|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
10-452 |
0e+00 |
|
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: 711.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 10 SAVLTLLLAGYLAQQYLPLPTPKVIGIDLGTTYCSVGVFFPGTGKVKVIPDENGHISIPSMVSFTD-GDVYVGYESLELA 88
Cdd:cd10237 1 SGILALLLAGYLGQQYLPPPKPKIVGIDLGTTYSCVGVYHAVTGEVEVIPDDDGHKSIPSVVAFTPdGGVLVGYDALAQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 89 DSNPQNTIYDAKRFIGKIFTPEELEAEVGRYPFKVLHRN-GMAEFSVTSN-ETIIVSPEFVGSRLLLKLKEMAEEYLGMP 166
Cdd:cd10237 81 EHNPSNTIYDAKRFIGKTFTKEELEEEAKRYPFKVVNDNiGSAFFEVPLNgSTLVVSPEDIGSLILLKLKKAAEAYLGVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 167 VANAVISVPAEFDLQQRNSTIQAANLAGLKILRVINEPTAAAMAYGLHKV-DVFYVLVIDLGGGTLDVSLLNKQGGMFLT 245
Cdd:cd10237 161 VAKAVISVPAEFDEKQRNATRKAANLAGLEVLRVINEPTAAAMAYGLHKKsDVNNVLVVDLGGGTLDVSLLNVQGGMFLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 246 RAMSGNNKLGGQDFNQRLLQHLYKEIYQTYGFLPSRKEEIHRLRQAVEMVKLNLTIHQSAQVSVLltvegkdskepqngd 325
Cdd:cd10237 241 RAMAGNNHLGGQDFNQRLFQYLIDRIAKKFGKTLTDKEDIQRLRQAVEEVKLNLTNHNSASLSLP--------------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 326 selpkdqltpgdghhvnrvfrpgLSESKSGKSQVLFETEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLV 405
Cdd:cd10237 306 -----------------------LQISLPSAFKVKFKEEITRDLFETLNEDLFQRVLEPIRQVLAEVELGKEDVDEIVLV 362
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 30089677 406 GGSTRIPRIRQVIQEFFGKDPNTSVDPDLAVVTGVAIQAGIDGGSWP 452
Cdd:cd10237 363 GGSTRIPRVRQLVREFFGKDPNTSVDPELAVVTGVAIQAGIIGGMWP 409
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
33-446 |
9.12e-170 |
|
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: 482.40 E-value: 9.12e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 33 VIGIDLGTTYCSVGVFFpgTGKVKVIPDENGHISIPSMVSFTDGDVYVGYESLELADSNPQNTIYDAKRFIGKIFTPEEL 112
Cdd:cd24028 1 AIGIDLGTTYSCVAVWR--NGKVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 113 EAEVGRYPFKVLHRN-GMAEFSVT-SNETIIVSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQAA 190
Cdd:cd24028 79 QSDIKHWPFKVVEDEdGKPKIEVTyKGEEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 191 NLAGLKILRVINEPTAAAMAYGLHKVD--VFYVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQHLY 268
Cdd:cd24028 159 TIAGLNVLRIINEPTAAALAYGLDKKSsgERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 269 KEIYQTYGF-LPSRKEEIHRLRQAVEMVKLNLTIHQSAQVSVLLTVEGKDskepqngdselpkdqltpgdghhvnrvfrp 347
Cdd:cd24028 239 EEFKKKHGKdLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGID------------------------------ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 348 glsesksgksqvlFETEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFF-GKDP 426
Cdd:cd24028 289 -------------FETTITRAKFEELCEDLFKKCLEPVEKVLKDAKLSKDDIDEVVLVGGSTRIPKIQELLSEFFgGKEL 355
|
410 420
....*....|....*....|
gi 30089677 427 NTSVDPDLAVVTGVAIQAGI 446
Cdd:cd24028 356 CKSINPDEAVAYGAAIQAAI 375
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
33-446 |
1.20e-127 |
|
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: 375.40 E-value: 1.20e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 33 VIGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFTDGDVYVGYESLELADSNPQNTIYDAKRFIGKIFTPEEL 112
Cdd:cd10241 3 VIGIDLGTTYSCVGVF--KNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 113 EAEVGRYPFKVLHRNGMAEFSV-TSNETIIVSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQAAN 191
Cdd:cd10241 81 QKDIKLLPFKIVNKNGKPYIQVeVKGEKKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 192 LAGLKILRVINEPTAAAMAYGLHKVDVFY-VLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQHLYKE 270
Cdd:cd10241 161 IAGLNVLRIINEPTAAAIAYGLDKKGGEKnILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFIKL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 271 IYQTYGFLPSR-KEEIHRLRQAVEMVKLNLTIHQSAQVSVLLTVEGKDskepqngdselpkdqltpgdghhvnrvfrpgL 349
Cdd:cd10241 241 FKKKTGKDISKdKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGED-------------------------------F 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 350 SESksgksqvlfeteVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFF-GKDPNT 428
Cdd:cd10241 290 SET------------LTRAKFEELNMDLFRKTLKPVQKVLEDAGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFnGKEPSR 357
|
410
....*....|....*...
gi 30089677 429 SVDPDLAVVTGVAIQAGI 446
Cdd:cd10241 358 GINPDEAVAYGAAVQAGI 375
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
33-446 |
1.23e-117 |
|
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: 357.34 E-value: 1.23e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 33 VIGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFTDGDVYVGYESLELADSNPQNTIYDAKRFIGKIFTPEEL 112
Cdd:pfam00012 1 VIGIDLGTTNSCVAVM--EGGGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 113 EAEVGRYPFK-VLHRNGMAEFSVTSNETIIvSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQAAN 191
Cdd:pfam00012 79 QRDIKHLPYKvVKLPNGDAGVEVRYLGETF-TPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 192 LAGLKILRVINEPTAAAMAYGLHKVDV-FYVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQHLYKE 270
Cdd:pfam00012 158 IAGLNVLRIVNEPTAAALAYGLDKTDKeRNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 271 IYQTYGF-LPSRKEEIHRLRQAVEMVKLNLTihqSAQVSVLLTVEGKDSkepqngdselpkdqltpgDGHHVNrvfrpgl 349
Cdd:pfam00012 238 FKKKYGIdLSKDKRALQRLREAAEKAKIELS---SNQTNINLPFITAMA------------------DGKDVS------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 350 sesksgksqvlfeTEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPNTS 429
Cdd:pfam00012 290 -------------GTLTRAKFEELVADLFERTLEPVEKALKDAGLSKSEIDEVVLVGGSTRIPAVQELVKEFFGKEPSKG 356
|
410
....*....|....*..
gi 30089677 430 VDPDLAVVTGVAIQAGI 446
Cdd:pfam00012 357 VNPDEAVAIGAAVQAGV 373
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
34-446 |
1.42e-116 |
|
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: 346.92 E-value: 1.42e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 34 IGIDLGTTYCSVGVFFpgTGKVKVIPDENGHISIPSMVSFTDGDVYVGYESLELADSNPQNTIYDAKRFIGKIFTPEELE 113
Cdd:cd10233 2 IGIDLGTTYSCVGVWQ--NDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 114 AEVGRYPFKVLHRNGMAEFSVT-SNETIIVSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQAANL 192
Cdd:cd10233 80 SDMKHWPFKVVSGGDKPKIQVEyKGETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 193 AGLKILRVINEPTAAAMAYGLHKVDV--FYVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQHLYKE 270
Cdd:cd10233 160 AGLNVLRIINEPTAAAIAYGLDKKGKgeRNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 271 IYQTY-GFLPSRKEEIHRLRQAVEMVKLNLTihQSAQVSVlltvegkdskepqngdsELpkDQLTPGdghhvnrvfrpgl 349
Cdd:cd10233 240 FKRKHkKDISGNPRALRRLRTACERAKRTLS--SSTQASI-----------------EI--DSLFEG------------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 350 sesksgksqVLFETEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFF-GKDPNT 428
Cdd:cd10233 286 ---------IDFYTSITRARFEELCADLFRSTLEPVEKVLRDAKLDKSQIHEIVLVGGSTRIPKVQKLLQDFFnGKELNK 356
|
410
....*....|....*...
gi 30089677 429 SVDPDLAVVTGVAIQAGI 446
Cdd:cd10233 357 SINPDEAVAYGAAVQAAI 374
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
33-449 |
1.70e-111 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 337.18 E-value: 1.70e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 33 VIGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFT-DGDVYVGYESLELADSNPQNTIYDAKRFIGKIFTPEE 111
Cdd:COG0443 1 AIGIDLGTTNSVVAVV--EGGEPQVIPNAEGRRTLPSVVAFPkDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFDEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 112 LEAEVGRYpfkvlhrngmaefsvtsnetiivSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQAAN 191
Cdd:COG0443 79 TEVGGKRY-----------------------SPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAAR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 192 LAGLKILRVINEPTAAAMAYGLHKVDVF-YVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQHLYKE 270
Cdd:COG0443 136 IAGLEVLRLLNEPTAAALAYGLDKGKEEeTILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 271 IYQTYGF-LPSRKEEIHRLRQAVEMVKLNLTIHQSAQVSVLLTvegkdskepqngdselpkdqltpGDGHhvnrvfrpgl 349
Cdd:COG0443 216 FGKEEGIdLRLDPAALQRLREAAEKAKIELSSADEAEINLPFS-----------------------GGKH---------- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 350 sesksgksqvlFETEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPNTS 429
Cdd:COG0443 263 -----------LDVELTRAEFEELIAPLVERTLDPVRQALADAGLSPSDIDAVLLVGGSTRMPAVRERVKELFGKEPLKG 331
|
410 420
....*....|....*....|
gi 30089677 430 VDPDLAVVTGVAIQAGIDGG 449
Cdd:COG0443 332 VDPDEAVALGAAIQAGVLAG 351
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
33-446 |
2.46e-110 |
|
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: 330.98 E-value: 2.46e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 33 VIGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFT-DGDVYVGYESLELADSNPQNTIYDAKRFIGKIFTPEE 111
Cdd:cd10234 1 IIGIDLGTTNSCVAVM--EGGKPTVIPNAEGGRTTPSVVAFTkDGERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 112 LEAEVGRYPFkVLHRNGMAEFSVTSNEtiiVSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQAAN 191
Cdd:cd10234 79 VERKQVPYPV-VSAGNGDAWVEIGGKE---YTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 192 LAGLKILRVINEPTAAAMAYGLHKVDVFYVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQHLYKEI 271
Cdd:cd10234 155 IAGLEVLRIINEPTAAALAYGLDKKKDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 272 YQTYGF-LPSRKEEIHRLRQAVEMVKLNLTIHQSAQVSV-LLTVegkdskepqngDSELPKdqltpgdgHhvnrvfrpgl 349
Cdd:cd10234 235 KKEEGIdLSKDKMALQRLKEAAEKAKIELSSVLETEINLpFITA-----------DASGPK--------H---------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 350 sesksgksqvlFETEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPNTS 429
Cdd:cd10234 286 -----------LEMKLTRAKFEELTEDLVERTIEPVEQALKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKG 354
|
410
....*....|....*..
