVnqAEEFKAADEAFAKKHEARQRLES 548
Cdd:TIGR01991 461 ADGLLTVSAQEQSTGVEQSIQVKPSYG-LSDEEIERML--KDSFKHAEEDMYARALAEQKVEA 520
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
9-385 |
1.80e-152 |
|
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: 443.81 E-value: 1.80e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 9 AIGIDLGTTYSCVATYESSV-EIIANEQGNRVTPSFVAFTPQ-ERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQ 86
Cdd:cd11734 3 VIGIDLGTTNSCVAVMEGKTpRVIENAEGARTTPSVVAFTKDgERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAEVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 87 KDMKTWPFKVID-VDGNPVIEVQyleeTKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGA 165
Cdd:cd11734 83 RDIKEVPYKIVKhSNGDAWVEAR----GQKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 166 ISGLNVLRIINEPTAAAIAYGLGagkSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFK 245
Cdd:cd11734 159 IAGLNVLRVINEPTAAALAYGLD---KSGDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 246 AEFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTtvEVDSLFDGED------FESSLTRARFEDLNAALFKSTLEP 319
Cdd:cd11734 236 SEFKKESGIDLSKDRMAIQRIREAAEKAKIELSSTLQT--DINLPFITADasgpkhINMKLTRAQFESLVKPLVDRTVEP 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324120 320 VEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAILTG 385
Cdd:cd11734 314 CKKALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIF-GREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
10-385 |
8.03e-146 |
|
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: 427.91 E-value: 8.03e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVATYES---SVEIIANEQGNRVTPSFVAFTPQER-LIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESV 85
Cdd:cd10237 25 VGIDLGTTYSCVGVYHAvtgEVEVIPDDDGHKSIPSVVAFTPDGGvLVGYDALAQAEHNPSNTIYDAKRFIGKTFTKEEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 86 QKDMKTWPFKVI-DVDGNPVIEVQYLEETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAG 164
Cdd:cd10237 105 EEEAKRYPFKVVnDNIGSAFFEVPLNGSTLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRKAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 165 AISGLNVLRIINEPTAAAIAYGLgaGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHF 244
Cdd:cd10237 185 NLAGLEVLRVINEPTAAAMAYGL--HKKSDVNNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQYL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 245 KAEFKKKTGLDISdDARALRRLRTAAERAKRTLSSVTQTTVEVD-----SLFDGEDFESSLTRARFEDLNAALFKSTLEP 319
Cdd:cd10237 263 IDRIAKKFGKTLT-DKEDIQRLRQAVEEVKLNLTNHNSASLSLPlqislPSAFKVKFKEEITRDLFETLNEDLFQRVLEP 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324120 320 VEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAILTG 385
Cdd:cd10237 342 IRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFF-GKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
9-385 |
1.02e-143 |
|
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: 421.24 E-value: 1.02e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 9 AIGIDLGTTYSCVATYES-SVEIIANEQGNRVTPSFVAFTPQERLI-GDAAKNQAALNPRNTVFDAKRLIGRRFDDesVQ 86
Cdd:cd10236 4 AVGIDLGTTNSLVATVRSgQPEVLPDEKGEALLPSVVHYGEDGKITvGEKAKENAITDPENTISSVKRLMGRSLAD--VK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 87 KDMKTWPFKVIDVDGN-PVIEVqyleETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGA 165
Cdd:cd10236 82 EELPLLPYRLVGDENElPRFRT----GAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 166 ISGLNVLRIINEPTAAAIAYGLGagkSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHfk 245
Cdd:cd10236 158 LAGLNVLRLLNEPTAAALAYGLD---QKKEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADW-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 246 aeFKKKTGLDISDDARALRRLRTAAERAKRTLSsvTQTTVEVDSLFDGEDFESSLTRARFEDLNAALFKSTLEPVEQVLK 325
Cdd:cd10236 233 --ILKQIGIDARLDPAVQQALLQAARRAKEALS--DADSASIEVEVEGKDWEREITREEFEELIQPLVKRTLEPCRRALK 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 326 DAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAILTG 385
Cdd:cd10236 309 DAGLEPADIDEVVLVGGSTRIPLVRQRVAEFF-GREPLTSINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
9-383 |
3.08e-141 |
|
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: 415.10 E-value: 3.08e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 9 AIGIDLGTTYSCVATY-ESSVEIIANEQGNRVTPSFVAFTPQERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 87
Cdd:cd10238 2 AFGVHFGNTNACVAVYkDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAVQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 88 DMKTWPFKVIDVDGNPVIEVQYLEETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIS 167
Cdd:cd10238 82 LKKESKCKIIEKDGKPGYEIELEEKKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 168 GLNVLRIINEPTAAAIAYGLGAGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAE 247
Cdd:cd10238 162 GFNVLRVISEPSAAALAYGIGQDDPTENSNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHLASE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 248 FKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSLTRARFEDLNAALFKSTLEPVEQVLKDA 327
Cdd:cd10238 242 FKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATCSVESLYDGMDFQCNVSRARFESLCSSLFQQCLEPIQEVLNSA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 6324120 328 KISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 383
Cdd:cd10238 322 GLTKEDIDKVILCGGSSRIPKLQQLIKDLFPSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
10-383 |
9.72e-139 |
|
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: 407.73 E-value: 9.72e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVATYES--SVEIIANEQGNRVTPSFVAFTP-QERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDesvq 86