gi 30089677 430 VDPDLAVVTGVAIQAGI 446
Cdd:cd10234 355 VNPDEVVAIGAAIQGGV 371
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
32-449 |
2.49e-104 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 323.59 E-value: 2.49e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 32 KVIGIDLGTTYCSVGVFfPGtGKVKVIPDENGHISIPSMVSFT-DGDVYVGyeslELAD----SNPQNTIYDAKRFIGKi 106
Cdd:PRK00290 3 KIIGIDLGTTNSCVAVM-EG-GEPKVIENAEGARTTPSVVAFTkDGERLVG----QPAKrqavTNPENTIFSIKRLMGR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 107 fTPEELEAEVGRYPFKVLHR-NGMAEFSVTSNEtiiVSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNS 185
Cdd:PRK00290 76 -RDEEVQKDIKLVPYKIVKAdNGDAWVEIDGKK---YTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 186 TIQAANLAGLKILRVINEPTAAAMAYGLHKVDVFYVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQ 265
Cdd:PRK00290 152 TKDAGKIAGLEVLRIINEPTAAALAYGLDKKGDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIID 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 266 HLYKEIYQTYGF-LPSRKEEIHRLRQAVEMVKLNLTIHQSAQVSV-LLTVegkdskepqngDSELPKdqltpgdghHVNr 343
Cdd:PRK00290 232 YLADEFKKENGIdLRKDKMALQRLKEAAEKAKIELSSAQQTEINLpFITA-----------DASGPK---------HLE- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 344 vfrpglsesksgksqvlfeTEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFFG 423
Cdd:PRK00290 291 -------------------IKLTRAKFEELTEDLVERTIEPCKQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFFG 351
|
410 420
....*....|....*....|....*.
gi 30089677 424 KDPNTSVDPDLAVVTGVAIQAGIDGG 449
Cdd:PRK00290 352 KEPNKGVNPDEVVAIGAAIQGGVLAG 377
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
34-446 |
7.11e-104 |
|
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: 313.74 E-value: 7.11e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 34 IGIDLGTTYcSVGVFFPGTGKVKVIPDENGHISIPSMVSFT-DGDVYVGYESLELADSNPQNTIYDAKRFIGKiftpeel 112
Cdd:cd24029 1 VGIDLGTTN-SAVAYWDGNGAEVIIENSEGKRTTPSVVYFDkDGEVLVGEEAKNQALLDPENTIYSVKRLMGR------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 113 eaevgrypfkvlhrngmAEFSVTSNETIIVSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQAANL 192
Cdd:cd24029 73 -----------------DTKDKEEIGGKEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 193 AGLKILRVINEPTAAAMAYGLHKVDVF-YVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQHLYKEI 271
Cdd:cd24029 136 AGLNVLRLINEPTAAALAYGLDKEGKDgTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEKI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 272 YQTYGFLPSRKEEI--HRLRQAVEMVKLNLTIHQSAQVSVLLTVEGKDskepqngdselpkdqltpgdghhvnrvfrpgl 349
Cdd:cd24029 216 GIETGILDDKEDERarARLREAAEEAKIELSSSDSTDILILDDGKGGE-------------------------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 350 sesksgksqvlFETEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPNTS 429
Cdd:cd24029 264 -----------LEIEITREEFEELIAPLIERTIDLLEKALKDAKLSPEDIDRVLLVGGSSRIPLVREMLEEYFGREPISS 332
|
410
....*....|....*..
gi 30089677 430 VDPDLAVVTGVAIQAGI 446
Cdd:cd24029 333 VDPDEAVAKGAAIYAAS 349
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
33-446 |
4.48e-103 |
|
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: 312.23 E-value: 4.48e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 33 VIGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFTDGD-VYVGYESLELADSNPQNTIYDAKRFIGKifTPEE 111
Cdd:cd10236 4 AVGIDLGTTNSLVATV--RSGQPEVLPDEKGEALLPSVVHYGEDGkITVGEKAKENAITDPENTISSVKRLMGR--SLAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 112 LEAEVGRYPFKVLHRNGMAEFSVTSNETIivSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQAAN 191
Cdd:cd10236 80 VKEELPLLPYRLVGDENELPRFRTGAGNL--TPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 192 LAGLKILRVINEPTAAAMAYGLHKVDVFYVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQHLYKEI 271
Cdd:cd10236 158 LAGLNVLRLLNEPTAAALAYGLDQKKEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWILKQI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 272 YQTygfLPSRKEEIHRLRQAVEMVKLNLTihQSAQVSVLLTVEGKDskepqngdselpkdqltpgdghhvnrvfrpglse 351
Cdd:cd10236 238 GID---ARLDPAVQQALLQAARRAKEALS--DADSASIEVEVEGKD---------------------------------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 352 sksgksqvlFETEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPNTSVD 431
Cdd:cd10236 279 ---------WEREITREEFEELIQPLVKRTLEPCRRALKDAGLEPADIDEVVLVGGSTRIPLVRQRVAEFFGREPLTSIN 349
|
410
....*....|....*
gi 30089677 432 PDLAVVTGVAIQAGI 446
Cdd:cd10236 350 PDEVVALGAAIQADI 364
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
34-446 |
9.38e-102 |
|
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar proteins; Ssb is ribosome-bound, Hsp70-type chaperone that assists in the co-translational folding of newly synthesized proteins in the cytosol. It stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Saccharmoyces cerevisiae Ssb are encoded by two genes, SSB1 and SSB2. Ssb1p is also known as cold-inducible protein YG101. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466943 [Multi-domain] Cd Length: 375 Bit Score: 309.22 E-value: 9.38e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 34 IGIDLGTTYCSVGVFfpgTGKVKVIPDENGHISIPSMVSFTDGDVYVGYESLELADSNPQNTIYDAKRFIGKIFTPEELE 113
Cdd:cd24093 2 IGIDLGTTYSCVATY---ESSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 114 AEVGRYPFKVLHRNGMAEFSVTS-NETIIVSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQAANL 192
Cdd:cd24093 79 KDMKTWPFKVIDVNGNPVIEVQYlGETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 193 AGLKILRVINEPTAAAMAYGL--HKVDV-FYVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQHLYK 269
Cdd:cd24093 159 AGLNVLRIINEPTAAAIAYGLgaGKSEKeRHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 270 EIYQTYGF-LPSRKEEIHRLRQAVEMVKLNLTIHQSAQVSVLLTVEGKDskepqngdselpkdqltpgdghhvnrvfrpg 348
Cdd:cd24093 239 EFKKKTGLdISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGED------------------------------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 349 lsesksgksqvlFETEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFF-GKDPN 427
Cdd:cd24093 288 ------------FESSITRARFEDLNAALFKSTLEPVEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLE 355
|
410
....*....|....*....
gi 30089677 428 TSVDPDLAVVTGVAIQAGI 446
Cdd:cd24093 356 KSINPDEAVAYGAAVQGAI 374
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
33-446 |
1.54e-99 |
|
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: 303.42 E-value: 1.54e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 33 VIGIDLGTTYCSVGVFfpgTGKV-KVIPDENGHISIPSMVSFT-DGDVYVGYESLELADSNPQNTIYDAKRFIGKIFTPE 110
Cdd:cd11733 3 VIGIDLGTTNSCVAVM---EGKTpKVIENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 111 ELEAEVGRYPFK-VLHRNGMAEFSVTSNEtiiVSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQA 189
Cdd:cd11733 80 EVQKDIKMVPYKiVKASNGDAWVEAHGKK---YSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 190 ANLAGLKILRVINEPTAAAMAYGLHKVDVFYVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQHLYK 269
Cdd:cd11733 157 GQIAGLNVLRIINEPTAAALAYGLDKKDDKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNYLVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 270 EIYQTYGF-LPSRKEEIHRLRQAVEMVKLNLTIHQSAQVSV-LLTVegkdskepqngDSELPKdqltpgdghHVNrvfrp 347
Cdd:cd11733 237 EFKKEQGIdLSKDNLALQRLREAAEKAKIELSSSLQTDINLpFITA-----------DASGPK---------HLN----- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 348 glsesksgksqvlfeTEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPN 427
Cdd:cd11733 292 ---------------MKLTRAKFESLVGDLIKRTVEPCKKCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIFGKAPS 356
|
410
....*....|....*....
gi 30089677 428 TSVDPDLAVVTGVAIQAGI 446
Cdd:cd11733 357 KGVNPDEAVAMGAAIQGGV 375
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
34-458 |
6.22e-96 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 302.87 E-value: 6.22e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 34 IGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFTDGDVYVGYESLELADSNPQNTIYDAKRFIGKIFTPEELE 113
Cdd:PTZ00009 7 IGIDLGTTYSCVGVW--KNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDSVVQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 114 AEVGRYPFKVLHR-NGMAEFSVT-SNETIIVSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQAAN 191
Cdd:PTZ00009 85 SDMKHWPFKVTTGgDDKPMIEVTyQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAGT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 192 LAGLKILRVINEPTAAAMAYGLHKVDV--FYVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQHLYK 269
Cdd:PTZ00009 165 IAGLNVLRIINEPTAAAIAYGLDKKGDgeKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEFCVQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 270 EIYQTYG--FLPSRKEEIHRLRQAVEMVKlnLTIHQSAQVSVLLtvegkdskepqngdselpkDQLTPGdghhvnrvfrp 347
Cdd:PTZ00009 245 DFKRKNRgkDLSSNQRALRRLRTQCERAK--RTLSSSTQATIEI-------------------DSLFEG----------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 348 glsesksgksqVLFETEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFF-GKDP 426
Cdd:PTZ00009 293 -----------IDYNVTISRARFEELCGDYFRNTLQPVEKVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFnGKEP 361
|
410 420 430
....*....|....*....|....*....|..
gi 30089677 427 NTSVDPDLAVVTGVAIQAGIDGGSWPLQVSAL 458
Cdd:PTZ00009 362 CKSINPDEAVAYGAAVQAAILTGEQSSQVQDL 393
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
32-449 |
1.73e-94 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 298.98 E-value: 1.73e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 32 KVIGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFT-DGDVYVGYESLELADSNPQNTIYDAKRFIGKIFtpE 110
Cdd:PRK13411 3 KVIGIDLGTTNSCVAVL--EGGKPIVIPNSEGGRTTPSIVGFGkSGDRLVGQLAKRQAVTNAENTVYSIKRFIGRRW--D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 111 ELEAEVGRYPFK-VLHRNGMAEFSVTSNEtiiVSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQA 189
Cdd:PRK13411 79 DTEEERSRVPYTcVKGRDDTVNVQIRGRN---YTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 190 ANLAGLKILRVINEPTAAAMAYGLHKVDV-FYVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQHLY 268
Cdd:PRK13411 156 GTIAGLEVLRIINEPTAAALAYGLDKQDQeQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWLV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 269 KEIYQTYGF-LPSRKEEIHRLRQAVEMVKLNLTIHQSAqvSVLLTVEGKDSKEPQNgdselpkdqltpgdghhvnrvfrp 347
Cdd:PRK13411 236 ENFQQQEGIdLSQDKMALQRLREAAEKAKIELSSMLTT--SINLPFITADETGPKH------------------------ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 348 glsesksgksqvlFETEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFF-GKDP 426
Cdd:PRK13411 290 -------------LEMELTRAKFEELTKDLVEATIEPMQQALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFgGKQP 356
|
410 420
....*....|....*....|...
gi 30089677 427 NTSVDPDLAVVTGVAIQAGIDGG 449
Cdd:PRK13411 357 DRSVNPDEAVALGAAIQAGVLGG 379
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
33-449 |
4.70e-93 |
|
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: 286.65 E-value: 4.70e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 33 VIGIDLGTTYCSVGVFfpgTGKV-KVIPDENGHISIPSMVSFT-DGDVYVGYESLELADSNPQNTIYDAKRFIGKIFTPE 110
Cdd:cd11734 3 VIGIDLGTTNSCVAVM---EGKTpRVIENAEGARTTPSVVAFTkDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 111 ELEAEVGRYPFKVL-HRNGMAEFSVTSNEtiiVSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQA 189
Cdd:cd11734 80 EVQRDIKEVPYKIVkHSNGDAWVEARGQK---YSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 190 ANLAGLKILRVINEPTAAAMAYGLHKVDVFYVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQHLYK 269
Cdd:cd11734 157 GQIAGLNVLRVINEPTAAALAYGLDKSGDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHIVS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 270 EIYQTYGF-LPSRKEEIHRLRQAVEMVKLNLTihQSAQVSVLLTVEGKDSKEPQngdselpkdqltpgdghHVNrvfrpg 348
Cdd:cd11734 237 EFKKESGIdLSKDRMAIQRIREAAEKAKIELS--STLQTDINLPFITADASGPK-----------------HIN------ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 349 lsesksgksqvlfeTEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPNT 428
Cdd:cd11734 292 --------------MKLTRAQFESLVKPLVDRTVEPCKKALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIFGREPSK 357
|
410 420
....*....|....*....|.
gi 30089677 429 SVDPDLAVVTGVAIQAGIDGG 449
Cdd:cd11734 358 GVNPDEAVAIGAAIQGGVLSG 378
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
32-449 |
4.86e-92 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 293.07 E-value: 4.86e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 32 KVIGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFT-DGDVYVGYESLELADSNPQNTIYDAKRFIGKIFtpE 110
Cdd:PRK13410 3 RIVGIDLGTTNSVVAVM--EGGKPVVIANAEGMRTTPSVVGFTkDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRY--D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 111 ELEAEVGRYPFKVlHRNGMAEFSV----TSNEtiiVSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNST 186
Cdd:PRK13410 79 ELDPESKRVPYTI-RRNEQGNVRIkcprLERE---FAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQAT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 187 IQAANLAGLKILRVINEPTAAAMAYGLHKVDVFYVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQH 266
Cdd:PRK13410 155 RDAGRIAGLEVERILNEPTAAALAYGLDRSSSQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 267 LYKEIYQTYGF-LPSRKEEIHRLRQAVEMVKLNLTIHQSAQVSVLLTVEGKDSkepqngdselPKdqltpgdghHVnrvf 345
Cdd:PRK13410 235 LAEQFLEKEGIdLRRDRQALQRLTEAAEKAKIELSGVSVTDISLPFITATEDG----------PK---------HI---- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 346 rpglsesksgksqvlfETEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFFGKD 425
Cdd:PRK13410 292 ----------------ETRLDRKQFESLCGDLLDRLLRPVKRALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLIPRE 355
|
410 420
....*....|....*....|....
gi 30089677 426 PNTSVDPDLAVVTGVAIQAGIDGG 449
Cdd:PRK13410 356 PNQNVNPDEVVAVGAAIQAGILAG 379
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
32-449 |
6.82e-91 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 288.94 E-value: 6.82e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 32 KVIGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFT-DGDVYVGYESLELADSNPQNTIYDAKRFIGKIFtpE 110
Cdd:CHL00094 3 KVVGIDLGTTNSVVAVM--EGGKPTVIPNAEGFRTTPSIVAYTkKGDLLVGQIAKRQAVINPENTFYSVKRFIGRKF--S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 111 ELEAEVGRYPFKVLHrngmaefsvTSNETIIV---------SPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQ 181
Cdd:CHL00094 79 EISEEAKQVSYKVKT---------DSNGNIKIecpalnkdfSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 182 QRNSTIQAANLAGLKILRVINEPTAAAMAYGLHKVDVFYVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQ 261
Cdd:CHL00094 150 QRQATKDAGKIAGLEVLRIINEPTAASLAYGLDKKNNETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 262 RLLQHLYKEIYQTYGF-LPSRKEEIHRLRQAVEMVKLNLTihQSAQVSVLLtvegkdskepqngdselpkdqltpgdghh 340
Cdd:CHL00094 230 KIVNWLIKEFKKKEGIdLSKDRQALQRLTEAAEKAKIELS--NLTQTEINL----------------------------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 341 vnrvfrPGLSESKSGKSQvlFETEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQE 420
Cdd:CHL00094 279 ------PFITATQTGPKH--IEKTLTRAKFEELCSDLINRCRIPVENALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKK 350
|
410 420
....*....|....*....|....*....
gi 30089677 421 FFGKDPNTSVDPDLAVVTGVAIQAGIDGG 449
Cdd:CHL00094 351 LLGKKPNQSVNPDEVVAIGAAVQAGVLAG 379
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
34-449 |
3.09e-90 |
|
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: 278.36 E-value: 3.09e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 34 IGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSF-TDGDVYVGYESLELADSNPQNTIYDAKRFIG-------- 104
Cdd:cd10235 1 IGIDLGTTNSLVAVW--RDGGAELIPNALGEYLTPSVVSVdEDGSILVGRAAKERLVTHPDRTAASFKRFMGtdkqyrlg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 105 -KIFTPEELEAEVgrypfkvlhrngmaefsvtsnetiivspefvgsrlLLKLKEMAEEYLGMPVANAVISVPAEFDLQQR 183
Cdd:cd10235 79 nHTFRAEELSALV-----------------------------------LKSLKEDAEAYLGEPVTEAVISVPAYFNDEQR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 184 NSTIQAANLAGLKILRVINEPTAAAMAYGLHKV-DVFYVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQR 262
Cdd:cd10235 124 KATKDAGELAGLKVERLINEPTAAALAYGLHKReDETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 263 LLQHLYKEiYQTYGFLPSRkEEIHRLRQAVEMVKLNLTIHQSAqvsvlltvegkdskepqngdselpkdqltpgdghhvn 342
Cdd:cd10235 204 LADYFLKK-HRLDFTSLSP-SELAALRKRAEQAKRQLSSQDSA------------------------------------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 343 rvfrpglsESKSGKSQVLFETEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFF 422
Cdd:cd10235 245 --------EIRLTYRGEELEIELTREEFEELCAPLLERLRQPIERALRDAGLKPSDIDAVILVGGATRMPLVRQLIARLF 316
|
410 420
....*....|....*....|....*..