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGngAEVIIENSEGKRTTPSVVYFDKdGEVLVGEEAKNQALLDPENTIYSVKRLMGRDTKD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 87 kdmktwpfkVIDVDGnpvievqyleetKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 166
Cdd:cd24029 77 ---------KEEIGG------------KEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 167 SGLNVLRIINEPTAAAIAYGLgaGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKA 246
Cdd:cd24029 136 AGLNVLRLINEPTAAALAYGL--DKEGKDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 247 EFKKKTG-LDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSLTRARFEDLNAALFKSTLEPVEQVLK 325
Cdd:cd24029 214 KIGIETGiLDDKEDERARARLREAAEEAKIELSSSDSTDILILDDGKGGELEIEITREEFEELIAPLIERTIDLLEKALK 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 6324120 326 DAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQlEKSINPDEAVAYGAAVQGAIL 383
Cdd:cd24029 294 DAKLSPEDIDRVLLVGGSSRIPLVREMLEEYFGREP-ISSVDPDEAVAKGAAIYAASL 350
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
10-381 |
9.21e-132 |
|
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: 390.77 E-value: 9.21e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVATYES-SVEIIANEQGNRVTPSFVAFTPQERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQKD 88
Cdd:cd11732 1 VGIDFGNQNSVVAAARRgGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 89 MKTWPFKVIDVDGNPV-IEVQYLEETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIS 167
Cdd:cd11732 81 IKLLPFKLVELEDGKVgIEVSYNGEEVVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 168 GLNVLRIINEPTAAAIAYGL----GAGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEH 243
Cdd:cd11732 161 GLNCLRLINETTAAALDYGIyksdLLESEEKPRIVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 244 FKAEFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSLTRARFEDLNAALFKSTLEPVEQV 323
Cdd:cd11732 241 FAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEDIDFSGQIKREEFEELIQPLLARLEAPIKKA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 6324120 324 LKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGA 381
Cdd:cd11732 321 LAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVF-GKDLSTTLNADEAVARGCALQAA 377
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
9-383 |
2.35e-126 |
|
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: 377.42 E-value: 2.35e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 9 AIGIDLGTTYSCVA-TYESSVEIIANEQGNRVTPSFVAFTPQERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 87
Cdd:cd24095 3 VVGIDFGNENCVVAvARKGGIDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEVQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 88 DMKTWPFKVIDV-DGNPVIEVQYLEETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 166
Cdd:cd24095 83 DLKLFPFKVTEGpDGEIGINVNYLGEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAAQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 167 SGLNVLRIINEPTAAAIAYGL--GAGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHF 244
Cdd:cd24095 163 AGLNCLRLMNETTATALAYGIykTDLPETDPTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFDHF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 245 KAEFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSLTRARFEDLNAALFKSTLEPVEQVL 324
Cdd:cd24095 243 AAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMEDKDVKGMITREEFEELAAPLLERLLEPLEKAL 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 6324120 325 KDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAIL 383
Cdd:cd24095 323 ADSGLTVDQIHSVEVVGSGSRIPAILKILTKFF-GKEPSRTMNASECVARGCALQCAML 380
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
10-381 |
9.08e-123 |
|
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: 367.76 E-value: 9.08e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVATYESS-VEIIANEQGNRVTPSFVAFTPQERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQKD 88
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGgIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 89 MKTWPFKVID-VDGNPVIEVQYLEETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIS 167
Cdd:cd10228 81 LKHLPYKVVKlPNGSVGIKVQYLGEEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 168 GLNVLRIINEPTAAAIAYGLGA----GKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEH 243
Cdd:cd10228 161 GLNCLRLLNDTTAVALAYGIYKqdlpAEEEKPRNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 244 FKAEFKKKTGLDISDDARALRRLRTAAERAKRTLSS-VTQTTVEVDSLFDGEDFESSLTRARFEDLNAALFKSTLEPVEQ 322
Cdd:cd10228 241 FAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSAnATELPLNIECFMDDKDVSGKMKRAEFEELCAPLFARVEVPLRS 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 6324120 323 VLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGA 381
Cdd:cd10228 321 ALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVF-GKEPSTTLNQDEAVARGCALQCA 378
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
10-384 |
8.18e-119 |
|
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: 357.84 E-value: 8.18e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVATYES-SVEIIANEQGNRVTPSFVAFTPQERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQKD 88
Cdd:cd24094 1 VGLDLGNLNSVIAVARNrGIDIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 89 MKTWPFKVIDVDGNPVIEVQYLEETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAISG 168
Cdd:cd24094 81 EKYFTAKLVDANGEVGAEVNYLGEKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 169 LNVLRIINEPTAAAIAYGLGA----GKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHF 244
Cdd:cd24094 161 LNPLRLMNDTTAAALGYGITKtdlpEPEEKPRIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDHF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 245 KAEFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSLTRARFEDLNAALFKSTLEPVEQVL 324
Cdd:cd24094 241 ADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVSSMLKREEFEELIAPLLERVTAPLEKAL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 325 KDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAILT 384
Cdd:cd24094 321 AQAGLTKDEIDFVELVGGTTRVPALKESISAFF-GKPLSTTLNQDEAVARGAAFACAILS 379
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
10-385 |
5.93e-118 |
|
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: 354.24 E-value: 5.93e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVATY-ESSVEIIANEQGNRVTPSFVAFTPQ-ERLIGDAAKNQAALNPRNTVFDAKRligrrfddesvqk 87
Cdd:cd10235 1 IGIDLGTTNSLVAVWrDGGAELIPNALGEYLTPSVVSVDEDgSILVGRAAKERLVTHPDRTAASFKR------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 88 DMKTwpfkvidvdgnpviEVQYLEETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIS 167
Cdd:cd10235 68 FMGT--------------DKQYRLGNHTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 168 GLNVLRIINEPTAAAIAYGLgaGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHfkae 247
Cdd:cd10235 134 GLKVERLINEPTAAALAYGL--HKREDETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADY---- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 248 FKKKTGLDI-SDDARALRRLRTAAERAKRTLSSvtQTTVEVDSLFDGEDFESSLTRARFEDLNAALFKSTLEPVEQVLKD 326
Cdd:cd10235 208 FLKKHRLDFtSLSPSELAALRKRAEQAKRQLSS--QDSAEIRLTYRGEELEIELTREEFEELCAPLLERLRQPIERALRD 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 6324120 327 AKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAILTG 385
Cdd:cd10235 286 AGLKPSDIDAVILVGGATRMPLVRQLIARLF-GRLPLSSLDPDEAVALGAAIQAALKAR 343
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
10-381 |
3.13e-106 |
|
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: 324.45 E-value: 3.13e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVATYESSV--EIIANEQGNRVTPSFVAFTPQERLIGDAAKNQAALNPRNTVFDAKRLIGrrfddesvqk 87
Cdd:cd10230 3 LGIDLGSEFIKVALVKPGVpfEIVLNEESKRKTPSAVAFRNGERLFGDDALALATRFPENTFSYLKDLLG---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 88 dmktwpfkvidvdgnpvievqyleetktFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIS 167
Cdd:cd10230 73 ----------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 168 GLNVLRIINEPTAAAIAYGLG-AGKSEKERHVLIFDLGGGTFDVSLLHIAggVYTVKSTSGNT--------------HLG 232
Cdd:cd10230 125 GLNVLSLINDNTAAALNYGIDrRFENNEPQNVLFYDMGASSTSATVVEFS--SVKEKDKGKNKtvpqvevlgvgwdrTLG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 233 GQDFDTNLLEHFKAEF--KKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSLTRARFEDLNA 310
Cdd:cd10230 203 GLEFDLRLADHLADEFneKHKKDKDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDDIDFRTKITREEFEELCA 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6324120 311 ALFKSTLEPVEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGA 381
Cdd:cd10230 283 DLFERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELGKHLNADEAAALGAAFYAA 353
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
7-557 |
3.09e-101 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 319.88 E-value: 3.09e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 7 QGAIGIDLGTTYSCVA-TYESSVEIIANEQGNRVTPSFVAFTPQERLIGdaakNQAALNprntvfDAKRLIGRRFDDESV 85
Cdd:PRK01433 19 QIAVGIDFGTTNSLIAiATNRKVKVIKSIDDKELIPTTIDFTSNNFTIG----NNKGLR------SIKRLFGKTLKEILN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 86 QKDMKTWPFKVIDVDGNpviEVQYLEETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGA 165
Cdd:PRK01433 89 TPALFSLVKDYLDVNSS---ELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLAAK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 166 ISGLNVLRIINEPTAAAIAYGLgaGKSEKERHvLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFK 245
Cdd:PRK01433 166 IAGFEVLRLIAEPTAAAYAYGL--NKNQKGCY-LVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQYLC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 246 AEFkkktglDISDDARALRrlrtAAERAKRTLSSvtQTTVEVDSLfdgedfesSLTRARFEDLNAALFKSTLEPVEQVLK 325
Cdd:PRK01433 243 NKF------DLPNSIDTLQ----LAKKAKETLTY--KDSFNNDNI--------SINKQTLEQLILPLVERTINIAQECLE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 326 DAKisKSQIDEVVLVGGSTRIPKVQKLLSDFFDgKQLEKSINPDEAVAYGAAVQGAILTGQSTsdetkDLLLLDVAPLSL 405
Cdd:PRK01433 303 QAG--NPNIDGVILVGGATRIPLIKDELYKAFK-VDILSDIDPDKAVVWGAALQAENLIAPHT-----NSLLIDVVPLSL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 406 GVGMQGDIFGIVVPRNTTVPTIKRRTFTTVSDNQTTVQFPVYQGER---VNCKEntlLGEFDLKNIPMMPAGEPVLEAIF 482
Cdd:PRK01433 375 GMELYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGERemaADCRS---LARFELKGLPPMKAGSIRAEVTF 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324120 483 EVDANGILKVTAVEKSTGKSSNITISNAVGrLSSEEIEKMVNQAEEFKAADEAFAKKHEARQRLESYVASIEQTV 557
Cdd:PRK01433 452 AIDADGILSVSAYEKISNTSHAIEVKPNHG-IDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAI 525
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
9-383 |
2.02e-95 |
|
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: 296.58 E-value: 2.02e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 9 AIGIDLGTTYSCVA--TYESSVEIIANEQGNRVTPSFVAFTPQERLIGDAAKNQAALNPRNTVFDAKRLIGrrfddesvq 86
Cdd:cd10232 2 VIGISFGNSNSSIAiiNKDGRAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPKNTVANFRDLLG--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 87 kdmktwpfkvidvdgnpvievqyleeTKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 166
Cdd:cd10232 73 --------------------------TTTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAAA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 167 SGLNVLRIINEPTAAAIAYGLGAGKS---EKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEH 243