gi 30089677 423 GKDPNTSVDPDLAVVTGVAIQAGIDGG 449
Cdd:cd10235 317 GRLPLSSLDPDEAVALGAAIQAALKAR 343
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
33-446 |
2.75e-89 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 285.57 E-value: 2.75e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 33 VIGIDLGTTYCSVGVFFPGTGKVkvIPDENGHISIPSMVSFT-DGDVYVGYESLELADSNPQNTIYDAKRFIGKIFTPEE 111
Cdd:PTZ00400 43 IVGIDLGTTNSCVAIMEGSQPKV--IENSEGMRTTPSVVAFTeDGQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEDA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 112 LEAEVGRYPFKVLH-RNGMAEFSVTSNEtiiVSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQAA 190
Cdd:PTZ00400 121 TKKEQKILPYKIVRaSNGDAWIEAQGKK---YSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 191 NLAGLKILRVINEPTAAAMAYGLHKVDVFYVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQHLYKE 270
Cdd:PTZ00400 198 KIAGLDVLRIINEPTAAALAFGMDKNDGKTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYLIAE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 271 IYQTYGF-LPSRKEEIHRLRQAVEMVKLNLTihQSAQVSVLLtvegkdskepqngdselpkdqltpgdghhvnrvfrPGL 349
Cdd:PTZ00400 278 FKKQQGIdLKKDKLALQRLREAAETAKIELS--SKTQTEINL-----------------------------------PFI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 350 SESKSGKSQVLFetEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPNTS 429
Cdd:PTZ00400 321 TADQSGPKHLQI--KLSRAKLEELTHDLLKKTIEPCEKCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIFGKEPSKG 398
|
410
....*....|....*..
gi 30089677 430 VDPDLAVVTGVAIQAGI 446
Cdd:PTZ00400 399 VNPDEAVAMGAAIQAGV 415
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
7-446 |
3.45e-85 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 275.02 E-value: 3.45e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 7 ILGSAVLTlllAGYLAQQYLPLPTPKVIGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFTDGDVYVGYESLE 86
Cdd:PTZ00186 6 VCGSAAAS---AARLARHESQKVQGDVIGVDLGTTYSCVATM--DGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 87 LADSNPQNTIYDAKRFIGKIFTPEELEAEVGRYPFKVLhRNGMAEFSVTSNETIIVSPEFVGSRLLLKLKEMAEEYLGMP 166
Cdd:PTZ00186 81 QAITNPQSTFYAVKRLIGRRFEDEHIQKDIKNVPYKIV-RAGNGDAWVQDGNGKQYSPSQIGAFVLEKMKETAENFLGHK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 167 VANAVISVPAEFDLQQRNSTIQAANLAGLKILRVINEPTAAAMAYGLHKVDVFYVLVIDLGGGTLDVSLLNKQGGMFLTR 246
Cdd:PTZ00186 160 VSNAVVTCPAYFNDAQRQATKDAGTIAGLNVIRVVNEPTAAALAYGMDKTKDSLIAVYDLGGGTFDISVLEIAGGVFEVK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 247 AMSGNNKLGGQDFNQRLLQHLYKEIYQTYGF-LPSRKEEIHRLRQAVEMVKLNLTIHQSAQVSVlltvegkdskepqngd 325
Cdd:PTZ00186 240 ATNGDTHLGGEDFDLALSDYILEEFRKTSGIdLSKERMALQRVREAAEKAKCELSSAMETEVNL---------------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 326 selpkdqltpgdghhvnrvfrPGLSESKSGKSQVlfETEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLV 405
Cdd:PTZ00186 304 ---------------------PFITANADGAQHI--QMHISRSKFEGITQRLIERSIAPCKQCMKDAGVELKEINDVVLV 360
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 30089677 406 GGSTRIPRIRQVIQEFFGKDPNTSVDPDLAVVTGVAIQAGI 446
Cdd:PTZ00186 361 GGMTRMPKVVEEVKKFFQKDPFRGVNPDEAVALGAATLGGV 401
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
34-446 |
1.02e-84 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 272.44 E-value: 1.02e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 34 IGIDLGTTYCSVGVFFpgTGKVKVIPDENGHISIPSMVSFTDGDVYVGYESLELADSNPQNTIYDAKRFIGKifTPEELE 113
Cdd:PRK05183 22 VGIDLGTTNSLVATVR--SGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKNTISSVKRFMGR--SLADIQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 114 AEVGRYPFK-VLHRNGMAEFSVTSNEtiiVSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQAANL 192
Cdd:PRK05183 98 QRYPHLPYQfVASENGMPLIRTAQGL---KSPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 193 AGLKILRVINEPTAAAMAYGLHKVDVFYVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQHLYKEIy 272
Cdd:PRK05183 175 AGLNVLRLLNEPTAAAIAYGLDSGQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWILEQA- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 273 qtyGFLPSRKEEIHR-LRQAVEMVKLNLTIHQSAQVSVlltvegkdskepqngdselpkdqltpgdghhvnrvfrpglse 351
Cdd:PRK05183 254 ---GLSPRLDPEDQRlLLDAARAAKEALSDADSVEVSV------------------------------------------ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 352 sksgksqVLFETEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPNTSVD 431
Cdd:PRK05183 289 -------ALWQGEITREQFNALIAPLVKRTLLACRRALRDAGVEADEVKEVVMVGGSTRVPLVREAVGEFFGRTPLTSID 361
|
410
....*....|....*
gi 30089677 432 PDLAVVTGVAIQAGI 446
Cdd:PRK05183 362 PDKVVAIGAAIQADI 376
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
33-446 |
8.45e-80 |
|
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: 252.55 E-value: 8.45e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 33 VIGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFTDGDVYVGYESLELADSNPQNTIYDAKRFIGKIFTPEEL 112
Cdd:cd10238 2 AFGVHFGNTNACVAVY--KDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 113 EAEVGRYPFKVLHRNGMAEFSVTSNETI-IVSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQAAN 191
Cdd:cd10238 80 QELKKESKCKIIEKDGKPGYEIELEEKKkLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 192 LAGLKILRVINEPTAAAMAYGLHKVD---VFYVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQHLY 268
Cdd:cd10238 160 KAGFNVLRVISEPSAAALAYGIGQDDpteNSNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 269 KEIYQTYGFLP-SRKEEIHRLRQAVEMVKLNLTIHQSAQVSVLLTVEGKDskepqngdselpkdqltpgdghhvnrvfrp 347
Cdd:cd10238 240 SEFKRQWKQDVrENKRAMAKLMNAAEVCKHVLSTLNTATCSVESLYDGMD------------------------------ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 348 glsesksgksqvlFETEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFF-GKDP 426
Cdd:cd10238 290 -------------FQCNVSRARFESLCSSLFQQCLEPIQEVLNSAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFpSAEV 356
|
410 420
....*....|....*....|
gi 30089677 427 NTSVDPDLAVVTGVAIQAGI 446
Cdd:cd10238 357 LSSIPPDEVIAIGAAKQAGL 376
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
34-444 |
1.22e-75 |
|
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa heat shock proteins family includes the human proteins, HSPA4 (also known as 70-kDa heat shock protein 4; APG-2; HS24/P52; hsp70 RY; HSPH2), HSPA4L (also known as 70-kDa heat shock protein 4-like; APG-1; HSPH3; OSP94), and HSPH1 (also known as heat shock 105kDa/110kDa protein 1; HSP105; HSP105A; HSP105B; NY-CO-25), Saccharomyces cerevisiae Sse1p, Sse2p and a sea urchin sperm receptor. They all belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466838 [Multi-domain] Cd Length: 377 Bit Score: 241.69 E-value: 1.22e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 34 IGIDLGTTYCSVGVffPGTGKVKVIPDENGHISIPSMVSFTDGDVYVGYESLELADSNPQNTIYDAKRFIGKIFTPEELE 113
Cdd:cd11732 1 VGIDFGNQNSVVAA--ARRGGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 114 AEVGRYPFK-VLHRNGMAEFSVT-SNETIIVSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQAAN 191
Cdd:cd11732 79 KEIKLLPFKlVELEDGKVGIEVSyNGEEVVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 192 LAGLKILRVINEPTAAAMAYGLHKVDVF-------YVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLL 264
Cdd:cd11732 159 IAGLNCLRLINETTAAALDYGIYKSDLLeseekprIVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 265 QHLYKEIYQTYGFLP-SRKEEIHRLRQAVEMVKLNLTIHQSAQVSVLLTVEGKDskepqngdselpkdqltpgdghhvnr 343
Cdd:cd11732 239 EHFAEEFKKKYKIDPlENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEDID-------------------------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 344 vfrpglsesksgksqvlFETEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFFG 423
Cdd:cd11732 293 -----------------FSGQIKREEFEELIQPLLARLEAPIKKALAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVFG 355
|
410 420
....*....|....*....|.
gi 30089677 424 KDPNTSVDPDLAVVTGVAIQA 444
Cdd:cd11732 356 KDLSTTLNADEAVARGCALQA 376
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
32-449 |
1.29e-74 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 247.46 E-value: 1.29e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 32 KVIGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFT-DGDVYVGYESLELADSNPQNTIYDAKRFIGKIFTpe 110
Cdd:PLN03184 40 KVVGIDLGTTNSAVAAM--EGGKPTIVTNAEGQRTTPSVVAYTkNGDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMS-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 111 ELEAEVGRYPFKVLH-RNGMAEFSvTSNETIIVSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQA 189
Cdd:PLN03184 116 EVDEESKQVSYRVVRdENGNVKLD-CPAIGKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 190 ANLAGLKILRVINEPTAAAMAYGLHKVDVFYVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQHLYK 269
Cdd:PLN03184 195 GRIAGLEVLRIINEPTAASLAYGFEKKSNETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLAS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 270 EIYQTYGF-LPSRKEEIHRLRQAVEMVKLNLTIHQSAQVS---VLLTVEGkdskepqngdselPKdqltpgdghHVnrvf 345
Cdd:PLN03184 275 NFKKDEGIdLLKDKQALQRLTEAAEKAKIELSSLTQTSISlpfITATADG-------------PK---------HI---- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 346 rpglsesksgksqvlfETEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFFGKD 425
Cdd:PLN03184 329 ----------------DTTLTRAKFEELCSDLLDRCKTPVENALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKLTGKD 392
|
410 420
....*....|....*....|....
gi 30089677 426 PNTSVDPDLAVVTGVAIQAGIDGG 449
Cdd:PLN03184 393 PNVTVNPDEVVALGAAVQAGVLAG 416
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
33-443 |
7.59e-71 |
|
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: 229.89 E-value: 7.59e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 33 VIGIDLGTTYCSVGVffPGTGKVKVIPDENGHISIPSMVSFTDGDVYVGYESLELADSNPQNTIYDAKRFIGKIFTPEEL 112
Cdd:cd24095 3 VVGIDFGNENCVVAV--ARKGGIDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 113 EAEVGRYPFKVLH-RNGMAEFSVT-SNETIIVSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQAA 190
Cdd:cd24095 81 QRDLKLFPFKVTEgPDGEIGINVNyLGEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 191 NLAGLKILRVINEPTAAAMAYGLHKVDVF-----YVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQ 265
Cdd:cd24095 161 QIAGLNCLRLMNETTATALAYGIYKTDLPetdptNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 266 HLYKEIYQTYGF-LPSRKEEIHRLRQAVEMVKLNLTIHQSAQVSVLLTVEGKDSKepqngdselpkdqltpgdghhvnrv 344
Cdd:cd24095 241 HFAAEFKEKYKIdVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMEDKDVK------------------------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 345 frpglsesksgksqvlfeTEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFFGK 424
Cdd:cd24095 296 ------------------GMITREEFEELAAPLLERLLEPLEKALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFFGK 357
|
410
....*....|....*....
gi 30089677 425 DPNTSVDPDLAVVTGVAIQ 443
Cdd:cd24095 358 EPSRTMNASECVARGCALQ 376
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
33-444 |
2.93e-65 |
|
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: 213.90 E-value: 2.93e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 33 VIGIDLGTTYCSVGVFFPGTgKVKVIPDENGHISIPSMVSFTDGDVYVGYESLELADSNPQNTIYDAKRFIGkiFTPEEL 112
Cdd:cd10230 2 VLGIDLGSEFIKVALVKPGV-PFEIVLNEESKRKTPSAVAFRNGERLFGDDALALATRFPENTFSYLKDLLG--YSVEEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 113 eaevgrypfkvlhrNGMaefsvtsnetiivspefvgsrLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQAANL 192
Cdd:cd10230 79 --------------VAM---------------------ILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEI 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 193 AGLKILRVINEPTAAAMAYGLHKV----DVFYVLVIDLGGGTLDVSLL------------NKQGGMFLTRAMSGNNKLGG 256
Cdd:cd10230 124 AGLNVLSLINDNTAAALNYGIDRRfennEPQNVLFYDMGASSTSATVVefssvkekdkgkNKTVPQVEVLGVGWDRTLGG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 257 QDFNQRLLQHLYKEIYQTYGFLPSRKEE---IHRLRQAVEMVKLNLTIHQSAQVSVLLTVEGKDskepqngdselpkdql 333
Cdd:cd10230 204 LEFDLRLADHLADEFNEKHKKDKDVRTNpraMAKLLKEANRVKEVLSANTEAPASIESLYDDID---------------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 334 tpgdghhvnrvfrpglsesksgksqvlFETEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPR 413
Cdd:cd10230 268 ---------------------------FRTKITREEFEELCADLFERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPK 320
|
410 420 430
....*....|....*....|....*....|..
gi 30089677 414 IRQVIQEFFGKDP-NTSVDPDLAVVTGVAIQA 444
Cdd:cd10230 321 VQEALKEALGRKElGKHLNADEAAALGAAFYA 352
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
34-444 |
3.00e-65 |
|
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: 214.83 E-value: 3.00e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 34 IGIDLGTTYCSVGVffPGTGKVKVIPDENGHISIPSMVSFTDGDVYVGYESLELADSNPQNTIYDAKRFIGKIFTPEELE 113
Cdd:cd10228 1 VGFDFGNLSCYIAV--ARAGGIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 114 AEVGRYPFKVLHR-NGMAEFSVT-SNETIIVSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQAAN 191
Cdd:cd10228 79 KELKHLPYKVVKLpNGSVGIKVQyLGEEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 192 LAGLKILRVINEPTAAAMAYGLHKVDVFY-------VLVIDLGGGTLDVSL--LNKQGGMFLTRAMSGNnkLGGQDFNQR 262
Cdd:cd10228 159 IAGLNCLRLLNDTTAVALAYGIYKQDLPAeeekprnVVFVDMGHSSLQVSVcaFNKGKLKVLATAADPN--LGGRDFDEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 263 LLQHLYKEIYQTYG--FLPSRKEEIhRLRQAVEMVKLNLtihqSAQVSVL-LTVEgkdskepqngdselpkdqltpgdgh 339
Cdd:cd10228 237 LVEHFAEEFKTKYKidVKSKPRALL-RLLTECEKLKKLM----SANATELpLNIE------------------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 340 hvnrvfrpGLSESK--SGKsqvlfeteVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQV 417
Cdd:cd10228 287 --------CFMDDKdvSGK--------MKRAEFEELCAPLFARVEVPLRSALADSKLKPEDIHSVEIVGGSTRIPAIKEI 350
|
410 420
....*....|....*....|....*..
gi 30089677 418 IQEFFGKDPNTSVDPDLAVVTGVAIQA 444
Cdd:cd10228 351 IKKVFGKEPSTTLNQDEAVARGCALQC 377
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
33-446 |
6.44e-65 |
|
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: 212.99 E-value: 6.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 33 VIGIDLGTTYCSVGvFFPGTGKVKVIPDENGHISIPSMVSFTDGDVYVGYESLELADSNPQNTIYDAKRFIGK-IFTPEE 111
Cdd:cd10232 2 VIGISFGNSNSSIA-IINKDGRAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPKNTVANFRDLLGTtTLTVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 112 leaevgrypfkvlhrngmaefsvtsnetiivspefVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQAAN 191
Cdd:cd10232 81 -----------------------------------VTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 192 LAGLKILRVINEPTAAAMAYGLHKVDVFY------VLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQ 265
Cdd:cd10232 126 AAGLEVLQLIPEPAAAALAYDLRAETSGDtikdktVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 266 HLYKEIYQTYGFLPSR-KEEIHRLRQAVEMVKLNLTIHQSAQVSVLLTVEGKDskepqngdselpkdqltpgdghhvnrv 344
Cdd:cd10232 206 HFAKEFKKKTKTDPRKnARSLAKLRNAAEITKRALSQGTSAPCSVESLADGID--------------------------- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 345 frpglsesksgksqvlFETEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFFGK 424
Cdd:cd10232 259 ----------------FHSSINRTRYELLASKVFQQFADLVTDAIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLFPE 322
|
410 420
....*....|....*....|....*.
gi 30089677 425 D----PNTSVDPDLAVVTGVAIQAGI 446
Cdd:cd10232 323 StiirAPTQINPDELIARGAALQASL 348
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
34-446 |
2.60e-56 |
|
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: 191.43 E-value: 2.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 34 IGIDLGTTYCSVGVffPGTGKVKVIPDENGHISIPSMVSFTDGDVYVGYESLELADSNPQNTIYDAKRFIGKIFTPEELE 113
Cdd:cd24094 1 VGLDLGNLNSVIAV--ARNRGIDIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 114 AEVGRYPFKVLHRNGMAEFSVT-SNETIIVSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQAANL 192
Cdd:cd24094 79 EEEKYFTAKLVDANGEVGAEVNyLGEKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 193 AGLKILRVINEPTAAAMAYGLHKVDV-------FYVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQ 265
Cdd:cd24094 159 AGLNPLRLMNDTTAAALGYGITKTDLpepeekpRIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 266 HLYKEIYQTYGF-LPSRKEEIHRLRQAVEMVKLNLTIHQSAQVSVLLTVEGKDSKepqngdselpkdqltpgdghhvnrv 344
Cdd:cd24094 239 HFADEFKEKYKIdVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVS------------------------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 345 frpglsesksgksqvlfeTEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFFGK 424
Cdd:cd24094 294 ------------------SMLKREEFEELIAPLLERVTAPLEKALAQAGLTKDEIDFVELVGGTTRVPALKESISAFFGK 355
|
410 420
....*....|....*....|..
gi 30089677 425 DPNTSVDPDLAVVTGVAIQAGI 446
Cdd:cd24094 356 PLSTTLNQDEAVARGAAFACAI 377
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
33-446 |
1.79e-52 |
|
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: 181.29 E-value: 1.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 33 VIGIDLGTTYCSVGVffPGTGKVKVIPDENGHISIPSMVSFTDGDVYVGYESLELADSNPQNTIYDAKRFIGKIFTPEEL 112
Cdd:cd11737 2 VVGFDLGFQSCYVAV--ARAGGIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 113 EAEVGRYPFKVLHR-NGMAEFSVT-SNETIIVSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQAA 190
Cdd:cd11737 80 QAEKPSLAYELVQLpTGTTGIKVMyMEEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 191 NLAGLKILRVINEPTAAAMAYGLHKVDV-------FYVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRL 263
Cdd:cd11737 160 QIAGLNCLRLMNETTAVALAYGIYKQDLpapeekpRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 264 LQHLYKEIYQTYGF-LPSRKEEIHRLRQAVEMVKLNLtihqSAQVSVLltvegkdskePQNGDSelpkdqltpgdghHVN 342
Cdd:cd11737 240 VNHFCEEFGKKYKLdIKSKIRALLRLFQECEKLKKLM----SANASDL----------PLNIEC-------------FMN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 343 RVfrpglseSKSGKsqvlfeteVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFF 422
Cdd:cd11737 293 DI-------DVSGT--------MNRGQFEEMCADLLARVEPPLRSVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFF 357
|
410 420
....*....|....*....|....