Cdd:cd10232 127 AGLEVLQLIPEPAAAALAYDLRAETSgdtIKDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVGH 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 244 FKAEFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSLTRARFEDLNAALFKSTLEPVEQV 323
Cdd:cd10232 207 FAKEFKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTSAPCSVESLADGIDFHSSINRTRYELLASKVFQQFADLVTDA 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324120 324 LKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEK----SINPDEAVAYGAAVQGAIL 383
Cdd:cd10232 287 IEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLF-PESTIIraptQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
10-382 |
8.64e-90 |
|
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: 282.98 E-value: 8.64e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVATYESS-VEIIANEQGNRVTPSFVAFTPQERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQKD 88
Cdd:cd11737 3 VGFDLGFQSCYVAVARAGgIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 89 MKTWPFKVIDV-DGNPVIEVQYLEETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIS 167
Cdd:cd11737 83 KPSLAYELVQLpTGTTGIKVMYMEEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 168 GLNVLRIINEPTAAAIAYGLGA----GKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEH 243
Cdd:cd11737 163 GLNCLRLMNETTAVALAYGIYKqdlpAPEEKPRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVLVNH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 244 FKAEFKKKTGLDISDDARALRRLRTAAERAKRTLSS-VTQTTVEVDSLFDGEDFESSLTRARFEDLNAALFKSTLEPVEQ 322
Cdd:cd11737 243 FCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSAnASDLPLNIECFMNDIDVSGTMNRGQFEEMCADLLARVEPPLRS 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 323 VLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAI 382
Cdd:cd11737 323 VLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFF-GKEVSTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
10-381 |
8.15e-87 |
|
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: 275.20 E-value: 8.15e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVATYESS-VEIIANEQGNRVTPSFVAFTPQERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQKD 88
Cdd:cd11739 3 VGFDVGFQNCYIAVARAGgIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFVQKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 89 MKTWPFKVIDVDGNPV-IEVQYLEETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIS 167
Cdd:cd11739 83 KENLSYDLVPLKNGGVgVKVMYLDEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 168 GLNVLRIINEPTAAAIAYGLGA----GKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEH 243
Cdd:cd11739 163 GLNCLRLMNDMTAVALNYGIYKqdlpAPDEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKLVEH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 244 FKAEFKKKTGLDISDDARALRRLRTAAERAKRTLSS-VTQTTVEVDSLFDGEDFESSLTRARFEDLNAALFKSTLEPVEQ 322
Cdd:cd11739 243 FCAEFKTKYKLDVKSKIRALLRLYQECEKLKKLMSSnSTDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEVPLYS 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 6324120 323 VLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGA 381
Cdd:cd11739 323 LMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFF-GKDVSTTLNADEAVARGCALQCA 380
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
10-384 |
1.55e-85 |
|
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: 272.18 E-value: 1.55e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVATYESS-VEIIANEQGNRVTPSFVAFTPQERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQKD 88
Cdd:cd11738 3 VGIDVGFQNCYIAVARSGgIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFVQAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 89 MKTWPFKVIDV-DGNPVIEVQYLEETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIS 167
Cdd:cd11738 83 KIKLPYELQKMpNGSTGVKVRYLDEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 168 GLNVLRIINEPTAAAIAYGLGA----GKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEH 243
Cdd:cd11738 163 GLNCLRLMNETTAVALAYGIYKqdlpALEEKPRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVLVDY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 244 FKAEFKKKTGLDISDDARALRRLRTAAERAKRTLSS-VTQTTVEVDSLFDGEDFESSLTRARFEDLNAALFKSTLEPVEQ 322
Cdd:cd11738 243 FCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSAnASDLPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEPPLKA 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6324120 323 VLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAILT 384
Cdd:cd11738 323 VMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCAILS 383
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
120-378 |
1.44e-56 |
|
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: 193.86 E-value: 1.44e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 120 EISAMVLTKMKEIAEAKIGKKVE-------KAVITVPAYFNDAQRQATKDAGAISGL----NVLRIINEPTAAAIAYGLG 188
Cdd:cd10170 46 EVVADFLRALLEHAKAELGDRIWelekapiEVVITVPAGWSDAAREALREAARAAGFgsdsDNVRLVSEPEAAALYALED 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 189 AGKS---EKERHVLIFDLGGGTFDVSLLHIAGGVYTVK---STSGNTHLGGQDFDTNLLEHFKAEFKKKTGLDISDDARA 262
Cdd:cd10170 126 KGDLlplKPGDVVLVCDAGGGTVDLSLYEVTSGSPLLLeevAPGGGALLGGTDIDEAFEKLLREKLGDKGKDLGRSDADA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 263 LRRLRTAAERAKRTLSSVTQTTVEVDSLFDG---EDFESSLTRARFEDLNAALFKSTLEPVEQVLKDAKISKS--QIDEV 337
Cdd:cd10170 206 LAKLLREFEEAKKRFSGGEEDERLVPSLLGGglpELGLEKGTLLLTEEEIRDLFDPVIDKILELIEEQLEAKSgtPPDAV 285
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 6324120 338 VLVGGSTRIPKVQKLLSDFFDGKQLE---KSINPDEAVAYGAAV 378
Cdd:cd10170 286 VLVGGFSRSPYLRERLRERFGSAGIIivlRSDDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
10-378 |
3.80e-27 |
|