gi 30089677 423 GKDPNTSVDPDLAVVTGVAIQAGI 446
Cdd:cd11737 358 GKEVSTTLNADEAVARGCALQCAI 381
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
33-444 |
7.71e-47 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 170.81 E-value: 7.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 33 VIGIDLGTTYCSVGVffPGTGKVKVIPDENGHISIPSMVSFTDGDVYVGyesleladSNpqNTIYDAKRFIGK----IFT 108
Cdd:PRK01433 21 AVGIDFGTTNSLIAI--ATNRKVKVIKSIDDKELIPTTIDFTSNNFTIG--------NN--KGLRSIKRLFGKtlkeILN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 109 PEELEAEVGRYpfkvlhrngmaeFSVTSNETII------VSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQ 182
Cdd:PRK01433 89 TPALFSLVKDY------------LDVNSSELKLnfankqLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 183 RNSTIQAANLAGLKILRVINEPTAAAMAYGLHKVDVFYVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQR 262
Cdd:PRK01433 157 RGEVMLAAKIAGFEVLRLIAEPTAAAYAYGLNKNQKGCYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 263 LLQHLYKeiyqtygflpsrkeeihrlrqavemvKLNLtihqsaqvsvlltvegkdskePQNGDS----ELPKDQLTPGDG 338
Cdd:PRK01433 237 ITQYLCN--------------------------KFDL---------------------PNSIDTlqlaKKAKETLTYKDS 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 339 HHVNRVfrpglsesksgksqvlfetEVSRKLFDALNEDLFQKILVPIQQVLKEGllDKTEIDEVVLVGGSTRIPRIRQVI 418
Cdd:PRK01433 270 FNNDNI-------------------SINKQTLEQLILPLVERTINIAQECLEQA--GNPNIDGVILVGGATRIPLIKDEL 328
|
410 420
....*....|....*....|....*.
gi 30089677 419 QEFFGKDPNTSVDPDLAVVTGVAIQA 444
Cdd:PRK01433 329 YKAFKVDILSDIDPDKAVVWGAALQA 354
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
33-443 |
1.41e-45 |
|
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar proteins; HSPH1, also called heat shock protein 105 kDa, antigen NY-CO-25, heat shock 110 kDa protein, acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release. It prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. It inhibits HSPA8/HSC70 ATPase and chaperone activities. HSPH1 belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466845 [Multi-domain] Cd Length: 380 Bit Score: 163.11 E-value: 1.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 33 VIGIDLGTTYCSVGVffPGTGKVKVIPDENGHISIPSMVSFTDGDVYVGYESLELADSNPQNTIYDAKRFIGKIFTPEEL 112
Cdd:cd11739 2 VVGFDVGFQNCYIAV--ARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 113 EAEVGRYPFK-VLHRNGMAEFSVTS-NETIIVSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQAA 190
Cdd:cd11739 80 QKEKENLSYDlVPLKNGGVGVKVMYlDEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 191 NLAGLKILRVINEPTAAAMAYGLHKVDV-------FYVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRL 263
Cdd:cd11739 160 QIVGLNCLRLMNDMTAVALNYGIYKQDLpapdekpRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 264 LQHLYKEIYQTYGFLP-SRKEEIHRLRQAVEMVKlnltihqsaqvsvlltvegkdsKEPQNGDSELPKDQLTPGDGHHVn 342
Cdd:cd11739 240 VEHFCAEFKTKYKLDVkSKIRALLRLYQECEKLK----------------------KLMSSNSTDLPLNIECFMNDKDV- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 343 rvfrpglseskSGKsqvlfeteVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFF 422
Cdd:cd11739 297 -----------SGK--------MNRSQFEELCADLLQRIEVPLYSLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFF 357
|
410 420
....*....|....*....|.
gi 30089677 423 GKDPNTSVDPDLAVVTGVAIQ 443
Cdd:cd11739 358 GKDVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
33-446 |
4.56e-45 |
|
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: 161.62 E-value: 4.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 33 VIGIDLGTTYCSVGVffPGTGKVKVIPDENGHISIPSMVSFTDGDVYVGYESLELADSNPQNTIYDAKRFIGKIFTPEEL 112
Cdd:cd11738 2 VVGIDVGFQNCYIAV--ARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 113 EAEVGRYPFKvLHR--NGMAEFSVTS-NETIIVSPEFVGSRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQA 189
Cdd:cd11738 80 QAEKIKLPYE-LQKmpNGSTGVKVRYlDEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 190 ANLAGLKILRVINEPTAAAMAYGLHKVDV-------FYVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQR 262
Cdd:cd11738 159 AQIAGLNCLRLMNETTAVALAYGIYKQDLpaleekpRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 263 LLQHLYKEIYQTYgflpsrkeeihrlrqavemvKLNLTIHQSAQVSVLLTVEgKDSKEPQNGDSELPKDQltpgdghhvn 342
Cdd:cd11738 239 LVDYFCEEFKTKY--------------------KLNVKENIRALLRLYQECE-KLKKLMSANASDLPLNI---------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 343 RVFRPGLSESksgksqvlfeTEVSRKLFDALNEDLFQKILVPIQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFF 422
Cdd:cd11738 288 ECFMNDIDVS----------SKMNRAQFEELCASLLARVEPPLKAVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFF 357
|
410 420
....*....|....*....|....
gi 30089677 423 GKDPNTSVDPDLAVVTGVAIQAGI 446
Cdd:cd11738 358 GKDISTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
34-442 |
6.12e-45 |
|
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: 159.96 E-value: 6.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 34 IGIDLGTTYCSVGVFFPGTGKVKVI-------PDENGHISIPSMVsftdgDVYVGYesleladsnpqntiydakrfigki 106
Cdd:cd10170 1 VGIDFGTTYSGVAYALLGPGEPPLVvlqlpwpGGDGGSSKVPSVL-----EVVADF------------------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 107 ftpeeleaevgrypFKVLHRNGMAEFSVTSNEtiivspefvgsrlllklkemaeeyLGMPVANAVISVPAEFDLQQRNST 186
Cdd:cd10170 52 --------------LRALLEHAKAELGDRIWE------------------------LEKAPIEVVITVPAGWSDAAREAL 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 187 IQAANLAGLK----ILRVINEPTAAAMAYGLHKVDVFY------VLVIDLGGGTLDVSLLNKQGGMFL---TRAMSGNNK 253
Cdd:cd10170 94 REAARAAGFGsdsdNVRLVSEPEAAALYALEDKGDLLPlkpgdvVLVCDAGGGTVDLSLYEVTSGSPLlleEVAPGGGAL 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 254 LGGQDFNQRLLQHLYKEIYQTYGFLP-SRKEEIHRLRQAVEMVKLNLTIHQSaqvsvlltvegkdskepqngdselpkdq 332
Cdd:cd10170 174 LGGTDIDEAFEKLLREKLGDKGKDLGrSDADALAKLLREFEEAKKRFSGGEE---------------------------- 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 333 ltpgDGHHVNRVFRPGLSEsksgksqvLFETEVSRKLFDALNEDLFQKILVPIQQVLKEGLL--DKTEIDEVVLVGGSTR 410
Cdd:cd10170 226 ----DERLVPSLLGGGLPE--------LGLEKGTLLLTEEEIRDLFDPVIDKILELIEEQLEakSGTPPDAVVLVGGFSR 293
|
410 420 430
....*....|....*....|....*....|....*.
gi 30089677 411 IPRIRQVIQEFFGKDP----NTSVDPDLAVVTGVAI 442
Cdd:cd10170 294 SPYLRERLRERFGSAGiiivLRSDDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
34-441 |
3.47e-24 |
|
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: 104.28 E-value: 3.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 34 IGIDLGTTYCSVGVFFpgTGKVKVIPDENGHISIPSMVSFTDgdvyvgyesleladsnpqntiYDAKRFIGKIFTPEELE 113
Cdd:cd10231 1 IGLDFGTSNSSLAVAD--DGKTDLVPFEGDSPTLPSLLYFPR---------------------REEEGAESIYFGNDAID 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 114 A-----EVGRY---PFKVLHRNGMAEFSVTSNETIIVspEFVGSrLLLKLKEMAEEYLGMPVANAVISVPAEF------- 178
Cdd:cd10231 58 AylndpEEGRLiksVKSFLGSSLFDETTIFGRRYPFE--DLVAA-ILRHLKRRAERQLGEEIDSVVVGRPVHFsgvgaed 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 179 DLQQRNSTIQAANLAGLKILRVINEPTAAAMAY--GLHKVDVfyVLVIDLGGGTLDVSLLNKQGGMFLTR----AMSGnN 252
Cdd:cd10231 135 DAQAESRLRDAARRAGFRNVEFQYEPIAAALDYeqRLDREEL--VLVVDFGGGTSDFSVLRLGPNRTDRRadilATSG-V 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 253 KLGGQDFNQRLLQHL------YKEIYQTYG---FLP-------SRKEEIHRLRQAVEMVKLNLTIHQSAQVSVLLTVEgk 316
Cdd:cd10231 212 GIGGDDFDRELALKKvmphlgRGSTYVSGDkglPVPawlyadlSNWHAISLLYTKKTLRLLLDLRRDAADPEKIERLL-- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 317 dskepqngdsELPKDQLtpgdGHHVNRVFRpglsESK---SGKSQVLFE---------TEVSRKLFDALNEDLFQKILVP 384
Cdd:cd10231 290 ----------SLVEDQL----GHRLFRAVE----QAKialSSADEATLSfdfieisikVTITRDEFETAIAFPLARILEA 351
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 30089677 385 IQQVLKEGLLDKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPNTSVDPDLAVVTGVA 441
Cdd:cd10231 352 LERTLNDAGVKPSDVDRVFLTGGSSQSPAVRQALASLFGQARLVEGDEFGSVAAGLA 408
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
34-442 |
3.56e-16 |
|
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: 79.05 E-value: 3.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 34 IGIDLGTTYCSVGVffPGTGKVkvipdenghISIPSMVSFtdgdvyvgyeslelaDSNPQNTIY---DAKRFIGKifTPE 110
Cdd:cd10225 2 IGIDLGTANTLVYV--KGKGIV---------LNEPSVVAV---------------DKNTGKVLAvgeEAKKMLGR--TPG 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 111 ELEAEvgrYPFkvlhRNG-MAEFSVTsnetiivspefvgsRLLLK-LKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQ 188
Cdd:cd10225 54 NIVAI---RPL----RDGvIADFEAT--------------EAMLRyFIRKAHRRRGFLRPRVVIGVPSGITEVERRAVKE 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 189 AANLAGLKILRVINEPTAAAMAYGLhkvDVFY---VLVIDLGGGTLDVSLLNkQGGMFLTRAMsgnnKLGGQDFNQRLLQ 265
Cdd:cd10225 113 AAEHAGAREVYLIEEPMAAAIGAGL---PIEEprgSMVVDIGGGTTEIAVIS-LGGIVTSRSV----RVAGDEMDEAIIN 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 266 HLYKEiyqtYGFLPSRkeeihrlRQAvEMVKLNLtihqsaqVSVL-------LTVEGKDSkepqngDSELPKdqltpgdg 338
Cdd:cd10225 185 YVRRK----YNLLIGE-------RTA-ERIKIEI-------GSAYpldeelsMEVRGRDL------VTGLPR-------- 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 339 hhvnrvfrpglsesksgksqvlfETEV-SRKLFDALNEdLFQKILVPIQQVLKE-------GLLDKteidEVVLVGGSTR 410
Cdd:cd10225 232 -----------------------TIEItSEEVREALEE-PVNAIVEAVRSTLERtppelaaDIVDR----GIVLTGGGAL 283
|
410 420 430
....*....|....*....|....*....|..
gi 30089677 411 IPRIRQVIQEFFGKDPNTSVDPDLAVVTGVAI 442
Cdd:cd10225 284 LRGLDELLREETGLPVHVADDPLTCVAKGAGK 315
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
32-442 |
6.50e-14 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 72.47 E-value: 6.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 32 KVIGIDLGTTycSVGVFFPGTGkvkVIPDEnghisiPSMVSF-TDGD--VYVGYEsleladsnpqntiydAKRFIGKifT 108
Cdd:PRK13930 9 KDIGIDLGTA--NTLVYVKGKG---IVLNE------PSVVAIdTKTGkvLAVGEE---------------AKEMLGR--T 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 109 PEELEAevgRYPFkvlhRNG-MAEFSVTsnETIIvspefvgsRLLLKlkeMAEEYLGMPVANAVISVPAEFDLQQRNSTI 187
Cdd:PRK13930 61 PGNIEA---IRPL----KDGvIADFEAT--EAML--------RYFIK---KARGRRFFRKPRIVICVPSGITEVERRAVR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 188 QAANLAGLKILRVINEPTAAAMAYGLhkvDVFYV---LVIDLGGGTLDV---SLlnkqGGMFLTRAMsgnnKLGGQDFNQ 261
Cdd:PRK13930 121 EAAEHAGAREVYLIEEPMAAAIGAGL---PVTEPvgnMVVDIGGGTTEVaviSL----GGIVYSESI----RVAGDEMDE 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 262 RLLQHLykeiyqtygflpsRKEeiHRLR---QAVEMVKLNL-TIHQSAQVSVlLTVEGKDSkepqngDSELPkdqltpgd 337
Cdd:PRK13930 190 AIVQYV-------------RRK--YNLLigeRTAEEIKIEIgSAYPLDEEES-MEVRGRDL------VTGLP-------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 338 ghhvnrvfrpglsesksgKSQVLFETEVSrklfDALNEDLfQKILVPIQQVLKE-------GLLDKTeideVVLVGGSTR 410
Cdd:PRK13930 240 ------------------KTIEISSEEVR----EALAEPL-QQIVEAVKSVLEKtppelaaDIIDRG----IVLTGGGAL 292
|
410 420 430
....*....|....*....|....*....|..
gi 30089677 411 IPRIRQVIQEFFGKDPNTSVDPDLAVVTGVAI 442
Cdd:PRK13930 293 LRGLDKLLSEETGLPVHIAEDPLTCVARGTGK 324
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
33-442 |
8.02e-14 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar proteins; The family includes heat shock 70 kDa proteins HSPA12A and HSPA12B. HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. Both HSPA12A and HSPA12B belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A and HSPA12B.
Pssm-ID: 466827 [Multi-domain] Cd Length: 372 Bit Score: 72.70 E-value: 8.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 33 VIGIDLGTTYCSVG-VFFPGTGKVKVI----PDENGHIS--IPSMVSFTDGDVYV--GYESLE----LADSNPQNTIYDA 99
Cdd:cd10229 2 VVAIDFGTTYSGYAySFITDPGDIHTMynwwGAPTGVSSpkTPTCLLLNPDGEFHsfGYEAREkysdLAEDEEHQWLYFF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 100 KRFIGKIFTPEELEAEvgrypfKVLHRNGmaefSVTSNETIIV-SPEFVGSRLLLKLKEMAEEYLgmPVANA--VISVPA 176
Cdd:cd10229 82 KFKMMLLSEKELTRDT------KVKAVNG----KSMPALEVFAeALRYLKDHALKELRDRSGSSL--DEDDIrwVLTVPA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 177 EFDLQQRNSTIQAANLAGLKI------LRVINEPTAAAMAYG-LHKVDVFYV-------LVIDLGGGTLDVS---LLNKQ 239
Cdd:cd10229 150 IWSDAAKQFMREAAVKAGLISeenseqLIIALEPEAAALYCQkLLAEGEEKElkpgdkyLVVDCGGGTVDITvheVLEDG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 240 GGMFLTRAmSGNNkLGGQDFNQRLLQHLYK----EIYQtyGFLPSRKEEIHRLRQAVEMVKLNLTIhqsaqvsvlltveg 315
Cdd:cd10229 230 KLEELLKA-SGGP-WGSTSVDEEFEELLEEifgdDFME--AFKQKYPSDYLDLLQAFERKKRSFKL-------------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 316 kdskepqngdsELPKDQLtpgdghhvnrvfrpglsesksgksqvlfetevsRKLFDalneDLFQKILVPIQQVLKEGLLD 395
Cdd:cd10229 292 -----------RLSPELM---------------------------------KSLFD----PVVKKIIEHIKELLEKPELK 323
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 30089677 396 KteIDEVVLVGGSTRIPRIRQVIQEFFGKDPN--TSVDPDLAVVTGVAI 442
Cdd:cd10229 324 G--VDYIFLVGGFAESPYLQKAVKEAFSTKVKiiIPPEPGLAVVKGAVL 370
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
34-442 |
2.34e-09 |
|
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: 58.55 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 34 IGIDLGTTycSVGVFFPGTGKVkvipdenghISIPSMVSF--TDGDVY-VGYEsleladsnpqntiydAKRFIGKifTPE 110
Cdd:COG1077 10 IGIDLGTA--NTLVYVKGKGIV---------LNEPSVVAIdkKTGKVLaVGEE---------------AKEMLGR--TPG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 111 ELEAevgRYPFKvlhrNG-MAEFSVTsnETIIvspefvgsRLLLKlKEMAEEYLGMPvaNAVISVPAEF-DLQQRnSTIQ 188
Cdd:COG1077 62 NIVA---IRPLK----DGvIADFEVT--EAML--------KYFIK-KVHGRRSFFRP--RVVICVPSGItEVERR-AVRD 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 189 AANLAGLKILRVINEPTAAAMAYGLhkvDVFY---VLVIDLGGGTLDV---SLlnkqGGMFLTRAMsgnnKLGGQDFNQR 262
Cdd:COG1077 121 AAEQAGAREVYLIEEPMAAAIGAGL---PIEEptgNMVVDIGGGTTEVaviSL----GGIVVSRSI----RVAGDELDEA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 263 LLQHLYKEiyqtYGFLPSRkeeihrlRQAvEMVKLNL-TIHQSAQVSVlLTVEGKDSkepqngDSELPKdqltpgdghhv 341
Cdd:COG1077 190 IIQYVRKK----YNLLIGE-------RTA-EEIKIEIgSAYPLEEELT-MEVRGRDL------VTGLPK----------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 342 nrvfrpglsesksgksqvlfETEVSRK-LFDALnEDLFQKILVPIQQVLKE-------GLLDKTeideVVLVGGSTRIPR 413
Cdd:COG1077 240 --------------------TITITSEeIREAL-EEPLNAIVEAIKSVLEKtppelaaDIVDRG----IVLTGGGALLRG 294
|
410 420
....*....|....*....|....*....
gi 30089677 414 IRQVIQEFFGKDPNTSVDPDLAVVTGVAI 442
Cdd:COG1077 295 LDKLLSEETGLPVHVAEDPLTCVARGTGK 323
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
149-427 |
3.87e-09 |
|
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466854 [Multi-domain] Cd Length: 282 Bit Score: 57.69 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 149 SRLLLKLKEMAEEYLGMPVANAVISVPaefdlQQRNSTIQAANLAGLKILRVINEPTAAAmaYGLHKVDV--FYVLVIDL 226
Cdd:cd24004 49 AESIKELLKELEEKLGSKLKDVVIAIA-----KVVESLLNVLEKAGLEPVGLTLEPFAAA--NLLIPYDMrdLNIALVDI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 227 GGGTLDVSLLNKqGGMFLTRamsgNNKLGGQDFNQRLLQHlykeiyqtygFLPSRKEeihrlrqaVEMVKLNLTIhqsaq 306
Cdd:cd24004 122 GAGTTDIALIRN-GGIEAYR----MVPLGGDDFTKAIAEG----------FLISFEE--------AEKIKRTYGI----- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 307 vsvlltvegkdskepqnGDSELPKDQLTPG-DGHHVNRVFRPGLSesksgksqvlfetEVSRKLFDALnEDLFQKILVPi 385
Cdd:cd24004 174 -----------------FLLIEAKDQLGFTiNKKEVYDIIKPVLE-------------ELASGIANAI-EEYNGKFKLP- 221
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 30089677 386 qqvlkeglldkteiDEVVLVGGSTRIPRIRQVIQEFFGKDPN 427
Cdd:cd24004 222 --------------DAVYLVGGGSKLPGLNEALAEKLGLPVE 249
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
123-254 |
6.90e-08 |
|
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity.