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: 113.91 E-value: 3.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVATY-ESSVEIIANEQGNRVTPSfVAFTPQER-------LIGDAAKNQAALNPRNTVF--DAKRLIGRR 79
Cdd:cd10231 1 IGLDFGTSNSSLAVAdDGKTDLVPFEGDSPTLPS-LLYFPRREeegaesiYFGNDAIDAYLNDPEEGRLikSVKSFLGSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 80 FDDEsvqkdmkTWPFkvidvdgnpvievqyleeTKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQA 159
Cdd:cd10231 80 LFDE-------TTIF------------------GRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAED 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 160 T-------KDAGAISGLNVLRIINEPTAAAIAYglgAGKSEKERHVLIFDLGGGTFDVSLLHIAGGVY----TVKSTSGn 228
Cdd:cd10231 135 DaqaesrlRDAARRAGFRNVEFQYEPIAAALDY---EQRLDREELVLVVDFGGGTSDFSVLRLGPNRTdrraDILATSG- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 229 THLGGQDFD-----TNLLEHF------------------------------------KAEFKKKTGLDISDDARALR--- 264
Cdd:cd10231 211 VGIGGDDFDrelalKKVMPHLgrgstyvsgdkglpvpawlyadlsnwhaisllytkkTLRLLLDLRRDAADPEKIERlls 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 265 --------RLRTAAERAKRTLSSVTQTTVEVDslFDGEDFESSLTRARFEDLNAALFKSTLEPVEQVLKDAKISKSQIDE 336
Cdd:cd10231 291 lvedqlghRLFRAVEQAKIALSSADEATLSFD--FIEISIKVTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDR 368
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 6324120 337 VVLVGGSTRIPKVQKLLSDFFDGKQLEKSiNPDEAVAYGAAV 378
Cdd:cd10231 369 VFLTGGSSQSPAVRQALASLFGQARLVEG-DEFGSVAAGLAL 409
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
10-385 |
7.73e-20 |
|
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: 91.57 E-value: 7.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVA----TYESSVEIIANEQG------NRVTPSFVAFTPQERLIG---DAAKNQAALNPRNtvfDAKRLI 76
Cdd:cd10229 3 VAIDFGTTYSGYAysfiTDPGDIHTMYNWWGaptgvsSPKTPTCLLLNPDGEFHSfgyEAREKYSDLAEDE---EHQWLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 77 GRRFDDESVQKDMKTWPFKVIDVDGN--PVIEV--QYLEETKTFSPQEISAMVLTKMKEIaEAKIgkkvekaVITVPAYF 152
Cdd:cd10229 80 FFKFKMMLLSEKELTRDTKVKAVNGKsmPALEVfaEALRYLKDHALKELRDRSGSSLDED-DIRW-------VLTVPAIW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 153 NDAQ----RQATKDAGAISGLN--VLRIINEPTAAAIAYGLGAGKSEKER-----HVLIFDLGGGTFDVSL--LHIAGGV 219
Cdd:cd10229 152 SDAAkqfmREAAVKAGLISEENseQLIIALEPEAAALYCQKLLAEGEEKElkpgdKYLVVDCGGGTVDITVheVLEDGKL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 220 YTVKSTSGNtHLGGQDFDTNLLE--------HFKAEFKKKTGLDISDdaralrrLRTAAERAKRTLSSVtqttvevdslf 291
Cdd:cd10229 232 EELLKASGG-PWGSTSVDEEFEElleeifgdDFMEAFKQKYPSDYLD-------LLQAFERKKRSFKLR----------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 292 dgedfessLTRARFEDLNAALFKSTLEPVEQVLKDAKISKsqIDEVVLVGGSTRIPKVQKLLSDFFDGKQleKSINPDEA 371
Cdd:cd10229 293 --------LSPELMKSLFDPVVKKIIEHIKELLEKPELKG--VDYIFLVGGFAESPYLQKAVKEAFSTKV--KIIIPPEP 360
|
410
....*....|....
gi 6324120 372 VAygAAVQGAILTG 385
Cdd:cd10229 361 GL--AVVKGAVLFG 372
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
10-378 |
9.30e-14 |
|
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins; MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466824 [Multi-domain] Cd Length: 317 Bit Score: 72.51 E-value: 9.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVatYESSVEIIANEqgnrvtPSFVAF---TPQERLIGDaaknqaalnprntvfDAKRLIGRrfddesVQ 86
Cdd:cd10225 2 IGIDLGTANTLV--YVKGKGIVLNE------PSVVAVdknTGKVLAVGE---------------EAKKMLGR------TP 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 87 KDMKT-WPFKvidvDGnpVIevqyleetktfSPQEISAMVLTKMkeIAEAKIGKKVEK--AVITVPAYFNDAQRQATKDA 163
Cdd:cd10225 53 GNIVAiRPLR----DG--VI-----------ADFEATEAMLRYF--IRKAHRRRGFLRprVVIGVPSGITEVERRAVKEA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 164 GAISGLNVLRIINEPTAAAIayglGAGKS-EKERHVLIFDLGGGTFDVSLLHiAGGVYTVKStsgnTHLGGQDFDTNLLE 242
Cdd:cd10225 114 AEHAGAREVYLIEEPMAAAI----GAGLPiEEPRGSMVVDIGGGTTEIAVIS-LGGIVTSRS----VRVAGDEMDEAIIN 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 243 HFKAEFkkktGLDISDdaralrrlRTaAERAKRTLSSVTQT----TVEVdslfDGEDFESSLTRAR---FEDLNAALfKS 315
Cdd:cd10225 185 YVRRKY----NLLIGE--------RT-AERIKIEIGSAYPLdeelSMEV----RGRDLVTGLPRTIeitSEEVREAL-EE 246
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324120 316 TLEPVEQVLKDA------KISKSQIDE-VVLVGGSTRIPKVQKLLSdffdgKQLEKSI----NPDEAVAYGAAV 378
Cdd:cd10225 247 PVNAIVEAVRSTlertppELAADIVDRgIVLTGGGALLRGLDELLR-----EETGLPVhvadDPLTCVAKGAGK 315
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
1-377 |
5.49e-12 |
|
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: 67.41 E-value: 5.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 1 MAEGVFQGAIGIDLGTTYSCVatYESSVEIIANEqgnrvtPSFVAF---TPQERLIGDaaknqaalnprntvfDAKRLIG 77
Cdd:COG1077 1 MLFGLFSKDIGIDLGTANTLV--YVKGKGIVLNE------PSVVAIdkkTGKVLAVGE---------------EAKEMLG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 78 RRFDDESVqkdmkTWPFKvidvDGnpVIevqyleetktfSPQEISAMVLTKMkeIAEAKIGKKVEKA--VITVPAYFNDA 155
Cdd:COG1077 58 RTPGNIVA-----IRPLK----DG--VI-----------ADFEVTEAMLKYF--IKKVHGRRSFFRPrvVICVPSGITEV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 156 QRQATKDAGAISGLNVLRIINEPTAAAIayglGAG-KSEKERHVLIFDLGGGTFDVSLlhIA-GGVytVKSTSgnTHLGG 233
Cdd:COG1077 114 ERRAVRDAAEQAGAREVYLIEEPMAAAI----GAGlPIEEPTGNMVVDIGGGTTEVAV--ISlGGI--VVSRS--IRVAG 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 234 QDFDTNLLEHfkaeFKKKTGLDISDdaralrrlRTaAERAKRTLSSVTQTTVEVDSLFDGEDFESSLTRARF---EDLNA 310
Cdd:COG1077 184 DELDEAIIQY----VRKKYNLLIGE--------RT-AEEIKIEIGSAYPLEEELTMEVRGRDLVTGLPKTITitsEEIRE 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 311 ALfkstLEPVEQVLKDAK-------------ISKSQIdevVLVGGSTRIPKVQKLLSDFFdgkQLEKSI--NPDEAVAYG 375
Cdd:COG1077 251 AL----EEPLNAIVEAIKsvlektppelaadIVDRGI---VLTGGGALLRGLDKLLSEET---GLPVHVaeDPLTCVARG 320
|
..