Pssm-ID: 466897 [Multi-domain] Cd Length: 241 Bit Score: 53.42 E-value: 6.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 123 VLHRNGMA-----EFSVTSNETIIVspEFVG-SRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQAANLAGLK 196
Cdd:cd24047 16 VVDEEGQPvagalERADVVRDGIVV--DYIGaIRIVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLE 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30089677 197 ILRVINEPTAAAMAYGLHKvdvfyVLVIDLGGGTLDVSLL-NKQ---------GGMFLTRAMSGNNKL 254
Cdd:cd24047 94 VSNVVDEPTAANAVLGIRD-----GAVVDIGGGTTGIAVLkDGKvvytadeptGGTHLSLVLAGNYGI 156
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
34-236 |
2.69e-07 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 52.56 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 34 IGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFTDGD-----VYVGYESLELADSNpQNTIYDAKRF-----I 103
Cdd:PRK11678 3 IGFDYGTANCSVAVM--RDGKPRLLPLENDSTYLPSTLCAPTREavsewLYRHLDVPAYDDER-QALLRRAIRYnreedI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 104 GkiFTPEEL---EAEVGRY------------PFKVLHRNGMAEFSVTSNETIIVSpefvgsrLLLKLKEMAEEYLGMPVA 168
Cdd:PRK11678 80 D--VTAQSVffgLAALAQYledpeevyfvksPKSFLGASGLKPQQVALFEDLVCA-------MMLHIKQQAEAQLQAAIT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30089677 169 NAVISVPAEF--------DLQQRNSTIQAANLAGLKILRVINEPTAAAMAY--GLHKVDVfyVLVIDLGGGTLDVSLL 236
Cdd:PRK11678 151 QAVIGRPVNFqglggeeaNRQAEGILERAAKRAGFKDVEFQFEPVAAGLDFeaTLTEEKR--VLVVDIGGGTTDCSML 226
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
34-270 |
3.35e-07 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 52.21 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 34 IGIDLGTTycSVGVFFPGTGkvkVIPDEnghisiPSMVSF---TDGDVYVGYEsleladsnpqntiydAKRFIGKifTPE 110
Cdd:PRK13928 6 IGIDLGTA--NVLVYVKGKG---IVLNE------PSVVAIdknTNKVLAVGEE---------------ARRMVGR--TPG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 111 ELEAevgrypFKVLhRNG-MAEFSVTSnetiIVSPEFV----GSRLLLKLKEMaeeylgmpvanavISVPAEF-DLQQRn 184
Cdd:PRK13928 58 NIVA------IRPL-RDGvIADYDVTE----KMLKYFInkacGKRFFSKPRIM-------------ICIPTGItSVEKR- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 185 STIQAANLAGLKILRVINEPTAAAMAYGLhkvDVFYV---LVIDLGGGTLDVSLLNkQGGMFLTRAMsgnnKLGGQDFNQ 261
Cdd:PRK13928 113 AVREAAEQAGAKKVYLIEEPLAAAIGAGL---DISQPsgnMVVDIGGGTTDIAVLS-LGGIVTSSSI----KVAGDKFDE 184
|
....*....
gi 30089677 262 RLLQHLYKE 270
Cdd:PRK13928 185 AIIRYIRKK 193
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
34-270 |
8.26e-07 |
|
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: 50.63 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 34 IGIDLGTtyCSVGVFFPGTGKVkvipdenghISIPSMVSF--TDGDVY-VGYEsleladsnpqntiydAKRFIGKifTPE 110
Cdd:pfam06723 4 IGIDLGT--ANTLVYVKGKGIV---------LNEPSVVAIntKTKKVLaVGNE---------------AKKMLGR--TPG 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 111 ELEAevgRYPFKvlhrNG-MAEFSVTSnetiivspefvgsRLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQA 189
Cdd:pfam06723 56 NIVA---VRPLK----DGvIADFEVTE-------------AMLKYFIKKVHGRRSFSKPRVVICVPSGITEVERRAVKEA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 190 ANLAGLKILRVINEPTAAAMAYGLhkvDVFYV---LVIDLGGGTLDVSLLNkQGGMFLTRAMsgnnKLGGQDFNQRLLQH 266
Cdd:pfam06723 116 AKNAGAREVFLIEEPMAAAIGAGL---PVEEPtgnMVVDIGGGTTEVAVIS-LGGIVTSKSV----RVAGDEFDEAIIKY 187
|
....
gi 30089677 267 LYKE 270
Cdd:pfam06723 188 IRKK 191
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
146-240 |
2.00e-06 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 49.06 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 146 FVGS-RLLLKLKEMAEEYLGMPVANAVISVPAEFDLQQRNSTIQAANLAGLKILRVINEPTAAAMAYGLHKvdvfyVLVI 224
Cdd:PRK15080 66 FIGAvTIVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGIDN-----GAVV 140
|
90
....*....|....*.
gi 30089677 225 DLGGGTLDVSLLnKQG 240
Cdd:PRK15080 141 DIGGGTTGISIL-KDG 155
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
98-270 |
6.87e-05 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 44.90 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 98 DAKRFIGKifTPEELEAevgrypFKVLHRNGMAEFSVTSNetiivspefvgsrLLLKLKEMAEEYLGMPV--ANAVISVP 175
Cdd:PRK13929 48 EAKNMIGK--TPGKIVA------VRPMKDGVIADYDMTTD-------------LLKQIMKKAGKNIGMTFrkPNVVVCTP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 176 AEFDLQQRNSTIQAANLAGLKILRVINEPTAAAMAYGLHKVDVFYVLVIDLGGGTLDVSLLNKQGgmfltrAMSGNN-KL 254
Cdd:PRK13929 107 SGSTAVERRAISDAVKNCGAKNVHLIEEPVAAAIGADLPVDEPVANVVVDIGGGTTEVAIISFGG------VVSCHSiRI 180
|
170
....*....|....*.
gi 30089677 255 GGQDFNQRLLQHLYKE 270
Cdd:PRK13929 181 GGDQLDEDIVSFVRKK 196
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
34-285 |
2.26e-04 |
|
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466825 [Multi-domain] Cd Length: 263 Bit Score: 42.89 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 34 IGIDLGTtycsvgvffpgtGKVKVIPDENGHISIPSMVSFTDGDVYVgyeslELADSNPQNTIYDAKRFIgkiftpeele 113
Cdd:cd10227 1 IGIDIGN------------GNTKVVTGGGKEFKFPSAVAEARESSLD-----DGLLEDDIIVEYNGKRYL---------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 114 aeVGRYPFKVLHRNG-MAEFSVTSNETIIvspefvgsRLLLKLKEMAEEYLGmpVANAVISVPAEFDLQQRNSTIQAANL 192
Cdd:cd10227 54 --VGELALREGGGGRsTGDDKKKSEDALL--------LLLAALALLGDDEEV--DVNLVVGLPISEYKEEKKELKKKLLK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 193 AGLKI-------------LRVINEPTAAAMAYGLHKVDVF--YVLVIDLGGGTLDVSLLNKQGGMfltRAMSGNNKLGGQ 257
Cdd:cd10227 122 GLHEFtfngkerritindVKVLPEGAGAYLDYLLDDDELEdgNVLVIDIGGGTTDILTFENGKPI---EESSDTLPGGEE 198
|
250 260
....*....|....*....|....*...
gi 30089677 258 DFNQrLLQHLYKEIYQTYGFLPSRKEEI 285
Cdd:cd10227 199 ALEK-YADDILNELLKKLGDELDSADKI 225
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
34-270 |
2.67e-04 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 42.77 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 34 IGIDLGT--TYcsvgVFFPGTGKVkvipdenghISIPSMVSF--TDGDVY-VGYEsleladsnpqntiydAKRFIGKifT 108
Cdd:PRK13927 8 LGIDLGTanTL----VYVKGKGIV---------LNEPSVVAIrtDTKKVLaVGEE---------------AKQMLGR--T 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 109 PEELEAevgRYPFKvlhrNG-MAEFSVTS----------NETIIVSPEFVgsrlllklkemaeeylgmpvanavISVPAE 177
Cdd:PRK13927 58 PGNIVA---IRPMK----DGvIADFDVTEkmlkyfikkvHKNFRPSPRVV------------------------ICVPSG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 178 FDLQQRNSTIQAANLAGLKILRVINEPTAAAMAYGLhkvDVFY---VLVIDLGGGTLDV---SLlnkqGGMFLTRAMsgn 251
Cdd:PRK13927 107 ITEVERRAVRESALGAGAREVYLIEEPMAAAIGAGL---PVTEptgSMVVDIGGGTTEVaviSL----GGIVYSKSV--- 176
|
250
....*....|....*....
gi 30089677 252 nKLGGQDFNQRLLQHLYKE 270
Cdd:PRK13927 177 -RVGGDKFDEAIINYVRRN 194
|
|
| ASKHA_NBD_MamK |
cd24009 |
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ... |
34-233 |
4.04e-04 |
|
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: 42.20 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 34 IGIDLGTtYCSVgvffpgtgkvkvIPDENGH-ISIPSmvsftdgdvYVGYesleladsnPQNTIydAKRFIGK--IFTPE 110
Cdd:cd24009 4 IGIDLGT-SRSA------------VVTSRGKrFSFRS---------VVGY---------PKDII--ARKLLGKevLFGDE 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089677 111 ELE---AEVGRYPFkvlhRNGMAEFSVTSNETiivspefVGSRLLLKLKEMAEEYLGMPVAnAVISVPAEFDLQQRNSTI 187
Cdd:cd24009 51 ALEnrlALDLRRPL----EDGVIKEGDDRDLE-------AARELLQHLIELALPGPDDEIY-AVIGVPARASAENKQALL 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 30089677 188 QAANLAGLKILrVINEPTAAAmaYGLHKVDvfYVLVIDLGGGTLDV 233
Cdd:cd24009 119 EIARELVDGVM-VVSEPFAVA--YGLDRLD--NSLIVDIGAGTTDL 159
|
|
| |