gi 6324120 376 AA 377
Cdd:COG1077 321 TG 322
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
4-383 |
1.85e-09 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 59.38 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 4 GVFQGAIGIDLGTTYSCVatYESSVEIIANEqgnrvtPSFVAF---TPQERLIGDaaknqaalnprntvfDAKRLIGRRF 80
Cdd:PRK13930 5 GFFSKDIGIDLGTANTLV--YVKGKGIVLNE------PSVVAIdtkTGKVLAVGE---------------EAKEMLGRTP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 81 DDESVQKDMKtwpfkvidvDGnpVIeVQYleetktfspqEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQAT 160
Cdd:PRK13930 62 GNIEAIRPLK---------DG--VI-ADF----------EATEAMLRYFIKKARGRRFFRKPRIVICVPSGITEVERRAV 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 161 KDAGAISGLNVLRIINEPTAAAIayglGAG--KSEKERHvLIFDLGGGTFDVSLLHIAGGVYTvKSTSgnthLGGQDFDT 238
Cdd:PRK13930 120 REAAEHAGAREVYLIEEPMAAAI----GAGlpVTEPVGN-MVVDIGGGTTEVAVISLGGIVYS-ESIR----VAGDEMDE 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 239 NLLEHFKAEFkkktGLDISDdaralrrlRTaAERAKRTLSSVTQ----TTVEVdslfDGEDFESSLTRARF---EDLNAA 311
Cdd:PRK13930 190 AIVQYVRRKY----NLLIGE--------RT-AEEIKIEIGSAYPldeeESMEV----RGRDLVTGLPKTIEissEEVREA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 312 LfkstLEPVEQVLKDAKISKSQ---------IDE-VVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAavqGA 381
Cdd:PRK13930 253 L----AEPLQQIVEAVKSVLEKtppelaadiIDRgIVLTGGGALLRGLDKLLSEET-GLPVHIAEDPLTCVARGT---GK 324
|
..
gi 6324120 382 IL 383
Cdd:PRK13930 325 AL 326
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
10-376 |
6.37e-09 |
|
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.
Pssm-ID: 399596 [Multi-domain] Cd Length: 327 Bit Score: 57.95 E-value: 6.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVatYESSVEIIANEqgnrvtPSFVAF--TPQERL-IGDaaknqaalnprntvfDAKRLIGRRFDDESVQ 86
Cdd:pfam06723 4 IGIDLGTANTLV--YVKGKGIVLNE------PSVVAIntKTKKVLaVGN---------------EAKKMLGRTPGNIVAV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 87 KDMKtwpfkvidvDGnpVIEvqYLEETktfspqeiSAMVLTKMKEIAEAKIGKKvEKAVITVPAYFNDAQRQATKDAGAI 166
Cdd:pfam06723 61 RPLK---------DG--VIA--DFEVT--------EAMLKYFIKKVHGRRSFSK-PRVVICVPSGITEVERRAVKEAAKN 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 167 SGLNVLRIINEPTAAAIAYGLGAGKSEKErhvLIFDLGGGTFDVSLLHiAGGVYTVKSTSgnthLGGQDFDTNLLEHFKA 246
Cdd:pfam06723 119 AGAREVFLIEEPMAAAIGAGLPVEEPTGN---MVVDIGGGTTEVAVIS-LGGIVTSKSVR----VAGDEFDEAIIKYIRK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 247 EFkkktGLDISDdaralrrlRTaAERAKRTLSSVTQT----TVEVdslfDGEDFESSLTRaRFEDLNAALFKSTLEPVEQ 322
Cdd:pfam06723 191 KY----NLLIGE--------RT-AERIKIEIGSAYPTeeeeKMEI----RGRDLVTGLPK-TIEISSEEVREALKEPVSA 252
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324120 323 VLKDAK---------ISKSQIDE-VVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGA 376
Cdd:pfam06723 253 IVEAVKevlektppeLAADIVDRgIVLTGGGALLRGLDKLLSDET-GLPVHIAEDPLTCVALGT 315
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
125-231 |
2.63e-07 |
|
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: 51.88 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 125 VLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAISGLNVLRIINEPTAAAIAYGLGAGksekerhvLIFDLG 204
Cdd:cd24047 48 IVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGIRDG--------AVVDIG 119
|
90 100
....*....|....*....|....*..
gi 6324120 205 GGTFDVSLLHIAGGVYTVKSTSGNTHL 231
Cdd:cd24047 120 GGTTGIAVLKDGKVVYTADEPTGGTHL 146
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
106-354 |
3.58e-07 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 52.94 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 106 EVQYLEETKTF------SPQEIS-------AMVLtKMKEIAEAKIGKKVEKAVITVPAYFN-----DAQRQAT---KDAG 164
Cdd:PRK11678 102 EVYFVKSPKSFlgasglKPQQVAlfedlvcAMML-HIKQQAEAQLQAAITQAVIGRPVNFQglggeEANRQAEgilERAA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 165 AISGLNVLRIINEPTAAAIAYglgAGKSEKERHVLIFDLGGGTFDVSLLHIaGGVYTVKSTSGNTHL-------GGQDFD 237
Cdd:PRK11678 181 KRAGFKDVEFQFEPVAAGLDF---EATLTEEKRVLVVDIGGGTTDCSMLLM-GPSWRGRADRSASLLghsgqriGGNDLD 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 238 -----TNLLEHFKAEFKKKTGL--------------DIS--------DDARALRRLRT---------------------- 268
Cdd:PRK11678 257 ialafKQLMPLLGMGSETEKGIalpslpfwnavainDVPaqsdfyslANGRLLNDLIRdarepekvarllkvwrqrlsyr 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 269 ---AAERAKRTLSSVTQTTVEVDSLFDGedFESSLTRARFEDLNAALFKSTLEPVEQVLKDAKIsksQIDEVVLVGGSTR 345
Cdd:PRK11678 337 lvrSAEEAKIALSDQAETRASLDFISDG--LATEISQQGLEEAISQPLARILELVQLALDQAQV---KPDVIYLTGGSAR 411
|
....*....
gi 6324120 346 IPKVQKLLS 354
Cdd:PRK11678 412 SPLIRAALA 420
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
123-358 |
1.17e-06 |
|
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466854 [Multi-domain] Cd Length: 282 Bit Score: 50.37 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 123 AMVLTKMKEIAEAKIGKKVEKAVITVP----AYFNDAQRqatkdagaiSGLNVLRIINEPTAAAIAYGLGagkSEKERHV 198
Cdd:cd24004 49 AESIKELLKELEEKLGSKLKDVVIAIAkvveSLLNVLEK---------AGLEPVGLTLEPFAAANLLIPY---DMRDLNI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 199 LIFDLGGGTFDVSLLHiAGGVytvkSTSGNTHLGGQDFDTNLLEHFKAEFKKktgldisddaralrrlrtaAERAKRTLS 278
Cdd:cd24004 117 ALVDIGAGTTDIALIR-NGGI----EAYRMVPLGGDDFTKAIAEGFLISFEE-------------------AEKIKRTYG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 279 SVtqttvevDSLFDGEDFESSLTRARFEDLNAALFKSTLEPVEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFD 358
Cdd:cd24004 173 IF-------LLIEAKDQLGFTINKKEVYDIIKPVLEELASGIANAIEEYNGKFKLPDAVYLVGGGSKLPGLNEALAEKLG 245
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
10-360 |
3.39e-06 |
|
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: 49.62 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVA---TYES-SVEIIANEQG------NRVTPSFVAFTPQERligdaaknqaalnprntvFDAKRLIGRR 79
Cdd:cd11735 3 VAIDFGTTSSGYAysfTKEPeCIHVMRRWEGgdpgvsNQKTPTTILLTPERK------------------FHSFGYAARD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 80 FDDESVQKDMKTW----PFKV-IDVDGNPVIEVQYLEET-KTFSPQEISAMVLTKMKEIAEAKI----GKKVEKA----V 145
Cdd:cd11735 65 FYHDLDPNESKQWlyfeKFKMkLHTTGNLTMETDLTAANgKKVKALEIFAYALQFFKEQALKELsdqaGSEFDNSdvrwV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 146 ITVPAYFNDAQRQATKDAGAISGLNV------LRIINEPTAAAIaYGLGAGKSEKERHVLIfDLGGGTFDVSLLHI---A 216
Cdd:cd11735 145 ITVPAIWKQPAKQFMRQAAYKAGLASpenpeqLIIALEPEAASI-YCRKLRLHQMDRYVVV-DCGGGTVDLTVHQIrlpE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 217 GGVYTVKSTSGNTHLG-GQDFDTNLL------EHFKAEFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVD- 288
Cdd:cd11735 223 GHLKELYKASGGPYGSlGVDYEFEKLlckifgEDFIDQFKIKRPAAWVDLMIAFESRKRAAAPDRTNPLNITLPFSFIDy 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 289 -SLFDGEDFESSLTRARFE--------------DLNAALFKSTLEPVEQVLKD--AKISKSQIDEVVLVGGSTRIPKVQK 351
Cdd:cd11735 303 yKKFRGHSVEHALRKSNVDfvkwssqgmlrmspDAMNALFKPTIDHIIQHLTDlfQKPEVSGVKFLFLVGGFAESPLLQQ 382
|
....*....
gi 6324120 352 LLSDFFDGK 360
Cdd:cd11735 383 AVQNAFGDQ 391
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
96-231 |
9.33e-06 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 47.52 E-value: 9.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 96 VIDVDGNPV-------------IEVQYLEETKtfspqeisamVLTKMKEIAEAKIGKKVEKAVITVPAyfndaqrqAT-- 160
Cdd:PRK15080 40 VLDEDGQPVagalewadvvrdgIVVDFIGAVT----------IVRRLKATLEEKLGRELTHAATAIPP--------GTse 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324120 161 KDAGAI------SGLNVLRIINEPTAAAIAYGLGAGksekerhvLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHL 231
Cdd:PRK15080 102 GDPRAIinvvesAGLEVTHVLDEPTAAAAVLGIDNG--------AVVDIGGGTTGISILKDGKVVYSADEPTGGTHM 170
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
143-355 |
1.43e-05 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 47.59 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 143 KAVITVPAYFNDAQRQATKDAGAISGLNVLRIINEPTAAAIayglGAGK--SEKERHVLIfDLGGGTFDVSLLHIAGGVy 220
Cdd:PRK13928 97 RIMICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAI----GAGLdiSQPSGNMVV-DIGGGTTDIAVLSLGGIV- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 221 tvksTSGNTHLGGQDFDTNLLEHFKAEFKkktgLDISDdaralrrlRTaAERAKRTLSSVTQTTVEVDSLFDGEDFESSL 300
Cdd:PRK13928 171 ----TSSSIKVAGDKFDEAIIRYIRKKYK----LLIGE--------RT-AEEIKIKIGTAFPGAREEEMEIRGRDLVTGL 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324120 301 TRA---RFEDLNAALfkstLEPVEQVLKDAK---------ISKSQIDE-VVLVGGSTRIPKVQKLLSD 355
Cdd:PRK13928 234 PKTitvTSEEIREAL----KEPVSAIVQAVKsvlertppeLSADIIDRgIIMTGGGALLHGLDKLLAE 297
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
5-248 |
1.48e-05 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 47.59 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 5 VFQGA-IGIDLGTtySCVATYESSVEIIANEqgnrvtPSFVAFTPQER---LIGDAAKNQAALNPRNTVfdAKRligrrf 80
Cdd:PRK13929 1 MFQSTeIGIDLGT--ANILVYSKNKGIILNE------PSVVAVDTETKavlAIGTEAKNMIGKTPGKIV--AVR------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 81 ddesvqkdmktwPFKvidvDGnpvievqyleetkTFSPQEISAMVLTKMKEIAEAKIGKKVEK--AVITVPAYFNDAQRQ 158
Cdd:PRK13929 65 ------------PMK----DG-------------VIADYDMTTDLLKQIMKKAGKNIGMTFRKpnVVVCTPSGSTAVERR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 159 ATKDAGAISGLNVLRIINEPTAAAIAYGLGAgkSEKERHVLIfDLGGGTFDVSLLHIAGGVytvksTSGNTHLGGQDFDT 238
Cdd:PRK13929 116 AISDAVKNCGAKNVHLIEEPVAAAIGADLPV--DEPVANVVV-DIGGGTTEVAIISFGGVV-----SCHSIRIGGDQLDE 187
|
250
....*....|
gi 6324120 239 NLLEHFKAEF 248
Cdd:PRK13929 188 DIVSFVRKKY 197
|
|
| ASKHA_NBD_MamK |
cd24009 |
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ... |
10-214 |
2.35e-05 |
|
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called magnetosome cytoskeleton protein MamK, is a protein with ATPase activity which forms dynamic cytoplasmic filaments (probably with paralog MamK-like) that may organize magnetosomes into long chains running parallel to the long axis of the cell. Turnover of MamK filaments is probably promoted by MamK-like (e.g.. MamJ and/or LimJ), which provides a monomer pool. MamK forms twisted filaments in the presence of ATP or GTP. It serves to close gaps between magnetosomes in the chain. Interaction with MCP10 is involved in controlling the response to magnetic fields, possibly by controlling flagellar rotation. The MamK family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466859 [Multi-domain] Cd Length: 328 Bit Score: 46.82 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 10 IGIDLGTTYSCVATyessveiianEQGNR-VTPSFVAFtPQ----------ERLIGDAA-KNQAALNPRntvfdakrlig 77
Cdd:cd24009 4 IGIDLGTSRSAVVT----------SRGKRfSFRSVVGY-PKdiiarkllgkEVLFGDEAlENRLALDLR----------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 78 rrfddesvqkdmktWPFKvidvDGnpVIevqyleetKTFSPQEISAMVLTKMKEIAEAKIGKKVEK-AVITVPAYFNDAQ 156
Cdd:cd24009 62 --------------RPLE----DG--VI--------KEGDDRDLEAARELLQHLIELALPGPDDEIyAVIGVPARASAEN 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6324120 157 RQATKDAGAISGLNVLrIINEPTAaaIAYGLGagkseKERHVLIFDLGGGTFDVSLLH 214
Cdd:cd24009 114 KQALLEIARELVDGVM-VVSEPFA--VAYGLD-----RLDNSLIVDIGAGTTDLCRMK 163
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
167-358 |
8.99e-05 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 45.12 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 167 SGLNVLRIINEPTAAAIAYgLGagKSEKERHVLIFDLGGGTFDVS------LLHIAggVYTVkstsgnthlGGQDFdTNl 240
Cdd:COG0849 174 AGLEVEDLVLSPLASAEAV-LT--EDEKELGVALVDIGGGTTDIAvfkdgaLRHTA--VIPV---------GGDHI-TN- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 241 lehfkaefkkktglDIsddARALRRLRTAAERAKRTLSSVTQTTVEVDSLFD----GEDFESSLTR--------ARFEDL 308
Cdd:COG0849 238 --------------DI---AIGLRTPLEEAERLKIKYGSALASLADEDETIEvpgiGGRPPREISRkelaeiieARVEEI 300
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6324120 309 naalfkstLEPVEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFD 358
Cdd:COG0849 301 --------FELVRKELKRSGYEEKLPAGVVLTGGGSQLPGLVELAEEILG 342
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
323-385 |
1.18e-04 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 44.82 E-value: 1.18e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324120 323 VLKDAKIsksQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSiNPDEAVAYGAAVQGAILTG 385
Cdd:COG1070 388 ALEEAGV---KIDRIRATGGGARSPLWRQILADVL-GRPVEVP-EAEEGGALGAALLAAVGLG 445
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
143-220 |
2.05e-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: 38.60 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 143 KAVITVPAYFNDAQRQAT-----------KDAGAISGLNVLRIINEPTAAAIAYGLGAGKsekeRHVLIFDLGGGTFDVS 211
Cdd:cd00012 15 PIVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGALLTLGP----EGLLVVDLGGGTDISA 90
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....*....
gi 6324120 212 LLHIAGGVY 220
Cdd:cd00012 91 NVVLVGGGA 99
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| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
145-279 |
6.61e-03 |
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rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 38.92 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324120 145 VITVPAYFNDAQRQATKDAGAISGLNVLRIINEPTAAAIayglGAGKSEKE-RHVLIFDLGGGTFDVSLLHIAGGVYtvk 223
Cdd:PRK13927 100 VICVPSGITEVERRAVRESALGAGAREVYLIEEPMAAAI----GAGLPVTEpTGSMVVDIGGGTTEVAVISLGGIVY--- 172
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 6324120 224 stSGNTHLGGQDFDTNLLEHfkaeFKKKTGLDISDdaralrrlRTaAERAKRTLSS 279
Cdd:PRK13927 173 --SKSVRVGGDKFDEAIINY----VRRNYNLLIGE--------RT-AERIKIEIGS 213
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| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
333-385 |
9.93e-03 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 38.69 E-value: 9.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 6324120 333 QIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKsINPDEAVAYGAAVQGAILTG 385
Cdd:cd07809 393 EIDEIRLIGGGSKSPVWRQILADVF-GVPVVV-PETGEGGALGAALQAAWGAG 443
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